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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)

 MP2K5_HUMAN             Reviewed;         448 AA.
Q13163; B4DE43; Q92961; Q92962;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
28-NOV-2006, sequence version 2.
05-DEC-2018, entry version 190.
RecName: Full=Dual specificity mitogen-activated protein kinase kinase 5;
Short=MAP kinase kinase 5;
Short=MAPKK 5;
EC=2.7.12.2;
AltName: Full=MAPK/ERK kinase 5;
Short=MEK 5;
Name=MAP2K5; Synonyms=MEK5, MKK5, PRKMK5;
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 A), FUNCTION, INTERACTION WITH
ERK5 AND MAPK7, MUTAGENESIS OF LYS-195; SER-311 AND THR-315, AND
PHOSPHORYLATION AT SER-311 AND THR-315.
TISSUE=Fetal brain;
PubMed=7759517; DOI=10.1074/jbc.270.21.12665;
Zhou G., Bao Z.Q., Dixon J.E.;
"Components of a new human protein kinase signal transduction
pathway.";
J. Biol. Chem. 270:12665-12669(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS B AND C), AND FUNCTION.
TISSUE=Placenta;
PubMed=9384584; DOI=10.1093/emboj/16.23.7054;
Kato Y., Kravchenko V.V., Tapping R.I., Han J., Ulevitch R.J.,
Lee J.-D.;
"BMK1/ERK5 regulates serum-induced early gene expression through
transcription factor MEF2C.";
EMBO J. 16:7054-7066(1997).
[3]
SEQUENCE REVISION TO C-TERMINUS OF ISOFORM C.
Lee J.D.;
Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
TISSUE=Cerebellum;
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).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S.,
Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W.,
Korn B., Zuo D., Hu Y., LaBaer J.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16572171; DOI=10.1038/nature04601;
Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R.,
Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G.,
Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A.,
Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W.,
Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X.,
Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K.,
Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S.,
Nusbaum C.;
"Analysis of the DNA sequence and duplication history of human
chromosome 15.";
Nature 440:671-675(2006).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
TISSUE=Brain;
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).
[9]
INTERACTION WITH YOPJ, AND ACETYLATION.
PubMed=16728640; DOI=10.1126/science.1126867;
Mukherjee S., Keitany G., Li Y., Wang Y., Ball H.L., Goldsmith E.J.,
Orth K.;
"Yersinia YopJ acetylates and inhibits kinase activation by blocking
phosphorylation.";
Science 312:1211-1214(2006).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-311, 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).
[12]
X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 4-108 IN COMPLEX WITH
MAP3K2.
Structural genomics consortium (SGC);
"Crystal structure of the complex of human mitogen activated protein
kinase kinase 5 phox domain (MAP2K5-Phox) with human mitogen activated
protein kinase kinase kinase 3 (MAP3K2B-Phox).";
Submitted (NOV-2006) to the PDB data bank.
[13]
X-RAY CRYSTALLOGRAPHY (1.83 ANGSTROMS) OF 4-108 IN COMPLEX WITH
MAP3K3.
Structural genomics consortium (SGC);
"Crystal structure of the complex of human mitogen activated protein
kinase kinase 5 phox domain (MAP2K5-Phox) with human mitogen activated
protein kinase kinase kinase 3 (MAP3K3B-Phox).";
Submitted (NOV-2006) to the PDB data bank.
[14]
VARIANTS [LARGE SCALE ANALYSIS] ARG-118; VAL-427 AND THR-428.
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: Acts as a scaffold for the formation of a ternary
MAP3K2/MAP3K3-MAP3K5-MAPK7 signaling complex. Activation of this
pathway appears to play a critical role in protecting cells from
stress-induced apoptosis, neuronal survival and cardiac
development and angiogenesis. {ECO:0000269|PubMed:7759517,
ECO:0000269|PubMed:9384584}.
-!- 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=2.7.12.2;
-!- 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=2.7.12.2;
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
-!- SUBUNIT: Interacts with PARD6A, MAP3K3 and MAPK7. Forms a complex
with SQSTM1 and PRKCZ or PRKCI (By similarity). Interacts with
Yersinia yopJ. {ECO:0000250, ECO:0000269|PubMed:16728640,
ECO:0000269|PubMed:7759517, ECO:0000269|Ref.12,
ECO:0000269|Ref.13}.
-!- INTERACTION:
P62993:GRB2; NbExp=2; IntAct=EBI-307294, EBI-401755;
Q99759:MAP3K3; NbExp=2; IntAct=EBI-307294, EBI-307281;
Q13164:MAPK7; NbExp=4; IntAct=EBI-307294, EBI-1213983;
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=B;
IsoId=Q13163-1; Sequence=Displayed;
Name=A;
IsoId=Q13163-2; Sequence=VSP_021825;
Name=C;
IsoId=Q13163-3; Sequence=VSP_021825, VSP_021826;
Note=Incomplete sequence.;
Name=4;
IsoId=Q13163-4; Sequence=VSP_043333;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Expressed in many adult tissues. Abundant in
heart and skeletal muscle.
-!- DOMAIN: Binds MAP3K2/MAP3K3 and MAPK7 via non-overlapping residues
of the PB1 domain. This domain also mediates interactions with
SQSTM1 and PARD6A (By similarity). {ECO:0000250}.
-!- PTM: Activated by phosphorylation on Ser/Thr by MAP kinase kinase
kinases. {ECO:0000250}.
-!- PTM: Yersinia yopJ may acetylate Ser/Thr residues, preventing
phosphorylation and activation, thus blocking the MAPK signaling
pathway. {ECO:0000269|PubMed:16728640,
ECO:0000269|PubMed:7759517}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
protein kinase family. MAP kinase kinase subfamily. {ECO:0000305}.
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EMBL; U25265; AAA96146.1; -; mRNA.
EMBL; U71087; AAB16851.1; -; mRNA.
EMBL; U71088; AAB16852.2; -; mRNA.
EMBL; BT006780; AAP35426.1; -; mRNA.
EMBL; AK293459; BAG56954.1; -; mRNA.
EMBL; CR542229; CAG47025.1; -; mRNA.
EMBL; AC009292; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC016355; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC103753; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC008838; AAH08838.1; -; mRNA.
CCDS; CCDS10224.1; -. [Q13163-1]
CCDS; CCDS42051.1; -. [Q13163-2]
CCDS; CCDS55970.1; -. [Q13163-4]
RefSeq; NP_001193733.1; NM_001206804.1. [Q13163-4]
RefSeq; NP_002748.1; NM_002757.3. [Q13163-2]
RefSeq; NP_660143.1; NM_145160.2. [Q13163-1]
UniGene; Hs.114198; -.
PDB; 2NPT; X-ray; 1.75 A; A/C=5-108.
PDB; 2O2V; X-ray; 1.83 A; A=5-108.
PDB; 4IC7; X-ray; 2.60 A; B/E=16-130.
PDBsum; 2NPT; -.
PDBsum; 2O2V; -.
PDBsum; 4IC7; -.
ProteinModelPortal; Q13163; -.
SMR; Q13163; -.
BioGrid; 111593; 57.
CORUM; Q13163; -.
DIP; DIP-27558N; -.
IntAct; Q13163; 21.
MINT; Q13163; -.
STRING; 9606.ENSP00000178640; -.
BindingDB; Q13163; -.
ChEMBL; CHEMBL4948; -.
GuidetoPHARMACOLOGY; 2066; -.
iPTMnet; Q13163; -.
PhosphoSitePlus; Q13163; -.
BioMuta; MAP2K5; -.
DMDM; 118572669; -.
EPD; Q13163; -.
MaxQB; Q13163; -.
PaxDb; Q13163; -.
PeptideAtlas; Q13163; -.
PRIDE; Q13163; -.
ProteomicsDB; 59199; -.
ProteomicsDB; 59200; -. [Q13163-2]
ProteomicsDB; 59201; -. [Q13163-3]
ProteomicsDB; 59202; -. [Q13163-4]
DNASU; 5607; -.
Ensembl; ENST00000178640; ENSP00000178640; ENSG00000137764. [Q13163-1]
Ensembl; ENST00000354498; ENSP00000346493; ENSG00000137764. [Q13163-4]
Ensembl; ENST00000395476; ENSP00000378859; ENSG00000137764. [Q13163-2]
GeneID; 5607; -.
KEGG; hsa:5607; -.
UCSC; uc002aqu.4; human. [Q13163-1]
CTD; 5607; -.
DisGeNET; 5607; -.
EuPathDB; HostDB:ENSG00000137764.19; -.
GeneCards; MAP2K5; -.
HGNC; HGNC:6845; MAP2K5.
HPA; CAB022094; -.
HPA; HPA027347; -.
HPA; HPA027755; -.
MIM; 602520; gene.
neXtProt; NX_Q13163; -.
OpenTargets; ENSG00000137764; -.
PharmGKB; PA30590; -.
eggNOG; KOG0581; Eukaryota.
eggNOG; ENOG410XQ5A; LUCA.
GeneTree; ENSGT00940000157505; -.
HOGENOM; HOG000234206; -.
HOVERGEN; HBG108518; -.
InParanoid; Q13163; -.
KO; K04463; -.
OMA; EDLMGHP; -.
OrthoDB; EOG091G06I7; -.
PhylomeDB; Q13163; -.
TreeFam; TF106468; -.
BRENDA; 2.7.12.2; 2681.
Reactome; R-HSA-198765; Signalling to ERK5.
SignaLink; Q13163; -.
SIGNOR; Q13163; -.
ChiTaRS; MAP2K5; human.
EvolutionaryTrace; Q13163; -.
GeneWiki; MAP2K5; -.
GenomeRNAi; 5607; -.
PRO; PR:Q13163; -.
Proteomes; UP000005640; Chromosome 15.
Bgee; ENSG00000137764; Expressed in 218 organ(s), highest expression level in frontal cortex.
CleanEx; HS_MAP2K5; -.
ExpressionAtlas; Q13163; baseline and differential.
Genevisible; Q13163; HS.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005829; C:cytosol; IEA:Ensembl.
GO; GO:0005634; C:nucleus; IEA:Ensembl.
GO; GO:0005819; C:spindle; IEA:Ensembl.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004708; F:MAP kinase kinase activity; IBA:GO_Central.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004672; F:protein kinase activity; TAS:ProtInc.
GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
GO; GO:0004713; F:protein tyrosine kinase activity; IEA:UniProtKB-KW.
GO; GO:0000187; P:activation of MAPK activity; ISS:BHF-UCL.
GO; GO:0032147; P:activation of protein kinase activity; IBA:GO_Central.
GO; GO:0071363; P:cellular response to growth factor stimulus; ISS:BHF-UCL.
GO; GO:0071499; P:cellular response to laminar fluid shear stress; TAS:BHF-UCL.
GO; GO:0070375; P:ERK5 cascade; IEA:Ensembl.
GO; GO:0007507; P:heart development; IEA:Ensembl.
GO; GO:0090051; P:negative regulation of cell migration involved in sprouting angiogenesis; ISS:BHF-UCL.
GO; GO:2000342; P:negative regulation of chemokine (C-X-C motif) ligand 2 production; ISS:BHF-UCL.
GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; ISS:BHF-UCL.
GO; GO:2001240; P:negative regulation of extrinsic apoptotic signaling pathway in absence of ligand; ISS:BHF-UCL.
GO; GO:0034115; P:negative regulation of heterotypic cell-cell adhesion; ISS:BHF-UCL.
GO; GO:0045415; P:negative regulation of interleukin-8 biosynthetic process; ISS:BHF-UCL.
GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; ISS:BHF-UCL.
GO; GO:0060761; P:negative regulation of response to cytokine stimulus; ISS:BHF-UCL.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:BHF-UCL.
GO; GO:0030307; P:positive regulation of cell growth; IEA:Ensembl.
GO; GO:0050679; P:positive regulation of epithelial cell proliferation; IEA:Ensembl.
GO; GO:0051247; P:positive regulation of protein metabolic process; ISS:BHF-UCL.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:BHF-UCL.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
GO; GO:0023014; P:signal transduction by protein phosphorylation; IBA:GO_Central.
GO; GO:0031098; P:stress-activated protein kinase signaling cascade; IBA:GO_Central.
CDD; cd06395; PB1_Map2k5; 1.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000270; PB1_dom.
InterPro; IPR034851; PB1_MAP2K5.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008271; Ser/Thr_kinase_AS.
Pfam; PF00564; PB1; 1.
Pfam; PF00069; Pkinase; 1.
SMART; SM00666; PB1; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS51745; PB1; 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; Acetylation; Alternative splicing; ATP-binding;
Complete proteome; Kinase; Magnesium; Metal-binding;
Nucleotide-binding; Phosphoprotein; Polymorphism; Reference proteome;
Serine/threonine-protein kinase; Transferase; Tyrosine-protein kinase.
CHAIN 1 448 Dual specificity mitogen-activated
protein kinase kinase 5.
/FTId=PRO_0000086383.
DOMAIN 18 109 PB1. {ECO:0000255|PROSITE-
ProRule:PRU01081}.
DOMAIN 166 409 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 172 180 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
REGION 18 25 Interaction with MAPK7. {ECO:0000250}.
REGION 64 68 Interaction with MAP3K2/MAP3K3.
{ECO:0000250}.
REGION 117 131 Interaction with MAPK7. {ECO:0000250}.
ACT_SITE 283 283 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 195 195 ATP.
MOD_RES 311 311 Phosphoserine.
{ECO:0000244|PubMed:19369195,
ECO:0000269|PubMed:7759517}.
MOD_RES 315 315 Phosphothreonine.
{ECO:0000269|PubMed:7759517}.
VAR_SEQ 1 45 MLWLALGPFPAMENQVLVIRIKIPNSGAVDWTVHSGPQLLF
RDVL -> MMEGHFPQS (in isoform 4).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_043333.
VAR_SEQ 349 358 Missing (in isoform A and isoform C).
{ECO:0000303|PubMed:7759517,
ECO:0000303|PubMed:9384584}.
/FTId=VSP_021825.
VAR_SEQ 444 448 QQGPP -> LASLPSPSPSV (in isoform C).
{ECO:0000303|PubMed:9384584}.
/FTId=VSP_021826.
VARIANT 118 118 H -> R (in dbSNP:rs56241934).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_040823.
VARIANT 427 427 A -> V (in dbSNP:rs1226964455).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_040824.
VARIANT 428 428 A -> T (in dbSNP:rs55811347).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_046070.
MUTAGEN 195 195 K->M: Inactivation.
{ECO:0000269|PubMed:7759517}.
MUTAGEN 311 311 S->A: Inactivation.
{ECO:0000269|PubMed:7759517}.
MUTAGEN 315 315 T->A: Inactivation.
{ECO:0000269|PubMed:7759517}.
STRAND 17 23 {ECO:0000244|PDB:2NPT}.
TURN 24 26 {ECO:0000244|PDB:2NPT}.
STRAND 27 33 {ECO:0000244|PDB:2NPT}.
HELIX 41 51 {ECO:0000244|PDB:2NPT}.
STRAND 58 63 {ECO:0000244|PDB:2NPT}.
STRAND 65 67 {ECO:0000244|PDB:4IC7}.
STRAND 69 72 {ECO:0000244|PDB:2NPT}.
HELIX 75 93 {ECO:0000244|PDB:2NPT}.
TURN 94 96 {ECO:0000244|PDB:2NPT}.
STRAND 102 107 {ECO:0000244|PDB:2NPT}.
SEQUENCE 448 AA; 50112 MW; F23BB327E2A9C7DC CRC64;
MLWLALGPFP AMENQVLVIR IKIPNSGAVD WTVHSGPQLL FRDVLDVIGQ VLPEATTTAF
EYEDEDGDRI TVRSDEEMKA MLSYYYSTVM EQQVNGQLIE PLQIFPRACK PPGERNIHGL
KVNTRAGPSQ HSSPAVSDSL PSNSLKKSSA ELKKILANGQ MNEQDIRYRD TLGHGNGGTV
YKAYHVPSGK ILAVKVILLD ITLELQKQIM SELEILYKCD SSYIIGFYGA FFVENRISIC
TEFMDGGSLD VYRKMPEHVL GRIAVAVVKG LTYLWSLKIL HRDVKPSNML VNTRGQVKLC
DFGVSTQLVN SIAKTYVGTN AYMAPERISG EQYGIHSDVW SLGISFMELA LGRFPYPQIQ
KNQGSLMPLQ LLQCIVDEDS PVLPVGEFSE PFVHFITQCM RKQPKERPAP EELMGHPFIV
QFNDGNAAVV SMWVCRALEE RRSQQGPP


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