Log page index: User:ProteinBoxBot/PBB_Log_Index
Protein Status Quick Log - Date: 19:50, 30 October 2007 (UTC)[edit]
Proteins without matches (9)[edit]
Proteins with a High Potential Match (16)[edit]
Created (2)[edit]
Manual Inspection (Page not found) (23)[edit]
Protein Status Grid - Date: 19:50, 30 October 2007 (UTC)[edit]
Vebose Log - Date: 19:50, 30 October 2007 (UTC)[edit]
- INFO: Beginning work on ALB... {October 30, 2007 11:54:52 AM PDT}
- AMBIGUITY: Did not locate an acceptable page to update. {October 30, 2007 11:56:10 AM PDT}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB = {{PDB2|1ao6}}, {{PDB2|1bj5}}, {{PDB2|1bke}}, {{PDB2|1bm0}}, {{PDB2|1e78}}, {{PDB2|1e7a}}, {{PDB2|1e7b}}, {{PDB2|1e7c}}, {{PDB2|1e7e}}, {{PDB2|1e7f}}, {{PDB2|1e7g}}, {{PDB2|1e7h}}, {{PDB2|1e7i}}, {{PDB2|1gni}}, {{PDB2|1gnj}}, {{PDB2|1h9z}}, {{PDB2|1ha2}}, {{PDB2|1hk1}}, {{PDB2|1hk2}}, {{PDB2|1hk3}}, {{PDB2|1hk4}}, {{PDB2|1hk5}}, {{PDB2|1n5u}}, {{PDB2|1o9x}}, {{PDB2|1tf0}}, {{PDB2|1uor}}, {{PDB2|1ysx}}, {{PDB2|2bx8}}, {{PDB2|2bxa}}, {{PDB2|2bxb}}, {{PDB2|2bxc}}, {{PDB2|2bxd}}, {{PDB2|2bxe}}, {{PDB2|2bxf}}, {{PDB2|2bxg}}, {{PDB2|2bxh}}, {{PDB2|2bxi}}, {{PDB2|2bxk}}, {{PDB2|2bxl}}, {{PDB2|2bxm}}, {{PDB2|2bxn}}, {{PDB2|2bxo}}, {{PDB2|2bxp}}, {{PDB2|2bxq}}, {{PDB2|2esg}}, {{PDB2|2i2z}}, {{PDB2|2i30}}
| Name = Albumin
| HGNCid = 399
| Symbol = ALB
| AltSymbols =; DKFZp779N1935; PRO0883; PRO0903; PRO1341
| OMIM = 103600
| ECnumber =
| Homologene = 405
| MGIid = 87991
| GeneAtlas_image1 = PBB_GE_ALB_211298_s_at_tn.png
| Function = {{GNF_GO|id=GO:0003677 |text = DNA binding}} {{GNF_GO|id=GO:0005386 |text = transmembrane transporter activity}} {{GNF_GO|id=GO:0005504 |text = fatty acid binding}} {{GNF_GO|id=GO:0005507 |text = copper ion binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008144 |text = drug binding}} {{GNF_GO|id=GO:0015643 |text = toxin binding}} {{GNF_GO|id=GO:0016209 |text = antioxidant activity}} {{GNF_GO|id=GO:0019825 |text = oxygen binding}} {{GNF_GO|id=GO:0030170 |text = pyridoxal phosphate binding}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}} {{GNF_GO|id=GO:0005615 |text = extracellular space}} {{GNF_GO|id=GO:0043234 |text = protein complex}}
| Process = {{GNF_GO|id=GO:0006810 |text = transport}} {{GNF_GO|id=GO:0009267 |text = cellular response to starvation}} {{GNF_GO|id=GO:0019836 |text = hemolysis by symbiont of host red blood cells}} {{GNF_GO|id=GO:0043066 |text = negative regulation of apoptosis}} {{GNF_GO|id=GO:0043072 |text = negative regulation of non-apoptotic programmed cell death}} {{GNF_GO|id=GO:0051659 |text = maintenance of mitochondrion localization}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 213
| Hs_Ensembl = ENSG00000163631
| Hs_RefseqProtein = NP_000468
| Hs_RefseqmRNA = NM_000477
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 4
| Hs_GenLoc_start = 74488870
| Hs_GenLoc_end = 74505996
| Hs_Uniprot = P02768
| Mm_EntrezGene = 11657
| Mm_Ensembl = ENSMUSG00000029368
| Mm_RefseqmRNA = NM_009654
| Mm_RefseqProtein = NP_033784
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 5
| Mm_GenLoc_start = 91536101
| Mm_GenLoc_end = 91551800
| Mm_Uniprot = Q3TV03
}}
}}
'''Albumin''', also known as '''ALB''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = Albumin is a soluble, monomeric protein which comprises about one-half of the blood serum protein. Albumin functions primarily as a carrier protein for steroids, fatty acids, and thyroid hormones and plays a role in stabilizing extracellular fluid volume. Mutations in this gene on chromosome 4 result in various anomalous proteins. Albumin is a globular unglycosylated serum protein of molecular weight 65,000. The human albumin gene is 16,961 nucleotides long from the putative 'cap' site to the first poly(A) addition site. It is split into 15 exons which are symmetrically placed within the 3 domains that are thought to have arisen by triplication of a single primordial domain. Albumin is synthesized in the liver as preproalbumin which has an N-terminal peptide that is removed before the nascent protein is released from the rough endoplasmic reticulum. The product, proalbumin, is in turn cleaved in the Golgi vesicles to produce the secreted albumin.<ref>{{cite web | title = Entrez Gene: ALB albumin| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=213| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Curry S |title=Beyond expansion: structural studies on the transport roles of human serum albumin. |journal=Vox Sang. |volume=83 Suppl 1 |issue= |pages= 315-9 |year= 2003 |pmid= 12617161 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on APOB... {October 30, 2007 11:56:10 AM PDT}
- AMBIGUITY: Did not locate an acceptable page to update. {October 30, 2007 11:56:46 AM PDT}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Apolipoprotein B (including Ag(x) antigen)
| HGNCid = 603
| Symbol = APOB
| AltSymbols =; FLDB
| OMIM = 107730
| ECnumber =
| Homologene = 328
| MGIid = 88052
| GeneAtlas_image1 = PBB_GE_APOB_205108_s_at_tn.png
| Function = {{GNF_GO|id=GO:0005102 |text = receptor binding}} {{GNF_GO|id=GO:0005319 |text = lipid transporter activity}} {{GNF_GO|id=GO:0008201 |text = heparin binding}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}} {{GNF_GO|id=GO:0005625 |text = soluble fraction}} {{GNF_GO|id=GO:0005783 |text = endoplasmic reticulum}} {{GNF_GO|id=GO:0005792 |text = microsome}} {{GNF_GO|id=GO:0042627 |text = chylomicron}}
| Process = {{GNF_GO|id=GO:0006629 |text = lipid metabolic process}} {{GNF_GO|id=GO:0006642 |text = triacylglycerol mobilization}} {{GNF_GO|id=GO:0006869 |text = lipid transport}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0008015 |text = circulation}} {{GNF_GO|id=GO:0008202 |text = steroid metabolic process}} {{GNF_GO|id=GO:0008203 |text = cholesterol metabolic process}} {{GNF_GO|id=GO:0030301 |text = cholesterol transport}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 338
| Hs_Ensembl = ENSG00000084674
| Hs_RefseqProtein = NP_000375
| Hs_RefseqmRNA = NM_000384
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 2
| Hs_GenLoc_start = 21077806
| Hs_GenLoc_end = 21120450
| Hs_Uniprot = P04114
| Mm_EntrezGene = 238055
| Mm_Ensembl = ENSMUSG00000020609
| Mm_RefseqmRNA = XM_001000646
| Mm_RefseqProtein = XP_001000646
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 12
| Mm_GenLoc_start = 8003681
| Mm_GenLoc_end = 8042507
| Mm_Uniprot =
}}
}}
'''Apolipoprotein B (including Ag(x) antigen)''', also known as '''APOB''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = Apolipoprotein B (ApoB) is the main apolipoprotein of chylomicrons and low density lipoproteins (LDL). The protein occurs in the plasma in 2 main isoforms, apoB-48 and apoB-100. The first is synthesized exclusively by the gut, the second by the liver. The intestinal (B-48) and hepatic (B-100) forms of apoB are coded by a single gene and by a single mRNA transcript larger than 16 kb. The 2 proteins share a common amino terminal sequence. From structural studies, it is thought that apoB-48 represents the amino-terminal 47% of apoB-100 and that the carboxyl terminus of apoB-48 is in the vicinity of residue 2151 of mature apoB-100. Apolipoprotein B-48, a shortened form of apoB-100 lacking the LDL-receptor region, is a product generated when a stop codon (UAA) at residue 2180 is created by RNA editing.<ref>{{cite web | title = Entrez Gene: APOB apolipoprotein B (including Ag(x) antigen)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=338| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Mahley RW, Innerarity TL, Rall SC, Weisgraber KH |title=Plasma lipoproteins: apolipoprotein structure and function. |journal=J. Lipid Res. |volume=25 |issue= 12 |pages= 1277-94 |year= 1985 |pmid= 6099394 |doi= }}
*{{cite journal | author=Itakura H, Matsumoto A |title=[Apolipoprotein B] |journal=Nippon Rinsho |volume=52 |issue= 12 |pages= 3113-8 |year= 1995 |pmid= 7853698 |doi= }}
*{{cite journal | author=Chumakova OS, Zateĭshchikov DA, Sidorenko BA |title=[Apolipoprotein B: structure, function, gene polymorphism, and relation to atherosclerosis] |journal=Kardiologiia |volume=45 |issue= 6 |pages= 43-55 |year= 2006 |pmid= 16007035 |doi= }}
*{{cite journal | author=Ye J |title=Reliance of host cholesterol metabolic pathways for the life cycle of hepatitis C virus. |journal=PLoS Pathog. |volume=3 |issue= 8 |pages= e108 |year= 2007 |pmid= 17784784 |doi= 10.1371/journal.ppat.0030108 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on BDNF... {October 30, 2007 11:56:46 AM PDT}
- AMBIGUITY: Did not locate an acceptable page to update. {October 30, 2007 11:57:58 AM PDT}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB = {{PDB2|1b8m}}, {{PDB2|1bnd}}
| Name = Brain-derived neurotrophic factor
| HGNCid = 1033
| Symbol = BDNF
| AltSymbols =; MGC34632
| OMIM = 113505
| ECnumber =
| Homologene = 7245
| MGIid = 88145
| GeneAtlas_image1 = PBB_GE_BDNF_206382_s_at_tn.png
| Function = {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008083 |text = growth factor activity}}
| Component = {{GNF_GO|id=GO:0016023 |text = cytoplasmic membrane-bound vesicle}}
| Process = {{GNF_GO|id=GO:0001657 |text = ureteric bud development}} {{GNF_GO|id=GO:0006916 |text = anti-apoptosis}} {{GNF_GO|id=GO:0007406 |text = negative regulation of neuroblast proliferation}} {{GNF_GO|id=GO:0007411 |text = axon guidance}} {{GNF_GO|id=GO:0007412 |text = axon target recognition}} {{GNF_GO|id=GO:0007631 |text = feeding behavior}} {{GNF_GO|id=GO:0008038 |text = neuron recognition}} {{GNF_GO|id=GO:0014047 |text = glutamate secretion}} {{GNF_GO|id=GO:0016358 |text = dendrite development}} {{GNF_GO|id=GO:0019222 |text = regulation of metabolic process}} {{GNF_GO|id=GO:0021675 |text = nerve development}} {{GNF_GO|id=GO:0042490 |text = mechanoreceptor differentiation}} {{GNF_GO|id=GO:0043523 |text = regulation of neuron apoptosis}} {{GNF_GO|id=GO:0045666 |text = positive regulation of neuron differentiation}} {{GNF_GO|id=GO:0046668 |text = regulation of retinal programmed cell death}} {{GNF_GO|id=GO:0048167 |text = regulation of synaptic plasticity}} {{GNF_GO|id=GO:0048839 |text = inner ear development}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 627
| Hs_Ensembl = ENSG00000176697
| Hs_RefseqProtein = NP_001700
| Hs_RefseqmRNA = NM_001709
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 11
| Hs_GenLoc_start = 27633022
| Hs_GenLoc_end = 27699872
| Hs_Uniprot = P23560
| Mm_EntrezGene = 12064
| Mm_Ensembl = ENSMUSG00000048482
| Mm_RefseqmRNA = NM_001048139
| Mm_RefseqProtein = NP_001041604
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 2
| Mm_GenLoc_start = 109475539
| Mm_GenLoc_end = 109527845
| Mm_Uniprot = Q541P3
}}
}}
'''Brain-derived neurotrophic factor''', also known as '''BDNF''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = The protein encoded by this gene is a member of the nerve growth factor family. It is induced by cortical neurons, and is necessary for survival of striatal neurons in the brain. Expression of this gene is reduced in both Alzheimer's and Huntington disease patients. This gene may play a role in the regulation of stress response and in the biology of mood disorders. Multiple transcript variants encoding distinct isoforms have been described for this gene, but the full-length nature of only some could be determined.<ref>{{cite web | title = Entrez Gene: BDNF brain-derived neurotrophic factor| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=627| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Yamada K, Nabeshima T |title=Brain-derived neurotrophic factor/TrkB signaling in memory processes. |journal=J. Pharmacol. Sci. |volume=91 |issue= 4 |pages= 267-70 |year= 2004 |pmid= 12719654 |doi= }}
*{{cite journal | author=Pang PT, Lu B |title=Regulation of late-phase LTP and long-term memory in normal and aging hippocampus: role of secreted proteins tPA and BDNF. |journal=Ageing Res. Rev. |volume=3 |issue= 4 |pages= 407-30 |year= 2005 |pmid= 15541709 |doi= 10.1016/j.arr.2004.07.002 }}
*{{cite journal | author=Hashimoto K, Koizumi H, Nakazato M, ''et al.'' |title=Role of brain-derived neurotrophic factor in eating disorders: recent findings and its pathophysiological implications. |journal=Prog. Neuropsychopharmacol. Biol. Psychiatry |volume=29 |issue= 4 |pages= 499-504 |year= 2005 |pmid= 15866349 |doi= 10.1016/j.pnpbp.2005.01.007 }}
*{{cite journal | author=Tsai SJ |title=Increased central brain-derived neurotrophic factor activity could be a risk factor for substance abuse: Implications for treatment. |journal=Med. Hypotheses |volume=68 |issue= 2 |pages= 410-4 |year= 2007 |pmid= 16824691 |doi= 10.1016/j.mehy.2006.05.035 }}
*{{cite journal | author=Bath KG, Lee FS |title=Variant BDNF (Val66Met) impact on brain structure and function. |journal=Cognitive, affective & behavioral neuroscience |volume=6 |issue= 1 |pages= 79-85 |year= 2006 |pmid= 16869232 |doi= }}
*{{cite journal | author=Nair A, Vaidya VA |title=Cyclic AMP response element binding protein and brain-derived neurotrophic factor: molecules that modulate our mood? |journal=J. Biosci. |volume=31 |issue= 3 |pages= 423-34 |year= 2006 |pmid= 17006024 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on CCL5... {October 30, 2007 12:40:12 PM PDT}
- AMBIGUITY: Did not locate an acceptable page to update. {October 30, 2007 12:44:05 PM PDT}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB = {{PDB2|1b3a}}, {{PDB2|1eqt}}, {{PDB2|1hrj}}, {{PDB2|1rtn}}, {{PDB2|1rto}}, {{PDB2|1u4l}}, {{PDB2|1u4m}}, {{PDB2|1u4p}}, {{PDB2|1u4r}}
| Name = Chemokine (C-C motif) ligand 5
| HGNCid = 10632
| Symbol = CCL5
| AltSymbols =; D17S136E; MGC17164; RANTES; SCYA5; SISd; TCP228
| OMIM = 187011
| ECnumber =
| Homologene = 2244
| MGIid = 98262
| GeneAtlas_image1 = PBB_GE_CCL5_1405_i_at_tn.png
| GeneAtlas_image2 = PBB_GE_CCL5_204655_at_tn.png
| Function = {{GNF_GO|id=GO:0004871 |text = signal transducer activity}} {{GNF_GO|id=GO:0008009 |text = chemokine activity}} {{GNF_GO|id=GO:0042056 |text = chemoattractant activity}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}} {{GNF_GO|id=GO:0005615 |text = extracellular space}}
| Process = {{GNF_GO|id=GO:0006874 |text = cellular calcium ion homeostasis}} {{GNF_GO|id=GO:0006887 |text = exocytosis}} {{GNF_GO|id=GO:0006928 |text = cell motility}} {{GNF_GO|id=GO:0006935 |text = chemotaxis}} {{GNF_GO|id=GO:0006954 |text = inflammatory response}} {{GNF_GO|id=GO:0006955 |text = immune response}} {{GNF_GO|id=GO:0006968 |text = cellular defense response}} {{GNF_GO|id=GO:0006979 |text = response to oxidative stress}} {{GNF_GO|id=GO:0007155 |text = cell adhesion}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007267 |text = cell-cell signaling}} {{GNF_GO|id=GO:0009615 |text = response to virus}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 6352
| Hs_Ensembl = ENSG00000161570
| Hs_RefseqProtein = NP_002976
| Hs_RefseqmRNA = NM_002985
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 17
| Hs_GenLoc_start = 31222613
| Hs_GenLoc_end = 31231490
| Hs_Uniprot = P13501
| Mm_EntrezGene = 20304
| Mm_Ensembl = ENSMUSG00000035042
| Mm_RefseqmRNA = NM_013653
| Mm_RefseqProtein = NP_038681
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 11
| Mm_GenLoc_start = 83341978
| Mm_GenLoc_end = 83346713
| Mm_Uniprot = Q5XZF2
}}
}}
'''Chemokine (C-C motif) ligand 5''', also known as '''CCL5''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene is one of several CC cytokine genes clustered on the q-arm of chromosome 17. Cytokines are a family of secreted proteins involved in immunoregulatory and inflammatory processes. The CC cytokines are proteins characterized by two adjacent cysteines. The cytokine encoded by this gene functions as a chemoattractant for blood monocytes, memory T helper cells and eosinophils. It causes the release of histamine from basophils and activates eosinophils. This cytokine is one of the major HIV-suppressive factors produced by CD8+ cells. It functions as one of the natural ligands for the chemokine receptor CCR5 and it suppresses in vitro replication of the R5 strains of HIV-1, which use CCR5 as a coreceptor.<ref>{{cite web | title = Entrez Gene: CCL5 chemokine (C-C motif) ligand 5| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6352| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Muthumani K, Desai BM, Hwang DS, ''et al.'' |title=HIV-1 Vpr and anti-inflammatory activity. |journal=DNA Cell Biol. |volume=23 |issue= 4 |pages= 239-47 |year= 2004 |pmid= 15142381 |doi= 10.1089/104454904773819824 }}
*{{cite journal | author=Zhao RY, Elder RT |title=Viral infections and cell cycle G2/M regulation. |journal=Cell Res. |volume=15 |issue= 3 |pages= 143-9 |year= 2005 |pmid= 15780175 |doi= 10.1038/sj.cr.7290279 }}
*{{cite journal | author=Zhao RY, Bukrinsky M, Elder RT |title=HIV-1 viral protein R (Vpr) & host cellular responses. |journal=Indian J. Med. Res. |volume=121 |issue= 4 |pages= 270-86 |year= 2005 |pmid= 15817944 |doi= }}
*{{cite journal | author=Li L, Li HS, Pauza CD, ''et al.'' |title=Roles of HIV-1 auxiliary proteins in viral pathogenesis and host-pathogen interactions. |journal=Cell Res. |volume=15 |issue= 11-12 |pages= 923-34 |year= 2006 |pmid= 16354571 |doi= 10.1038/sj.cr.7290370 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on CHEK2... {October 30, 2007 12:46:51 PM PDT}
- AMBIGUITY: Did not locate an acceptable page to update. {October 30, 2007 12:48:54 PM PDT}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB = {{PDB2|1gxc}}, {{PDB2|2cn5}}, {{PDB2|2cn8}}
| Name = CHK2 checkpoint homolog (S. pombe)
| HGNCid = 16627
| Symbol = CHEK2
| AltSymbols =; CDS1; CHK2; HuCds1; LFS2; PP1425; RAD53
| OMIM = 604373
| ECnumber =
| Homologene = 38289
| MGIid = 1355321
| GeneAtlas_image1 = PBB_GE_CHEK2_210416_s_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0000287 |text = magnesium ion binding}} {{GNF_GO|id=GO:0004674 |text = protein serine/threonine kinase activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0016740 |text = transferase activity}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}}
| Process = {{GNF_GO|id=GO:0000077 |text = DNA damage checkpoint}} {{GNF_GO|id=GO:0006468 |text = protein amino acid phosphorylation}} {{GNF_GO|id=GO:0006974 |text = response to DNA damage stimulus}} {{GNF_GO|id=GO:0007049 |text = cell cycle}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 11200
| Hs_Ensembl = ENSG00000183765
| Hs_RefseqProtein = NP_001005735
| Hs_RefseqmRNA = NM_001005735
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 22
| Hs_GenLoc_start = 27413731
| Hs_GenLoc_end = 27467822
| Hs_Uniprot = O96017
| Mm_EntrezGene = 50883
| Mm_Ensembl = ENSMUSG00000029521
| Mm_RefseqmRNA = NM_016681
| Mm_RefseqProtein = NP_057890
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 5
| Mm_GenLoc_start = 111080319
| Mm_GenLoc_end = 111114435
| Mm_Uniprot = Q543W6
}}
}}
'''CHK2 checkpoint homolog (S. pombe)''', also known as '''CHEK2''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = In response to DNA damage and replication blocks, cell cycle progression is halted through the control of critical cell cycle regulators. The protein encoded by this gene is a cell cycle checkpoint regulator and putative tumor suppressor. It contains a forkhead-associated protein interaction domain essential for activation in response to DNA damage and is rapidly phosphorylated in response to replication blocks and DNA damage. When activated, the encoded protein is known to inhibit CDC25C phosphatase, preventing entry into mitosis, and has been shown to stabilize the tumor suppressor protein p53, leading to cell cycle arrest in G1. In addition, this protein interacts with and phosphorylates BRCA1, allowing BRCA1 to restore survival after DNA damage. Mutations in this gene have been linked with Li-Fraumeni syndrome, a highly penetrant familial cancer phenotype usually associated with inherited mutations in TP53. Also, mutations in this gene are thought to confer a predisposition to sarcomas, breast cancer, and brain tumors. This nuclear protein is a member of the CDS1 subfamily of serine/threonine protein kinases. Three transcript variants encoding different isoforms have been found for this gene.<ref>{{cite web | title = Entrez Gene: CHEK2 CHK2 checkpoint homolog (S. pombe)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=11200| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Caspari T |title=How to activate p53. |journal=Curr. Biol. |volume=10 |issue= 8 |pages= R315-7 |year= 2000 |pmid= 10801407 |doi= }}
*{{cite journal | author=McGowan CH |title=Checking in on Cds1 (Chk2): A checkpoint kinase and tumor suppressor. |journal=Bioessays |volume=24 |issue= 6 |pages= 502-11 |year= 2002 |pmid= 12111733 |doi= 10.1002/bies.10101 }}
*{{cite journal | author=Honrado E, Osorio A, Palacios J, Benitez J |title=Pathology and gene expression of hereditary breast tumors associated with BRCA1, BRCA2 and CHEK2 gene mutations. |journal=Oncogene |volume=25 |issue= 43 |pages= 5837-45 |year= 2006 |pmid= 16998498 |doi= 10.1038/sj.onc.1209875 }}
*{{cite journal | author=Nevanlinna H, Bartek J |title=The CHEK2 gene and inherited breast cancer susceptibility. |journal=Oncogene |volume=25 |issue= 43 |pages= 5912-9 |year= 2006 |pmid= 16998506 |doi= 10.1038/sj.onc.1209877 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on COMT... {October 30, 2007 12:05:28 PM PDT}
- AMBIGUITY: Did not locate an acceptable page to update. {October 30, 2007 12:07:30 PM PDT}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Catechol-O-methyltransferase
| HGNCid = 2228
| Symbol = COMT
| AltSymbols =;
| OMIM = 116790
| ECnumber =
| Homologene = 30982
| MGIid = 88470
| GeneAtlas_image1 = PBB_GE_COMT_208818_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_COMT_208817_at_tn.png
| GeneAtlas_image3 = PBB_GE_COMT_213981_at_tn.png
| Function = {{GNF_GO|id=GO:0000287 |text = magnesium ion binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008171 |text = O-methyltransferase activity}} {{GNF_GO|id=GO:0016206 |text = catechol O-methyltransferase activity}} {{GNF_GO|id=GO:0016740 |text = transferase activity}}
| Component = {{GNF_GO|id=GO:0005625 |text = soluble fraction}} {{GNF_GO|id=GO:0005792 |text = microsome}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process = {{GNF_GO|id=GO:0006584 |text = catecholamine metabolic process}} {{GNF_GO|id=GO:0042420 |text = dopamine catabolic process}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 1312
| Hs_Ensembl = ENSG00000093010
| Hs_RefseqProtein = NP_000745
| Hs_RefseqmRNA = NM_000754
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 22
| Hs_GenLoc_start = 18309334
| Hs_GenLoc_end = 18337450
| Hs_Uniprot = P21964
| Mm_EntrezGene = 12846
| Mm_Ensembl = ENSMUSG00000000326
| Mm_RefseqmRNA = NM_007744
| Mm_RefseqProtein = NP_031770
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 16
| Mm_GenLoc_start = 18321400
| Mm_GenLoc_end = 18325520
| Mm_Uniprot = Q91XH4
}}
}}
'''Catechol-O-methyltransferase''', also known as '''COMT''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = Catechol-O-methyltransferase catalyzes the transfer of a methyl group from S-adenosylmethionine to catecholamines, including the neurotransmitters dopamine, epinephrine, and norepinephrine. This O-methylation results in one of the major degradative pathways of the catecholamine transmitters. In addition to its role in the metabolism of endogenous substances, COMT is important in the metabolism of catechol drugs used in the treatment of hypertension, asthma, and Parkinson disease. COMT is found in two forms in tissues, a soluble form (S-COMT) and a membrane-bound form (MB-COMT). The differences between S-COMT and MB-COMT reside within the N-termini. The transcript variants are formed through the use of alternative translation initiation sites and promoters.<ref>{{cite web | title = Entrez Gene: COMT catechol-O-methyltransferase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1312| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Trendelenburg U |title=The interaction of transport mechanisms and intracellular enzymes in metabolizing systems. |journal=J. Neural Transm. Suppl. |volume=32 |issue= |pages= 3-18 |year= 1991 |pmid= 2089098 |doi= }}
*{{cite journal | author=Tai CH, Wu RM |title=Catechol-O-methyltransferase and Parkinson's disease. |journal=Acta Med. Okayama |volume=56 |issue= 1 |pages= 1-6 |year= 2002 |pmid= 11873938 |doi= }}
*{{cite journal | author=Zhu BT |title=On the mechanism of homocysteine pathophysiology and pathogenesis: a unifying hypothesis. |journal=Histol. Histopathol. |volume=17 |issue= 4 |pages= 1283-91 |year= 2003 |pmid= 12371153 |doi= }}
*{{cite journal | author=Oroszi G, Goldman D |title=Alcoholism: genes and mechanisms. |journal=Pharmacogenomics |volume=5 |issue= 8 |pages= 1037-48 |year= 2005 |pmid= 15584875 |doi= 10.1517/14622416.5.8.1037 }}
*{{cite journal | author=Fan JB, Zhang CS, Gu NF, ''et al.'' |title=Catechol-O-methyltransferase gene Val/Met functional polymorphism and risk of schizophrenia: a large-scale association study plus meta-analysis. |journal=Biol. Psychiatry |volume=57 |issue= 2 |pages= 139-44 |year= 2005 |pmid= 15652872 |doi= 10.1016/j.biopsych.2004.10.018 }}
*{{cite journal | author=Tunbridge EM, Harrison PJ, Weinberger DR |title=Catechol-o-methyltransferase, cognition, and psychosis: Val158Met and beyond. |journal=Biol. Psychiatry |volume=60 |issue= 2 |pages= 141-51 |year= 2006 |pmid= 16476412 |doi= 10.1016/j.biopsych.2005.10.024 }}
*{{cite journal | author=Diaz-Asper CM, Weinberger DR, Goldberg TE |title=Catechol-O-methyltransferase polymorphisms and some implications for cognitive therapeutics. |journal=NeuroRx : the journal of the American Society for Experimental NeuroTherapeutics |volume=3 |issue= 1 |pages= 97-105 |year= 2006 |pmid= 16490416 |doi= 10.1016/j.nurx.2005.12.010 }}
*{{cite journal | author=Craddock N, Owen MJ, O'Donovan MC |title=The catechol-O-methyl transferase (COMT) gene as a candidate for psychiatric phenotypes: evidence and lessons. |journal=Mol. Psychiatry |volume=11 |issue= 5 |pages= 446-58 |year= 2006 |pmid= 16505837 |doi= 10.1038/sj.mp.4001808 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on FGFR3... {October 30, 2007 12:07:30 PM PDT}
- AMBIGUITY: Did not locate an acceptable page to update. {October 30, 2007 12:10:00 PM PDT}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB = {{PDB2|1ry7}}
| Name = Fibroblast growth factor receptor 3 (achondroplasia, thanatophoric dwarfism)
| HGNCid = 3690
| Symbol = FGFR3
| AltSymbols =; ACH; CD333; CEK2; HSFGFR3EX; JTK4
| OMIM = 134934
| ECnumber =
| Homologene = 55437
| MGIid = 95524
| GeneAtlas_image1 = PBB_GE_FGFR3_204379_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_FGFR3_204380_s_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0004713 |text = protein-tyrosine kinase activity}} {{GNF_GO|id=GO:0004872 |text = receptor activity}} {{GNF_GO|id=GO:0005007 |text = fibroblast growth factor receptor activity}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0016740 |text = transferase activity}} {{GNF_GO|id=GO:0042802 |text = identical protein binding}}
| Component = {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0016020 |text = membrane}}
| Process = {{GNF_GO|id=GO:0000165 |text = MAPKKK cascade}} {{GNF_GO|id=GO:0001501 |text = skeletal development}} {{GNF_GO|id=GO:0006468 |text = protein amino acid phosphorylation}} {{GNF_GO|id=GO:0007259 |text = JAK-STAT cascade}} {{GNF_GO|id=GO:0008543 |text = fibroblast growth factor receptor signaling pathway}} {{GNF_GO|id=GO:0016049 |text = cell growth}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 2261
| Hs_Ensembl = ENSG00000068078
| Hs_RefseqProtein = NP_000133
| Hs_RefseqmRNA = NM_000142
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 4
| Hs_GenLoc_start = 1764832
| Hs_GenLoc_end = 1780396
| Hs_Uniprot = P22607
| Mm_EntrezGene = 14184
| Mm_Ensembl = ENSMUSG00000054252
| Mm_RefseqmRNA = NM_008010
| Mm_RefseqProtein = NP_032036
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 5
| Mm_GenLoc_start = 34038581
| Mm_GenLoc_end = 34053924
| Mm_Uniprot = Q3TQL1
}}
}}
'''Fibroblast growth factor receptor 3 (achondroplasia, thanatophoric dwarfism)''', also known as '''FGFR3''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = The protein encoded by this gene is a member of the fibroblast growth factor receptor family, where amino acid sequence is highly conserved between members and throughout evolution. FGFR family members differ from one another in their ligand affinities and tissue distribution. A full-length representative protein would consist of an extracellular region, composed of three immunoglobulin-like domains, a single hydrophobic membrane-spanning segment and a cytoplasmic tyrosine kinase domain. The extracellular portion of the protein interacts with fibroblast growth factors, setting in motion a cascade of downstream signals, ultimately influencing mitogenesis and differentiation. This particular family member binds acidic and basic fibroblast growth hormone and plays a role in bone development and maintenance. Mutations in this gene lead to craniosynostosis and multiple types of skeletal dysplasia. Alternative splicing occurs and additional variants have been described, including those utilizing alternate exon 8 rather than 9, but their full-length nature has not been determined.<ref>{{cite web | title = Entrez Gene: FGFR3 fibroblast growth factor receptor 3 (achondroplasia, thanatophoric dwarfism)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2261| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Schweitzer DN, Graham JM, Lachman RS, ''et al.'' |title=Subtle radiographic findings of achondroplasia in patients with Crouzon syndrome with acanthosis nigricans due to an Ala391Glu substitution in FGFR3. |journal=Am. J. Med. Genet. |volume=98 |issue= 1 |pages= 75-91 |year= 2001 |pmid= 11426459 |doi= }}
*{{cite journal | author=Horton WA, Lunstrum GP |title=Fibroblast growth factor receptor 3 mutations in achondroplasia and related forms of dwarfism. |journal=Reviews in endocrine & metabolic disorders |volume=3 |issue= 4 |pages= 381-5 |year= 2003 |pmid= 12424440 |doi= }}
*{{cite journal | author=Bonaventure J, Silve C |title=[Hereditary skeletal dysplasias and FGFR3 and PTHR1 signaling pathways] |journal=Med Sci (Paris) |volume=21 |issue= 11 |pages= 954-61 |year= 2006 |pmid= 16274647 |doi= }}
*{{cite journal | author=Hernández S, Toll A, Baselga E, ''et al.'' |title=Fibroblast growth factor receptor 3 mutations in epidermal nevi and associated low grade bladder tumors. |journal=J. Invest. Dermatol. |volume=127 |issue= 7 |pages= 1664-6 |year= 2007 |pmid= 17255960 |doi= 10.1038/sj.jid.5700705 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on HLA-C... {October 30, 2007 12:10:00 PM PDT}
- AMBIGUITY: Did not locate an acceptable page to update. {October 30, 2007 12:13:34 PM PDT}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB = {{PDB2|1efx}}, {{PDB2|1im9}}, {{PDB2|1qqd}}
| Name = Major histocompatibility complex, class I, C
| HGNCid = 4933
| Symbol = HLA-C
| AltSymbols =; Cw*1701; D6S204; FLJ27082; HLA-JY3; HLC-C; PSORS1
| OMIM = 142840
| ECnumber =
| Homologene = 86715
| MGIid =
| GeneAtlas_image1 = PBB_GE_HLA-C_209140_x_at_tn.png
| GeneAtlas_image2 = PBB_GE_HLA-C_216526_x_at_tn.png
| GeneAtlas_image3 = PBB_GE_HLA-C_208729_x_at_tn.png
| Function = {{GNF_GO|id=GO:0003777 |text = microtubule motor activity}} {{GNF_GO|id=GO:0032393 |text = MHC class I receptor activity}} {{GNF_GO|id=GO:0032395 |text = MHC class II receptor activity}}
| Component = {{GNF_GO|id=GO:0005858 |text = axonemal dynein complex}} {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}} {{GNF_GO|id=GO:0042612 |text = MHC class I protein complex}}
| Process = {{GNF_GO|id=GO:0001539 |text = ciliary or flagellar motility}} {{GNF_GO|id=GO:0002474 |text = antigen processing and presentation of peptide antigen via MHC class I}} {{GNF_GO|id=GO:0006955 |text = immune response}} {{GNF_GO|id=GO:0019882 |text = antigen processing and presentation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 3107
| Hs_Ensembl = ENSG00000204525
| Hs_RefseqProtein = XP_001131707
| Hs_RefseqmRNA = XM_001131707
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 6
| Hs_GenLoc_start = 31344499
| Hs_GenLoc_end = 31347914
| Hs_Uniprot = P10321
| Mm_EntrezGene = 667977
| Mm_Ensembl =
| Mm_RefseqmRNA = XM_001003863
| Mm_RefseqProtein = XP_001003863
| Mm_GenLoc_db =
| Mm_GenLoc_chr =
| Mm_GenLoc_start =
| Mm_GenLoc_end =
| Mm_Uniprot =
}}
}}
'''Major histocompatibility complex, class I, C''', also known as '''HLA-C''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = HLA-C belongs to the HLA class I heavy chain paralogues. This class I molecule is a heterodimer consisting of a heavy chain and a light chain (beta-2 microglobulin). The heavy chain is anchored in the membrane. Class I molecules play a central role in the immune system by presenting peptides derived from endoplasmic reticulum lumen. They are expressed in nearly all cells. The heavy chain is approximately 45 kDa and its gene contains 8 exons. Exon one encodes the leader peptide, exons 2 and 3 encode the alpha1 and alpha2 domain, which both bind the peptide, exon 4 encodes the alpha3 domain, exon 5 encodes the transmembrane region, and exons 6 and 7 encode the cytoplasmic tail. Polymorphisms within exon 2 and exon 3 are responsible for the peptide binding specificity of each class one molecule. Typing for these polymorphisms is routinely done for bone marrow and kidney transplantation. Over one hundred HLA-C alleles have been described<ref>{{cite web | title = Entrez Gene: HLA-C major histocompatibility complex, class I, C| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3107| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Geyer M, Fackler OT, Peterlin BM |title=Structure--function relationships in HIV-1 Nef. |journal=EMBO Rep. |volume=2 |issue= 7 |pages= 580-5 |year= 2001 |pmid= 11463741 |doi= 10.1093/embo-reports/kve141 }}
*{{cite journal | author=Greenway AL, Holloway G, McPhee DA, ''et al.'' |title=HIV-1 Nef control of cell signalling molecules: multiple strategies to promote virus replication. |journal=J. Biosci. |volume=28 |issue= 3 |pages= 323-35 |year= 2004 |pmid= 12734410 |doi= }}
*{{cite journal | author=Bénichou S, Benmerah A |title=[The HIV nef and the Kaposi-sarcoma-associated virus K3/K5 proteins: "parasites"of the endocytosis pathway] |journal=Med Sci (Paris) |volume=19 |issue= 1 |pages= 100-6 |year= 2003 |pmid= 12836198 |doi= }}
*{{cite journal | author=Leavitt SA, SchOn A, Klein JC, ''et al.'' |title=Interactions of HIV-1 proteins gp120 and Nef with cellular partners define a novel allosteric paradigm. |journal=Curr. Protein Pept. Sci. |volume=5 |issue= 1 |pages= 1-8 |year= 2004 |pmid= 14965316 |doi= }}
*{{cite journal | author=Tolstrup M, Ostergaard L, Laursen AL, ''et al.'' |title=HIV/SIV escape from immune surveillance: focus on Nef. |journal=Curr. HIV Res. |volume=2 |issue= 2 |pages= 141-51 |year= 2004 |pmid= 15078178 |doi= }}
*{{cite journal | author=Joseph AM, Kumar M, Mitra D |title=Nef: "necessary and enforcing factor" in HIV infection. |journal=Curr. HIV Res. |volume=3 |issue= 1 |pages= 87-94 |year= 2005 |pmid= 15638726 |doi= }}
*{{cite journal | author=Anderson JL, Hope TJ |title=HIV accessory proteins and surviving the host cell. |journal=Current HIV/AIDS reports |volume=1 |issue= 1 |pages= 47-53 |year= 2005 |pmid= 16091223 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on HLA-DQB1... {October 30, 2007 12:13:34 PM PDT}
- AMBIGUITY: Did not locate an acceptable page to update. {October 30, 2007 12:17:07 PM PDT}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB = {{PDB2|1jk8}}, {{PDB2|1s9v}}
| Name = Major histocompatibility complex, class II, DQ beta 1
| HGNCid = 4944
| Symbol = HLA-DQB1
| AltSymbols =; CELIAC1; HLA-DQB; IDDM1
| OMIM = 604305
| ECnumber =
| Homologene =
| MGIid =
| GeneAtlas_image1 = PBB_GE_HLA-DQB1_209823_x_at_tn.png
| GeneAtlas_image2 = PBB_GE_HLA-DQB1_211656_x_at_tn.png
| GeneAtlas_image3 = PBB_GE_HLA-DQB1_212998_x_at_tn.png
| Function = {{GNF_GO|id=GO:0005525 |text = GTP binding}} {{GNF_GO|id=GO:0032395 |text = MHC class II receptor activity}}
| Component = {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}} {{GNF_GO|id=GO:0042613 |text = MHC class II protein complex}}
| Process = {{GNF_GO|id=GO:0002504 |text = antigen processing and presentation of peptide or polysaccharide antigen via MHC class II}} {{GNF_GO|id=GO:0006955 |text = immune response}} {{GNF_GO|id=GO:0007049 |text = cell cycle}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 3119
| Hs_Ensembl = ENSG00000206237
| Hs_RefseqProtein = NP_002114
| Hs_RefseqmRNA = NM_002123
| Hs_GenLoc_db =
| Hs_GenLoc_chr = c6_COX
| Hs_GenLoc_start = 32697517
| Hs_GenLoc_end = 32704934
| Hs_Uniprot = P01918
| Mm_EntrezGene =
| Mm_Ensembl =
| Mm_RefseqmRNA =
| Mm_RefseqProtein =
| Mm_GenLoc_db =
| Mm_GenLoc_chr =
| Mm_GenLoc_start =
| Mm_GenLoc_end =
| Mm_Uniprot =
}}
}}
'''Major histocompatibility complex, class II, DQ beta 1''', also known as '''HLA-DQB1''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = HLA-DQB1 belongs to the HLA class II beta chain paralogues. This class II molecule is a heterodimer consisting of an alpha (DQA) and a beta chain (DQB), both anchored in the membrane. It plays a central role in the immune system by presenting peptides derived from extracellular proteins. Class II molecules are expressed in antigen presenting cells (APC: B lymphocytes, dendritic cells, macrophages). The beta chain is approximately 26-28 kDa and it contains 6 exons. Exon one encodes the leader peptide, exons 2 and 3 encode the two extracellular domains, exon 4 encodes the transmembrane domain and exon 5 encodes the cytoplasmic tail. Within the DQ molecule both the alpha chain and the beta chain contain the polymorphisms specifying the peptide binding specificities, resulting in up to 4 different molecules. Typing for these polymorphisms is routinely done for bone marrow transplantation.<ref>{{cite web | title = Entrez Gene: HLA-DQB1 major histocompatibility complex, class II, DQ beta 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3119| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Todd JA |title=Genetic control of autoimmunity in type 1 diabetes. |journal=Immunol. Today |volume=11 |issue= 4 |pages= 122-9 |year= 1990 |pmid= 2187469 |doi= }}
*{{cite journal | author=Lau M, Terasaki PI, Park MS |title=International Cell Exchange, 1994. |journal=Clinical transplants |volume= |issue= |pages= 467-88 |year= 1995 |pmid= 7547576 |doi= }}
*{{cite journal | author=Todd JA |title=Genetics of type 1 diabetes. |journal=Pathol. Biol. |volume=45 |issue= 3 |pages= 219-27 |year= 1997 |pmid= 9296067 |doi= }}
*{{cite journal | author=Schmidt H, Williamson D, Ashley-Koch A |title=HLA-DR15 haplotype and multiple sclerosis: a HuGE review. |journal=Am. J. Epidemiol. |volume=165 |issue= 10 |pages= 1097-109 |year= 2007 |pmid= 17329717 |doi= 10.1093/aje/kwk118 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on IL1RN... {October 30, 2007 12:17:07 PM PDT}
- AMBIGUITY: Did not locate an acceptable page to update. {October 30, 2007 12:20:30 PM PDT}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB = {{PDB2|1ilr}}, {{PDB2|1ilt}}, {{PDB2|1ira}}, {{PDB2|1irp}}, {{PDB2|2irt}}
| Name = Interleukin 1 receptor antagonist
| HGNCid = 6000
| Symbol = IL1RN
| AltSymbols =; IL1RA; ICIL-1RA; IL-1ra3; IL1F3; IRAP; MGC10430
| OMIM = 147679
| ECnumber =
| Homologene = 11163
| MGIid = 96547
| GeneAtlas_image1 = PBB_GE_IL1RN_212657_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_IL1RN_212659_s_at_tn.png
| GeneAtlas_image3 = PBB_GE_IL1RN_216243_s_at_tn.png
| Function = {{GNF_GO|id=GO:0005152 |text = interleukin-1 receptor antagonist activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}} {{GNF_GO|id=GO:0005615 |text = extracellular space}} {{GNF_GO|id=GO:0005622 |text = intracellular}}
| Process = {{GNF_GO|id=GO:0006954 |text = inflammatory response}} {{GNF_GO|id=GO:0006955 |text = immune response}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 3557
| Hs_Ensembl = ENSG00000136689
| Hs_RefseqProtein = NP_000568
| Hs_RefseqmRNA = NM_000577
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 2
| Hs_GenLoc_start = 113591941
| Hs_GenLoc_end = 113608063
| Hs_Uniprot = P18510
| Mm_EntrezGene = 16181
| Mm_Ensembl = ENSMUSG00000026981
| Mm_RefseqmRNA = NM_001039701
| Mm_RefseqProtein = NP_001034790
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 2
| Mm_GenLoc_start = 24158869
| Mm_GenLoc_end = 24173490
| Mm_Uniprot = Q3TBV5
}}
}}
'''Interleukin 1 receptor antagonist''', also known as '''IL1RN''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = The protein encoded by this gene is a member of the interleukin 1 cytokine family. This protein inhibits the activities of interleukin 1, alpha (IL1A) and interleukin 1, beta (IL1B), and modulates a variety of interleukin 1 related immune and inflammatory responses. This gene and five other closely related cytokine genes form a gene cluster spanning approximately 400 kb on chromosome 2. A polymorphism of this gene is reported to be associated with increased risk of osteoporotic fractures and gastric cancer. Four alternatively spliced transcript variants encoding distinct isoforms have been reported.<ref>{{cite web | title = Entrez Gene: IL1RN interleukin 1 receptor antagonist| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3557| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Arend WP, Malyak M, Guthridge CJ, Gabay C |title=Interleukin-1 receptor antagonist: role in biology. |journal=Annu. Rev. Immunol. |volume=16 |issue= |pages= 27-55 |year= 1998 |pmid= 9597123 |doi= 10.1146/annurev.immunol.16.1.27 }}
*{{cite journal | author=Adcock IM, Ito K |title=Molecular mechanisms of corticosteroid actions. |journal=Monaldi archives for chest disease = Archivio Monaldi per le malattie del torace / Fondazione clinica del lavoro, IRCCS [and] Istituto di clinica tisiologica e malattie apparato respiratorio, Università di Napoli, Secondo ateneo |volume=55 |issue= 3 |pages= 256-66 |year= 2000 |pmid= 10948677 |doi= }}
*{{cite journal | author=Arend WP |title=The balance between IL-1 and IL-1Ra in disease. |journal=Cytokine Growth Factor Rev. |volume=13 |issue= 4-5 |pages= 323-40 |year= 2003 |pmid= 12220547 |doi= }}
*{{cite journal | author=Sehouli J, Mustea A, Könsgen D, ''et al.'' |title=Polymorphism of IL-1 receptor antagonist gene: role in cancer. |journal=Anticancer Res. |volume=22 |issue= 6A |pages= 3421-4 |year= 2003 |pmid= 12530098 |doi= }}
*{{cite journal | author=Kamangar F, Cheng C, Abnet CC, Rabkin CS |title=Interleukin-1B polymorphisms and gastric cancer risk--a meta-analysis. |journal=Cancer Epidemiol. Biomarkers Prev. |volume=15 |issue= 10 |pages= 1920-8 |year= 2007 |pmid= 17035400 |doi= 10.1158/1055-9965.EPI-06-0267 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on IRS1... {October 30, 2007 12:20:30 PM PDT}
- CREATE: Found no pages, creating new page. {October 30, 2007 12:21:30 PM PDT}
- CREATED: Created new protein page: IRS1 {October 30, 2007 12:21:44 PM PDT}
- INFO: Beginning work on ITGAV... {October 30, 2007 12:21:44 PM PDT}
- AMBIGUITY: Did not locate an acceptable page to update. {October 30, 2007 12:22:45 PM PDT}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB = {{PDB2|1jv2}}, {{PDB2|1l5g}}, {{PDB2|1m1x}}, {{PDB2|1u8c}}
| Name = Integrin, alpha V (vitronectin receptor, alpha polypeptide, antigen CD51)
| HGNCid = 6150
| Symbol = ITGAV
| AltSymbols =; CD51; MSK8; VNRA
| OMIM = 193210
| ECnumber =
| Homologene = 20510
| MGIid = 96608
| GeneAtlas_image1 = PBB_GE_ITGAV_202351_at_tn.png
| Function = {{GNF_GO|id=GO:0004872 |text = receptor activity}} {{GNF_GO|id=GO:0005509 |text = calcium ion binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0008305 |text = integrin complex}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process = {{GNF_GO|id=GO:0007155 |text = cell adhesion}} {{GNF_GO|id=GO:0007160 |text = cell-matrix adhesion}} {{GNF_GO|id=GO:0007229 |text = integrin-mediated signaling pathway}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 3685
| Hs_Ensembl = ENSG00000138448
| Hs_RefseqProtein = NP_002201
| Hs_RefseqmRNA = NM_002210
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 2
| Hs_GenLoc_start = 187163045
| Hs_GenLoc_end = 187253872
| Hs_Uniprot = P06756
| Mm_EntrezGene = 16410
| Mm_Ensembl = ENSMUSG00000027087
| Mm_RefseqmRNA = NM_008402
| Mm_RefseqProtein = NP_032428
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 2
| Mm_GenLoc_start = 83525354
| Mm_GenLoc_end = 83604646
| Mm_Uniprot = Q3U4C8
}}
}}
'''Integrin, alpha V (vitronectin receptor, alpha polypeptide, antigen CD51)''', also known as '''ITGAV''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = ITAGV encodes integrin alpha chain V. Integrins are heterodimeric integral membrane proteins composed of an alpha chain and a beta chain. The I-domain containing integrin alpha V undergoes post-translational cleavage to yield disulfide-linked heavy and light chains, that combine with multiple integrin beta chains to form different integrins. Among the known associating beta chains (beta chains 1,3,5,6, and 8; 'ITGB1', 'ITGB3', 'ITGB5', 'ITGB6', and 'ITGB8'), each can interact with extracellular matrix ligands; the alpha V beta 3 integrin, perhaps the most studied of these, is referred to as the Vitronectin receptor (VNR). In addition to adhesion, many integrins are known to facilitate signal transduction.<ref>{{cite web | title = Entrez Gene: ITGAV integrin, alpha V (vitronectin receptor, alpha polypeptide, antigen CD51)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3685| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Horton MA |title=The alpha v beta 3 integrin "vitronectin receptor". |journal=Int. J. Biochem. Cell Biol. |volume=29 |issue= 5 |pages= 721-5 |year= 1997 |pmid= 9251239 |doi= }}
*{{cite journal | author=Porter JC, Hogg N |title=Integrins take partners: cross-talk between integrins and other membrane receptors. |journal=Trends Cell Biol. |volume=8 |issue= 10 |pages= 390-6 |year= 1999 |pmid= 9789327 |doi= }}
*{{cite journal | author=Sajid M, Stouffer GA |title=The role of alpha(v)beta3 integrins in vascular healing. |journal=Thromb. Haemost. |volume=87 |issue= 2 |pages= 187-93 |year= 2002 |pmid= 11858476 |doi= }}
*{{cite journal | author=Cooper CR, Chay CH, Pienta KJ |title=The role of alpha(v)beta(3) in prostate cancer progression. |journal=Neoplasia |volume=4 |issue= 3 |pages= 191-4 |year= 2002 |pmid= 11988838 |doi= 10.1038/sj/neo/7900224 }}
*{{cite journal | author=Cacciari B, Spalluto G |title=Non peptidic alphavbeta3 antagonists: recent developments. |journal=Curr. Med. Chem. |volume=12 |issue= 1 |pages= 51-70 |year= 2005 |pmid= 15638730 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on KDR... {October 30, 2007 12:22:45 PM PDT}
- AMBIGUITY: Did not locate an acceptable page to update. {October 30, 2007 12:26:33 PM PDT}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB = {{PDB2|1y6a}}, {{PDB2|1y6b}}
| Name = Kinase insert domain receptor (a type III receptor tyrosine kinase)
| HGNCid = 6307
| Symbol = KDR
| AltSymbols =; CD309; FLK1; VEGFR; VEGFR2
| OMIM = 191306
| ECnumber =
| Homologene = 55639
| MGIid = 96683
| GeneAtlas_image1 = PBB_GE_KDR_203934_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0004872 |text = receptor activity}} {{GNF_GO|id=GO:0005021 |text = vascular endothelial growth factor receptor activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0016740 |text = transferase activity}}
| Component = {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0016020 |text = membrane}}
| Process = {{GNF_GO|id=GO:0001525 |text = angiogenesis}} {{GNF_GO|id=GO:0001570 |text = vasculogenesis}} {{GNF_GO|id=GO:0006468 |text = protein amino acid phosphorylation}} {{GNF_GO|id=GO:0007169 |text = transmembrane receptor protein tyrosine kinase signaling pathway}} {{GNF_GO|id=GO:0007275 |text = multicellular organismal development}} {{GNF_GO|id=GO:0016477 |text = cell migration}} {{GNF_GO|id=GO:0030097 |text = hemopoiesis}} {{GNF_GO|id=GO:0045165 |text = cell fate commitment}} {{GNF_GO|id=GO:0045446 |text = endothelial cell differentiation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 3791
| Hs_Ensembl = ENSG00000128052
| Hs_RefseqProtein = NP_002244
| Hs_RefseqmRNA = NM_002253
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 4
| Hs_GenLoc_start = 55639401
| Hs_GenLoc_end = 55686519
| Hs_Uniprot = P35968
| Mm_EntrezGene = 16542
| Mm_Ensembl = ENSMUSG00000062960
| Mm_RefseqmRNA = XM_984991
| Mm_RefseqProtein = XP_990085
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 5
| Mm_GenLoc_start = 76214954
| Mm_GenLoc_end = 76260125
| Mm_Uniprot = Q3UQZ6
}}
}}
'''Kinase insert domain receptor (a type III receptor tyrosine kinase)''', also known as '''KDR''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text =
}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Petrova TV, Makinen T, Alitalo K |title=Signaling via vascular endothelial growth factor receptors. |journal=Exp. Cell Res. |volume=253 |issue= 1 |pages= 117-30 |year= 1999 |pmid= 10579917 |doi= 10.1006/excr.1999.4707 }}
*{{cite journal | author=Sato Y, Kanno S, Oda N, ''et al.'' |title=Properties of two VEGF receptors, Flt-1 and KDR, in signal transduction. |journal=Ann. N. Y. Acad. Sci. |volume=902 |issue= |pages= 201-5; discussion 205-7 |year= 2000 |pmid= 10865839 |doi= }}
*{{cite journal | author=Zachary I, Gliki G |title=Signaling transduction mechanisms mediating biological actions of the vascular endothelial growth factor family. |journal=Cardiovasc. Res. |volume=49 |issue= 3 |pages= 568-81 |year= 2001 |pmid= 11166270 |doi= }}
*{{cite journal | author=Vené R, Benelli R, Noonan DM, Albini A |title=HIV-Tat dependent chemotaxis and invasion, key aspects of tat mediated pathogenesis. |journal=Clin. Exp. Metastasis |volume=18 |issue= 7 |pages= 533-8 |year= 2001 |pmid= 11688957 |doi= }}
*{{cite journal | author=Lenton K |title=VEGFR-2 (KDR/Flk-1). |journal=J. Biol. Regul. Homeost. Agents |volume=16 |issue= 3 |pages= 227-32 |year= 2003 |pmid= 12456025 |doi= }}
*{{cite journal | author=Matsumoto T, Mugishima H |title=Signal transduction via vascular endothelial growth factor (VEGF) receptors and their roles in atherogenesis. |journal=J. Atheroscler. Thromb. |volume=13 |issue= 3 |pages= 130-5 |year= 2006 |pmid= 16835467 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on KRAS... {October 30, 2007 12:26:33 PM PDT}
- AMBIGUITY: Did not locate an acceptable page to update. {October 30, 2007 12:28:44 PM PDT}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB = {{PDB2|121p}}, {{PDB2|1aa9}}, {{PDB2|1agp}}, {{PDB2|1bkd}}, {{PDB2|1clu}}, {{PDB2|1crp}}, {{PDB2|1crq}}, {{PDB2|1crr}}, {{PDB2|1ctq}}, {{PDB2|1gnp}}, {{PDB2|1gnq}}, {{PDB2|1gnr}}, {{PDB2|1he8}}, {{PDB2|1iaq}}, {{PDB2|1ioz}}, {{PDB2|1jah}}, {{PDB2|1jai}}, {{PDB2|1k8r}}, {{PDB2|1lf0}}, {{PDB2|1lf5}}, {{PDB2|1lfd}}, {{PDB2|1nvu}}, {{PDB2|1nvv}}, {{PDB2|1nvw}}, {{PDB2|1nvx}}, {{PDB2|1p2s}}, {{PDB2|1p2t}}, {{PDB2|1p2u}}, {{PDB2|1p2v}}, {{PDB2|1plj}}, {{PDB2|1plk}}, {{PDB2|1pll}}, {{PDB2|1q21}}, {{PDB2|1qra}}, {{PDB2|1rvd}}, {{PDB2|1wq1}}, {{PDB2|1xcm}}, {{PDB2|1xd2}}, {{PDB2|1xj0}}, {{PDB2|1zvq}}, {{PDB2|1zw6}}, {{PDB2|221p}}, {{PDB2|2c5l}}, {{PDB2|2ce2}}, {{PDB2|2cl0}}, {{PDB2|2cl6}}, {{PDB2|2cl7}}, {{PDB2|2clc}}, {{PDB2|2cld}}, {{PDB2|2evw}}, {{PDB2|2pmx}}, {{PDB2|2q21}}, {{PDB2|421p}}, {{PDB2|521p}}, {{PDB2|5p21}}, {{PDB2|621p}}, {{PDB2|6q21}}, {{PDB2|721p}}, {{PDB2|821p}}
| Name = V-Ki-ras2 Kirsten rat sarcoma viral oncogene homolog
| HGNCid = 6407
| Symbol = KRAS
| AltSymbols =; C-K-RAS; K-RAS2A; K-RAS2B; K-RAS4A; K-RAS4B; KI-RAS; KRAS1; KRAS2; NS3; RASK2
| OMIM = 190070
| ECnumber =
| Homologene = 37990
| MGIid = 96680
| GeneAtlas_image1 = PBB_GE_KRAS_204009_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_KRAS_204010_s_at_tn.png
| GeneAtlas_image3 = PBB_GE_KRAS_214352_s_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0003924 |text = GTPase activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0005525 |text = GTP binding}}
| Component = {{GNF_GO|id=GO:0005622 |text = intracellular}} {{GNF_GO|id=GO:0005624 |text = membrane fraction}} {{GNF_GO|id=GO:0016020 |text = membrane}}
| Process = {{GNF_GO|id=GO:0000074 |text = regulation of progression through cell cycle}} {{GNF_GO|id=GO:0007264 |text = small GTPase mediated signal transduction}} {{GNF_GO|id=GO:0007605 |text = sensory perception of sound}} {{GNF_GO|id=GO:0051146 |text = striated muscle cell differentiation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 3845
| Hs_Ensembl = ENSG00000133703
| Hs_RefseqProtein = NP_004976
| Hs_RefseqmRNA = NM_004985
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 12
| Hs_GenLoc_start = 25249449
| Hs_GenLoc_end = 25295121
| Hs_Uniprot = P01116
| Mm_EntrezGene = 16653
| Mm_Ensembl = ENSMUSG00000030265
| Mm_RefseqmRNA = NM_021284
| Mm_RefseqProtein = NP_067259
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 6
| Mm_GenLoc_start = 145173866
| Mm_GenLoc_end = 145207390
| Mm_Uniprot = O70564
}}
}}
'''V-Ki-ras2 Kirsten rat sarcoma viral oncogene homolog''', also known as '''KRAS''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene, a Kirsten ras oncogene homolog from the mammalian ras gene family, encodes a protein that is a member of the small GTPase superfamily. A single amino acid substitution is responsible for an activating mutation. The transforming protein that results is implicated in various malignancies, including lung adenocarcinoma, mucinous adenoma, ductal carcinoma of the pancreas and colorectal carcinoma. Alternative splicing leads to variants encoding two isoforms that differ in the C-terminal region.<ref>{{cite web | title = Entrez Gene: KRAS v-Ki-ras2 Kirsten rat sarcoma viral oncogene homolog| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3845| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Kahn S, Yamamoto F, Almoguera C, ''et al.'' |title=The c-K-ras gene and human cancer (review). |journal=Anticancer Res. |volume=7 |issue= 4A |pages= 639-52 |year= 1987 |pmid= 3310850 |doi= }}
*{{cite journal | author=Yamamoto F, Nakano H, Neville C, Perucho M |title=Structure and mechanisms of activation of c-K-ras oncogenes in human lung cancer. |journal=Prog. Med. Virol. |volume=32 |issue= |pages= 101-14 |year= 1985 |pmid= 3895297 |doi= }}
*{{cite journal | author=Porta M, Ayude D, Alguacil J, Jariod M |title=Exploring environmental causes of altered ras effects: fragmentation plus integration? |journal=Mol. Carcinog. |volume=36 |issue= 2 |pages= 45-52 |year= 2003 |pmid= 12557259 |doi= 10.1002/mc.10093 }}
*{{cite journal | author=Smakman N, Borel Rinkes IH, Voest EE, Kranenburg O |title=Control of colorectal metastasis formation by K-Ras. |journal=Biochim. Biophys. Acta |volume=1756 |issue= 2 |pages= 103-14 |year= 2006 |pmid= 16098678 |doi= 10.1016/j.bbcan.2005.07.001 }}
*{{cite journal | author=Castagnola P, Giaretti W |title=Mutant KRAS, chromosomal instability and prognosis in colorectal cancer. |journal=Biochim. Biophys. Acta |volume=1756 |issue= 2 |pages= 115-25 |year= 2006 |pmid= 16112461 |doi= 10.1016/j.bbcan.2005.06.003 }}
*{{cite journal | author=Deramaudt T, Rustgi AK |title=Mutant KRAS in the initiation of pancreatic cancer. |journal=Biochim. Biophys. Acta |volume=1756 |issue= 2 |pages= 97-101 |year= 2006 |pmid= 16169155 |doi= 10.1016/j.bbcan.2005.08.003 }}
*{{cite journal | author=Pretlow TP, Pretlow TG |title=Mutant KRAS in aberrant crypt foci (ACF): initiation of colorectal cancer? |journal=Biochim. Biophys. Acta |volume=1756 |issue= 2 |pages= 83-96 |year= 2006 |pmid= 16219426 |doi= 10.1016/j.bbcan.2005.06.002 }}
*{{cite journal | author=Su YH, Wang M, Aiamkitsumrit B, ''et al.'' |title=Detection of a K-ras mutation in urine of patients with colorectal cancer. |journal=Cancer biomarkers : section A of Disease markers |volume=1 |issue= 2-3 |pages= 177-82 |year= 2007 |pmid= 17192038 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on LPL... {October 30, 2007 12:28:44 PM PDT}
- AMBIGUITY: Did not locate an acceptable page to update. {October 30, 2007 12:29:42 PM PDT}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Lipoprotein lipase
| HGNCid = 6677
| Symbol = LPL
| AltSymbols =; LIPD
| OMIM = 238600
| ECnumber =
| Homologene = 200
| MGIid = 96820
| GeneAtlas_image1 = PBB_GE_LPL_203549_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_LPL_203548_s_at_tn.png
| Function = {{GNF_GO|id=GO:0004465 |text = lipoprotein lipase activity}} {{GNF_GO|id=GO:0005319 |text = lipid transporter activity}} {{GNF_GO|id=GO:0008201 |text = heparin binding}} {{GNF_GO|id=GO:0016787 |text = hydrolase activity}} {{GNF_GO|id=GO:0048503 |text = GPI anchor binding}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0042627 |text = chylomicron}}
| Process = {{GNF_GO|id=GO:0006631 |text = fatty acid metabolic process}} {{GNF_GO|id=GO:0008015 |text = circulation}} {{GNF_GO|id=GO:0016042 |text = lipid catabolic process}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 4023
| Hs_Ensembl = ENSG00000175445
| Hs_RefseqProtein = NP_000228
| Hs_RefseqmRNA = NM_000237
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 8
| Hs_GenLoc_start = 19841232
| Hs_GenLoc_end = 19867912
| Hs_Uniprot = P06858
| Mm_EntrezGene = 16956
| Mm_Ensembl =
| Mm_RefseqmRNA = XM_977885
| Mm_RefseqProtein = XP_982979
| Mm_GenLoc_db =
| Mm_GenLoc_chr =
| Mm_GenLoc_start =
| Mm_GenLoc_end =
| Mm_Uniprot =
}}
}}
'''Lipoprotein lipase''', also known as '''LPL''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = LPL encodes lipoprotein lipase, which is expressed in heart, muscle, and adipose tissue. LPL functions as a homodimer, and has the dual functions of triglyceride hydrolase and ligand/bridging factor for receptor-mediated lipoprotein uptake. Severe mutations that cause LPL deficiency result in type I hyperlipoproteinemia, while less extreme mutations in LPL are linked to many disorders of lipoprotein metabolism.<ref>{{cite web | title = Entrez Gene: LPL lipoprotein lipase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4023| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Zechner R |title=The tissue-specific expression of lipoprotein lipase: implications for energy and lipoprotein metabolism. |journal=Curr. Opin. Lipidol. |volume=8 |issue= 2 |pages= 77-88 |year= 1997 |pmid= 9183545 |doi= }}
*{{cite journal | author=Fisher RM, Humphries SE, Talmud PJ |title=Common variation in the lipoprotein lipase gene: effects on plasma lipids and risk of atherosclerosis. |journal=Atherosclerosis |volume=135 |issue= 2 |pages= 145-59 |year= 1998 |pmid= 9430364 |doi= }}
*{{cite journal | author=Beisiegel U |title=Lipoprotein metabolism. |journal=Eur. Heart J. |volume=19 Suppl A |issue= |pages= A20-3 |year= 1998 |pmid= 9519338 |doi= }}
*{{cite journal | author=Pentikäinen MO, Oksjoki R, Oörni K, Kovanen PT |title=Lipoprotein lipase in the arterial wall: linking LDL to the arterial extracellular matrix and much more. |journal=Arterioscler. Thromb. Vasc. Biol. |volume=22 |issue= 2 |pages= 211-7 |year= 2002 |pmid= 11834518 |doi= }}
*{{cite journal | author=Mead JR, Irvine SA, Ramji DP |title=Lipoprotein lipase: structure, function, regulation, and role in disease. |journal=J. Mol. Med. |volume=80 |issue= 12 |pages= 753-69 |year= 2003 |pmid= 12483461 |doi= 10.1007/s00109-002-0384-9 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on MUC1... {October 30, 2007 12:29:42 PM PDT}
- AMBIGUITY: Did not locate an acceptable page to update. {October 30, 2007 12:32:13 PM PDT}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB = {{PDB2|2acm}}
| Name = Mucin 1, cell surface associated
| HGNCid = 7508
| Symbol = MUC1
| AltSymbols =; EMA; CD227; H23AG; MAM6; PEM; PEMT; PUM
| OMIM = 158340
| ECnumber =
| Homologene = 8416
| MGIid = 97231
| GeneAtlas_image1 = PBB_GE_MUC1_207847_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_MUC1_211695_x_at_tn.png
| GeneAtlas_image3 = PBB_GE_MUC1_213693_s_at_tn.png
| Function = {{GNF_GO|id=GO:0003779 |text = actin binding}} {{GNF_GO|id=GO:0005179 |text = hormone activity}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}} {{GNF_GO|id=GO:0005856 |text = cytoskeleton}} {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process =
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 4582
| Hs_Ensembl = ENSG00000185499
| Hs_RefseqProtein = NP_001018021
| Hs_RefseqmRNA = NM_001018021
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 1
| Hs_GenLoc_start = 153388480
| Hs_GenLoc_end = 153429330
| Hs_Uniprot = P15941
| Mm_EntrezGene = 17829
| Mm_Ensembl = ENSMUSG00000042784
| Mm_RefseqmRNA = NM_013605
| Mm_RefseqProtein = NP_038633
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 3
| Mm_GenLoc_start = 89314979
| Mm_GenLoc_end = 89319296
| Mm_Uniprot = Q99K60
}}
}}
'''Mucin 1, cell surface associated''', also known as '''MUC1''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene is a member of the mucin family and encodes a membrane bound, glycosylated phosphoprotein. The protein is anchored to the apical surface of many epithelia by a transmembrane domain, with the degree of glycosylation varying with cell type. It also includes a 20 aa variable number tandem repeat (VNTR) domain, with the number of repeats varying from 20 to 120 in different individuals. The protein serves a protective function by binding to pathogens and also functions in a cell signaling capacity. Overexpression, aberrant intracellular localization, and changes in glycosylation of this protein have been associated with carcinomas. Multiple alternatively spliced transcript variants that encode different isoforms of this gene have been reported, but the full-length nature of only some has been determined.<ref>{{cite web | title = Entrez Gene: MUC1 mucin 1, cell surface associated| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4582| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Peterson JA, Scallan CD, Ceriani RL, Hamosh M |title=Structural and functional aspects of three major glycoproteins of the human milk fat globule membrane. |journal=Adv. Exp. Med. Biol. |volume=501 |issue= |pages= 179-87 |year= 2002 |pmid= 11787681 |doi= }}
*{{cite journal | author=Hu XF, Yang E, Li J, Xing PX |title=MUC1 cytoplasmic tail: a potential therapeutic target for ovarian carcinoma. |journal=Expert Rev Anticancer Ther |volume=6 |issue= 8 |pages= 1261-71 |year= 2006 |pmid= 16925492 |doi= 10.1586/14737140.6.8.1261 }}
*{{cite journal | author=Leroy X, Buisine MP, Leteurtre E, ''et al.'' |title=[MUC1 (EMA): A key molecule of carcinogenesis?] |journal=Annales de pathologie |volume=26 |issue= 4 |pages= 257-66 |year= 2007 |pmid= 17128152 |doi= }}
*{{cite journal | author=Li Y, Cozzi PJ |title=MUC1 is a promising therapeutic target for prostate cancer therapy. |journal=Current cancer drug targets |volume=7 |issue= 3 |pages= 259-71 |year= 2007 |pmid= 17504123 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on NOD2... {October 30, 2007 12:48:54 PM PDT}
- AMBIGUITY: Did not locate an acceptable page to update. {October 30, 2007 12:50:24 PM PDT}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Nucleotide-binding oligomerization domain containing 2
| HGNCid = 5331
| Symbol = NOD2
| AltSymbols =; CD; ACUG; BLAU; CARD15; CLR16.3; IBD1; NLRC2; NOD2B; PSORAS1
| OMIM = 605956
| ECnumber =
| Homologene = 11156
| MGIid = 2429397
| GeneAtlas_image1 = PBB_GE_NOD2_220066_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0019899 |text = enzyme binding}} {{GNF_GO|id=GO:0019901 |text = protein kinase binding}} {{GNF_GO|id=GO:0042834 |text = peptidoglycan binding}} {{GNF_GO|id=GO:0050700 |text = CARD domain binding}}
| Component = {{GNF_GO|id=GO:0005622 |text = intracellular}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0005829 |text = cytosol}} {{GNF_GO|id=GO:0005886 |text = plasma membrane}} {{GNF_GO|id=GO:0031982 |text = vesicle}}
| Process = {{GNF_GO|id=GO:0001816 |text = cytokine production}} {{GNF_GO|id=GO:0007242 |text = intracellular signaling cascade}} {{GNF_GO|id=GO:0008063 |text = Toll signaling pathway}} {{GNF_GO|id=GO:0016045 |text = detection of bacterium}} {{GNF_GO|id=GO:0042742 |text = defense response to bacterium}} {{GNF_GO|id=GO:0042981 |text = regulation of apoptosis}} {{GNF_GO|id=GO:0043123 |text = positive regulation of I-kappaB kinase/NF-kappaB cascade}} {{GNF_GO|id=GO:0050718 |text = positive regulation of interleukin-1 beta secretion}} {{GNF_GO|id=GO:0051092 |text = activation of NF-kappaB transcription factor}} {{GNF_GO|id=GO:0051259 |text = protein oligomerization}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 64127
| Hs_Ensembl = ENSG00000167207
| Hs_RefseqProtein = NP_071445
| Hs_RefseqmRNA = NM_022162
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 16
| Hs_GenLoc_start = 49288551
| Hs_GenLoc_end = 49324488
| Hs_Uniprot = Q9HC29
| Mm_EntrezGene = 257632
| Mm_Ensembl = ENSMUSG00000055994
| Mm_RefseqmRNA = XM_989552
| Mm_RefseqProtein = XP_994646
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 8
| Mm_GenLoc_start = 91537452
| Mm_GenLoc_end = 91578579
| Mm_Uniprot = Q2PZA3
}}
}}
'''Nucleotide-binding oligomerization domain containing 2''', also known as '''NOD2''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene is a member of the Nod1/Apaf-1 family and encodes a protein with two caspase recruitment (CARD) domains and six leucine-rich repeats (LRRs). The protein is primarily expressed in the peripheral blood leukocytes. It plays a role in the immune response to intracellular bacterial lipopolysaccharides (LPS) by recognizing the muramyl dipeptide (MDP) derived from them and activating the NFKB protein. Mutations in this gene have been associated with Crohn disease and Blau syndrome.<ref>{{cite web | title = Entrez Gene: NOD2 nucleotide-binding oligomerization domain containing 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=64127| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Inohara N, Ogura Y, Nuñez G |title=Nods: a family of cytosolic proteins that regulate the host response to pathogens. |journal=Curr. Opin. Microbiol. |volume=5 |issue= 1 |pages= 76-80 |year= 2002 |pmid= 11834373 |doi= }}
*{{cite journal | author=Punchard NA |title=Overview: Nod2, cause of, or contributor to, Crohn's disease. |journal=Current opinion in investigational drugs (London, England : 2000) |volume=2 |issue= 10 |pages= 1378-81 |year= 2002 |pmid= 11890351 |doi= }}
*{{cite journal | author=Hugot JP |title=[Role of NOD2 gene in Crohn's disease] |journal=Gastroenterol. Clin. Biol. |volume=26 |issue= 1 |pages= 13-5 |year= 2002 |pmid= 11938034 |doi= }}
*{{cite journal | author=Satsangi J, Morecroft J, Shah NB, Nimmo E |title=Genetics of inflammatory bowel disease: scientific and clinical implications. |journal=Best practice & research. Clinical gastroenterology |volume=17 |issue= 1 |pages= 3-18 |year= 2003 |pmid= 12617879 |doi= }}
*{{cite journal | author=Rosenbaum JT, Planck SR, Davey MP, ''et al.'' |title=With a mere nod, uveitis enters a new era. |journal=Am. J. Ophthalmol. |volume=136 |issue= 4 |pages= 729-32 |year= 2003 |pmid= 14516815 |doi= }}
*{{cite journal | author=Kurokawa T, Kikuchi T, Ohta K, ''et al.'' |title=Ocular manifestations in Blau syndrome associated with a CARD15/Nod2 mutation. |journal=Ophthalmology |volume=110 |issue= 10 |pages= 2040-4 |year= 2003 |pmid= 14522785 |doi= 10.1016/S0161-6420(03)00717-6 }}
*{{cite journal | author=Girardin SE, Hugot JP, Sansonetti PJ |title=Lessons from Nod2 studies: towards a link between Crohn's disease and bacterial sensing. |journal=Trends Immunol. |volume=24 |issue= 12 |pages= 652-8 |year= 2004 |pmid= 14644139 |doi= }}
*{{cite journal | author=Newman B, Siminovitch K |title=Inflammatory bowel disease: Crohn's disease and the success of NODern genetics. |journal=Clinical and investigative medicine. Médecine clinique et experimentale |volume=26 |issue= 6 |pages= 303-14 |year= 2004 |pmid= 14690304 |doi= }}
*{{cite journal | author=Oostenbrug LE, van Dullemen HM, te Meerman GJ, Jansen PL |title=IBD and genetics: new developments. |journal=Scand. J. Gastroenterol. Suppl. |volume= |issue= 239 |pages= 63-8 |year= 2004 |pmid= 14743885 |doi= }}
*{{cite journal | author=Kambe N, Nishikomori R, Kanazawa N |title=The cytosolic pattern-recognition receptor Nod2 and inflammatory granulomatous disorders. |journal=J. Dermatol. Sci. |volume=39 |issue= 2 |pages= 71-80 |year= 2005 |pmid= 15927452 |doi= 10.1016/j.jdermsci.2005.04.001 }}
*{{cite journal | author=Newman B, Siminovitch KA |title=Recent advances in the genetics of inflammatory bowel disease. |journal=Curr. Opin. Gastroenterol. |volume=21 |issue= 4 |pages= 401-7 |year= 2005 |pmid= 15930978 |doi= }}
*{{cite journal | author=Martinon F, Tschopp J |title=NLRs join TLRs as innate sensors of pathogens. |journal=Trends Immunol. |volume=26 |issue= 8 |pages= 447-54 |year= 2006 |pmid= 15967716 |doi= 10.1016/j.it.2005.06.004 }}
*{{cite journal | author=Strober W, Murray PJ, Kitani A, Watanabe T |title=Signalling pathways and molecular interactions of NOD1 and NOD2. |journal=Nat. Rev. Immunol. |volume=6 |issue= 1 |pages= 9-20 |year= 2006 |pmid= 16493424 |doi= 10.1038/nri1747 }}
*{{cite journal | author=Cavanaugh J |title=NOD2: ethnic and geographic differences. |journal=World J. Gastroenterol. |volume=12 |issue= 23 |pages= 3673-7 |year= 2006 |pmid= 16773683 |doi= }}
*{{cite journal | author=Hugot JP |title=CARD15/NOD2 mutations in Crohn's disease. |journal=Ann. N. Y. Acad. Sci. |volume=1072 |issue= |pages= 9-18 |year= 2006 |pmid= 17057186 |doi= 10.1196/annals.1326.011 }}
*{{cite journal | author=Radford-Smith G, Pandeya N |title=Associations between NOD2/CARD15 genotype and phenotype in Crohn's disease--Are we there yet? |journal=World J. Gastroenterol. |volume=12 |issue= 44 |pages= 7097-103 |year= 2007 |pmid= 17131470 |doi= }}
*{{cite journal | author=Vignal C, Singer E, Peyrin-Biroulet L, ''et al.'' |title=How NOD2 mutations predispose to Crohn's disease? |journal=Microbes Infect. |volume=9 |issue= 5 |pages= 658-63 |year= 2007 |pmid= 17379562 |doi= 10.1016/j.micinf.2007.01.016 }}
*{{cite journal | author=Quaglietta L, te Velde A, Staiano A, ''et al.'' |title=Functional consequences of NOD2/CARD15 mutations in Crohn disease. |journal=J. Pediatr. Gastroenterol. Nutr. |volume=44 |issue= 5 |pages= 529-39 |year= 2007 |pmid= 17460484 |doi= 10.1097/MPG.0b013e31803815ee }}
*{{cite journal | author=van der Linde K, Boor PP, Houwing-Duistermaat JJ, ''et al.'' |title=CARD15 mutations in Dutch familial and sporadic inflammatory bowel disease and an overview of European studies. |journal=European journal of gastroenterology & hepatology |volume=19 |issue= 6 |pages= 449-59 |year= 2007 |pmid= 17489054 |doi= 10.1097/01.meg.0000236887.44214.6a }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on PARP1... {October 30, 2007 11:51:33 AM PDT}
- AMBIGUITY: Did not locate an acceptable page to update. {October 30, 2007 11:54:51 AM PDT}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB = {{PDB2|1uk0}}, {{PDB2|1uk1}}, {{PDB2|1wok}}, {{PDB2|2cok}}, {{PDB2|2cr9}}, {{PDB2|2cs2}}, {{PDB2|2dmj}}
| Name = Poly (ADP-ribose) polymerase family, member 1
| HGNCid = 270
| Symbol = PARP1
| AltSymbols =; ADPRT; ADPRT1; PARP; PARP-1; PPOL; pADPRT-1
| OMIM = 173870
| ECnumber =
| Homologene = 1222
| MGIid = 1340806
| GeneAtlas_image1 = PBB_GE_PARP1_208644_at_tn.png
| Function = {{GNF_GO|id=GO:0003677 |text = DNA binding}} {{GNF_GO|id=GO:0003950 |text = NAD+ ADP-ribosyltransferase activity}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0016757 |text = transferase activity, transferring glycosyl groups}} {{GNF_GO|id=GO:0042802 |text = identical protein binding}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}} {{GNF_GO|id=GO:0051287 |text = NAD binding}}
| Component = {{GNF_GO|id=GO:0005622 |text = intracellular}} {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005635 |text = nuclear envelope}} {{GNF_GO|id=GO:0005730 |text = nucleolus}}
| Process = {{GNF_GO|id=GO:0000723 |text = telomere maintenance}} {{GNF_GO|id=GO:0006284 |text = base-excision repair}} {{GNF_GO|id=GO:0006366 |text = transcription from RNA polymerase II promoter}} {{GNF_GO|id=GO:0006471 |text = protein amino acid ADP-ribosylation}} {{GNF_GO|id=GO:0040009 |text = regulation of growth rate}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 142
| Hs_Ensembl = ENSG00000143799
| Hs_RefseqProtein = NP_001609
| Hs_RefseqmRNA = NM_001618
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 1
| Hs_GenLoc_start = 224615015
| Hs_GenLoc_end = 224662414
| Hs_Uniprot = P09874
| Mm_EntrezGene = 11545
| Mm_Ensembl =
| Mm_RefseqmRNA = NM_007415
| Mm_RefseqProtein = NP_031441
| Mm_GenLoc_db =
| Mm_GenLoc_chr =
| Mm_GenLoc_start =
| Mm_GenLoc_end =
| Mm_Uniprot =
}}
}}
'''Poly (ADP-ribose) polymerase family, member 1''', also known as '''PARP1''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene encodes a chromatin-associated enzyme, poly(ADP-ribosyl)transferase, which modifies various nuclear proteins by poly(ADP-ribosyl)ation. The modification is dependent on DNA and is involved in the regulation of various important cellular processes such as differentiation, proliferation, and tumor transformation and also in the regulation of the molecular events involved in the recovery of cell from DNA damage. In addition, this enzyme may be the site of mutation in Fanconi anemia, and may participate in the pathophysiology of type I diabetes.<ref>{{cite web | title = Entrez Gene: PARP1 poly (ADP-ribose) polymerase family, member 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=142| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Helleday T, Bryant HE, Schultz N |title=Poly(ADP-ribose) polymerase (PARP-1) in homologous recombination and as a target for cancer therapy. |journal=Cell Cycle |volume=4 |issue= 9 |pages= 1176-8 |year= 2006 |pmid= 16123586 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on PLAUR... {October 30, 2007 12:34:25 PM PDT}
- AMBIGUITY: Did not locate an acceptable page to update. {October 30, 2007 12:36:58 PM PDT}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB = {{PDB2|1ywh}}, {{PDB2|2fd6}}, {{PDB2|2i9b}}
| Name = Plasminogen activator, urokinase receptor
| HGNCid = 9053
| Symbol = PLAUR
| AltSymbols =; CD87; UPAR; URKR
| OMIM = 173391
| ECnumber =
| Homologene = 48120
| MGIid = 97612
| GeneAtlas_image1 = PBB_GE_PLAUR_210845_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_PLAUR_211924_s_at_tn.png
| GeneAtlas_image3 = PBB_GE_PLAUR_214866_at_tn.png
| Function = {{GNF_GO|id=GO:0019899 |text = enzyme binding}} {{GNF_GO|id=GO:0030377 |text = U-plasminogen activator receptor activity}} {{GNF_GO|id=GO:0048503 |text = GPI anchor binding}}
| Component = {{GNF_GO|id=GO:0005886 |text = plasma membrane}} {{GNF_GO|id=GO:0009986 |text = cell surface}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}} {{GNF_GO|id=GO:0019898 |text = extrinsic to membrane}}
| Process = {{GNF_GO|id=GO:0006928 |text = cell motility}} {{GNF_GO|id=GO:0006935 |text = chemotaxis}} {{GNF_GO|id=GO:0007166 |text = cell surface receptor linked signal transduction}} {{GNF_GO|id=GO:0007596 |text = blood coagulation}} {{GNF_GO|id=GO:0030162 |text = regulation of proteolysis}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5329
| Hs_Ensembl = ENSG00000011422
| Hs_RefseqProtein = NP_001005376
| Hs_RefseqmRNA = NM_001005376
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 19
| Hs_GenLoc_start = 48842111
| Hs_GenLoc_end = 48866539
| Hs_Uniprot = Q03405
| Mm_EntrezGene = 18793
| Mm_Ensembl = ENSMUSG00000046223
| Mm_RefseqmRNA = NM_011113
| Mm_RefseqProtein = NP_035243
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 7
| Mm_GenLoc_start = 24171260
| Mm_GenLoc_end = 24184727
| Mm_Uniprot = Q3U2D1
}}
}}
'''Plasminogen activator, urokinase receptor''', also known as '''PLAUR''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene encodes the receptor for urokinase plasminogen activator and, given its role in localizing and promoting plasmin formation, likely influences many normal and pathological processes related to cell-surface plasminogen activation and localized degradation of the extracellular matrix. It binds both the proprotein and mature forms of urokinase plasminogen activator and permits the activation of the receptor-bound pro-enzyme by plasmin. The protein lacks transmembrane or cytoplasmic domains and may be anchored to the plasma membrane by a glycosyl-phosphatidylinositol (GPI) moiety following cleavage of the nascent polypeptide near its carboxy-terminus. However, a soluble protein is also produced in some cell types. Alternative splicing results in multiple transcript variants encoding different isoforms. The proprotein experiences several post-translational cleavage reactions that have not yet been fully defined.<ref>{{cite web | title = Entrez Gene: PLAUR plasminogen activator, urokinase receptor| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5329| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Kjøller L |title=The urokinase plasminogen activator receptor in the regulation of the actin cytoskeleton and cell motility. |journal=Biol. Chem. |volume=383 |issue= 1 |pages= 5-19 |year= 2003 |pmid= 11928822 |doi= }}
*{{cite journal | author=Chavakis T, Kanse SM, May AE, Preissner KT |title=Haemostatic factors occupy new territory: the role of the urokinase receptor system and kininogen in inflammation. |journal=Biochem. Soc. Trans. |volume=30 |issue= 2 |pages= 168-73 |year= 2002 |pmid= 12023845 |doi= 10.1042/ }}
*{{cite journal | author=Ploug M, Gårdsvoll H, Jørgensen TJ, ''et al.'' |title=Structural analysis of the interaction between urokinase-type plasminogen activator and its receptor: a potential target for anti-invasive cancer therapy. |journal=Biochem. Soc. Trans. |volume=30 |issue= 2 |pages= 177-83 |year= 2002 |pmid= 12023847 |doi= 10.1042/ }}
*{{cite journal | author=Alfano M, Sidenius N, Blasi F, Poli G |title=The role of urokinase-type plasminogen activator (uPA)/uPA receptor in HIV-1 infection. |journal=J. Leukoc. Biol. |volume=74 |issue= 5 |pages= 750-6 |year= 2004 |pmid= 12960238 |doi= 10.1189/jlb.0403176 }}
*{{cite journal | author=Alfano D, Franco P, Vocca I, ''et al.'' |title=The urokinase plasminogen activator and its receptor: role in cell growth and apoptosis. |journal=Thromb. Haemost. |volume=93 |issue= 2 |pages= 205-11 |year= 2005 |pmid= 15711734 |doi= 10.1267/THRO05020205 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on PLCG1... {October 30, 2007 12:36:58 PM PDT}
- AMBIGUITY: Did not locate an acceptable page to update. {October 30, 2007 12:38:51 PM PDT}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB = {{PDB2|1hsq}}, {{PDB2|1y0m}}, {{PDB2|1ywo}}, {{PDB2|1ywp}}, {{PDB2|2fci}}, {{PDB2|2hsp}}, {{PDB2|2pld}}, {{PDB2|2ple}}
| Name = Phospholipase C, gamma 1
| HGNCid = 9065
| Symbol = PLCG1
| AltSymbols =; PLC-II; PLC1; PLC148; PLCgamma1
| OMIM = 172420
| ECnumber =
| Homologene = 1997
| MGIid = 97615
| GeneAtlas_image1 = PBB_GE_PLCG1_202789_at_tn.png
| GeneAtlas_image2 = PBB_GE_PLCG1_216551_x_at_tn.png
| Function = {{GNF_GO|id=GO:0004435 |text = phosphoinositide phospholipase C activity}} {{GNF_GO|id=GO:0004871 |text = signal transducer activity}} {{GNF_GO|id=GO:0005057 |text = receptor signaling protein activity}} {{GNF_GO|id=GO:0005509 |text = calcium ion binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0016787 |text = hydrolase activity}}
| Component = {{GNF_GO|id=GO:0005575 |text = cellular_component}}
| Process = {{GNF_GO|id=GO:0001701 |text = in utero embryonic development}} {{GNF_GO|id=GO:0007242 |text = intracellular signaling cascade}} {{GNF_GO|id=GO:0016042 |text = lipid catabolic process}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5335
| Hs_Ensembl = ENSG00000124181
| Hs_RefseqProtein = NP_002651
| Hs_RefseqmRNA = NM_002660
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 20
| Hs_GenLoc_start = 39199291
| Hs_GenLoc_end = 39237775
| Hs_Uniprot = P19174
| Mm_EntrezGene = 18803
| Mm_Ensembl = ENSMUSG00000016933
| Mm_RefseqmRNA = NM_021280
| Mm_RefseqProtein = NP_067255
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 2
| Mm_GenLoc_start = 160422751
| Mm_GenLoc_end = 160467201
| Mm_Uniprot = Q2M4I9
}}
}}
'''Phospholipase C, gamma 1''', also known as '''PLCG1''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = The protein encoded by this gene catalyzes the formation of inositol 1,4,5-trisphosphate and diacylglycerol from phosphatidylinositol 4,5-bisphosphate. This reaction uses calcium as a cofactor and plays an important role in the intracellular transduction of receptor-mediated tyrosine kinase activators. For example, when activated by SRC, the encoded protein causes the Ras guanine nucleotide exchange factor RasGRP1 to translocate to the Golgi, where it activates Ras. Also, this protein has been shown to be a major substrate for heparin-binding growth factor 1 (acidic fibroblast growth factor)-activated tyrosine kinase. Two transcript variants encoding different isoforms have been found for this gene.<ref>{{cite web | title = Entrez Gene: PLCG1 phospholipase C, gamma 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5335| accessdate = }}</ref>
}}
==References==
{{reflist}}
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on PON1... {October 30, 2007 12:38:51 PM PDT}
- AMBIGUITY: Did not locate an acceptable page to update. {October 30, 2007 12:40:12 PM PDT}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Paraoxonase 1
| HGNCid = 9204
| Symbol = PON1
| AltSymbols =; ESA; PON
| OMIM = 168820
| ECnumber =
| Homologene = 68058
| MGIid = 103295
| GeneAtlas_image1 = PBB_GE_PON1_206344_at_tn.png
| GeneAtlas_image2 = PBB_GE_PON1_206345_s_at_tn.png
| Function = {{GNF_GO|id=GO:0004063 |text = aryldialkylphosphatase activity}} {{GNF_GO|id=GO:0004064 |text = arylesterase activity}} {{GNF_GO|id=GO:0005319 |text = lipid transporter activity}} {{GNF_GO|id=GO:0016787 |text = hydrolase activity}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}}
| Process = {{GNF_GO|id=GO:0009605 |text = response to external stimulus}} {{GNF_GO|id=GO:0009636 |text = response to toxin}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5444
| Hs_Ensembl = ENSG00000005421
| Hs_RefseqProtein = NP_000437
| Hs_RefseqmRNA = NM_000446
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 7
| Hs_GenLoc_start = 94764924
| Hs_GenLoc_end = 94791780
| Hs_Uniprot = P27169
| Mm_EntrezGene = 18979
| Mm_Ensembl = ENSMUSG00000002588
| Mm_RefseqmRNA = NM_011134
| Mm_RefseqProtein = NP_035264
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 6
| Mm_GenLoc_start = 5118105
| Mm_GenLoc_end = 5143824
| Mm_Uniprot = Q91X30
}}
}}
'''Paraoxonase 1''', also known as '''PON1''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text =
}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Furlong CE, Costa LG, Hassett C, ''et al.'' |title=Human and rabbit paraoxonases: purification, cloning, sequencing, mapping and role of polymorphism in organophosphate detoxification. |journal=Chem. Biol. Interact. |volume=87 |issue= 1-3 |pages= 35-48 |year= 1993 |pmid= 8393745 |doi= }}
*{{cite journal | author=Furlong CE, Cole TB, Jarvik GP, Costa LG |title=Pharmacogenomic considerations of the paraoxonase polymorphisms. |journal=Pharmacogenomics |volume=3 |issue= 3 |pages= 341-8 |year= 2002 |pmid= 12052142 |doi= 10.1517/14622416.3.3.341 }}
*{{cite journal | author=Mackness B, Durrington PN, Mackness MI |title=The paraoxonase gene family and coronary heart disease. |journal=Curr. Opin. Lipidol. |volume=13 |issue= 4 |pages= 357-62 |year= 2003 |pmid= 12151850 |doi= }}
*{{cite journal | author=Costa LG, Cole TB, Furlong CE |title=Polymorphisms of paraoxonase (PON1) and their significance in clinical toxicology of organophosphates. |journal=J. Toxicol. Clin. Toxicol. |volume=41 |issue= 1 |pages= 37-45 |year= 2003 |pmid= 12645966 |doi= }}
*{{cite journal | author=Getz GS, Reardon CA |title=Paraoxonase, a cardioprotective enzyme: continuing issues. |journal=Curr. Opin. Lipidol. |volume=15 |issue= 3 |pages= 261-7 |year= 2005 |pmid= 15166781 |doi= }}
*{{cite journal | author=Mackness M, Mackness B |title=Paraoxonase 1 and atherosclerosis: is the gene or the protein more important? |journal=Free Radic. Biol. Med. |volume=37 |issue= 9 |pages= 1317-23 |year= 2005 |pmid= 15454272 |doi= 10.1016/j.freeradbiomed.2004.07.034 }}
*{{cite journal | author=Furlong CE, Cole TB, Jarvik GP, ''et al.'' |title=Role of paraoxonase (PON1) status in pesticide sensitivity: genetic and temporal determinants. |journal=Neurotoxicology |volume=26 |issue= 4 |pages= 651-9 |year= 2005 |pmid= 16112327 |doi= 10.1016/j.neuro.2004.08.002 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on RUNX1... {October 30, 2007 11:57:58 AM PDT}
- AMBIGUITY: Did not locate an acceptable page to update. {October 30, 2007 12:05:28 PM PDT}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB = {{PDB2|1cmo}}, {{PDB2|1co1}}, {{PDB2|1e50}}, {{PDB2|1ean}}, {{PDB2|1eao}}, {{PDB2|1eaq}}, {{PDB2|1h9d}}, {{PDB2|1hjb}}, {{PDB2|1hjc}}, {{PDB2|1io4}}, {{PDB2|1ljm}}
| Name = Runt-related transcription factor 1 (acute myeloid leukemia 1; aml1 oncogene)
| HGNCid = 10471
| Symbol = RUNX1
| AltSymbols =; AML1; AML1-EVI-1; AMLCR1; CBFA2; EVI-1; PEBP2aB
| OMIM = 151385
| ECnumber =
| Homologene = 1331
| MGIid =
| GeneAtlas_image1 = PBB_GE_RUNX1_208129_x_at_tn.png
| GeneAtlas_image2 = PBB_GE_RUNX1_209359_x_at_tn.png
| GeneAtlas_image3 = PBB_GE_RUNX1_209360_s_at_tn.png
| Function = {{GNF_GO|id=GO:0003674 |text = molecular_function}} {{GNF_GO|id=GO:0003700 |text = transcription factor activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0016563 |text = transcription activator activity}} {{GNF_GO|id=GO:0031404 |text = chloride ion binding}}
| Component = {{GNF_GO|id=GO:0005575 |text = cellular_component}} {{GNF_GO|id=GO:0005634 |text = nucleus}}
| Process = {{GNF_GO|id=GO:0001501 |text = skeletal development}} {{GNF_GO|id=GO:0006350 |text = transcription}} {{GNF_GO|id=GO:0006355 |text = regulation of transcription, DNA-dependent}} {{GNF_GO|id=GO:0007275 |text = multicellular organismal development}} {{GNF_GO|id=GO:0008150 |text = biological_process}} {{GNF_GO|id=GO:0030097 |text = hemopoiesis}} {{GNF_GO|id=GO:0030854 |text = positive regulation of granulocyte differentiation}} {{GNF_GO|id=GO:0045766 |text = positive regulation of angiogenesis}} {{GNF_GO|id=GO:0045944 |text = positive regulation of transcription from RNA polymerase II promoter}} {{GNF_GO|id=GO:0048266 |text = behavioral response to pain}} {{GNF_GO|id=GO:0048666 |text = neuron development}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 861
| Hs_Ensembl = ENSG00000159216
| Hs_RefseqProtein = NP_001001890
| Hs_RefseqmRNA = NM_001001890
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 21
| Hs_GenLoc_start = 35081975
| Hs_GenLoc_end = 35343511
| Hs_Uniprot = Q01196
| Mm_EntrezGene =
| Mm_Ensembl =
| Mm_RefseqmRNA =
| Mm_RefseqProtein =
| Mm_GenLoc_db =
| Mm_GenLoc_chr =
| Mm_GenLoc_start =
| Mm_GenLoc_end =
| Mm_Uniprot =
}}
}}
'''Runt-related transcription factor 1 (acute myeloid leukemia 1; aml1 oncogene)''', also known as '''RUNX1''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = Core binding factor (CBF) is a heterodimeric transcription factor that binds to the core element of many enhancers and promoters. The protein encoded by this gene represents the alpha subunit of CBF and is thought to be involved in the development of normal hematopoiesis. Chromosomal translocations involving this gene are well-documented and have been associated with several types of leukemia. Two transcript variants encoding different isoforms have been found for this gene.<ref>{{cite web | title = Entrez Gene: RUNX1 runt-related transcription factor 1 (acute myeloid leukemia 1; aml1 oncogene)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=861| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Nucifora G, Rowley JD |title=AML1 and the 8;21 and 3;21 translocations in acute and chronic myeloid leukemia. |journal=Blood |volume=86 |issue= 1 |pages= 1-14 |year= 1995 |pmid= 7795214 |doi= }}
*{{cite journal | author=Perry C, Eldor A, Soreq H |title=Runx1/AML1 in leukemia: disrupted association with diverse protein partners. |journal=Leuk. Res. |volume=26 |issue= 3 |pages= 221-8 |year= 2002 |pmid= 11792409 |doi= }}
*{{cite journal | author=Imai O, Kurokawa M, Izutsu K, ''et al.'' |title=Mutational analyses of the AML1 gene in patients with myelodysplastic syndrome. |journal=Leuk. Lymphoma |volume=43 |issue= 3 |pages= 617-21 |year= 2003 |pmid= 12002768 |doi= }}
*{{cite journal | author=Hart SM, Foroni L |title=Core binding factor genes and human leukemia. |journal=Haematologica |volume=87 |issue= 12 |pages= 1307-23 |year= 2003 |pmid= 12495904 |doi= }}
*{{cite journal | author=Asou N |title=The role of a Runt domain transcription factor AML1/RUNX1 in leukemogenesis and its clinical implications. |journal=Crit. Rev. Oncol. Hematol. |volume=45 |issue= 2 |pages= 129-50 |year= 2003 |pmid= 12604126 |doi= }}
*{{cite journal | author=Michaud J, Scott HS, Escher R |title=AML1 interconnected pathways of leukemogenesis. |journal=Cancer Invest. |volume=21 |issue= 1 |pages= 105-36 |year= 2003 |pmid= 12643014 |doi= }}
*{{cite journal | author=Ganly P, Walker LC, Morris CM |title=Familial mutations of the transcription factor RUNX1 (AML1, CBFA2) predispose to acute myeloid leukemia. |journal=Leuk. Lymphoma |volume=45 |issue= 1 |pages= 1-10 |year= 2004 |pmid= 15061191 |doi= }}
*{{cite journal | author=Yamada R, Tokuhiro S, Chang X, Yamamoto K |title=SLC22A4 and RUNX1: identification of RA susceptible genes. |journal=J. Mol. Med. |volume=82 |issue= 9 |pages= 558-64 |year= 2005 |pmid= 15184985 |doi= 10.1007/s00109-004-0547-y }}
*{{cite journal | author=Harada H, Harada Y, Kimura A |title=Implications of somatic mutations in the AML1/RUNX1 gene in myelodysplastic syndrome (MDS): future molecular therapeutic directions for MDS. |journal=Current cancer drug targets |volume=6 |issue= 6 |pages= 553-65 |year= 2006 |pmid= 17017876 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on SERPINA1... {October 30, 2007 12:32:13 PM PDT}
- AMBIGUITY: Did not locate an acceptable page to update. {October 30, 2007 12:34:25 PM PDT}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB = {{PDB2|1atu}}, {{PDB2|1d5s}}, {{PDB2|1ezx}}, {{PDB2|1hp7}}, {{PDB2|1iz2}}, {{PDB2|1kct}}, {{PDB2|1oo8}}, {{PDB2|1oph}}, {{PDB2|1psi}}, {{PDB2|1qlp}}, {{PDB2|1qmb}}, {{PDB2|2d26}}, {{PDB2|7api}}, {{PDB2|8api}}, {{PDB2|9api}}
| Name = Serpin peptidase inhibitor, clade A (alpha-1 antiproteinase, antitrypsin), member 1
| HGNCid = 8941
| Symbol = SERPINA1
| AltSymbols =; PI; A1A; A1AT; AAT; MGC23330; MGC9222; PI1; PRO2275
| OMIM = 107400
| ECnumber =
| Homologene = 20103
| MGIid = 891971
| GeneAtlas_image1 = PBB_GE_SERPINA1_211429_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_SERPINA1_202833_s_at_tn.png
| Function = {{GNF_GO|id=GO:0004867 |text = serine-type endopeptidase inhibitor activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}} {{GNF_GO|id=GO:0005615 |text = extracellular space}}
| Process = {{GNF_GO|id=GO:0006953 |text = acute-phase response}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5265
| Hs_Ensembl = ENSG00000197249
| Hs_RefseqProtein = NP_000286
| Hs_RefseqmRNA = NM_000295
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 14
| Hs_GenLoc_start = 93914453
| Hs_GenLoc_end = 93919327
| Hs_Uniprot = P01009
| Mm_EntrezGene = 20700
| Mm_Ensembl = ENSMUSG00000071178
| Mm_RefseqmRNA = NM_009243
| Mm_RefseqProtein = NP_033269
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 12
| Mm_GenLoc_start = 104129206
| Mm_GenLoc_end = 104139239
| Mm_Uniprot = Q3KQQ4
}}
}}
'''Serpin peptidase inhibitor, clade A (alpha-1 antiproteinase, antitrypsin), member 1''', also known as '''SERPINA1''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = Alpha-1-antitrypsin is a protease inhibitor, deficiency of which is associated with emphysema and liver disease. The protein is encoded by a gene (PI) located on the distal long arm of chromosome 14.[supplied by OMIM]<ref>{{cite web | title = Entrez Gene: SERPINA1 serpin peptidase inhibitor, clade A (alpha-1 antiproteinase, antitrypsin), member 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5265| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Wu Y, Foreman RC |title=The molecular genetics of alpha 1 antitrypsin deficiency. |journal=Bioessays |volume=13 |issue= 4 |pages= 163-9 |year= 1991 |pmid= 1859394 |doi= 10.1002/bies.950130404 }}
*{{cite journal | author=Kalsheker N |title=Alpha 1-antitrypsin: structure, function and molecular biology of the gene. |journal=Biosci. Rep. |volume=9 |issue= 2 |pages= 129-38 |year= 1989 |pmid= 2669992 |doi= }}
*{{cite journal | author=Crystal RG |title=The alpha 1-antitrypsin gene and its deficiency states. |journal=Trends Genet. |volume=5 |issue= 12 |pages= 411-7 |year= 1990 |pmid= 2696185 |doi= }}
*{{cite journal | author=Carrell RW, Jeppsson JO, Laurell CB, ''et al.'' |title=Structure and variation of human alpha 1-antitrypsin. |journal=Nature |volume=298 |issue= 5872 |pages= 329-34 |year= 1982 |pmid= 7045697 |doi= }}
*{{cite journal | author=Elliott PR, Abrahams JP, Lomas DA |title=Wild-type alpha 1-antitrypsin is in the canonical inhibitory conformation. |journal=J. Mol. Biol. |volume=275 |issue= 3 |pages= 419-25 |year= 1998 |pmid= 9466920 |doi= 10.1006/jmbi.1997.1458 }}
*{{cite journal | author=Miyamoto Y, Akaike T, Maeda H |title=S-nitrosylated human alpha(1)-protease inhibitor. |journal=Biochim. Biophys. Acta |volume=1477 |issue= 1-2 |pages= 90-7 |year= 2000 |pmid= 10708851 |doi= }}
*{{cite journal | author=Coakley RJ, Taggart C, O'Neill S, McElvaney NG |title=Alpha1-antitrypsin deficiency: biological answers to clinical questions. |journal=Am. J. Med. Sci. |volume=321 |issue= 1 |pages= 33-41 |year= 2001 |pmid= 11202478 |doi= }}
*{{cite journal | author=Lomas DA, Lourbakos A, Cumming SA, Belorgey D |title=Hypersensitive mousetraps, alpha1-antitrypsin deficiency and dementia. |journal=Biochem. Soc. Trans. |volume=30 |issue= 2 |pages= 89-92 |year= 2002 |pmid= 12023831 |doi= 10.1042/ }}
*{{cite journal | author=Kalsheker N, Morley S, Morgan K |title=Gene regulation of the serine proteinase inhibitors alpha1-antitrypsin and alpha1-antichymotrypsin. |journal=Biochem. Soc. Trans. |volume=30 |issue= 2 |pages= 93-8 |year= 2002 |pmid= 12023832 |doi= 10.1042/ }}
*{{cite journal | author=Perlmutter DH |title=Liver injury in alpha1-antitrypsin deficiency: an aggregated protein induces mitochondrial injury. |journal=J. Clin. Invest. |volume=110 |issue= 11 |pages= 1579-83 |year= 2003 |pmid= 12464659 |doi= }}
*{{cite journal | author=Lomas DA, Mahadeva R |title=Alpha1-antitrypsin polymerization and the serpinopathies: pathobiology and prospects for therapy. |journal=J. Clin. Invest. |volume=110 |issue= 11 |pages= 1585-90 |year= 2003 |pmid= 12464660 |doi= }}
*{{cite journal | author=Lisowska-Myjak B |title=AAT as a diagnostic tool. |journal=Clin. Chim. Acta |volume=352 |issue= 1-2 |pages= 1-13 |year= 2005 |pmid= 15653097 |doi= 10.1016/j.cccn.2004.03.012 }}
*{{cite journal | author=Lomas DA |title=Molecular mousetraps, alpha1-antitrypsin deficiency and the serpinopathies. |journal=Clinical medicine (London, England) |volume=5 |issue= 3 |pages= 249-57 |year= 2005 |pmid= 16011217 |doi= }}
*{{cite journal | author=Rudnick DA, Perlmutter DH |title=Alpha-1-antitrypsin deficiency: a new paradigm for hepatocellular carcinoma in genetic liver disease. |journal=Hepatology |volume=42 |issue= 3 |pages= 514-21 |year= 2005 |pmid= 16044402 |doi= 10.1002/hep.20815 }}
*{{cite journal | author=Mahr AD, Neogi T, Merkel PA |title=Epidemiology of Wegener's granulomatosis: Lessons from descriptive studies and analyses of genetic and environmental risk determinants. |journal=Clin. Exp. Rheumatol. |volume=24 |issue= 2 Suppl 41 |pages= S82-91 |year= 2006 |pmid= 16859601 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on SYK... {October 30, 2007 12:44:05 PM PDT}
- CREATE: Found no pages, creating new page. {October 30, 2007 12:45:13 PM PDT}
- CREATED: Created new protein page: SYK {October 30, 2007 12:45:22 PM PDT}
- INFO: Beginning work on TIMP1... {October 30, 2007 12:45:22 PM PDT}
- AMBIGUITY: Did not locate an acceptable page to update. {October 30, 2007 12:46:51 PM PDT}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB = {{PDB2|1d2b}}, {{PDB2|1oo9}}, {{PDB2|1uea}}, {{PDB2|2j0t}}
| Name = TIMP metallopeptidase inhibitor 1
| HGNCid = 11820
| Symbol = TIMP1
| AltSymbols =; EPO; CLGI; EPA; FLJ90373; HCI; TIMP
| OMIM = 305370
| ECnumber =
| Homologene = 36321
| MGIid = 98752
| GeneAtlas_image1 = PBB_GE_TIMP1_201666_at_tn.png
| Function = {{GNF_GO|id=GO:0004857 |text = enzyme inhibitor activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008191 |text = metalloendopeptidase inhibitor activity}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}} {{GNF_GO|id=GO:0005578 |text = proteinaceous extracellular matrix}} {{GNF_GO|id=GO:0005604 |text = basement membrane}}
| Process = {{GNF_GO|id=GO:0007275 |text = multicellular organismal development}} {{GNF_GO|id=GO:0008284 |text = positive regulation of cell proliferation}} {{GNF_GO|id=GO:0043249 |text = erythrocyte maturation}} {{GNF_GO|id=GO:0051045 |text = negative regulation of membrane protein ectodomain proteolysis}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 7076
| Hs_Ensembl = ENSG00000102265
| Hs_RefseqProtein = NP_003245
| Hs_RefseqmRNA = NM_003254
| Hs_GenLoc_db =
| Hs_GenLoc_chr = X
| Hs_GenLoc_start = 47326634
| Hs_GenLoc_end = 47331132
| Hs_Uniprot = P01033
| Mm_EntrezGene = 21857
| Mm_Ensembl = ENSMUSG00000001131
| Mm_RefseqmRNA = NM_001044384
| Mm_RefseqProtein = NP_001037849
| Mm_GenLoc_db =
| Mm_GenLoc_chr = X
| Mm_GenLoc_start = 20027223
| Mm_GenLoc_end = 20031691
| Mm_Uniprot = Q6GXA9
}}
}}
'''TIMP metallopeptidase inhibitor 1''', also known as '''TIMP1''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene belongs to the TIMP gene family. The proteins encoded by this gene family are natural inhibitors of the matrix metalloproteinases (MMPs), a group of peptidases involved in degradation of the extracellular matrix. In addition to its inhibitory role against most of the known MMPs, the encoded protein is able to promote cell proliferation in a wide range of cell types, and may also have an anti-apoptotic function. Transcription of this gene is highly inducible in response to many cytokines and hormones. In addition, the expression from some but not all inactive X chromosomes suggests that this gene inactivation is polymorphic in human females. This gene is located within intron 6 of the synapsin I gene and is transcribed in the opposite direction.<ref>{{cite web | title = Entrez Gene: TIMP1 TIMP metallopeptidase inhibitor 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7076| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Hornebeck W |title=Down-regulation of tissue inhibitor of matrix metalloprotease-1 (TIMP-1) in aged human skin contributes to matrix degradation and impaired cell growth and survival. |journal=Pathol. Biol. |volume=51 |issue= 10 |pages= 569-73 |year= 2004 |pmid= 14622947 |doi= }}
*{{cite journal | author=Gardner J, Ghorpade A |title=Tissue inhibitor of metalloproteinase (TIMP)-1: the TIMPed balance of matrix metalloproteinases in the central nervous system. |journal=J. Neurosci. Res. |volume=74 |issue= 6 |pages= 801-6 |year= 2004 |pmid= 14648584 |doi= 10.1002/jnr.10835 }}
}}
{{refend}}
{{protein-stub}}
end log.
