MAPK1

MAPK1
PDBに登録とうろくされている構造こうぞう
PDB	オルソログ検索けんさく: RCSB PDBe PDBj
PDBのIDコード一覧いちらん
	1PME, 1TVO, 1WZY, 2OJG, 2OJI, 2OJJ, 2Y9Q, 3D42, 3D44, 3I5Z, 3I60, 3SA0, 3TEI, 3W55, 4FMQ, 4FUX, 4FUY, 4FV0, 4FV1, 4FV2, 4FV3, 4FV4, 4FV5, 4FV6, 4FV7, 4FV8, 4FV9, 4G6N, 4G6O, 4H3P, 4H3Q, 4IZ5, 4IZ7, 4IZA, 4N0S, 4NIF, 4O6E, 4QTA, 4QTE, 4ZZM, 4ZZN, 4ZZO, 5BUE, 5BUI, 5BUJ, 4QP1, 4QP2, 4QP3, 4QP4, 4QP6, 4QP7, 4QP8, 4QP9, 4QPA, 4XJ0, 5BVD, 5BVE, 5BVF, 5AX3, 4ZXT, 5K4I
識別子しきべつし
記号きごう	MAPK1, ERK, ERK-2, ERK2, ERT1, MAPK2, P42MAPK, PRKM1, PRKM2, p38, p40, p41, p41mapk, p42-MAPK, mitogen-activated protein kinase 1, NS13
外部がいぶID	OMIM: 176948 MGI: 1346858 HomoloGene: 37670 GeneCards: MAPK1
遺伝子いでんしの位置いち (ヒト)
染色せんしょく体たい	22番ばん染色せんしょく体たい (ヒト)
終点しゅうてん	21,867,680 bp
遺伝子いでんしの位置いち (マウス)
染色せんしょく体たい	16番ばん染色せんしょく体たい (マウス)
終点しゅうてん	16,865,317 bp
RNA発現はつげんパターン
	; ;
	さらなる参照さんしょう発現はつげんデータ
遺伝子いでんしオントロジー
分子ぶんし機能きのう	• phosphatase binding; • ATP binding; • protein kinase activity; • 転写てんしゃ因子いんし結合けつごう; • トランスフェラーゼ活性かっせい; • mitogen-activated protein kinase kinase kinase binding; • phosphotyrosine residue binding; • 血漿けっしょうタンパク結合けつごう; • プロテインキナーゼ結合けつごう; • DNA結合けつごう; • ヌクレオチド結合けつごう; • RNA polymerase II CTD heptapeptide repeat kinase activity; • protein serine/threonine kinase activity; • キナーゼ活性かっせい; • identical protein binding; • MAP kinase activity; • 二に本ほん鎖くさりDNA結合けつごう; • MAP kinase kinase activity;
細胞さいぼうの構成こうせい要素ようそ	• 細胞さいぼう質しつ; • 細胞さいぼう質しつ基質きしつ; • 焦点しょうてん接着せっちゃく; • 微小びしょう管かん形成けいせい中心ちゅうしん; • ミトコンドリア; • カベオラ; • dendrite cytoplasm; • 細胞さいぼう骨格こっかく; • 細胞さいぼう核かく; • エキソソーム; • 細胞さいぼう体たい; • late endosome; • ゴルジ体たい; • 紡錘ぼうすい体たい; • 神経しんけい繊維せんい; • early endosome; • mitotic spindle; • 仮かり足あし; • 細胞さいぼう外がい領域りょういき; • 核質かくしつ; • azurophil granule lumen; • ficolin-1-rich granule lumen; • 細胞さいぼう膜まく; • シナプス後ご肥厚ひこう; • 膜まく; • 高分子こうぶんし複ふく合体がったい;
生物せいぶつ学がく的てきプロセス	• caveolin-mediated endocytosis; • positive regulation of telomere capping; • response to exogenous dsRNA; • cardiac neural crest cell development involved in heart development; • positive regulation of translation; • cellular response to DNA damage stimulus; • platelet activation; • Fc-epsilon receptor signaling pathway; • タンパク質たんぱくしつリン酸化さんか; • face development; • cellular response to granulocyte macrophage colony-stimulating factor stimulus; • regulation of DNA-binding transcription factor activity; • animal organ morphogenesis; • 細胞さいぼう周期しゅうき; • ERBB signaling pathway; • アポトーシス; • B cell receptor signaling pathway; • regulation of transcription, DNA-templated; • タンパク質たんぱくしつ安定あんてい性せいの制御せいぎょ; • Fc-gamma receptor signaling pathway involved in phagocytosis; • 胸腺きょうせん発生はっせい; • negative regulation of cell differentiation; • ERK1 and ERK2 cascade; • labyrinthine layer blood vessel development; • transcription, DNA-templated; • positive regulation of transcription, DNA-templated; • 心臓しんぞう発生はっせい; • viral process; • 毒性どくせい物質ぶっしつへの反応はんのう; • regulation of stress-activated MAPK cascade; • 化学かがく的てきシナプス伝達でんたつ; • growth hormone receptor signaling pathway via JAK-STAT; • cytosine metabolic process; • リン酸化さんか; • outer ear morphogenesis; • response to estrogen; • 走はし化か性せい; • リポ多た糖とうへの反応はんのう; • 甲状腺こうじょうせん発生はっせい; • response to epidermal growth factor; • positive regulation of telomerase activity; • 侵害しんがい受容じゅよう; • peptidyl-threonine phosphorylation; • trachea formation; • リポ多た糖とうを介かいしたシグナル伝達でんたつ経路けいろ; • mammary gland epithelial cell proliferation; • intracellular signal transduction; • lung morphogenesis; • neural crest cell development; • positive regulation of cell migration; • regulation of early endosome to late endosome transport; • ストレスへの反応はんのう; • positive regulation of telomere maintenance via telomerase; • MAPK cascade; • 軸じく索さく誘導ゆうどう; • fibroblast growth factor receptor signaling pathway; • positive regulation of peptidyl-threonine phosphorylation; • peptidyl-serine phosphorylation; • positive regulation of cell population proliferation; • regulation of cellular response to heat; • Bergmann glial cell differentiation; • regulation of Golgi inheritance; • T cell receptor signaling pathway; • regulation of cytoskeleton organization; • シグナル伝達でんたつ; • 長期ちょうき増強ぞうきょう; • regulation of ossification; • regulation of phosphatidylinositol 3-kinase signaling; • 好こう中ちゅう球だま脱だつ顆粒かりゅう; • 遺伝子いでんし発現はつげん調節ちょうせつ; • 有機物ゆうきぶつへの細胞さいぼう応答おうとう; • 老化ろうか; • 学習がくしゅうと記憶きおく; • positive regulation of gene expression; • diadenosine tetraphosphate biosynthetic process; • regulation of cellular pH; • cellular response to amino acid starvation; • cellular response to reactive oxygen species; • response to nicotine; • 脱落だつらく膜まく化か; • stress-activated MAPK cascade; • positive regulation of cardiac muscle cell proliferation; • cellular response to cadmium ion; • cellular response to tumor necrosis factor; • cellular response to dopamine; • positive regulation of protein import into nucleus;
	出典しゅってん:Amigo / QuickGO
オルソログ
	5594
	26413
	ENSG00000100030
	ENSMUSG00000063358
	P28482
	P63085
	NM_138957; NM_002745
	NM_001038663; NM_011949; NM_001357115; NM_028991
	NP_002736; NP_620407
	NP_001033752; NP_036079; NP_001344044
	ウィキデータ
閲覧えつらん/編集へんしゅうヒト	閲覧えつらん/編集へんしゅうマウス

MAPK1（mitogen-activated protein kinase 1）またはERK2（extracellular signal-regulated kinase 2）は、ヒトではMAPK1遺伝子いでんしにコードされる酵素こうそ（プロテインキナーゼ）である^[5]。

機能きのう

MAPK1はMAPキナーゼファミリーの一員いちいんである。ERK（extracellular signal-regulated kinase）としても知しられるMAPキナーゼは、複数ふくすうの生化学せいかがく的てきシグナルの統合とうごう点てんとして作用さようしており、細胞さいぼう増殖ぞうしょく、分化ぶんか、転写てんしゃ調節ちょうせつ、発生はっせいなど幅広はばひろい細胞さいぼう過程かていに関与かんよしている。このキナーゼの活性かっせい化かには、上流じょうりゅうのキナーゼによるリン酸化さんかが必要ひつようである。活性かっせい化かに伴ともなって、このキナーゼは刺激しげきされた細胞さいぼうの核かく内うちへ移行いこうし、そこで核かく内ないの標的ひょうてきをリン酸化さんかする。MAPK1遺伝子いでんしには、同一どういつのタンパク質たんぱくしつをコードするもののUTRが異ことなる、2種類しゅるいの選択せんたく的てきスプライシングバリアントが報告ほうこくされている^[6]。MAPK1には複数ふくすうのリン酸化さんか部位ぶいやユビキチン化か部位ぶいが存在そんざいする^[7]。

モデル生物せいぶつ

MAPK1の機能きのうの研究けんきゅうにはモデル生物せいぶつが広ひろく利用りようされている。疾患しっかんの動物どうぶつモデルを作製さくせいして関心かんしんのある科学かがく者しゃに頒布はんぷするハイスループット変異へんい体たい作製さくせいプロジェクトである国際こくさいノックアウトマウスコンソーシアム（英語えいご版ばん）プログラムの一環いっかんとして、Mapk1^{tm1a(EUCOMM)Wtsi}^[8]^[9]と呼よばれるコンディショナルノックアウトマウスが作製さくせいされている^[10]^[11]^[12]。

オスとメスのマウスに対たいし、遺伝子いでんし欠かけ失しつの影響えいきょうを調しらべるための規格きかく化かされた表現ひょうげん型がたスクリーニングが行おこなわれている^[13]^[14]。変異へんい体たいマウスに対たいして27種類しゅるいの試験しけんが行おこなわれており、3つの重大じゅうだいな異常いじょうが観察かんさつされている^[13]。妊娠にんしん中ちゅうにホモ接合せつごう型がた変異へんい体たいの胚はいは観察かんさつされず、そのため離乳りにゅう期きまで生存せいぞんした個体こたいはなかった。その他たの試験しけんはヘテロ接合せつごう型がた変異へんい体たいの成体せいたいマウスに対たいして行おこなわれ、オスでは血ち中ちゅうアミラーゼ濃度のうどの低下ていかが観察かんさつされた^[13]。

B細胞さいぼうでのMapk1のコンディショナル欠かけ失しつによって、MAPK1がT細胞さいぼう依存いぞん的てきな抗体こうたい産さん生せいに関与かんよしていることが示しめされている^[15]。Mapk1に優性ゆうせい機能きのう獲得かくとく型がた変異へんいを有ゆうするトランスジェニックマウスでは、MAPK1がT細胞さいぼうの発生はっせいに関与かんよしていることが示しめされている^[16]。発生はっせい中ちゅうの大脳皮質だいのうひしつの神経しんけい前駆ぜんく細胞さいぼうにおけるMapk1のコンディショナル不ふ活性かっせい化かは、皮質ひしつの厚あつさの減少げんしょうと神経しんけい前駆ぜんく細胞さいぼうの増殖ぞうしょくの低下ていかをもたらす^[17]。

相互そうご作用さよう

MAPK1は次つぎに挙あげる因子いんしと相互そうご作用さようすることが示しめされている。

臨床りんしょう的てき意義いぎ

MAPK1の変異へんいは多おおくの種類しゅるいのがんへの関与かんよが示唆しさされている^[56]。

出典しゅってん

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000100030 - Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000063358 - Ensembl, May 2017
^ Human PubMed Reference:
^ Mouse PubMed Reference:
^ “Extracellular signal-regulated kinases in T cells: characterization of human ERK1 and ERK2 cDNAs”. Biochem. Biophys. Res. Commun. 182 (3): 1416–22. (February 1992). doi:10.1016/0006-291X(92)91891-S. PMID 1540184.
^ “Entrez Gene: MAPK1 mitogen-activated protein kinase 1”. 2023年ねん7月がつ17日にち閲覧えつらん。
^ “ERK2 (human)”. www.phosphosite.org. 2020年ねん10月がつ31日にち閲覧えつらん。
^ “Mapk1 Mouse Gene Details | mitogen-activated protein kinase 1 | International Mouse Phenotyping Consortium” (英語えいご). www.mousephenotype.org. 2023年ねん7月がつ17日にち閲覧えつらん。
^ “Mapk1 Targeted Allele Detail MGI Mouse (MGI:4432537)”. www.informatics.jax.org. 2023年ねん7月がつ17日にち閲覧えつらん。
^ “A conditional knockout resource for the genome-wide study of mouse gene function”. Nature 474 (7351): 337–42. (2011). doi:10.1038/nature10163. PMC 3572410. PMID 21677750.
^ “Mouse library set to be knockout”. Nature 474 (7351): 262–3. (2011). doi:10.1038/474262a. PMID 21677718.
^ “A mouse for all reasons”. Cell 128 (1): 9–13. (2007). doi:10.1016/j.cell.2006.12.018. PMID 17218247.
^ ^a ^b ^c “The Sanger Mouse Genetics Programme: High throughput characterisation of knockout mice”. Acta Ophthalmologica 88: 925–7. (2010). doi:10.1111/j.1755-3768.2010.4142.x.
^ “The mouse genetics toolkit: revealing function and mechanism”. Genome Biol. 12 (6): 224. (2011). doi:10.1186/gb-2011-12-6-224. PMC 3218837. PMID 21722353.
^ “Extracellular signal-regulated protein kinase 2 is required for efficient generation of B cells bearing antigen-specific immunoglobulin G”. Molecular and Cellular Biology 27 (4): 1236–46. (February 2007). doi:10.1128/MCB.01530-06. PMC 1800707. PMID 17145771.
^ “The influence of the MAPK pathway on T cell lineage commitment”. Immunity 7 (5): 609–18. (November 1997). doi:10.1016/s1074-7613(00)80382-9. PMID 9390685.
^ “Deletion of ERK2 mitogen-activated protein kinase identifies its key roles in cortical neurogenesis and cognitive function”. The Journal of Neuroscience 28 (27): 6983–95. (July 2008). doi:10.1523/JNEUROSCI.0679-08.2008. PMC 4364995. PMID 18596172.
^ “Extracellular signal-regulated kinase phosphorylates tumor necrosis factor alpha-converting enzyme at threonine 735: a potential role in regulated shedding”. Mol. Biol. Cell 13 (6): 2031–44. (June 2002). doi:10.1091/mbc.01-11-0561. PMC 117622. PMID 12058067.
^ “Mitogen-activated protein kinase ERK1/2 regulates the class II transactivator”. J. Biol. Chem. 283 (14): 9031–9. (April 2008). doi:10.1074/jbc.M706487200. PMC 2431044. PMID 18245089.
^ “Distinct binding determinants for ERK2/p38alpha and JNK map kinases mediate catalytic activation and substrate selectivity of map kinase phosphatase-1”. J. Biol. Chem. 276 (19): 16491–500. (May 2001). doi:10.1074/jbc.M010966200. PMID 11278799.
^ “Dual-specificity phosphatase 1 ubiquitination in extracellular signal-regulated kinase-mediated control of growth in human hepatocellular carcinoma”. Cancer Res. 68 (11): 4192–200. (June 2008). doi:10.1158/0008-5472.CAN-07-6157. PMID 18519678.
^ “Molecular cloning and characterization of a novel dual specificity phosphatase, LMW-DSP2, that lacks the cdc25 homology domain”. J. Biol. Chem. 276 (29): 27575–83. (July 2001). doi:10.1074/jbc.M100408200. PMID 11346645.
^ “Extracellular regulated kinases (ERK) 1 and ERK2 are authentic substrates for the dual-specificity protein-tyrosine phosphatase VHR. A novel role in down-regulating the ERK pathway”. J. Biol. Chem. 274 (19): 13271–80. (May 1999). doi:10.1074/jbc.274.19.13271. PMID 10224087.
^ ^a ^b ^c “Identification of novel ERK2 substrates through use of an engineered kinase and ATP analogs”. J. Biol. Chem. 278 (17): 14926–35. (April 2003). doi:10.1074/jbc.M300485200. PMID 12594221.
^ “Neither ERK nor JNK/SAPK MAP kinase subtypes are essential for histone H3/HMG-14 phosphorylation or c-fos and c-jun induction”. J. Cell Sci. 108 (11): 3599–609. (November 1995). doi:10.1242/jcs.108.11.3599. PMID 8586671.
^ “Extracellular signal-regulated kinase 2 interacts with and is negatively regulated by the LIM-only protein FHL2 in cardiomyocytes”. Mol. Cell. Biol. 24 (3): 1081–95. (February 2004). doi:10.1128/mcb.24.3.1081-1095.2004. PMC 321437. PMID 14729955.
^ “Histone deacetylase 4 associates with extracellular signal-regulated kinases 1 and 2, and its cellular localization is regulated by oncogenic Ras”. Proc. Natl. Acad. Sci. U.S.A. 97 (26): 14329–33. (December 2000). Bibcode: 2000PNAS...9714329Z. doi:10.1073/pnas.250494697. PMC 18918. PMID 11114188.
^ ^a ^b “p38alpha isoform Mxi2 binds to extracellular signal-regulated kinase 1 and 2 mitogen-activated protein kinase and regulates its nuclear activity by sustaining its phosphorylation levels”. Mol. Cell. Biol. 23 (9): 3079–90. (May 2003). doi:10.1128/mcb.23.9.3079-3090.2003. PMC 153192. PMID 12697810.
^ “Identification of novel point mutations in ERK2 that selectively disrupt binding to MEK1”. J. Biol. Chem. 277 (17): 14844–52. (April 2002). doi:10.1074/jbc.M107776200. PMID 11823456.
^ ^a ^b “Mechanism of suppression of the Raf/MEK/extracellular signal-regulated kinase pathway by the raf kinase inhibitor protein”. Mol. Cell. Biol. 20 (9): 3079–85. (May 2000). doi:10.1128/mcb.20.9.3079-3085.2000. PMC 85596. PMID 10757792.
^ “A novel 14-kilodalton protein interacts with the mitogen-activated protein kinase scaffold mp1 on a late endosomal/lysosomal compartment”. J. Cell Biol. 152 (4): 765–76. (February 2001). doi:10.1083/jcb.152.4.765. PMC 2195784. PMID 11266467.
^ “Hydrophobic as well as charged residues in both MEK1 and ERK2 are important for their proper docking”. J. Biol. Chem. 276 (28): 26509–15. (July 2001). doi:10.1074/jbc.M102769200. PMID 11352917.
^ “Regulation of stress-responsive mitogen-activated protein (MAP) kinase pathways by TAO2”. J. Biol. Chem. 276 (19): 16070–5. (May 2001). doi:10.1074/jbc.M100681200. PMID 11279118.
^ “MEKK1 binds raf-1 and the ERK2 cascade components”. J. Biol. Chem. 275 (51): 40120–7. (December 2000). doi:10.1074/jbc.M005926200. PMID 10969079.
^ “Identification of a docking groove on ERK and p38 MAP kinases that regulates the specificity of docking interactions”. EMBO J. 20 (3): 466–79. (February 2001). doi:10.1093/emboj/20.3.466. PMC 133461. PMID 11157753.
^ ^a ^b “Mitogen-activated protein kinases activate the serine/threonine kinases Mnk1 and Mnk2”. EMBO J. 16 (8): 1909–20. (April 1997). doi:10.1093/emboj/16.8.1909. PMC 1169794. PMID 9155017.
^ “The N and C termini of the splice variants of the human mitogen-activated protein kinase-interacting kinase Mnk2 determine activity and localization”. Mol. Cell. Biol. 23 (16): 5692–705. (August 2003). doi:10.1128/mcb.23.16.5692-5705.2003. PMC 166352. PMID 12897141.
^ “Tobacco-specific nitrosamine 4-(methylnitrosamino)-1-(3-pyridyl)-1-butanone promotes functional cooperation of Bcl2 and c-Myc through phosphorylation in regulating cell survival and proliferation”. J. Biol. Chem. 279 (38): 40209–19. (September 2004). doi:10.1074/jbc.M404056200. PMID 15210690.
^ “MAP kinase binds to the NH2-terminal activation domain of c-Myc”. FEBS Lett. 353 (3): 281–5. (October 1994). doi:10.1016/0014-5793(94)01052-8. PMID 7957875.
^ “Mitogen-activated protein kinase kinase 7 is an activator of the c-Jun NH2-terminal kinase”. Proc. Natl. Acad. Sci. U.S.A. 94 (14): 7337–42. (July 1997). Bibcode: 1997PNAS...94.7337T. doi:10.1073/pnas.94.14.7337. PMC 23822. PMID 9207092.
^ “Nek2A specifies the centrosomal localization of Erk2”. Biochem. Biophys. Res. Commun. 321 (2): 495–501. (August 2004). doi:10.1016/j.bbrc.2004.06.171. PMID 15358203.
^ “PEA-15 mediates cytoplasmic sequestration of ERK MAP kinase”. Dev. Cell 1 (2): 239–50. (August 2001). doi:10.1016/s1534-5807(01)00035-1. PMID 11702783.
^ “The MAP-kinase ERK2 is a specific substrate of the protein tyrosine phosphatase HePTP”. Oncogene 19 (7): 858–69. (February 2000). doi:10.1038/sj.onc.1203408. PMID 10702794.
^ “Inhibition of T cell signaling by mitogen-activated protein kinase-targeted hematopoietic tyrosine phosphatase (HePTP)”. J. Biol. Chem. 274 (17): 11693–700. (April 1999). doi:10.1074/jbc.274.17.11693. PMID 10206983.
^ ^a ^b “Identification of an extracellular signal-regulated kinase (ERK) docking site in ribosomal S6 kinase, a sequence critical for activation by ERK in vivo”. J. Biol. Chem. 274 (5): 2893–8. (January 1999). doi:10.1074/jbc.274.5.2893. PMID 9915826.
^ ^a ^b “Phosphorylation of p90 ribosomal S6 kinase (RSK) regulates extracellular signal-regulated kinase docking and RSK activity”. Mol. Cell. Biol. 23 (14): 4796–804. (July 2003). doi:10.1128/mcb.23.14.4796-4804.2003. PMC 162206. PMID 12832467.
^ ^a ^b “Regulation and interaction of pp90(rsk) isoforms with mitogen-activated protein kinases”. J. Biol. Chem. 271 (47): 29773–9. (November 1996). doi:10.1074/jbc.271.47.29773. PMID 8939914.
^ “Extracellular signal-regulated kinase activated by epidermal growth factor and cell adhesion interacts with and phosphorylates vinexin”. J. Biol. Chem. 279 (33): 34570–7. (August 2004). doi:10.1074/jbc.M402304200. PMID 15184391.
^ “Extracellular signal-regulated kinase (ERK) interacts with signal transducer and activator of transcription (STAT) 5a”. Mol. Endocrinol. 13 (4): 555–65. (April 1999). doi:10.1210/mend.13.4.0263. PMID 10194762.
^ “Growth hormone (GH) induces the formation of protein complexes involving Stat5, Erk2, Shc and serine phosphorylated proteins”. Mol. Cell. Endocrinol. 166 (2): 89–99. (August 2000). doi:10.1016/s0303-7207(00)00277-x. PMID 10996427.
^ “A new ERK2 binding protein, Naf1, attenuates the EGF/ERK2 nuclear signaling”. Biochem. Biophys. Res. Commun. 297 (1): 17–23. (September 2002). doi:10.1016/s0006-291x(02)02086-7. PMID 12220502.
^ “Identification of the Anti-proliferative protein Tob as a MAPK substrate”. J. Biol. Chem. 277 (40): 37783–7. (October 2002). doi:10.1074/jbc.M204506200. PMID 12151396.
^ “Phosphorylation and functional inactivation of TSC2 by Erk implications for tuberous sclerosis and cancer pathogenesis”. Cell 121 (2): 179–93. (April 2005). doi:10.1016/j.cell.2005.02.031. PMID 15851026.
^ “Association of a p95 Vav-containing signaling complex with the FcepsilonRI gamma chain in the RBL-2H3 mast cell line. Evidence for a constitutive in vivo association of Vav with Grb2, Raf-1, and ERK2 in an active complex”. J. Biol. Chem. 271 (43): 26962–70. (October 1996). doi:10.1074/jbc.271.43.26962. PMID 8900182.
^ “Vav is associated with signal transducing molecules gp130, Grb2 and Erk2, and is tyrosine phosphorylated in response to interleukin-6”. FEBS Lett. 401 (2–3): 133–7. (January 1997). doi:10.1016/s0014-5793(96)01456-1. PMID 9013873.
^ “Expression of MAPK1 in cancer - Summary - The Human Protein Atlas”. www.proteinatlas.org. 2023年ねん7月がつ17日にち閲覧えつらん。

外部がいぶリンク

MAP Kinase Resource Archived 2021-04-15 at the Wayback Machine.

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000100030 - Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000063358 - Ensembl, May 2017

[3] Human PubMed Reference:

[4] Mouse PubMed Reference:

[pmid1540184-5] “Extracellular signal-regulated kinases in T cells: characterization of human ERK1 and ERK2 cDNAs”. Biochem. Biophys. Res. Commun. 182 (3): 1416–22. (February 1992). doi:10.1016/0006-291X(92)91891-S. PMID 1540184.

[:0-6] “Entrez Gene: MAPK1 mitogen-activated protein kinase 1”. 2023年ねん7月がつ17日にち閲覧えつらん。

[:1-7] “ERK2 (human)”. www.phosphosite.org. 2020年ねん10月がつ31日にち閲覧えつらん。

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