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Mitogen-activated protein kinase kinase kinase 5 (EC 2.7.11.25) (Apoptosis signal-regulating kinase 1) (ASK-1) (MAPK/ERK kinase kinase 5) (MEK kinase 5) (MEKK 5)

 M3K5_HUMAN              Reviewed;        1374 AA.
Q99683; A6NIA0; B4DGB2; Q5THN3; Q99461;
30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
01-MAY-1997, sequence version 1.
12-AUG-2020, entry version 212.
RecName: Full=Mitogen-activated protein kinase kinase kinase 5;
EC=2.7.11.25;
AltName: Full=Apoptosis signal-regulating kinase 1;
Short=ASK-1;
AltName: Full=MAPK/ERK kinase kinase 5;
Short=MEK kinase 5;
Short=MEKK 5;
Name=MAP3K5; Synonyms=ASK1, MAPKKK5, MEKK5;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND FUNCTION.
PubMed=8940179; DOI=10.1074/jbc.271.49.31607;
Wang X.S., Diener K., Jannuzzi D., Trollinger D., Tan T.-H.,
Lichenstein H., Zukowski M., Yao Z.;
"Molecular cloning and characterization of a novel protein kinase with a
catalytic domain homologous to mitogen-activated protein kinase kinase
kinase.";
J. Biol. Chem. 271:31607-31611(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND FUNCTION.
PubMed=8974401; DOI=10.1126/science.275.5296.90;
Ichijo H., Nishida E., Irie K., ten Dijke P., Saitoh M., Moriguchi T.,
Takagi M., Matsumoto K., Miyazono K., Gotoh Y.;
"Induction of apoptosis by ASK1, a mammalian MAPKKK that activates SAPK/JNK
and p38 signaling pathways.";
Science 275:90-94(1997).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Amygdala;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=14574404; DOI=10.1038/nature02055;
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
Rogers J., Beck S.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Eye, and Lung;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project:
the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
INTERACTION WITH TXN, ACTIVITY REGULATION, AND FUNCTION.
PubMed=9564042; DOI=10.1093/emboj/17.9.2596;
Saitoh M., Nishitoh H., Fujii M., Takeda K., Tobiume K., Sawada Y.,
Kawabata M., Miyazono K., Ichijo H.;
"Mammalian thioredoxin is a direct inhibitor of apoptosis signal-regulating
kinase (ASK) 1.";
EMBO J. 17:2596-2606(1998).
[7]
ACTIVITY REGULATION, INTERACTION WITH TRAF2, AND FUNCTION.
PubMed=9774977; DOI=10.1016/s1097-2765(00)80283-x;
Nishitoh H., Saitoh M., Mochida Y., Takeda K., Nakano H., Rothe M.,
Miyazono K., Ichijo H.;
"ASK1 is essential for JNK/SAPK activation by TRAF2.";
Mol. Cell 2:389-395(1998).
[8]
INTERACTION WITH DAXX, AND MUTAGENESIS OF LYS-709.
PubMed=9743501; DOI=10.1126/science.281.5384.1860;
Chang H.Y., Nishitoh H., Yang X., Ichijo H., Baltimore D.;
"Activation of apoptosis signal-regulating kinase 1 (ASK1) by the adapter
protein Daxx.";
Science 281:1860-1863(1998).
[9]
INTERACTION WITH 14-3-3 PROTEINS, ACTIVITY REGULATION, MUTAGENESIS OF
SER-966, AND FUNCTION.
PubMed=10411906; DOI=10.1073/pnas.96.15.8511;
Zhang L., Chen J., Fu H.;
"Suppression of apoptosis signal-regulating kinase 1-induced cell death by
14-3-3 proteins.";
Proc. Natl. Acad. Sci. U.S.A. 96:8511-8515(1999).
[10]
FUNCTION IN APOPTOSIS.
PubMed=10849426; DOI=10.1074/jbc.m003412200;
Hatai T., Matsuzawa A., Inoshita S., Mochida Y., Kuroda T., Sakamaki K.,
Kuida K., Yonehara S., Ichijo H., Takeda K.;
"Execution of apoptosis signal-regulating kinase 1 (ASK1)-induced apoptosis
by the mitochondria-dependent caspase activation.";
J. Biol. Chem. 275:26576-26581(2000).
[11]
SUBUNIT, INTERACTION WITH TRAF2, ACTIVITY REGULATION, AND FUNCTION.
PubMed=10688666; DOI=10.1128/mcb.20.6.2198-2208.2000;
Liu H., Nishitoh H., Ichijo H., Kyriakis J.M.;
"Activation of apoptosis signal-regulating kinase 1 (ASK1) by tumor
necrosis factor receptor-associated factor 2 requires prior dissociation of
the ASK1 inhibitor thioredoxin.";
Mol. Cell. Biol. 20:2198-2208(2000).
[12]
INTERACTION WITH ARRB2.
PubMed=11090355; DOI=10.1126/science.290.5496.1574;
McDonald P.H., Chow C.W., Miller W.E., Laporte S.A., Field M.E., Lin F.-T.,
Davis R.J., Lefkowitz R.J.;
"Beta-arrestin 2: a receptor-regulated MAPK scaffold for the activation of
JNK3.";
Science 290:1574-1577(2000).
[13]
INTERACTION WITH PPP5C, DEPHOSPHORYLATION AT THR-838, SUBCELLULAR LOCATION,
ACTIVITY REGULATION, AND FUNCTION.
PubMed=11689443; DOI=10.1093/emboj/20.21.6028;
Morita K., Saitoh M., Tobiume K., Matsuura H., Enomoto S., Nishitoh H.,
Ichijo H.;
"Negative feedback regulation of ASK1 by protein phosphatase 5 (PP5) in
response to oxidative stress.";
EMBO J. 20:6028-6036(2001).
[14]
FUNCTION IN KERATINOCYTE DIFFERENTIATION.
PubMed=11029458; DOI=10.1074/jbc.m003425200;
Sayama K., Hanakawa Y., Shirakata Y., Yamasaki K., Sawada Y., Sun L.,
Yamanishi K., Ichijo H., Hashimoto K.;
"Apoptosis signal-regulating kinase 1 (ASK1) is an intracellular inducer of
keratinocyte differentiation.";
J. Biol. Chem. 276:999-1004(2001).
[15]
PHOSPHORYLATION AT SER-83, ACTIVITY REGULATION, AND FUNCTION.
PubMed=11154276; DOI=10.1128/mcb.21.3.893-901.2001;
Kim A.H., Khursigara G., Sun X., Franke T.F., Chao M.V.;
"Akt phosphorylates and negatively regulates apoptosis signal-regulating
kinase 1.";
Mol. Cell. Biol. 21:893-901(2001).
[16]
INTERACTION WITH HIV-1 NEF (MICROBIAL INFECTION), AND INHIBITION BY HIV-1
NEF (MICROBIAL INFECTION).
PubMed=11298454; DOI=10.1038/35071111;
Geleziunas R., Xu W., Takeda K., Ichijo H., Greene W.C.;
"HIV-1 Nef inhibits ASK1-dependent death signalling providing a potential
mechanism for protecting the infected host cell.";
Nature 410:834-838(2001).
[17]
INTERACTION WITH RAF1.
PubMed=11427728; DOI=10.1073/pnas.141224398;
Chen J., Fujii K., Zhang L., Roberts T., Fu H.;
"Raf-1 promotes cell survival by antagonizing apoptosis signal-regulating
kinase 1 through a MEK-ERK independent mechanism.";
Proc. Natl. Acad. Sci. U.S.A. 98:7783-7788(2001).
[18]
INTERACTION WITH TRAF2 AND ERN1, ACTIVITY REGULATION, AND FUNCTION IN ER
STRESS RESPONSE.
PubMed=14749717; DOI=10.1038/sj.embor.7400072;
Takeda K., Matsuzawa A., Nishitoh H., Tobiume K., Kishida S.,
Ninomiya-Tsuji J., Matsumoto K., Ichijo H.;
"Involvement of ASK1 in Ca2+-induced p38 MAP kinase activation.";
EMBO Rep. 5:161-166(2004).
[19]
FUNCTION, HOMODIMERIZATION, ACTIVITY REGULATION, AND PHOSPHORYLATION AT
THR-838.
PubMed=11920685; DOI=10.1002/jcp.10080;
Tobiume K., Saitoh M., Ichijo H.;
"Activation of apoptosis signal-regulating kinase 1 by the stress-induced
activating phosphorylation of pre-formed oligomer.";
J. Cell. Physiol. 191:95-104(2002).
[20]
INTERACTION WITH IGF1R, PHOSPHORYLATION, ACTIVITY REGULATION, AND
SUBCELLULAR LOCATION.
PubMed=12556535; DOI=10.1074/jbc.m211398200;
Galvan V., Logvinova A., Sperandio S., Ichijo H., Bredesen D.E.;
"Type 1 insulin-like growth factor receptor (IGF-IR) signaling inhibits
apoptosis signal-regulating kinase 1 (ASK1).";
J. Biol. Chem. 278:13325-13332(2003).
[21]
PHOSPHORYLATION AT SER-83, ACTIVITY REGULATION, AND FUNCTION.
PubMed=12697749; DOI=10.1074/jbc.m302674200;
Yuan Z.Q., Feldman R.I., Sussman G.E., Coppola D., Nicosia S.V.,
Cheng J.Q.;
"AKT2 inhibition of cisplatin-induced JNK/p38 and Bax activation by
phosphorylation of ASK1: implication of AKT2 in chemoresistance.";
J. Biol. Chem. 278:23432-23440(2003).
[22]
INTERACTION WITH DAB2IP.
PubMed=12813029; DOI=10.1172/jci200317790;
Zhang R., He X., Liu W., Lu M., Hsieh J.-T., Min W.;
"AIP1 mediates TNF-alpha-induced ASK1 activation by facilitating
dissociation of ASK1 from its inhibitor 14-3-3.";
J. Clin. Invest. 111:1933-1943(2003).
[23]
INTERACTION WITH YWHAB; YWHAE; YWHAH; YWHAQ; YWHAZ AND SFN, FUNCTION, AND
SUBCELLULAR LOCATION.
PubMed=15023544; DOI=10.1016/j.yexcr.2003.12.009;
Subramanian R.R., Zhang H., Wang H., Ichijo H., Miyashita T., Fu H.;
"Interaction of apoptosis signal-regulating kinase 1 with isoforms of 14-3-
3 proteins.";
Exp. Cell Res. 294:581-591(2004).
[24]
PHOSPHORYLATION AT SER-966, ACTIVITY REGULATION, AND FUNCTION.
PubMed=14688258; DOI=10.1074/jbc.m311129200;
Goldman E.H., Chen L., Fu H.;
"Activation of apoptosis signal-regulating kinase 1 by reactive oxygen
species through dephosphorylation at serine 967 and 14-3-3 dissociation.";
J. Biol. Chem. 279:10442-10449(2004).
[25]
INTERACTION WITH DAB2IP.
PubMed=15310755; DOI=10.1074/jbc.m407617200;
Zhang H., Zhang R., Luo Y., D'Alessio A., Pober J.S., Min W.;
"AIP1/DAB2IP, a novel member of the Ras-GAP family, transduces TRAF2-
induced ASK1-JNK activation.";
J. Biol. Chem. 279:44955-44965(2004).
[26]
ACTIVITY REGULATION, PHOSPHORYLATION AT SER-966 AND SER-1033, MUTAGENESIS
OF SER-966 AND SER-1033, AND INTERACTION WITH YWHAG.
PubMed=15094778; DOI=10.1038/sj.onc.1207668;
Fujii K., Goldman E.H., Park H.R., Zhang L., Chen J., Fu H.;
"Negative control of apoptosis signal-regulating kinase 1 through
phosphorylation of Ser-1034.";
Oncogene 23:5099-5104(2004).
[27]
INTERACTION WITH STUB1, AND UBIQUITINATION.
PubMed=16038411; DOI=10.1379/csc-90r.1;
Hwang J.R., Zhang C., Patterson C.;
"C-terminus of heat shock protein 70-interacting protein facilitates
degradation of apoptosis signal-regulating kinase 1 and inhibits apoptosis
signal-regulating kinase 1-dependent apoptosis.";
Cell Stress Chaperones 10:147-156(2005).
[28]
INTERACTION WITH HIPK1, AND SUBCELLULAR LOCATION.
PubMed=15701637; DOI=10.1074/jbc.m414262200;
Li X., Zhang R., Luo D., Park S.-J., Wang Q., Kim Y., Min W.;
"Tumor necrosis factor alpha-induced desumoylation and cytoplasmic
translocation of homeodomain-interacting protein kinase 1 are critical for
apoptosis signal-regulating kinase 1-JNK/p38 activation.";
J. Biol. Chem. 280:15061-15070(2005).
[29]
SUBUNIT, INTERACTION WITH TRAF2, AND FUNCTION.
PubMed=16129676; DOI=10.1074/jbc.m506771200;
Noguchi T., Takeda K., Matsuzawa A., Saegusa K., Nakano H., Gohda J.,
Inoue J., Ichijo H.;
"Recruitment of tumor necrosis factor receptor-associated factor family
proteins to apoptosis signal-regulating kinase 1 signalosome is essential
for oxidative stress-induced cell death.";
J. Biol. Chem. 280:37033-37040(2005).
[30]
PHOSPHORYLATION AT TYR-718, INTERACTION WITH SOCS1, AND ACTIVITY
REGULATION.
PubMed=16407264; DOI=10.1074/jbc.m512338200;
He Y., Zhang W., Zhang R., Zhang H., Min W.;
"SOCS1 inhibits tumor necrosis factor-induced activation of ASK1-JNK
inflammatory signaling by mediating ASK1 degradation.";
J. Biol. Chem. 281:5559-5566(2006).
[31]
INTERACTION WITH PPM1L.
PubMed=17456047; DOI=10.1042/bj20070231;
Saito J., Toriumi S., Awano K., Ichijo H., Sasaki K., Kobayashi T.,
Tamura S.;
"Regulation of apoptosis signal-regulating kinase 1 by protein phosphatase
2Cepsilon.";
Biochem. J. 405:591-596(2007).
[32]
ACTIVITY REGULATION, INTERACTION WITH MAP3K5, PHOSPHORYLATION AT THR-838,
AND MUTAGENESIS OF LYS-709.
PubMed=17210579; DOI=10.1074/jbc.m607177200;
Takeda K., Shimozono R., Noguchi T., Umeda T., Morimoto Y., Naguro I.,
Tobiume K., Saitoh M., Matsuzawa A., Ichijo H.;
"Apoptosis signal-regulating kinase (ASK) 2 functions as a mitogen-
activated protein kinase kinase kinase in a heteromeric complex with
ASK1.";
J. Biol. Chem. 282:7522-7531(2007).
[33]
INTERACTION WITH BIRC2, UBIQUITINATION, AND FUNCTION.
PubMed=17220297; DOI=10.1074/jbc.m609146200;
Zhao Y., Conze D.B., Hanover J.A., Ashwell J.D.;
"Tumor necrosis factor receptor 2 signaling induces selective c-IAP1-
dependent ASK1 ubiquitination and terminates mitogen-activated protein
kinase signaling.";
J. Biol. Chem. 282:7777-7782(2007).
[34]
INTERACTION WITH DAB2IP.
PubMed=17389591; DOI=10.1074/jbc.m701148200;
Zhang H., Zhang H., Lin Y., Li J., Pober J.S., Min W.;
"RIP1-mediated AIP1 phosphorylation at a 14-3-3-binding site is critical
for tumor necrosis factor-induced ASK1-JNK/p38 activation.";
J. Biol. Chem. 282:14788-14796(2007).
[35]
INTERACTION WITH TRAF2; TRAF6 AND TXN.
PubMed=17724081; DOI=10.1128/mcb.00227-07;
Fujino G., Noguchi T., Matsuzawa A., Yamauchi S., Saitoh M., Takeda K.,
Ichijo H.;
"Thioredoxin and TRAF family proteins regulate reactive oxygen species-
dependent activation of ASK1 through reciprocal modulation of the N-
terminal homophilic interaction of ASK1.";
Mol. Cell. Biol. 27:8152-8163(2007).
[36]
INTERACTION WITH ARRB2.
PubMed=18408005; DOI=10.1074/jbc.m710006200;
Guo C., Whitmarsh A.J.;
"The beta-arrestin-2 scaffold protein promotes c-Jun N-terminal kinase-3
activation by binding to its nonconserved N terminus.";
J. Biol. Chem. 283:15903-15911(2008).
[37]
PHOSPHORYLATION AT THR-838.
PubMed=18948261; DOI=10.1074/jbc.m807219200;
Jung H., Seong H.A., Ha H.;
"Murine protein serine/threonine kinase 38 activates apoptosis signal-
regulating kinase 1 via Thr 838 phosphorylation.";
J. Biol. Chem. 283:34541-34553(2008).
[38]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1029 AND SER-1033, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Platelet;
PubMed=18088087; DOI=10.1021/pr0704130;
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
Schuetz C., Walter U., Gambaryan S., Sickmann A.;
"Phosphoproteome of resting human platelets.";
J. Proteome Res. 7:526-534(2008).
[39]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1029 AND SER-1033, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[40]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1033, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[41]
PHOSPHORYLATION AT SER-83 BY PIM1, AND INTERACTION WITH PIM1.
PubMed=19749799; DOI=10.1038/onc.2009.276;
Gu J.J., Wang Z., Reeves R., Magnuson N.S.;
"PIM1 phosphorylates and negatively regulates ASK1-mediated apoptosis.";
Oncogene 28:4261-4271(2009).
[42]
INTERACTION WITH PGAM5, AND PHOSPHORYLATION AT THR-838; SER-966 AND
SER-1033.
PubMed=19590015; DOI=10.1073/pnas.0901823106;
Takeda K., Komuro Y., Hayakawa T., Oguchi H., Ishida Y., Murakami S.,
Noguchi T., Kinoshita H., Sekine Y., Iemura S., Natsume T., Ichijo H.;
"Mitochondrial phosphoglycerate mutase 5 uses alternate catalytic activity
as a protein serine/threonine phosphatase to activate ASK1.";
Proc. Natl. Acad. Sci. U.S.A. 106:12301-12305(2009).
[43]
REVIEW ON ACTIVITY REGULATION, AND REVIEW ON FUNCTION.
PubMed=17883330; DOI=10.1146/annurev.pharmtox.48.113006.094606;
Takeda K., Noguchi T., Naguro I., Ichijo H.;
"Apoptosis signal-regulating kinase 1 in stress and immune response.";
Annu. Rev. Pharmacol. Toxicol. 48:199-225(2008).
[44]
REVIEW ON ACTIVITY REGULATION, AND REVIEW ON FUNCTION.
PubMed=19389260; DOI=10.1186/1478-811x-7-9;
Hattori K., Naguro I., Runchel C., Ichijo H.;
"The roles of ASK family proteins in stress responses and diseases.";
Cell Commun. Signal. 7:9-9(2009).
[45]
INTERACTION WITH DUSP13.
PubMed=20358250; DOI=10.1007/s00018-010-0353-3;
Park J.E., Park B.C., Kim H.A., Song M., Park S.G., Lee D.H., Kim H.J.,
Choi H.K., Kim J.T., Cho S.;
"Positive regulation of apoptosis signal-regulating kinase 1 by dual-
specificity phosphatase 13A.";
Cell. Mol. Life Sci. 67:2619-2629(2010).
[46]
FUNCTION, PHOSPHORYLATION AT THR-838, AND DEPHOSPHORYLATION AT THR-838 BY
PPP5C.
PubMed=23102700; DOI=10.1016/j.molcel.2012.09.018;
Sekine Y., Hatanaka R., Watanabe T., Sono N., Iemura S., Natsume T.,
Kuranaga E., Miura M., Takeda K., Ichijo H.;
"The Kelch repeat protein KLHDC10 regulates oxidative stress-induced ASK1
activation by suppressing PP5.";
Mol. Cell 48:692-704(2012).
[47]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-958, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[48]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
phosphoproteome.";
J. Proteomics 96:253-262(2014).
[49]
INTERACTION WITH RC3H2, AND MUTAGENESIS OF LYS-709.
PubMed=24448648; DOI=10.1126/scisignal.2004822;
Maruyama T., Araki T., Kawarazaki Y., Naguro I., Heynen S., Aza-Blanc P.,
Ronai Z., Matsuzawa A., Ichijo H.;
"Roquin-2 promotes ubiquitin-mediated degradation of ASK1 to regulate
stress responses.";
Sci. Signal. 7:RA8-RA8(2014).
[50]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 659-951, AND PHOSPHORYLATION AT
THR-813; THR-838 AND THR-842.
PubMed=17937911; DOI=10.1016/j.str.2007.08.011;
Bunkoczi G., Salah E., Filippakopoulos P., Fedorov O., Muller S.,
Sobott F., Parker S.A., Zhang H., Min W., Turk B.E., Knapp S.;
"Structural and functional characterization of the human protein kinase
ASK1.";
Structure 15:1215-1226(2007).
[51]
VARIANTS [LARGE SCALE ANALYSIS] ARG-1006; THR-1214; VAL-1250; ILE-1314 AND
ASN-1315.
PubMed=17344846; DOI=10.1038/nature05610;
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G.,
Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S.,
Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.,
Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K.,
Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D.,
Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R.,
Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A.,
Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F.,
Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F.,
Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G.,
Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R.,
Futreal P.A., Stratton M.R.;
"Patterns of somatic mutation in human cancer genomes.";
Nature 446:153-158(2007).
-!- FUNCTION: Serine/threonine kinase which acts as an essential component
of the MAP kinase signal transduction pathway. Plays an important role
in the cascades of cellular responses evoked by changes in the
environment. Mediates signaling for determination of cell fate such as
differentiation and survival. Plays a crucial role in the apoptosis
signal transduction pathway through mitochondria-dependent caspase
activation. MAP3K5/ASK1 is required for the innate immune response,
which is essential for host defense against a wide range of pathogens.
Mediates signal transduction of various stressors like oxidative stress
as well as by receptor-mediated inflammatory signals, such as the tumor
necrosis factor (TNF) or lipopolysaccharide (LPS). Once activated, acts
as an upstream activator of the MKK/JNK signal transduction cascade and
the p38 MAPK signal transduction cascade through the phosphorylation
and activation of several MAP kinase kinases like MAP2K4/SEK1,
MAP2K3/MKK3, MAP2K6/MKK6 and MAP2K7/MKK7. These MAP2Ks in turn activate
p38 MAPKs and c-jun N-terminal kinases (JNKs). Both p38 MAPK and JNKs
control the transcription factors activator protein-1 (AP-1).
{ECO:0000269|PubMed:10411906, ECO:0000269|PubMed:10688666,
ECO:0000269|PubMed:10849426, ECO:0000269|PubMed:11029458,
ECO:0000269|PubMed:11154276, ECO:0000269|PubMed:11689443,
ECO:0000269|PubMed:11920685, ECO:0000269|PubMed:12697749,
ECO:0000269|PubMed:14688258, ECO:0000269|PubMed:14749717,
ECO:0000269|PubMed:15023544, ECO:0000269|PubMed:16129676,
ECO:0000269|PubMed:17220297, ECO:0000269|PubMed:23102700,
ECO:0000269|PubMed:8940179, ECO:0000269|PubMed:8974401,
ECO:0000269|PubMed:9564042, ECO:0000269|PubMed:9774977}.
-!- CATALYTIC ACTIVITY:
Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.25;
-!- CATALYTIC ACTIVITY:
Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
EC=2.7.11.25;
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
-!- ACTIVITY REGULATION: Activated by various stressors, including
oxidative stress, endoplasmic reticulum stress, and calcium overload,
as well as by receptor-mediated inflammatory signals, such as the tumor
necrosis factor (TNF) and lipopolysaccharide (LPS). Homophilic
association of MAP3K5/ASK1 through the C-terminal coiled-coil domains
and the heteromeric complex formation of MAP3K5/ASK1 with the reduced
form of thioredoxin (TXN), constitutes an inactive form of the kinase
(PubMed:17210579, PubMed:9564042). Upon ROS-induced dissociation of TXN
from MAP3K5/ASK1, TRAF2 and TRAF6 are reciprocally recruited to
MAP3K5/ASK1 and form the active MAP3K5/ASK1 signalosome, in which TRAF2
and TRAF6 appear to facilitate the active configuration of MAP3K5/ASK1
(PubMed:9774977, PubMed:10688666, PubMed:11920685). MAP3K5/ASK1
activity is also regulated through several phosphorylation and
dephosphorylation events. Thr-838 is an activating phosphorylation site
that is autophosphorylated and phosphorylated by MAP3K6/ASK2 and
dephosphorylated by PPP5C (PubMed:11689443). Ser-83 and Ser-1033 are
inactivating phosphorylation sites, the former of which is
phosphorylated by AKT1 and AKT2 (PubMed:11154276, PubMed:12697749,
PubMed:15094778). Phosphorylation of Ser-966 induces association of
MAP3K5/ASK1 with the 14-3-3 family proteins, which suppresses
MAP3K5/ASK1 activity (PubMed:10411906, PubMed:14688258).
Calcium/calmodulin-activated protein phosphatase calcineurin (PPP3CA)
has been shown to directly dephosphorylate this site (PubMed:14749717).
SOCS1 binds to ASK1 by recognizing phosphorylation of Tyr-718 and
induces MAP3K5/ASK1 degradation in endothelial cells (PubMed:16407264).
Also dephosphorylated and activated by PGAM5. Contains an N-terminal
autoinhibitory domain. Once activated targeted for proteosomal
degradation by RC3H2-mediated ubiquitination (PubMed:24448648).
{ECO:0000269|PubMed:10411906, ECO:0000269|PubMed:10688666,
ECO:0000269|PubMed:11154276, ECO:0000269|PubMed:11689443,
ECO:0000269|PubMed:11920685, ECO:0000269|PubMed:12556535,
ECO:0000269|PubMed:12697749, ECO:0000269|PubMed:14688258,
ECO:0000269|PubMed:14749717, ECO:0000269|PubMed:15094778,
ECO:0000269|PubMed:16407264, ECO:0000269|PubMed:17210579,
ECO:0000269|PubMed:24448648, ECO:0000269|PubMed:9564042,
ECO:0000269|PubMed:9774977}.
-!- SUBUNIT: Homodimer when inactive. Binds both upstream activators and
downstream substrates in multimolecular complexes. Part of a
cytoplasmic complex made of HIPK1, DAB2IP and MAP3K5 in response to TNF
(PubMed:15310755, PubMed:15701637, PubMed:17210579, PubMed:17389591).
This complex formation promotes MAP3K5-JNK activation and subsequent
apoptosis. Interacts with SOCS1 which recognizes phosphorylation of
Tyr-718 and induces MAP3K5/ASK1 degradation in endothelial cells.
Interacts with the 14-3-3 family proteins such as YWHAB, YWHAE, YWHAQ,
YWHAH, YWHAZ and SFN (PubMed:10411906, PubMed:15023544,
PubMed:15094778). Interacts with ARRB2, BIRC2, DAB2IP, IGF1R,
MAP3K6/ASK2, PGAM5, PIM1, PPP5C, SOCS1, STUB1, TRAF2, TRAF6 and TXN
(PubMed:9564042,PubMed:9774977, PubMed:10688666, PubMed:11090355,
PubMed:11689443, PubMed:12556535, PubMed:12813029, PubMed:15310755,
PubMed:16038411, PubMed:16129676, PubMed:16407264, PubMed:17220297,
PubMed:17724081, PubMed:18408005, PubMed:19590015, PubMed:19749799).
Interacts with ERN1 in a TRAF2-dependent manner (PubMed:14749717).
Interacts with calcineurin subunit PPP3R1 and with PPM1L
(PubMed:17456047) (By similarity). Interacts (via N-terminus) with RAF1
and this interaction inhibits the proapoptotic function of MAP3K5
(PubMed:11427728). Interacts with DAB2IP (via N-terminus C2 domain);
the interaction occurs in a TNF-alpha-dependent manner
(PubMed:15310755). Interacts with DUSP13/DUSP13A; may positively
regulate apoptosis (PubMed:20358250). Interacts with DAXX
(PubMed:9743501). Interacts with RC3H2 (PubMed:24448648). {ECO:0000250,
ECO:0000269|PubMed:10411906, ECO:0000269|PubMed:10688666,
ECO:0000269|PubMed:11090355, ECO:0000269|PubMed:11427728,
ECO:0000269|PubMed:11689443, ECO:0000269|PubMed:12556535,
ECO:0000269|PubMed:12813029, ECO:0000269|PubMed:14749717,
ECO:0000269|PubMed:15023544, ECO:0000269|PubMed:15094778,
ECO:0000269|PubMed:15310755, ECO:0000269|PubMed:15701637,
ECO:0000269|PubMed:16038411, ECO:0000269|PubMed:16129676,
ECO:0000269|PubMed:16407264, ECO:0000269|PubMed:17210579,
ECO:0000269|PubMed:17220297, ECO:0000269|PubMed:17389591,
ECO:0000269|PubMed:17456047, ECO:0000269|PubMed:17724081,
ECO:0000269|PubMed:18408005, ECO:0000269|PubMed:19590015,
ECO:0000269|PubMed:19749799, ECO:0000269|PubMed:20358250,
ECO:0000269|PubMed:24448648, ECO:0000269|PubMed:9564042,
ECO:0000269|PubMed:9743501, ECO:0000269|PubMed:9774977}.
-!- SUBUNIT: (Microbial infection) Interacts with HIV-1 Nef; this
interaction inhibits MAP3K5 signaling. {ECO:0000269|PubMed:11298454}.
-!- INTERACTION:
Q99683; P31749: AKT1; NbExp=2; IntAct=EBI-476263, EBI-296087;
Q99683; P05067: APP; NbExp=2; IntAct=EBI-476263, EBI-77613;
Q99683; P49407: ARRB1; NbExp=3; IntAct=EBI-476263, EBI-743313;
Q99683; P32121: ARRB2; NbExp=2; IntAct=EBI-476263, EBI-714559;
Q99683; Q99828: CIB1; NbExp=7; IntAct=EBI-476263, EBI-372594;
Q99683; Q5VWQ8: DAB2IP; NbExp=2; IntAct=EBI-476263, EBI-2871881;
Q99683; Q9UER7: DAXX; NbExp=7; IntAct=EBI-476263, EBI-77321;
Q99683; P25445: FAS; NbExp=2; IntAct=EBI-476263, EBI-494743;
Q99683; P46734: MAP2K3; NbExp=6; IntAct=EBI-476263, EBI-602462;
Q99683; Q99683: MAP3K5; NbExp=5; IntAct=EBI-476263, EBI-476263;
Q99683; Q96EZ8: MCRS1; NbExp=3; IntAct=EBI-476263, EBI-348259;
Q99683; Q96HS1: PGAM5; NbExp=2; IntAct=EBI-476263, EBI-713608;
Q99683; P63098: PPP3R1; NbExp=2; IntAct=EBI-476263, EBI-915984;
Q99683; Q16637: SMN2; NbExp=3; IntAct=EBI-476263, EBI-395421;
Q99683; Q12933: TRAF2; NbExp=4; IntAct=EBI-476263, EBI-355744;
Q99683; P10599: TXN; NbExp=4; IntAct=EBI-476263, EBI-594644;
Q99683; P31946: YWHAB; NbExp=3; IntAct=EBI-476263, EBI-359815;
Q99683; Q04917: YWHAH; NbExp=3; IntAct=EBI-476263, EBI-306940;
Q99683; P63104: YWHAZ; NbExp=4; IntAct=EBI-476263, EBI-347088;
Q99683; Q969S3: ZNF622; NbExp=14; IntAct=EBI-476263, EBI-2687480;
Q99683; Q9WTR2: Map3k6; Xeno; NbExp=3; IntAct=EBI-476263, EBI-1254790;
Q99683; Q9D1C8: Vps28; Xeno; NbExp=5; IntAct=EBI-476263, EBI-309205;
-!- SUBCELLULAR LOCATION: Cytoplasm. Endoplasmic reticulum.
Note=Interaction with 14-3-3 proteins alters the distribution of
MAP3K5/ASK1 and restricts it to the perinuclear endoplasmic reticulum
region.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q99683-1; Sequence=Displayed;
Name=2;
IsoId=Q99683-2; Sequence=VSP_056182;
-!- TISSUE SPECIFICITY: Abundantly expressed in heart and pancreas.
-!- INDUCTION: By TNF. Inhibited by HIV-1 Nef.
-!- PTM: Phosphorylated at Thr-838 through autophosphorylation and by
MAP3K6/ASK2 which leads to activation. Thr-838 is dephosphorylated by
PPP5C. Ser-83 and Ser-1033 are inactivating phosphorylation sites, the
former of which is phosphorylated by AKT1 and AKT2. Phosphorylated at
Ser-966 which induces association of MAP3K5/ASK1 with the 14-3-3 family
proteins and suppresses MAP3K5/ASK1 activity. Calcineurin (CN)
dephosphorylates this site. Also dephosphorylated and activated by
PGAM5. {ECO:0000269|PubMed:11154276, ECO:0000269|PubMed:11920685,
ECO:0000269|PubMed:12556535, ECO:0000269|PubMed:12697749,
ECO:0000269|PubMed:14688258, ECO:0000269|PubMed:15094778,
ECO:0000269|PubMed:16407264, ECO:0000269|PubMed:17210579,
ECO:0000269|PubMed:17937911, ECO:0000269|PubMed:18948261,
ECO:0000269|PubMed:19590015, ECO:0000269|PubMed:19749799,
ECO:0000269|PubMed:23102700}.
-!- PTM: Ubiquitinated. Tumor necrosis factor (TNF) induces TNFR2-dependent
ubiquitination leading to proteasomal degradation.
{ECO:0000269|PubMed:16038411, ECO:0000269|PubMed:17220297}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
protein kinase family. MAP kinase kinase kinase subfamily.
{ECO:0000305}.
---------------------------------------------------------------------------
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EMBL; U67156; AAC50894.1; -; mRNA.
EMBL; D84476; BAA12684.2; -; mRNA.
EMBL; AK294507; BAG57723.1; -; mRNA.
EMBL; AL024508; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL121933; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC054503; AAH54503.1; -; mRNA.
EMBL; BC088829; AAH88829.1; -; mRNA.
CCDS; CCDS5179.1; -. [Q99683-1]
RefSeq; NP_005914.1; NM_005923.3. [Q99683-1]
PDB; 2CLQ; X-ray; 2.30 A; A/B=659-951.
PDB; 3VW6; X-ray; 2.40 A; A/B=671-939.
PDB; 4BF2; X-ray; 2.11 A; A/B=660-977.
PDB; 4BHN; X-ray; 2.30 A; A/B=660-977.
PDB; 4BIB; X-ray; 2.43 A; A/B=660-977.
PDB; 4BIC; X-ray; 2.62 A; A/B=660-977.
PDB; 4BID; X-ray; 2.80 A; A/B=660-977.
PDB; 4BIE; X-ray; 2.36 A; A/B=660-977.
PDB; 5ULM; X-ray; 2.10 A; A/B=269-658.
PDB; 5UOR; X-ray; 2.75 A; A/B=670-939.
PDB; 5UOX; X-ray; 2.50 A; A/B=670-940.
PDB; 5UP3; X-ray; 2.95 A; A/B=670-940.
PDB; 5V19; X-ray; 3.10 A; A/B=670-940.
PDB; 5V24; X-ray; 2.50 A; A/B=670-940.
PDB; 5VIL; X-ray; 2.64 A; A/B/C/D=659-951.
PDB; 5VIO; X-ray; 2.84 A; A/B/C/D=659-951.
PDB; 6E2M; X-ray; 2.25 A; A/B=659-951.
PDB; 6E2N; X-ray; 2.10 A; A/B=659-951.
PDB; 6E2O; X-ray; 2.39 A; A/B=659-951.
PDB; 6EJL; X-ray; 2.38 A; C/D=963-970.
PDB; 6OYT; X-ray; 2.82 A; A/B/C/D=667-939.
PDB; 6OYW; X-ray; 2.60 A; A/B/C/D=658-951.
PDB; 6VRE; X-ray; 2.29 A; A/B=661-951.
PDBsum; 2CLQ; -.
PDBsum; 3VW6; -.
PDBsum; 4BF2; -.
PDBsum; 4BHN; -.
PDBsum; 4BIB; -.
PDBsum; 4BIC; -.
PDBsum; 4BID; -.
PDBsum; 4BIE; -.
PDBsum; 5ULM; -.
PDBsum; 5UOR; -.
PDBsum; 5UOX; -.
PDBsum; 5UP3; -.
PDBsum; 5V19; -.
PDBsum; 5V24; -.
PDBsum; 5VIL; -.
PDBsum; 5VIO; -.
PDBsum; 6E2M; -.
PDBsum; 6E2N; -.
PDBsum; 6E2O; -.
PDBsum; 6EJL; -.
PDBsum; 6OYT; -.
PDBsum; 6OYW; -.
PDBsum; 6VRE; -.
SMR; Q99683; -.
BioGRID; 110381; 110.
CORUM; Q99683; -.
DIP; DIP-29516N; -.
ELM; Q99683; -.
IntAct; Q99683; 48.
MINT; Q99683; -.
STRING; 9606.ENSP00000351908; -.
BindingDB; Q99683; -.
ChEMBL; CHEMBL5285; -.
GuidetoPHARMACOLOGY; 2080; -.
CarbonylDB; Q99683; -.
iPTMnet; Q99683; -.
PhosphoSitePlus; Q99683; -.
BioMuta; MAP3K5; -.
DMDM; 6685617; -.
CPTAC; CPTAC-849; -.
CPTAC; CPTAC-850; -.
EPD; Q99683; -.
jPOST; Q99683; -.
MassIVE; Q99683; -.
MaxQB; Q99683; -.
PaxDb; Q99683; -.
PeptideAtlas; Q99683; -.
PRIDE; Q99683; -.
ProteomicsDB; 1258; -.
ProteomicsDB; 78395; -. [Q99683-1]
Antibodypedia; 3592; 1498 antibodies.
DNASU; 4217; -.
Ensembl; ENST00000359015; ENSP00000351908; ENSG00000197442. [Q99683-1]
GeneID; 4217; -.
KEGG; hsa:4217; -.
UCSC; uc003qhc.4; human. [Q99683-1]
CTD; 4217; -.
DisGeNET; 4217; -.
EuPathDB; HostDB:ENSG00000197442.9; -.
GeneCards; MAP3K5; -.
HGNC; HGNC:6857; MAP3K5.
HPA; ENSG00000197442; Tissue enhanced (adrenal).
MIM; 602448; gene.
neXtProt; NX_Q99683; -.
OpenTargets; ENSG00000197442; -.
PharmGKB; PA30601; -.
eggNOG; KOG4279; Eukaryota.
GeneTree; ENSGT00940000159155; -.
HOGENOM; CLU_003687_1_0_1; -.
InParanoid; Q99683; -.
KO; K04426; -.
OMA; YHYGVRE; -.
OrthoDB; 226722at2759; -.
PhylomeDB; Q99683; -.
TreeFam; TF105115; -.
BRENDA; 2.7.12.2; 2681.
PathwayCommons; Q99683; -.
Reactome; R-HSA-2559580; Oxidative Stress Induced Senescence.
SignaLink; Q99683; -.
SIGNOR; Q99683; -.
BioGRID-ORCS; 4217; 5 hits in 901 CRISPR screens.
ChiTaRS; MAP3K5; human.
EvolutionaryTrace; Q99683; -.
GeneWiki; ASK1; -.
GenomeRNAi; 4217; -.
Pharos; Q99683; Tchem.
PRO; PR:Q99683; -.
Proteomes; UP000005640; Chromosome 6.
RNAct; Q99683; protein.
Bgee; ENSG00000197442; Expressed in primary visual cortex and 235 other tissues.
Genevisible; Q99683; HS.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
GO; GO:1990604; C:IRE1-TRAF2-ASK1 complex; IDA:ParkinsonsUK-UCL.
GO; GO:1902911; C:protein kinase complex; IDA:ParkinsonsUK-UCL.
GO; GO:0032991; C:protein-containing complex; IMP:CAFA.
GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
GO; GO:0004709; F:MAP kinase kinase kinase activity; IDA:UniProtKB.
GO; GO:0019904; F:protein domain specific binding; IPI:CAFA.
GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
GO; GO:0004672; F:protein kinase activity; IDA:UniProtKB.
GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
GO; GO:0019903; F:protein phosphatase binding; IPI:BHF-UCL.
GO; GO:0004674; F:protein serine/threonine kinase activity; TAS:Reactome.
GO; GO:0007257; P:activation of JUN kinase activity; TAS:ProtInc.
GO; GO:0000186; P:activation of MAPKK activity; IDA:BHF-UCL.
GO; GO:0097190; P:apoptotic signaling pathway; TAS:ProtInc.
GO; GO:0034198; P:cellular response to amino acid starvation; IDA:CAFA.
GO; GO:0070301; P:cellular response to hydrogen peroxide; IDA:BHF-UCL.
GO; GO:1902170; P:cellular response to reactive nitrogen species; IEA:Ensembl.
GO; GO:0071356; P:cellular response to tumor necrosis factor; IEA:Ensembl.
GO; GO:0072577; P:endothelial cell apoptotic process; IEA:Ensembl.
GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
GO; GO:0070059; P:intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress; ISS:ParkinsonsUK-UCL.
GO; GO:0008631; P:intrinsic apoptotic signaling pathway in response to oxidative stress; IDA:UniProtKB.
GO; GO:0007254; P:JNK cascade; IDA:UniProtKB.
GO; GO:0000165; P:MAPK cascade; IDA:UniProtKB.
GO; GO:0038066; P:p38MAPK cascade; IEA:Ensembl.
GO; GO:0043065; P:positive regulation of apoptotic process; IDA:UniProtKB.
GO; GO:0010666; P:positive regulation of cardiac muscle cell apoptotic process; IEA:Ensembl.
GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:BHF-UCL.
GO; GO:0046330; P:positive regulation of JNK cascade; ISS:ParkinsonsUK-UCL.
GO; GO:0043507; P:positive regulation of JUN kinase activity; IMP:ParkinsonsUK-UCL.
GO; GO:0045663; P:positive regulation of myoblast differentiation; IEA:Ensembl.
GO; GO:1901216; P:positive regulation of neuron death; IGI:ParkinsonsUK-UCL.
GO; GO:1900745; P:positive regulation of p38MAPK cascade; IEA:Ensembl.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:CAFA.
GO; GO:1904707; P:positive regulation of vascular smooth muscle cell proliferation; IEA:Ensembl.
GO; GO:0097300; P:programmed necrotic cell death; IEA:Ensembl.
GO; GO:0006468; P:protein phosphorylation; IDA:CAFA.
GO; GO:0034976; P:response to endoplasmic reticulum stress; IMP:ParkinsonsUK-UCL.
GO; GO:0002931; P:response to ischemia; IEA:Ensembl.
GO; GO:0051403; P:stress-activated MAPK cascade; IDA:CAFA.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
GO; GO:0042060; P:wound healing; IEA:Ensembl.
InterPro; IPR025136; DUF4071.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR013761; SAM/pointed_sf.
InterPro; IPR008271; Ser/Thr_kinase_AS.
Pfam; PF13281; DUF4071; 1.
Pfam; PF00069; Pkinase; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF47769; SSF47769; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Apoptosis; ATP-binding; Coiled coil;
Cytoplasm; Endoplasmic reticulum; Host-virus interaction; Immunity;
Innate immunity; Kinase; Magnesium; Metal-binding; Nucleotide-binding;
Phosphoprotein; Polymorphism; Reference proteome;
Serine/threonine-protein kinase; Stress response; Transferase;
Ubl conjugation.
CHAIN 1..1374
/note="Mitogen-activated protein kinase kinase kinase 5"
/id="PRO_0000086249"
DOMAIN 680..938
/note="Protein kinase"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
NP_BIND 686..694
/note="ATP"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
COILED 1245..1285
/evidence="ECO:0000255"
ACT_SITE 803
/note="Proton acceptor"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
ECO:0000255|PROSITE-ProRule:PRU10027"
BINDING 709
/note="ATP"
MOD_RES 83
/note="Phosphoserine; by PIM1, PKB/AKT1 and PKB/AKT2"
/evidence="ECO:0000269|PubMed:11154276,
ECO:0000269|PubMed:12697749, ECO:0000269|PubMed:19749799"
MOD_RES 718
/note="Phosphotyrosine"
/evidence="ECO:0000269|PubMed:16407264"
MOD_RES 813
/note="Phosphothreonine; by autocatalysis"
/evidence="ECO:0000269|PubMed:17937911"
MOD_RES 838
/note="Phosphothreonine; by autocatalysis, MELK and MAP3K6"
/evidence="ECO:0000269|PubMed:11920685,
ECO:0000269|PubMed:17210579, ECO:0000269|PubMed:17937911,
ECO:0000269|PubMed:18948261, ECO:0000269|PubMed:19590015,
ECO:0000269|PubMed:23102700"
MOD_RES 842
/note="Phosphothreonine; by autocatalysis"
/evidence="ECO:0000269|PubMed:17937911"
MOD_RES 958
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:23186163"
MOD_RES 966
/note="Phosphoserine"
/evidence="ECO:0000269|PubMed:14688258,
ECO:0000269|PubMed:15094778, ECO:0000269|PubMed:19590015"
MOD_RES 1029
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:18088087,
ECO:0000244|PubMed:18669648"
MOD_RES 1033
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:18088087,
ECO:0000244|PubMed:18669648, ECO:0000244|PubMed:19369195,
ECO:0000269|PubMed:15094778, ECO:0000269|PubMed:19590015"
VAR_SEQ 1..753
/note="Missing (in isoform 2)"
/evidence="ECO:0000303|PubMed:14702039"
/id="VSP_056182"
VARIANT 1006
/note="G -> R (in dbSNP:rs45626535)"
/evidence="ECO:0000269|PubMed:17344846"
/id="VAR_040693"
VARIANT 1214
/note="I -> T (in dbSNP:rs56379668)"
/evidence="ECO:0000269|PubMed:17344846"
/id="VAR_040694"
VARIANT 1250
/note="I -> V (in dbSNP:rs35551087)"
/evidence="ECO:0000269|PubMed:17344846"
/id="VAR_040695"
VARIANT 1314
/note="T -> I (in dbSNP:rs45599539)"
/evidence="ECO:0000269|PubMed:17344846"
/id="VAR_040696"
VARIANT 1315
/note="D -> N (in dbSNP:rs41288957)"
/evidence="ECO:0000269|PubMed:17344846"
/id="VAR_040697"
MUTAGEN 709
/note="K->M: Loss of kinase activity. Inhibits activation
of JNK and apoptosis mediated by TNFRSF6 and DAXX."
/evidence="ECO:0000269|PubMed:17210579,
ECO:0000269|PubMed:9743501"
MUTAGEN 709
/note="K->R: Loss of kinase activity. Abolishes DAXX-
mediated apoptosis. Loss of RC3H2-mediated ubiquitination."
/evidence="ECO:0000269|PubMed:17210579,
ECO:0000269|PubMed:24448648, ECO:0000269|PubMed:9743501"
MUTAGEN 966
/note="S->A: Enhanced induction of apoptosis, increased
kinase activity, and loss of YWHAG binding."
/evidence="ECO:0000269|PubMed:10411906,
ECO:0000269|PubMed:15094778"
MUTAGEN 1033
/note="S->A: Enhanced induction of apoptosis and increased
kinase activity."
/evidence="ECO:0000269|PubMed:15094778"
HELIX 273..286
/evidence="ECO:0000244|PDB:5ULM"
HELIX 289..303
/evidence="ECO:0000244|PDB:5ULM"
HELIX 311..323
/evidence="ECO:0000244|PDB:5ULM"
HELIX 327..339
/evidence="ECO:0000244|PDB:5ULM"
HELIX 345..347
/evidence="ECO:0000244|PDB:5ULM"
HELIX 349..362
/evidence="ECO:0000244|PDB:5ULM"
HELIX 367..379
/evidence="ECO:0000244|PDB:5ULM"
HELIX 387..403
/evidence="ECO:0000244|PDB:5ULM"
TURN 404..406
/evidence="ECO:0000244|PDB:5ULM"
HELIX 409..425
/evidence="ECO:0000244|PDB:5ULM"
HELIX 429..441
/evidence="ECO:0000244|PDB:5ULM"
HELIX 452..466
/evidence="ECO:0000244|PDB:5ULM"
HELIX 469..471
/evidence="ECO:0000244|PDB:5ULM"
HELIX 475..487
/evidence="ECO:0000244|PDB:5ULM"
HELIX 491..503
/evidence="ECO:0000244|PDB:5ULM"
HELIX 508..524
/evidence="ECO:0000244|PDB:5ULM"
HELIX 536..548
/evidence="ECO:0000244|PDB:5ULM"
STRAND 557..564
/evidence="ECO:0000244|PDB:5ULM"
STRAND 570..578
/evidence="ECO:0000244|PDB:5ULM"
STRAND 581..583
/evidence="ECO:0000244|PDB:5ULM"
STRAND 585..592
/evidence="ECO:0000244|PDB:5ULM"
STRAND 601..605
/evidence="ECO:0000244|PDB:5ULM"
HELIX 606..608
/evidence="ECO:0000244|PDB:5ULM"
STRAND 609..614
/evidence="ECO:0000244|PDB:5ULM"
STRAND 621..626
/evidence="ECO:0000244|PDB:5ULM"
STRAND 633..636
/evidence="ECO:0000244|PDB:5ULM"
HELIX 640..654
/evidence="ECO:0000244|PDB:5ULM"
STRAND 673..675
/evidence="ECO:0000244|PDB:6E2N"
STRAND 681..683
/evidence="ECO:0000244|PDB:2CLQ"
STRAND 685..688
/evidence="ECO:0000244|PDB:6E2N"
STRAND 690..699
/evidence="ECO:0000244|PDB:6E2N"
TURN 700..702
/evidence="ECO:0000244|PDB:6E2N"
STRAND 705..712
/evidence="ECO:0000244|PDB:6E2N"
TURN 716..718
/evidence="ECO:0000244|PDB:5UOX"
HELIX 719..729
/evidence="ECO:0000244|PDB:6E2N"
STRAND 740..746
/evidence="ECO:0000244|PDB:6E2N"
STRAND 749..755
/evidence="ECO:0000244|PDB:6E2N"
STRAND 758..761
/evidence="ECO:0000244|PDB:4BF2"
HELIX 762..768
/evidence="ECO:0000244|PDB:6E2N"
TURN 774..776
/evidence="ECO:0000244|PDB:5V19"
HELIX 777..796
/evidence="ECO:0000244|PDB:6E2N"
HELIX 806..808
/evidence="ECO:0000244|PDB:6E2N"
STRAND 809..811
/evidence="ECO:0000244|PDB:6E2N"
TURN 813..815
/evidence="ECO:0000244|PDB:6E2N"
STRAND 818..820
/evidence="ECO:0000244|PDB:6E2N"
TURN 823..825
/evidence="ECO:0000244|PDB:2CLQ"
STRAND 827..829
/evidence="ECO:0000244|PDB:2CLQ"
STRAND 832..835
/evidence="ECO:0000244|PDB:5VIL"
HELIX 843..845
/evidence="ECO:0000244|PDB:6E2N"
HELIX 848..851
/evidence="ECO:0000244|PDB:6E2N"
HELIX 854..857
/evidence="ECO:0000244|PDB:4BF2"
HELIX 861..876
/evidence="ECO:0000244|PDB:6E2N"
HELIX 882..884
/evidence="ECO:0000244|PDB:6E2N"
HELIX 887..897
/evidence="ECO:0000244|PDB:6E2N"
HELIX 909..918
/evidence="ECO:0000244|PDB:6E2N"
TURN 923..925
/evidence="ECO:0000244|PDB:6E2N"
HELIX 929..933
/evidence="ECO:0000244|PDB:6E2N"
HELIX 936..938
/evidence="ECO:0000244|PDB:4BF2"
SEQUENCE 1374 AA; 154537 MW; 265BDC65968AF985 CRC64;
MSTEADEGIT FSVPPFAPSG FCTIPEGGIC RRGGAAAVGE GEEHQLPPPP PGSFWNVESA
AAPGIGCPAA TSSSSATRGR GSSVGGGSRR TTVAYVINEA SQGQLVVAES EALQSLREAC
ETVGATLETL HFGKLDFGET TVLDRFYNAD IAVVEMSDAF RQPSLFYHLG VRESFSMANN
IILYCDTNSD SLQSLKEIIC QKNTMCTGNY TFVPYMITPH NKVYCCDSSF MKGLTELMQP
NFELLLGPIC LPLVDRFIQL LKVAQASSSQ YFRESILNDI RKARNLYTGK ELAAELARIR
QRVDNIEVLT ADIVINLLLS YRDIQDYDSI VKLVETLEKL PTFDLASHHH VKFHYAFALN
RRNLPGDRAK ALDIMIPMVQ SEGQVASDMY CLVGRIYKDM FLDSNFTDTE SRDHGASWFK
KAFESEPTLQ SGINYAVLLL AAGHQFESSF ELRKVGVKLS SLLGKKGNLE KLQSYWEVGF
FLGASVLAND HMRVIQASEK LFKLKTPAWY LKSIVETILI YKHFVKLTTE QPVAKQELVD
FWMDFLVEAT KTDVTVVRFP VLILEPTKIY QPSYLSINNE VEEKTISIWH VLPDDKKGIH
EWNFSASSVR GVSISKFEER CCFLYVLHNS DDFQIYFCTE LHCKKFFEMV NTITEEKGRS
TEEGDCESDL LEYDYEYDEN GDRVVLGKGT YGIVYAGRDL SNQVRIAIKE IPERDSRYSQ
PLHEEIALHK HLKHKNIVQY LGSFSENGFI KIFMEQVPGG SLSALLRSKW GPLKDNEQTI
GFYTKQILEG LKYLHDNQIV HRDIKGDNVL INTYSGVLKI SDFGTSKRLA GINPCTETFT
GTLQYMAPEI IDKGPRGYGK AADIWSLGCT IIEMATGKPP FYELGEPQAA MFKVGMFKVH
PEIPESMSAE AKAFILKCFE PDPDKRACAN DLLVDEFLKV SSKKKKTQPK LSALSAGSNE
YLRSISLPVP VLVEDTSSSS EYGSVSPDTE LKVDPFSFKT RAKSCGERDV KGIRTLFLGI
PDENFEDHSA PPSPEEKDSG FFMLRKDSER RATLHRILTE DQDKIVRNLM ESLAQGAEEP
KLKWEHITTL IASLREFVRS TDRKIIATTL SKLKLELDFD SHGISQVQVV LFGFQDAVNK
VLRNHNIKPH WMFALDSIIR KAVQTAITIL VPELRPHFSL ASESDTADQE DLDVEDDHEE
QPSNQTVRRP QAVIEDAVAT SGVSTLSSTV SHDSQSAHRS LNVQLGRMKI ETNRLLEELV
RKEKELQALL HRAIEEKDQE IKHLKLKSQP IEIPELPVFH LNSSGTNTED SELTDWLRVN
GADEDTISRF LAEDYTLLDV LYYVTRDDLK CLRLRGGMLC TLWKAIIDFR NKQT


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Pathways :
WP1493: Carbon assimilation C4 pathway
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WP1653: Galactose metabolism
WP253: Glycolysis
WP1703: Streptomycin biosynthesis
WP32: Translation Factors
WP1701: Starch and sucrose metabolism
WP1567: Glycolysis and Gluconeogenesis
WP2341: vitamin B1 (thiamin) biosynthesis and salvage pathway
WP1619: Amino sugar and nucleotide sugar metabolism
WP2152: BDNF
WP402: ERK1 - ERK2 MAPK cascade
WP1909: Signal regulatory protein (SIRP) family interactions
WP2292: Chemokine signaling pathway
WP2272: Pathogenic Escherichia coli infection
WP1965: VEGF-receptor Signal Transduction
WP1644: DNA replication
WP2435: Quercetin and Nf-kB/ AP-1 induced cell apoptosis
WP799: NLR proteins
WP1009: MAPK Cascade
WP1391: Signal Transduction of S1P
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Related Genes :
[MAP3K5 ASK1 MAPKKK5 MEKK5] Mitogen-activated protein kinase kinase kinase 5 (EC 2.7.11.25) (Apoptosis signal-regulating kinase 1) (ASK-1) (MAPK/ERK kinase kinase 5) (MEK kinase 5) (MEKK 5)
[Map3k5 Ask1 Mekk5] Mitogen-activated protein kinase kinase kinase 5 (EC 2.7.11.25) (Apoptosis signal-regulating kinase 1) (ASK-1) (MAPK/ERK kinase kinase 5) (MEK kinase 5) (MEKK 5)
[Map3k1 Mekk Mekk1] Mitogen-activated protein kinase kinase kinase 1 (EC 2.7.11.25) (MAPK/ERK kinase kinase 1) (MEK kinase 1) (MEKK 1)
[MAP3K1 MAPKKK1 MEKK MEKK1] Mitogen-activated protein kinase kinase kinase 1 (EC 2.7.11.25) (MAPK/ERK kinase kinase 1) (MEK kinase 1) (MEKK 1)
[Map3k1 Mekk Mekk1] Mitogen-activated protein kinase kinase kinase 1 (EC 2.7.11.25) (MAPK/ERK kinase kinase 1) (MEK kinase 1) (MEKK 1)
[Map3k2 Mekk2] Mitogen-activated protein kinase kinase kinase 2 (EC 2.7.11.25) (MAPK/ERK kinase kinase 2) (MEK kinase 2) (MEKK 2)
[mkkA DDB_G0283265] Mitogen-activated protein kinase kinase kinase A (EC 2.7.11.25) (MAPK/ERK kinase 1) (MEK kinase 1) (MEKK 1) (MAPK/ERK kinase A) (MEK kinase A) (MEKK A) (MEKKalpha)
[MAP3K6 ASK2 MAPKKK6 MEKK6] Mitogen-activated protein kinase kinase kinase 6 (EC 2.7.11.25) (Apoptosis signal-regulating kinase 2)
[Map3k6 Ask2 Mapkkk6 Mekk6] Mitogen-activated protein kinase kinase kinase 6 (EC 2.7.11.25) (Apoptosis signal-regulating kinase 2)
[MAP2K1 MEK1 PRKMK1] Dual specificity mitogen-activated protein kinase kinase 1 (MAP kinase kinase 1) (MAPKK 1) (MKK1) (EC 2.7.12.2) (ERK activator kinase 1) (MAPK/ERK kinase 1) (MEK 1)
[MAPK1 ERK2 PRKM1 PRKM2] Mitogen-activated protein kinase 1 (MAP kinase 1) (MAPK 1) (EC 2.7.11.24) (ERT1) (Extracellular signal-regulated kinase 2) (ERK-2) (MAP kinase isoform p42) (p42-MAPK) (Mitogen-activated protein kinase 2) (MAP kinase 2) (MAPK 2)
[Mapk1 Erk2 Mapk Prkm1] Mitogen-activated protein kinase 1 (MAP kinase 1) (MAPK 1) (EC 2.7.11.24) (ERT1) (Extracellular signal-regulated kinase 2) (ERK-2) (MAP kinase isoform p42) (p42-MAPK) (Mitogen-activated protein kinase 2) (MAP kinase 2) (MAPK 2)
[Map2k1 Mek1 Prkmk1] Dual specificity mitogen-activated protein kinase kinase 1 (MAP kinase kinase 1) (MAPKK 1) (EC 2.7.12.2) (ERK activator kinase 1) (MAPK/ERK kinase 1) (MEK 1)
[Map2k1 Mek1 Prkmk1] Dual specificity mitogen-activated protein kinase kinase 1 (MAP kinase kinase 1) (MAPKK 1) (EC 2.7.12.2) (ERK activator kinase 1) (MAPK/ERK kinase 1) (MEK 1)
[MAPK7 BMK1 ERK5 PRKM7] Mitogen-activated protein kinase 7 (MAP kinase 7) (MAPK 7) (EC 2.7.11.24) (Big MAP kinase 1) (BMK-1) (Extracellular signal-regulated kinase 5) (ERK-5)
[MAP2K1 MEK1 PRKMK1] Dual specificity mitogen-activated protein kinase kinase 1 (MAP kinase kinase 1) (MAPKK 1) (EC 2.7.12.2) (ERK activator kinase 1) (MAPK/ERK kinase 1) (MEK 1)
[Mapk7 Bmk1 Erk5] Mitogen-activated protein kinase 7 (MAP kinase 7) (MAPK 7) (EC 2.7.11.24) (Big MAP kinase 1) (BMK-1) (Extracellular signal-regulated kinase 5) (ERK-5)
[Map2k5 Mek5 Mkk5 Prkmk5] Dual specificity mitogen-activated protein kinase kinase 5 (MAP kinase kinase 5) (MAPKK 5) (EC 2.7.12.2) (MAPK/ERK kinase 5) (MEK 5)
[MAP2K1 MEK1 PRKMK1] Dual specificity mitogen-activated protein kinase kinase 1 (MAP kinase kinase 1) (MAPKK 1) (EC 2.7.12.2) (ERK activator kinase 1) (MAPK/ERK kinase 1) (MEK 1)
[Mapk7 Bmk1 Erk5] Mitogen-activated protein kinase 7 (MAP kinase 7) (MAPK 7) (EC 2.7.11.24) (Big MAP kinase 1) (BMK-1) (Extracellular signal-regulated kinase 5) (ERK-5)
[MAPK3 ERK1 PRKM3] Mitogen-activated protein kinase 3 (MAP kinase 3) (MAPK 3) (EC 2.7.11.24) (ERT2) (Extracellular signal-regulated kinase 1) (ERK-1) (Insulin-stimulated MAP2 kinase) (MAP kinase isoform p44) (p44-MAPK) (Microtubule-associated protein 2 kinase) (p44-ERK1)
[nsy-1 F59A6.1] Mitogen-activated protein kinase kinase kinase nsy-1 (EC 2.7.11.25) (Apoptosis signal-regulating kinase 1) (ASK-1) (Neuronal symmetry kinase 1)
[MAP2K6 MEK6 MKK6 PRKMK6 SKK3] Dual specificity mitogen-activated protein kinase kinase 6 (MAP kinase kinase 6) (MAPKK 6) (EC 2.7.12.2) (MAPK/ERK kinase 6) (MEK 6) (Stress-activated protein kinase kinase 3) (SAPK kinase 3) (SAPKK-3) (SAPKK3)
[Map2k5 Mek5 Mkk5 Prkmk5] Dual specificity mitogen-activated protein kinase kinase 5 (MAP kinase kinase 5) (MAPKK 5) (EC 2.7.12.2) (MAPK/ERK kinase 5) (MEK 5)
[Mapk1 Erk2 Mapk Prkm1] Mitogen-activated protein kinase 1 (MAP kinase 1) (MAPK 1) (EC 2.7.11.24) (ERT1) (Extracellular signal-regulated kinase 2) (ERK-2) (MAP kinase isoform p42) (p42-MAPK) (Mitogen-activated protein kinase 2) (MAP kinase 2) (MAPK 2)
[MAP2K1 MEK1 PRKMK1] Dual specificity mitogen-activated protein kinase kinase 1 (MAP kinase kinase 1) (MAPKK 1) (EC 2.7.12.2) (ERK activator kinase 1) (MAPK/ERK kinase 1) (MEK 1)
[MAP2K5 MEK5 MKK5 PRKMK5] Dual specificity mitogen-activated protein kinase kinase 5 (MAP kinase kinase 5) (MAPKK 5) (EC 2.7.12.2) (MAPK/ERK kinase 5) (MEK 5)
[MAPK1 ERK2 PRKM1] Mitogen-activated protein kinase 1 (MAP kinase 1) (MAPK 1) (EC 2.7.11.24) (ERT1) (Extracellular signal-regulated kinase 2) (ERK-2) (Mitogen-activated protein kinase 2) (MAP kinase 2) (MAPK 2)
[Mapk3 Erk1 Prkm3] Mitogen-activated protein kinase 3 (MAP kinase 3) (MAPK 3) (EC 2.7.11.24) (ERT2) (Extracellular signal-regulated kinase 1) (ERK-1) (Insulin-stimulated MAP2 kinase) (MAP kinase isoform p44) (p44-MAPK) (MNK1) (Microtubule-associated protein 2 kinase) (p44-ERK1)
[Mapk3 Erk1 Prkm3] Mitogen-activated protein kinase 3 (MAP kinase 3) (MAPK 3) (EC 2.7.11.24) (ERT2) (Extracellular signal-regulated kinase 1) (ERK-1) (Insulin-stimulated MAP2 kinase) (MAP kinase isoform p44) (p44-MAPK) (MNK1) (Microtubule-associated protein 2 kinase) (p44-ERK1)

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