MAPK7

MAPK7
Доступные структуры
PDB	Поиск ортологов: PDBe RCSB
List of PDB id codes
	2Q8Y, 4B99, 4IC7, 4IC8, 4ZSJ, 4ZSL, 5BYZ, 5BYY, 4ZSG
Идентификаторы
Символы	MAPK7, BMK1, ERK4, ERK5, PRKM7, mitogen-activated protein kinase 7
Внешние IDs	OMIM: 602521 MGI: 1346347 HomoloGene: 2060 GeneCards: MAPK7
Расположение гена (человек)
Хр.	17-я хромосома человека
Конец	19,383,544 bp
Расположение гена (мышь)
Хр.	Chromosome 11 (mouse)
Конец	61,494,406 bp
Паттерн экспрессии РНК
	Top expressed in
	stromal cell of endometrium; ; popliteal artery; ; sural nerve; ; left uterine tube; ; skin of abdomen;
	Top expressed in
	condyle; ; cerebellar cortex;
	More reference expression data
	; ;
	More reference expression data
Генная онтология
Функции	трансферазная активность; нуклеотид-связывающий; protein kinase activity; mitogen-activated protein kinase binding; kinase activity; связывание с белками плазмы; АТФ-связанные; protein serine/threonine kinase activity; MAP kinase activity;
Компонент клетки	цитоплазма; цитозоль; PML body; нуклеоплазма; клеточное ядро;
Биологический процесс	cellular response to transforming growth factor beta stimulus; negative regulation of endothelial cell apoptotic process; Дифференцировка клеток; фосфорилирование; negative regulation of ERK5 cascade; cellular response to laminar fluid shear stress; positive regulation of transcription from RNA polymerase II promoter in response to stress; cellular response to growth factor stimulus; негативная регуляция апоптоза; regulation of angiogenesis; negative regulation of response to cytokine stimulus; фосфорилация белка; negative regulation of MAP kinase activity; peptidyl-serine phosphorylation; клеточный цикл; negative regulation of cyclic-nucleotide phosphodiesterase activity; negative regulation of heterotypic cell-cell adhesion; negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway; negative regulation of extrinsic apoptotic signaling pathway in absence of ligand; negative regulation of inflammatory response; cAMP-mediated signaling; передача сигнала; положительная регуляция транскрипции РНК полимеразой II промотор; cellular response to hydrogen peroxide; MAPK cascade; Аксональное наведение; negative regulation of calcineurin-NFAT signaling cascade; regulation of gene expression; intracellular signal transduction; cellular response to organic substance;
	Sources:Amigo / QuickGO
Ортологи
	5598
	23939
	ENSG00000166484
	ENSMUSG00000001034
	Q13164
	Q9WVS8
	NM_002749; NM_139032; NM_139033; NM_139034
NM_001291033; NM_001291034; NM_001291035; NM_001291036; NM_001291037;
	NM_011841; NM_001361989
	NP_002740; NP_620601; NP_620602; NP_620603
NP_001277962; NP_001277963; NP_001277964; NP_001277965; NP_001277966;
	NP_035971; NP_001348918
	Викиданные
Править (человек)	Править (мышь)

MAPK7 («митоген-активируемая белковая киназа 7»; англ. mitogen-activated protein kinase 7; ERK5) — цитозольная серин/треониновая протеинкиназа, семейства MAPK группы ERK, продукт гена MAPK7^[5]^[6].

СтруктураПравить

MAPK7 состоит из 816 аминокислот, молекулярная масса 88,4 кДа. Описано 4 изоформы белка, предполагается существование ещё 5 изоформ.

ФункцияПравить

MAPK7, или ERK5, — фермент семейства MAPK из группы киназ, регулируемых внеклеточными сигналами (ERK). Киназа отвечает на разнообразные внешние сигналы и вовлечёна во множество клеточных процессов, таких как пролиферация, клеточная дифференцировка, регуляция клеточного цикла. Активация MAPK7 требует её фосфорилирования киназой MAP2K5/MEK5. После активации MAPK7 транслоцируется в клеточное ядро, где активирует факторы транскрипции. Известны 4 изоформы белка^[7].

MAPK7 игрет критическую роль в развитии сердечно-сосудистой системы^[8] и функционировании эндотелиальных клеток^[9]^[10].

ВзаимодействияПравить

ERK5/MAPK7 взаимодействует со следующими белками:

ПримечанияПравить

↑ ¹ ² ³ GRCh38: Ensembl release 89: ENSG00000166484 - Ensembl, May 2017
↑ ¹ ² ³ GRCm38: Ensembl release 89: ENSMUSG00000001034 - Ensembl, May 2017
↑ Human PubMed Reference: (неопр.) National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ Mouse PubMed Reference: (неопр.) National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ Purandare SM, Lee JD, Patel PI (March 1999). “Assignment of big MAP kinase (PRKM7) to human chromosome 17 band p11.2 with somatic cell hybrids”. Cytogenet. Cell Genet. 83 (3—4): 258—9. DOI:10.1159/000015199. PMID 10072598. S2CID 31186896.
↑ ¹ ² Zhou G, Bao ZQ, Dixon JE (Jun 1995). “Components of a new human protein kinase signal transduction pathway”. J. Biol. Chem. 270 (21): 12665—9. DOI:10.1074/jbc.270.21.12665. PMID 7759517.
↑ Entrez Gene: MAPK7 mitogen-activated protein kinase 7 (неопр.).
↑ Hayashi M, Lee JD (Oct 2004). “Role of the BMK1/ERK5 signaling pathway: lessons from knockout mice”. J. Mol. Med. 82 (12): 800—8. DOI:10.1007/s00109-004-0602-8. PMID 15517128. S2CID 8499230.
↑ Roberts OL, Holmes K, Müller J, Cross DA, Cross MJ (Dec 2009). “ERK5 and the regulation of endothelial cell function”. Biochem. Soc. Trans. 37 (Pt 6): 1254—9. DOI:10.1042/BST0371254. PMID 19909257.
↑ Roberts OL, Holmes K, Müller J, Cross DA, Cross MJ (Sep 2010). “ERK5 is required for VEGF-mediated survival and tubular morphogenesis of primary human microvascular endothelial cells”. J. Cell Sci. 123 (Pt 18): 3189—200. DOI:10.1242/jcs.072801. PMID 20736307.
↑ English JM, Pearson G, Hockenberry T, Shivakumar L, White MA, Cobb MH (Oct 1999). “Contribution of the ERK5/MEK5 pathway to Ras/Raf signaling and growth control”. J. Biol. Chem. 274 (44): 31588—92. DOI:10.1074/jbc.274.44.31588. PMID 10531364.
↑ Cameron SJ, Malik S, Akaike M, Lerner-Marmarosh N, Yan C, Lee JD, Abe J, Yang J (May 2003). “Regulation of epidermal growth factor-induced connexin 43 gap junction communication by big mitogen-activated protein kinase1/ERK5 but not ERK1/2 kinase activation”. J. Biol. Chem. 278 (20): 18682—8. DOI:10.1074/jbc.M213283200. PMID 12637502.
↑ ¹ ² Yang CC, Ornatsky OI, McDermott JC, Cruz TF, Prody CA (Oct 1998). “Interaction of myocyte enhancer factor 2 (MEF2) with a mitogen-activated protein kinase, ERK5/BMK1”. Nucleic Acids Res. 26 (20): 4771—7. DOI:10.1093/nar/26.20.4771. PMC 147902. PMID 9753748.
↑ Buschbeck M, Eickhoff J, Sommer MN, Ullrich A (Aug 2002). “Phosphotyrosine-specific phosphatase PTP-SL regulates the ERK5 signaling pathway”. J. Biol. Chem. 277 (33): 29503—9. DOI:10.1074/jbc.M202149200. PMID 12042304.
↑ Hayashi M, Tapping RI, Chao TH, Lo JF, King CC, Yang Y, Lee JD (Mar 2001). “BMK1 mediates growth factor-induced cell proliferation through direct cellular activation of serum and glucocorticoid-inducible kinase”. J. Biol. Chem. 276 (12): 8631—4. DOI:10.1074/jbc.C000838200. PMID 11254654.
↑ Zheng Q, Yin G, Yan C, Cavet M, Berk BC (Mar 2004). “14-3-3beta binds to big mitogen-activated protein kinase 1 (BMK1/ERK5) and regulates BMK1 function”. J. Biol. Chem. 279 (10): 8787—91. DOI:10.1074/jbc.M310212200. PMID 14679215.

ЛитератураПравить

Lee JD, Ulevitch RJ, Han J (1995). “Primary structure of BMK1: a new mammalian map kinase”. Biochem. Biophys. Res. Commun. 213 (2): 715—24. DOI:10.1006/bbrc.1995.2189. PMID 7646528.
Warn-Cramer BJ, Lampe PD, Kurata WE, Kanemitsu MY, Loo LW, Eckhart W, Lau AF (1996). “Characterization of the mitogen-activated protein kinase phosphorylation sites on the connexin-43 gap junction protein”. J. Biol. Chem. 271 (7): 3779—86. DOI:10.1074/jbc.271.7.3779. PMID 8631994.
Kato Y, Kravchenko VV, Tapping RI, Han J, Ulevitch RJ, Lee JD (1997). “BMK1/ERK5 regulates serum-induced early gene expression through transcription factor MEF2C”. EMBO J. 16 (23): 7054—66. DOI:10.1093/emboj/16.23.7054. PMC 1170308. PMID 9384584.
English JM, Pearson G, Baer R, Cobb MH (1998). “Identification of substrates and regulators of the mitogen-activated protein kinase ERK5 using chimeric protein kinases”. J. Biol. Chem. 273 (7): 3854—60. DOI:10.1074/jbc.273.7.3854. PMID 9461566.
Grunwald ME, Yu WP, Yu HH, Yau KW (1998). “Identification of a domain on the beta-subunit of the rod cGMP-gated cation channel that mediates inhibition by calcium-calmodulin”. J. Biol. Chem. 273 (15): 9148—57. DOI:10.1074/jbc.273.15.9148. PMID 9535905.
Warn-Cramer BJ, Cottrell GT, Burt JM, Lau AF (1998). “Regulation of connexin-43 gap junctional intercellular communication by mitogen-activated protein kinase”. J. Biol. Chem. 273 (15): 9188—96. DOI:10.1074/jbc.273.15.9188. PMID 9535909.
Yang CC, Ornatsky OI, McDermott JC, Cruz TF, Prody CA (1998). “Interaction of myocyte enhancer factor 2 (MEF2) with a mitogen-activated protein kinase, ERK5/BMK1”. Nucleic Acids Res. 26 (20): 4771—7. DOI:10.1093/nar/26.20.4771. PMC 147902. PMID 9753748.
Kato Y, Tapping RI, Huang S, Watson MH, Ulevitch RJ, Lee JD (1998). “Bmk1/Erk5 is required for cell proliferation induced by epidermal growth factor”. Nature. 395 (6703): 713—6. DOI:10.1038/27234. PMID 9790194. S2CID 204997780.
Zhao M, New L, Kravchenko VV, Kato Y, Gram H, di Padova F, Olson EN, Ulevitch RJ, Han J (1999). “Regulation of the MEF2 family of transcription factors by p38”. Mol. Cell. Biol. 19 (1): 21—30. DOI:10.1128/mcb.19.1.21. PMC 83862. PMID 9858528.
Kamakura S, Moriguchi T, Nishida E (1999). “Activation of the protein kinase ERK5/BMK1 by receptor tyrosine kinases. Identification and characterization of a signaling pathway to the nucleus”. J. Biol. Chem. 274 (37): 26563—71. DOI:10.1074/jbc.274.37.26563. PMID 10473620.
English JM, Pearson G, Hockenberry T, Shivakumar L, White MA, Cobb MH (1999). “Contribution of the ERK5/MEK5 pathway to Ras/Raf signaling and growth control”. J. Biol. Chem. 274 (44): 31588—92. DOI:10.1074/jbc.274.44.31588. PMID 10531364.
Fukuhara S, Marinissen MJ, Chiariello M, Gutkind JS (2000). “Signaling from G protein-coupled receptors to ERK5/Big MAPK 1 involves Galpha q and Galpha 12/13 families of heterotrimeric G proteins. Evidence for the existence of a novel Ras AND Rho-independent pathway”. J. Biol. Chem. 275 (28): 21730—6. DOI:10.1074/jbc.M002410200. PMID 10781600.
Kato Y, Zhao M, Morikawa A, Sugiyama T, Chakravortty D, Koide N, Yoshida T, Tapping RI, Yang Y, Yokochi T, Lee JD (2000). “Big mitogen-activated kinase regulates multiple members of the MEF2 protein family”. J. Biol. Chem. 275 (24): 18534—40. DOI:10.1074/jbc.M001573200. PMID 10849446.
Yan C, Luo H, Lee JD, Abe J, Berk BC (2001). “Molecular cloning of mouse ERK5/BMK1 splice variants and characterization of ERK5 functional domains”. J. Biol. Chem. 276 (14): 10870—8. DOI:10.1074/jbc.M009286200. PMID 11139578.
Hayashi M, Tapping RI, Chao TH, Lo JF, King CC, Yang Y, Lee JD (2001). “BMK1 mediates growth factor-induced cell proliferation through direct cellular activation of serum and glucocorticoid-inducible kinase”. J. Biol. Chem. 276 (12): 8631—4. DOI:10.1074/jbc.C000838200. PMID 11254654.
Dong F, Gutkind JS, Larner AC (2001). “Granulocyte colony-stimulating factor induces ERK5 activation, which is differentially regulated by protein-tyrosine kinases and protein kinase C. Regulation of cell proliferation and survival”. J. Biol. Chem. 276 (14): 10811—6. DOI:10.1074/jbc.M008748200. PMID 11278431.
Watson FL, Heerssen HM, Bhattacharyya A, Klesse L, Lin MZ, Segal RA (2001). “Neurotrophins use the Erk5 pathway to mediate a retrograde survival response”. Nat. Neurosci. 4 (10): 981—8. DOI:10.1038/nn720. PMID 11544482. S2CID 3164934.
Esparís-Ogando A, Díaz-Rodríguez E, Montero JC, Yuste L, Crespo P, Pandiella A (2002). “Erk5 participates in neuregulin signal transduction and is constitutively active in breast cancer cells overexpressing ErbB2”. Mol. Cell. Biol. 22 (1): 270—85. DOI:10.1128/MCB.22.1.270-285.2002. PMC 134212. PMID 11739740.

СсылкиПравить

[refGRCh38Ensembl-1] ¹ ² ³ GRCh38: Ensembl release 89: ENSG00000166484 - Ensembl, May 2017

[refGRCm38Ensembl-2] ¹ ² ³ GRCm38: Ensembl release 89: ENSMUSG00000001034 - Ensembl, May 2017

[3] Human PubMed Reference: (неопр.) National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] Mouse PubMed Reference: (неопр.) National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid10072598-5] Purandare SM, Lee JD, Patel PI (March 1999). “Assignment of big MAP kinase (PRKM7) to human chromosome 17 band p11.2 with somatic cell hybrids”. Cytogenet. Cell Genet. 83 (3—4): 258—9. DOI:10.1159/000015199. PMID 10072598. S2CID 31186896.

[pmid7759517-6] ¹ ² Zhou G, Bao ZQ, Dixon JE (Jun 1995). “Components of a new human protein kinase signal transduction pathway”. J. Biol. Chem. 270 (21): 12665—9. DOI:10.1074/jbc.270.21.12665. PMID 7759517.

[entrez-7] Entrez Gene: MAPK7 mitogen-activated protein kinase 7 (неопр.).

[pmid15517128-8] Hayashi M, Lee JD (Oct 2004). “Role of the BMK1/ERK5 signaling pathway: lessons from knockout mice”. J. Mol. Med. 82 (12): 800—8. DOI:10.1007/s00109-004-0602-8. PMID 15517128. S2CID 8499230.

[pmid19909257-9] Roberts OL, Holmes K, Müller J, Cross DA, Cross MJ (Dec 2009). “ERK5 and the regulation of endothelial cell function”. Biochem. Soc. Trans. 37 (Pt 6): 1254—9. DOI:10.1042/BST0371254. PMID 19909257.

[pmid20736307-10] Roberts OL, Holmes K, Müller J, Cross DA, Cross MJ (Sep 2010). “ERK5 is required for VEGF-mediated survival and tubular morphogenesis of primary human microvascular endothelial cells”. J. Cell Sci. 123 (Pt 18): 3189—200. DOI:10.1242/jcs.072801. PMID 20736307.

[pmid10531364-11] English JM, Pearson G, Hockenberry T, Shivakumar L, White MA, Cobb MH (Oct 1999). “Contribution of the ERK5/MEK5 pathway to Ras/Raf signaling and growth control”. J. Biol. Chem. 274 (44): 31588—92. DOI:10.1074/jbc.274.44.31588. PMID 10531364.

[pmid12637502-12] Cameron SJ, Malik S, Akaike M, Lerner-Marmarosh N, Yan C, Lee JD, Abe J, Yang J (May 2003). “Regulation of epidermal growth factor-induced connexin 43 gap junction communication by big mitogen-activated protein kinase1/ERK5 but not ERK1/2 kinase activation”. J. Biol. Chem. 278 (20): 18682—8. DOI:10.1074/jbc.M213283200. PMID 12637502.

[pmid9753748-13] ¹ ² Yang CC, Ornatsky OI, McDermott JC, Cruz TF, Prody CA (Oct 1998). “Interaction of myocyte enhancer factor 2 (MEF2) with a mitogen-activated protein kinase, ERK5/BMK1”. Nucleic Acids Res. 26 (20): 4771—7. DOI:10.1093/nar/26.20.4771. PMC 147902. PMID 9753748.

[pmid12042304-14] Buschbeck M, Eickhoff J, Sommer MN, Ullrich A (Aug 2002). “Phosphotyrosine-specific phosphatase PTP-SL regulates the ERK5 signaling pathway”. J. Biol. Chem. 277 (33): 29503—9. DOI:10.1074/jbc.M202149200. PMID 12042304.

[pmid11254654-15] Hayashi M, Tapping RI, Chao TH, Lo JF, King CC, Yang Y, Lee JD (Mar 2001). “BMK1 mediates growth factor-induced cell proliferation through direct cellular activation of serum and glucocorticoid-inducible kinase”. J. Biol. Chem. 276 (12): 8631—4. DOI:10.1074/jbc.C000838200. PMID 11254654.

[pmid14679215-16] Zheng Q, Yin G, Yan C, Cavet M, Berk BC (Mar 2004). “14-3-3beta binds to big mitogen-activated protein kinase 1 (BMK1/ERK5) and regulates BMK1 function”. J. Biol. Chem. 279 (10): 8787—91. DOI:10.1074/jbc.M310212200. PMID 14679215.

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