TNIP2

TNIP2
Identifikatori
Aliasi	TNIP2
Vanjski ID-jevi	OMIM: 610669 MGI: 2386643 HomoloGene: 11515 GeneCards: TNIP2
Lokacija gena (čovjek) Hrom. Hromosom 4 (čovjek) Bend 4p16.3 Početak 2,741,648 bp Kraj 2,756,342 bp
Lokacija gena (miš) Hrom. Hromosom 5 (miš) Bend 5|5 B2 Početak 34,653,431 bp Kraj 34,671,335 bp
Obrazac RNK ekspresije Više referentnih podataka o ekspresiji
Ontologija gena Molekularna funkcija • GO:0001948, GO:0016582 vezivanje za proteine • protein kinase binding • vezivanje iona metala • polyubiquitin modification-dependent protein binding • K63-linked polyubiquitin modification-dependent protein binding Ćelijska komponenta • jedro • citosol • citoplazma • nukleoplazma Biološki proces • negative regulation of endothelial cell apoptotic process • GO:0009373 regulation of transcription, DNA-templated • CD40 signaling pathway • protein stabilization • positive regulation of macrophage activation • transcription, DNA-templated • stress-activated MAPK cascade • positive regulation of I-kappaB kinase/NF-kappaB signaling • positive regulation of B cell activation • inflammatory response • I-kappaB kinase/NF-kappaB signaling • GO:0003257, GO:0010735, GO:1901228, GO:1900622, GO:1904488 positive regulation of transcription by RNA polymerase II • GO:0097285 apoptoza • toll-like receptor 9 signaling pathway • toll-like receptor 2 signaling pathway • toll-like receptor 3 signaling pathway • protein deubiquitination • cellular response to lipopolysaccharide • interleukin-1-mediated signaling pathway Izvori:Amigo / QuickGO
Ortolozi
Vrste	Čovjek	Miš
Entrez	79155	231130
Ensembl	ENSG00000168884	ENSMUSG00000059866
UniProt	Q8NFZ5	Q99JG7
RefSeq (mRNK)	NM_024309 NM_001161527 NM_001292016	NM_139064
RefSeq (bjelančevina)	NP_001154999 NP_001278945 NP_077285	NP_620703
Lokacija (UCSC)	Chr 4: 2.74 – 2.76 Mb	Chr 5: 34.65 – 34.67 Mb
PubMed pretraga
Wikipodaci
Pogledaj/uredi – čovjek Pogledaj/uredi – miš

TNFAIP3-interaktivirajući protein 2 jest protein koji je kod ljudi kodiran genom TNIP2 sa hromosoma 4. TNIP2 sadrži višestruka aminokiselinska mjesta koja su fosforilirana i ubikvitinirana.

Aminokiselinska sekvenca

Dužina polipeptidnog lanca je 429 aminokiselina, а molekulska težina 48.700 Da.

• C: Cistein
• D: Asparaginska kiselina
• E: Glutaminska kiselina
• F: Fenilalanin
• G: Glicin
• H: Histidin
• I: Izoleucin
• K: Lizin
• L: Leucin
• M: Metionin
• N: Asparagin
• P: Prolin
• Q: Glutamin
• R: Arginin
• S: Serin
• T: Treonin
• V: Valin
• W: Triptofan
• Y: Tirozin

10		20		30		40		50
MSRDPGSGGW		EEAPRAAAAL		CTLYHEAGQR		LRRLQDQLAA		RDALIARLRA
RLAALEGDAA		PSLVDALLEQ		VARFREQLRR		QEGGAAEAQM		RQEIERLTER
LEEKEREMQQ		LLSQPQHERE		KEVVLLRRSM		AEGERARAAS		DVLCRSLANE
THQLRRTLTA		TAHMCQHLAK		CLDERQHAQR		NVGERSPDQS		EHTDGHTSVQ
SVIEKLQEEN		RLLKQKVTHV		EDLNAKWQRY		NASRDEYVRG		LHAQLRGLQI
PHEPELMRKE		ISRLNRQLEE		KINDCAEVKQ		ELAASRTARD		AALERVQMLE
QQILAYKDDF		MSERADRERA		QSRIQELEEK		VASLLHQVSW		RQDSREPDAG
RIHAGSKTAK		YLAADALELM		VPGGWRPGTG		SQQPEPPAEG		GHPGAAQRGQ
GDLQCPHCLQ		CFSDEQGEEL		LRHVAECCQ

Dopunska literatura

• Heyninck K, De Valck D, Vanden Berghe W, et al. (1999). "The Zinc Finger Protein A20 Inhibits TNF-induced NF-κかっぱB–dependent Gene Expression by Interfering with an RIP- or TRAF2-mediated Transactivation Signal and Directly Binds to a Novel NF-κかっぱB–inhibiting Protein ABIN". J. Cell Biol. 145 (7): 1471–82. doi:10.1083/jcb.145.7.1471. hdl:1854/LU-113881. PMC 2133159. PMID 10385526.
• Klinkenberg M, Van Huffel S, Heyninck K, Beyaert R (2001). "Functional redundancy of the zinc fingers of A20 for inhibition of NF-kappaB activation and protein-protein interactions". FEBS Lett. 498 (1): 93–7. doi:10.1016/S0014-5793(01)02504-2. PMID 11389905. S2CID 32414520.
• Wu WS, Xu ZX, Chang KS (2002). "The promyelocytic leukemia protein represses A20-mediated transcription". J. Biol. Chem. 277 (35): 31734–9. doi:10.1074/jbc.M201648200. PMID 12080044.
• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Liu WK, Chien CY, Chou CK, Su JY (2003). "An LKB1-interacting protein negatively regulates TNFalpha-induced NF-kappaB activation". J. Biomed. Sci. 10 (2): 242–52. doi:10.1159/000068708. PMID 12595760. S2CID 202644741.
• Hughes DP, Marron MB, Brindle NP (2003). "The antiinflammatory endothelial tyrosine kinase Tie2 interacts with a novel nuclear factor-kappaB inhibitor ABIN-2". Circ. Res. 92 (6): 630–6. doi:10.1161/01.RES.0000063422.38690.DC. PMID 12609966.
• Chien CY, Liu WK, Chou CK, Su JY (2003). "The A20-binding protein ABIN-2 exerts unexpected function in mediating transcriptional coactivation". FEBS Lett. 543 (1–3): 55–60. doi:10.1016/S0014-5793(03)00401-0. PMID 12753905. S2CID 31400521.
• Liu WK, Yen PF, Chien CY, et al. (2004). "The inhibitor ABIN-2 disrupts the interaction of receptor-interacting protein with the kinase subunit IKKgamma to block activation of the transcription factor NF-kappaB and potentiate apoptosis". Biochem. J. 378 (Pt 3): 867–76. doi:10.1042/BJ20031736. PMC 1224013. PMID 14653779.
• Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
• Bouwmeester T, Bauch A, Ruffner H, et al. (2004). "A physical and functional map of the human TNF-alpha/NF-kappa B signal transduction pathway". Nat. Cell Biol. 6 (2): 97–105. doi:10.1038/ncb1086. PMID 14743216. S2CID 11683986.
• Lang V, Symons A, Watton SJ, et al. (2004). "ABIN-2 Forms a Ternary Complex with TPL-2 and NF-κかっぱB1 p105 and Is Essential for TPL-2 Protein Stability". Mol. Cell. Biol. 24 (12): 5235–48. doi:10.1128/MCB.24.12.5235-5248.2004. PMC 419892. PMID 15169888.
• Li CC, Chou CK, Wang MH, Tsai TF (2006). "Overexpression of ABIN-2, a negative regulator of NF-kappaB, delays liver regeneration in the ABIN-2 transgenic mice". Biochem. Biophys. Res. Commun. 342 (1): 300–9. doi:10.1016/j.bbrc.2006.01.114. PMID 16480954.
• Greenberg H, Ye X, Wilson D, et al. (2006). "Chronic intermittent hypoxia activates nuclear factor-kappaB in cardiovascular tissues in vivo". Biochem. Biophys. Res. Commun. 343 (2): 591–6. doi:10.1016/j.bbrc.2006.03.015. PMID 16554025.
• Liu Y, Nakahara T, Miyakoshi J, et al. (2007). "Nuclear accumulation and activation of nuclear factor kappaB after split-dose irradiation in LS174T cells". J. Radiat. Res. 48 (1): 13–20. doi:10.1269/jrr.0615. PMID 17038805.