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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.
22-NOV-2017, entry version 189.
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, ENZYME 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]
ENZYME 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, ENZYME 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, ENZYME 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, ENZYME 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, ENZYME 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, AND INHIBITION BY HIV-1 NEF.
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, ENZYME 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, ENZYME 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, ENZYME 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, ENZYME 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, ENZYME 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]
ENZYME 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 ENZYME
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]
ENZYME 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 ENZYME 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 ENZYME 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: ATP + a protein = ADP + a phosphoprotein.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
-!- ENZYME 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. Associates
with and inhibited by HIV-1 Nef (PubMed:11298454). 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:11298454,
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}.
-!- INTERACTION:
Self; NbExp=5; IntAct=EBI-476263, EBI-476263;
P31749:AKT1; NbExp=2; IntAct=EBI-476263, EBI-296087;
P05067:APP; NbExp=2; IntAct=EBI-476263, EBI-77613;
P49407:ARRB1; NbExp=3; IntAct=EBI-476263, EBI-743313;
P32121:ARRB2; NbExp=2; IntAct=EBI-476263, EBI-714559;
Q99828:CIB1; NbExp=7; IntAct=EBI-476263, EBI-372594;
Q5VWQ8:DAB2IP; NbExp=2; IntAct=EBI-476263, EBI-2871881;
Q9UER7:DAXX; NbExp=7; IntAct=EBI-476263, EBI-77321;
P25445:FAS; NbExp=2; IntAct=EBI-476263, EBI-494743;
P46734:MAP2K3; NbExp=4; IntAct=EBI-476263, EBI-602462;
Q9WTR2:Map3k6 (xeno); NbExp=3; IntAct=EBI-476263, EBI-1254790;
Q96EZ8:MCRS1; NbExp=3; IntAct=EBI-476263, EBI-348259;
Q96HS1:PGAM5; NbExp=2; IntAct=EBI-476263, EBI-713608;
P63098:PPP3R1; NbExp=2; IntAct=EBI-476263, EBI-915984;
Q16637:SMN2; NbExp=3; IntAct=EBI-476263, EBI-395421;
Q12933:TRAF2; NbExp=4; IntAct=EBI-476263, EBI-355744;
P10599:TXN; NbExp=4; IntAct=EBI-476263, EBI-594644;
P31946:YWHAB; NbExp=3; IntAct=EBI-476263, EBI-359815;
P63104:YWHAZ; NbExp=4; IntAct=EBI-476263, EBI-347088;
Q969S3:ZNF622; NbExp=14; IntAct=EBI-476263, EBI-2687480;
-!- 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;
Note=No experimental confirmation available.;
-!- 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; CAI20176.1; -; Genomic_DNA.
EMBL; AL121933; CAI20176.1; JOINED; Genomic_DNA.
EMBL; AL121933; CAI15470.1; -; Genomic_DNA.
EMBL; AL024508; CAI15470.1; JOINED; 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]
UniGene; Hs.186486; -.
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.
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; -.
ProteinModelPortal; Q99683; -.
SMR; Q99683; -.
BioGrid; 110381; 83.
CORUM; Q99683; -.
DIP; DIP-29516N; -.
ELM; Q99683; -.
IntAct; Q99683; 42.
MINT; MINT-99796; -.
STRING; 9606.ENSP00000351908; -.
BindingDB; Q99683; -.
ChEMBL; CHEMBL5285; -.
GuidetoPHARMACOLOGY; 2080; -.
iPTMnet; Q99683; -.
PhosphoSitePlus; Q99683; -.
BioMuta; MAP3K5; -.
DMDM; 6685617; -.
EPD; Q99683; -.
MaxQB; Q99683; -.
PaxDb; Q99683; -.
PeptideAtlas; Q99683; -.
PRIDE; Q99683; -.
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; CAB007824; -.
HPA; HPA063245; -.
HPA; HPA064423; -.
MIM; 602448; gene.
neXtProt; NX_Q99683; -.
OpenTargets; ENSG00000197442; -.
PharmGKB; PA30601; -.
eggNOG; KOG4279; Eukaryota.
eggNOG; ENOG410XQGS; LUCA.
GeneTree; ENSGT00900000140948; -.
HOGENOM; HOG000293286; -.
HOVERGEN; HBG006305; -.
InParanoid; Q99683; -.
KO; K04426; -.
OMA; TELHCKK; -.
OrthoDB; EOG091G00SJ; -.
PhylomeDB; Q99683; -.
TreeFam; TF105115; -.
BRENDA; 2.7.12.2; 2681.
Reactome; R-HSA-2559580; Oxidative Stress Induced Senescence.
SignaLink; Q99683; -.
SIGNOR; Q99683; -.
ChiTaRS; MAP3K5; human.
EvolutionaryTrace; Q99683; -.
GeneWiki; ASK1; -.
GenomeRNAi; 4217; -.
PRO; PR:Q99683; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000197442; -.
CleanEx; HS_MAP3K5; -.
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:0043234; C:protein complex; IMP:CAFA.
GO; GO:1902911; C:protein kinase complex; IDA:ParkinsonsUK-UCL.
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; Complete proteome; 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 Mitogen-activated protein kinase kinase
kinase 5.
/FTId=PRO_0000086249.
DOMAIN 680 938 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 686 694 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
COILED 1245 1285 {ECO:0000255}.
ACT_SITE 803 803 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 709 709 ATP.
MOD_RES 83 83 Phosphoserine; by PIM1, PKB/AKT1 and
PKB/AKT2. {ECO:0000269|PubMed:11154276,
ECO:0000269|PubMed:12697749,
ECO:0000269|PubMed:19749799}.
MOD_RES 718 718 Phosphotyrosine.
{ECO:0000269|PubMed:16407264}.
MOD_RES 813 813 Phosphothreonine; by autocatalysis.
{ECO:0000269|PubMed:17937911}.
MOD_RES 838 838 Phosphothreonine; by autocatalysis, MELK
and MAP3K6. {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 842 842 Phosphothreonine; by autocatalysis.
{ECO:0000269|PubMed:17937911}.
MOD_RES 958 958 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 966 966 Phosphoserine.
{ECO:0000269|PubMed:14688258,
ECO:0000269|PubMed:15094778,
ECO:0000269|PubMed:19590015}.
MOD_RES 1029 1029 Phosphoserine.
{ECO:0000244|PubMed:18088087,
ECO:0000244|PubMed:18669648}.
MOD_RES 1033 1033 Phosphoserine.
{ECO:0000244|PubMed:18088087,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19369195,
ECO:0000269|PubMed:15094778,
ECO:0000269|PubMed:19590015}.
VAR_SEQ 1 753 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_056182.
VARIANT 1006 1006 G -> R (in dbSNP:rs45626535).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_040693.
VARIANT 1214 1214 I -> T (in dbSNP:rs56379668).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_040694.
VARIANT 1250 1250 I -> V (in dbSNP:rs35551087).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_040695.
VARIANT 1314 1314 T -> I (in dbSNP:rs45599539).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_040696.
VARIANT 1315 1315 D -> N (in dbSNP:rs41288957).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_040697.
MUTAGEN 709 709 K->M: Loss of kinase activity. Inhibits
activation of JNK and apoptosis mediated
by TNFRSF6 and DAXX.
{ECO:0000269|PubMed:17210579,
ECO:0000269|PubMed:9743501}.
MUTAGEN 709 709 K->R: Loss of kinase activity. Abolishes
DAXX-mediated apoptosis. Loss of RC3H2-
mediated ubiquitination.
{ECO:0000269|PubMed:17210579,
ECO:0000269|PubMed:24448648,
ECO:0000269|PubMed:9743501}.
MUTAGEN 966 966 S->A: Enhanced induction of apoptosis,
increased kinase activity, and loss of
YWHAG binding.
{ECO:0000269|PubMed:10411906,
ECO:0000269|PubMed:15094778}.
MUTAGEN 1033 1033 S->A: Enhanced induction of apoptosis and
increased kinase activity.
{ECO:0000269|PubMed:15094778}.
HELIX 273 286 {ECO:0000244|PDB:5ULM}.
HELIX 289 303 {ECO:0000244|PDB:5ULM}.
HELIX 311 323 {ECO:0000244|PDB:5ULM}.
HELIX 327 339 {ECO:0000244|PDB:5ULM}.
HELIX 345 347 {ECO:0000244|PDB:5ULM}.
HELIX 349 362 {ECO:0000244|PDB:5ULM}.
HELIX 367 379 {ECO:0000244|PDB:5ULM}.
HELIX 387 403 {ECO:0000244|PDB:5ULM}.
TURN 404 406 {ECO:0000244|PDB:5ULM}.
HELIX 409 425 {ECO:0000244|PDB:5ULM}.
HELIX 429 441 {ECO:0000244|PDB:5ULM}.
HELIX 452 466 {ECO:0000244|PDB:5ULM}.
HELIX 469 471 {ECO:0000244|PDB:5ULM}.
HELIX 475 487 {ECO:0000244|PDB:5ULM}.
HELIX 491 503 {ECO:0000244|PDB:5ULM}.
HELIX 508 524 {ECO:0000244|PDB:5ULM}.
HELIX 536 548 {ECO:0000244|PDB:5ULM}.
STRAND 557 564 {ECO:0000244|PDB:5ULM}.
STRAND 570 578 {ECO:0000244|PDB:5ULM}.
STRAND 581 583 {ECO:0000244|PDB:5ULM}.
STRAND 585 592 {ECO:0000244|PDB:5ULM}.
STRAND 601 605 {ECO:0000244|PDB:5ULM}.
HELIX 606 608 {ECO:0000244|PDB:5ULM}.
STRAND 609 614 {ECO:0000244|PDB:5ULM}.
STRAND 621 626 {ECO:0000244|PDB:5ULM}.
STRAND 633 636 {ECO:0000244|PDB:5ULM}.
HELIX 640 654 {ECO:0000244|PDB:5ULM}.
STRAND 673 675 {ECO:0000244|PDB:4BF2}.
STRAND 681 683 {ECO:0000244|PDB:2CLQ}.
STRAND 685 688 {ECO:0000244|PDB:4BF2}.
STRAND 693 699 {ECO:0000244|PDB:4BF2}.
TURN 700 702 {ECO:0000244|PDB:4BF2}.
STRAND 705 712 {ECO:0000244|PDB:4BF2}.
TURN 716 718 {ECO:0000244|PDB:5UOX}.
HELIX 725 729 {ECO:0000244|PDB:4BF2}.
STRAND 740 746 {ECO:0000244|PDB:4BF2}.
STRAND 749 755 {ECO:0000244|PDB:4BF2}.
STRAND 758 761 {ECO:0000244|PDB:4BF2}.
HELIX 762 768 {ECO:0000244|PDB:4BF2}.
TURN 774 776 {ECO:0000244|PDB:5V19}.
HELIX 777 796 {ECO:0000244|PDB:4BF2}.
HELIX 806 808 {ECO:0000244|PDB:4BF2}.
STRAND 809 812 {ECO:0000244|PDB:4BF2}.
TURN 813 815 {ECO:0000244|PDB:4BF2}.
STRAND 818 820 {ECO:0000244|PDB:4BF2}.
TURN 823 825 {ECO:0000244|PDB:2CLQ}.
STRAND 827 829 {ECO:0000244|PDB:2CLQ}.
HELIX 843 845 {ECO:0000244|PDB:4BF2}.
HELIX 848 853 {ECO:0000244|PDB:4BF2}.
HELIX 854 857 {ECO:0000244|PDB:4BF2}.
HELIX 860 876 {ECO:0000244|PDB:4BF2}.
HELIX 882 884 {ECO:0000244|PDB:4BF2}.
HELIX 887 897 {ECO:0000244|PDB:4BF2}.
HELIX 909 918 {ECO:0000244|PDB:4BF2}.
TURN 923 925 {ECO:0000244|PDB:4BF2}.
HELIX 929 933 {ECO:0000244|PDB:4BF2}.
HELIX 936 938 {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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