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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)

 MK07_HUMAN              Reviewed;         816 AA.
Q13164; Q16634; Q59F50; Q6QLU7; Q7L4P4; Q969G1; Q96G51;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
02-SEP-2008, sequence version 2.
27-SEP-2017, entry version 175.
RecName: Full=Mitogen-activated protein kinase 7;
Short=MAP kinase 7;
Short=MAPK 7;
EC=2.7.11.24;
AltName: Full=Big MAP kinase 1;
Short=BMK-1;
AltName: Full=Extracellular signal-regulated kinase 5;
Short=ERK-5;
Name=MAPK7; Synonyms=BMK1, ERK5, PRKM7;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
TISSUE=Placenta;
PubMed=7646528; DOI=10.1006/bbrc.1995.2189;
Lee J.-D., Ulevitch R.J., Han J.;
"Primary structure of BMK1: a new mammalian map kinase.";
Biochem. Biophys. Res. Commun. 213:715-724(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH MAP2K5, AND TISSUE
SPECIFICITY.
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).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
TISSUE=Placenta;
PubMed=15716121; DOI=10.1016/j.gene.2004.11.011;
McCaw B.J., Chow S.Y., Wong E.S.M., Tan K.L., Guo H., Guy G.R.;
"Identification and characterization of mErk5-T, a novel Erk5/Bmk1
splice variant.";
Gene 345:183-190(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
TISSUE=Spleen;
Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
Ohara O., Nagase T., Kikuno R.F.;
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Muscle, and Pancreas;
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).
[7]
PROTEIN SEQUENCE OF 2-35; 75-98; 119-131; 198-205; 296-343; 377-392;
468-485; 489-505; 544-571; 720-735 AND 798-816, CLEAVAGE OF INITIATOR
METHIONINE, ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS
SPECTROMETRY.
TISSUE=Hepatoma;
Bienvenut W.V., Fleming J., Leug H.Y.;
Submitted (JAN-2010) to UniProtKB.
[8]
FUNCTION, ENZYME REGULATION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
219-THR--TYR-221.
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).
[9]
FUNCTION, AND ENZYME REGULATION.
PubMed=9790194; DOI=10.1038/27234;
Kato Y., Tapping R.I., Huang S., Watson M.H., Ulevitch R.J.,
Lee J.-D.;
"Bmk1/Erk5 is required for cell proliferation induced by epidermal
growth factor.";
Nature 395:713-716(1998).
[10]
FUNCTION, AND INTERACTION WITH SGK1.
PubMed=11254654; DOI=10.1074/jbc.C000838200;
Hayashi M., Tapping R.I., Chao T.H., Lo J.F., King C.C., Yang Y.,
Lee J.D.;
"BMK1 mediates growth factor-induced cell proliferation through direct
cellular activation of serum and glucocorticoid-inducible kinase.";
J. Biol. Chem. 276:8631-8634(2001).
[11]
FUNCTION.
PubMed=11278431; DOI=10.1074/jbc.M008748200;
Dong F., Gutkind J.S., Larner A.C.;
"Granulocyte colony-stimulating factor induces ERK5 activation, which
is differentially regulated by protein-tyrosine kinases and protein
kinase C. Regulation of cell proliferation and survival.";
J. Biol. Chem. 276:10811-10816(2001).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-720 AND THR-733, 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).
[13]
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).
[14]
INTERACTION WITH HSP90AB1.
PubMed=23428871; DOI=10.1128/MCB.01246-12;
Erazo T., Moreno A., Ruiz-Babot G., Rodriguez-Asiain A., Morrice N.A.,
Espadamala J., Bayascas J.R., Gomez N., Lizcano J.M.;
"Canonical and kinase activity-independent mechanisms for
extracellular signal-regulated kinase 5 (ERK5) nuclear translocation
require dissociation of Hsp90 from the ERK5-Cdc37 complex.";
Mol. Cell. Biol. 33:1671-1686(2013).
[15]
FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION, AND INTERACTION WITH
PML.
PubMed=22869143; DOI=10.1038/onc.2012.332;
Yang Q., Liao L., Deng X., Chen R., Gray N.S., Yates J.R. III,
Lee J.D.;
"BMK1 is involved in the regulation of p53 through disrupting the PML-
MDM2 interaction.";
Oncogene 32:3156-3164(2013).
[16]
VARIANTS [LARGE SCALE ANALYSIS] HIS-535 AND ALA-550.
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: Plays a role in various cellular processes such as
proliferation, differentiation and cell survival. The upstream
activator of MAPK7 is the MAPK kinase MAP2K5. Upon activation, it
translocates to the nucleus and phosphorylates various downstream
targets including MEF2C. EGF activates MAPK7 through a Ras-
independent and MAP2K5-dependent pathway. May have a role in
muscle cell differentiation. May be important for endothelial
function and maintenance of blood vessel integrity. MAP2K5 and
MAPK7 interact specifically with one another and not with
MEK1/ERK1 or MEK2/ERK2 pathways. Phosphorylates SGK1 at Ser-78 and
this is required for growth factor-induced cell cycle progression.
Involved in the regulation of p53/TP53 by disrupting the PML-MDM2
interaction. {ECO:0000269|PubMed:11254654,
ECO:0000269|PubMed:11278431, ECO:0000269|PubMed:22869143,
ECO:0000269|PubMed:9384584, ECO:0000269|PubMed:9790194}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
-!- ENZYME REGULATION: Activated by tyrosine and threonine
phosphorylation (By similarity). Activated in response to
hyperosmolarity, hydrogen peroxide, and epidermal growth factor
(EGF). {ECO:0000250, ECO:0000269|PubMed:9384584,
ECO:0000269|PubMed:9790194}.
-!- SUBUNIT: Interacts with MAP2K5. Forms oligomers (By similarity).
Interacts with MEF2A, MEF2C and MEF2D; the interaction
phosphorylates the MEF2s and enhances transcriptional activity of
MEF2A, MEF2C but not MEF2D (By similarity). Interacts with SGK1.
Preferentially interacts with PML isoform PML-4 but shows
interaction also with its other isoforms: isoform PML-1, isoform
PML-2, isoform PML-3 and isoform PML-6. Interacts (via N-terminal
half) with HSP90AB1-CDC37 chaperone complex in resting cells; the
interaction is MAP2K5-independent and prevents MAPK7 from
ubiquitination and proteasomal degradation (PubMed:23428871).
{ECO:0000250, ECO:0000269|PubMed:11254654,
ECO:0000269|PubMed:22869143, ECO:0000269|PubMed:23428871,
ECO:0000269|PubMed:7759517}.
-!- INTERACTION:
Q12156:AIM7 (xeno); NbExp=3; IntAct=EBI-1213983, EBI-30371;
P53286:BTN2 (xeno); NbExp=3; IntAct=EBI-1213983, EBI-3796;
Q12055:FAP7 (xeno); NbExp=3; IntAct=EBI-1213983, EBI-22197;
Q13163:MAP2K5; NbExp=4; IntAct=EBI-1213983, EBI-307294;
P29590:PML; NbExp=6; IntAct=EBI-1213983, EBI-295890;
Q5TZN3:UBE2C; NbExp=3; IntAct=EBI-1213983, EBI-10247554;
-!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Nucleus, PML body.
Note=Translocates to the nucleus upon activation.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1;
IsoId=Q13164-1; Sequence=Displayed;
Name=2;
IsoId=Q13164-2; Sequence=VSP_035198;
Note=No experimental confirmation available.;
Name=3;
IsoId=Q13164-3; Sequence=VSP_035200;
Name=4;
IsoId=Q13164-4; Sequence=VSP_035199, VSP_035200;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Expressed in many adult tissues. Abundant in
heart, placenta, lung, kidney and skeletal muscle. Not detectable
in liver. {ECO:0000269|PubMed:7759517}.
-!- DOMAIN: The second proline-rich region may interact with actin
targeting the kinase to a specific location in the cell.
-!- DOMAIN: The TXY motif contains the threonine and tyrosine residues
whose phosphorylation activates the MAP kinases.
-!- PTM: Dually phosphorylated on Thr-219 and Tyr-221, which activates
the enzyme (By similarity). Autophosphorylated in vitro on
threonine and tyrosine residues when the C-terminal part of the
kinase, which could have a regulatory role, is absent.
{ECO:0000250, ECO:0000269|PubMed:22869143}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC
Ser/Thr protein kinase family. MAP kinase subfamily.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAA81381.1; Type=Frameshift; Positions=19, 32; Evidence={ECO:0000305};
Sequence=BAD92848.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/MAPK7ID41294ch17p11.html";
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EMBL; U29725; AAA82931.1; -; mRNA.
EMBL; U29726; AAA82932.1; -; mRNA.
EMBL; U29727; AAA82933.1; -; Genomic_DNA.
EMBL; U25278; AAA81381.1; ALT_FRAME; mRNA.
EMBL; AY534741; AAS38577.1; -; mRNA.
EMBL; AB209611; BAD92848.1; ALT_INIT; mRNA.
EMBL; CH471212; EAW50883.1; -; Genomic_DNA.
EMBL; CH471212; EAW50886.1; -; Genomic_DNA.
EMBL; BC007404; AAH07404.1; -; mRNA.
EMBL; BC007992; AAH07992.1; -; mRNA.
EMBL; BC009963; AAH09963.1; -; mRNA.
EMBL; BC030134; AAH30134.1; -; mRNA.
CCDS; CCDS11206.1; -. [Q13164-1]
CCDS; CCDS11207.1; -. [Q13164-2]
PIR; B56708; B56708.
RefSeq; NP_002740.2; NM_002749.3. [Q13164-1]
RefSeq; NP_620601.1; NM_139032.2. [Q13164-2]
RefSeq; NP_620602.2; NM_139033.2. [Q13164-1]
RefSeq; NP_620603.2; NM_139034.2. [Q13164-1]
RefSeq; XP_011522259.1; XM_011523957.2. [Q13164-2]
UniGene; Hs.150136; -.
PDB; 2Q8Y; X-ray; 2.00 A; B=215-223.
PDB; 4B99; X-ray; 2.80 A; A=1-397.
PDB; 4IC7; X-ray; 2.60 A; A/D=1-431.
PDB; 4IC8; X-ray; 2.80 A; A/B=1-431.
PDB; 4ZSG; X-ray; 1.79 A; A=47-393.
PDB; 4ZSJ; X-ray; 2.48 A; A=50-393.
PDB; 4ZSL; X-ray; 2.25 A; A=53-393.
PDB; 5BYY; X-ray; 2.79 A; A=49-394.
PDB; 5BYZ; X-ray; 1.65 A; A=48-395.
PDBsum; 2Q8Y; -.
PDBsum; 4B99; -.
PDBsum; 4IC7; -.
PDBsum; 4IC8; -.
PDBsum; 4ZSG; -.
PDBsum; 4ZSJ; -.
PDBsum; 4ZSL; -.
PDBsum; 5BYY; -.
PDBsum; 5BYZ; -.
ProteinModelPortal; Q13164; -.
SMR; Q13164; -.
BioGrid; 111584; 64.
IntAct; Q13164; 38.
STRING; 9606.ENSP00000311005; -.
BindingDB; Q13164; -.
ChEMBL; CHEMBL5332; -.
GuidetoPHARMACOLOGY; 2093; -.
iPTMnet; Q13164; -.
PhosphoSitePlus; Q13164; -.
BioMuta; MAPK7; -.
DMDM; 205371766; -.
EPD; Q13164; -.
MaxQB; Q13164; -.
PaxDb; Q13164; -.
PeptideAtlas; Q13164; -.
PRIDE; Q13164; -.
DNASU; 5598; -.
Ensembl; ENST00000299612; ENSP00000299612; ENSG00000166484. [Q13164-2]
Ensembl; ENST00000308406; ENSP00000311005; ENSG00000166484. [Q13164-1]
Ensembl; ENST00000395602; ENSP00000378966; ENSG00000166484. [Q13164-1]
Ensembl; ENST00000395604; ENSP00000378968; ENSG00000166484. [Q13164-1]
GeneID; 5598; -.
KEGG; hsa:5598; -.
UCSC; uc002gvn.4; human. [Q13164-1]
CTD; 5598; -.
DisGeNET; 5598; -.
EuPathDB; HostDB:ENSG00000166484.19; -.
GeneCards; MAPK7; -.
HGNC; HGNC:6880; MAPK7.
HPA; CAB018561; -.
HPA; HPA031031; -.
MIM; 602521; gene.
neXtProt; NX_Q13164; -.
OpenTargets; ENSG00000166484; -.
PharmGKB; PA30625; -.
eggNOG; KOG0660; Eukaryota.
eggNOG; ENOG410XNY0; LUCA.
GeneTree; ENSGT00550000074298; -.
HOVERGEN; HBG108137; -.
InParanoid; Q13164; -.
KO; K04464; -.
OMA; IIETIGT; -.
OrthoDB; EOG091G08QL; -.
PhylomeDB; Q13164; -.
TreeFam; TF105099; -.
BRENDA; 2.7.11.24; 2681.
Reactome; R-HSA-198753; ERK/MAPK targets.
Reactome; R-HSA-198765; Signalling to ERK5.
Reactome; R-HSA-202670; ERKs are inactivated.
Reactome; R-HSA-2559582; Senescence-Associated Secretory Phenotype (SASP).
Reactome; R-HSA-881907; Gastrin-CREB signalling pathway via PKC and MAPK.
Reactome; R-HSA-8853659; RET signaling.
SignaLink; Q13164; -.
SIGNOR; Q13164; -.
ChiTaRS; MAPK7; human.
GeneWiki; MAPK7; -.
GenomeRNAi; 5598; -.
PRO; PR:Q13164; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000166484; -.
CleanEx; HS_MAPK7; -.
ExpressionAtlas; Q13164; baseline and differential.
Genevisible; Q13164; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:BHF-UCL.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0016605; C:PML body; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004707; F:MAP kinase activity; IBA:GO_Central.
GO; GO:0051019; F:mitogen-activated protein kinase binding; IPI:BHF-UCL.
GO; GO:0004674; F:protein serine/threonine kinase activity; TAS:Reactome.
GO; GO:0007411; P:axon guidance; TAS:Reactome.
GO; GO:0019933; P:cAMP-mediated signaling; NAS:BHF-UCL.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0071363; P:cellular response to growth factor stimulus; IGI:BHF-UCL.
GO; GO:0070301; P:cellular response to hydrogen peroxide; IMP:BHF-UCL.
GO; GO:0071499; P:cellular response to laminar fluid shear stress; IMP:BHF-UCL.
GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IDA:UniProtKB.
GO; GO:0030821; P:negative regulation of cAMP catabolic process; NAS:BHF-UCL.
GO; GO:0051344; P:negative regulation of cyclic-nucleotide phosphodiesterase activity; NAS:BHF-UCL.
GO; GO:2000352; P:negative regulation of endothelial cell apoptotic process; IMP:BHF-UCL.
GO; GO:0070377; P:negative regulation of ERK5 cascade; IEA:Ensembl.
GO; GO:2001240; P:negative regulation of extrinsic apoptotic signaling pathway in absence of ligand; IGI:BHF-UCL.
GO; GO:0034115; P:negative regulation of heterotypic cell-cell adhesion; IGI:BHF-UCL.
GO; GO:0050728; P:negative regulation of inflammatory response; TAS:BHF-UCL.
GO; GO:0043407; P:negative regulation of MAP kinase activity; IEA:Ensembl.
GO; GO:0051534; P:negative regulation of NFAT protein import into nucleus; IEA:Ensembl.
GO; GO:1902176; P:negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway; IMP:BHF-UCL.
GO; GO:0060761; P:negative regulation of response to cytokine stimulus; IGI:BHF-UCL.
GO; GO:0018105; P:peptidyl-serine phosphorylation; IEA:Ensembl.
GO; GO:0051247; P:positive regulation of protein metabolic process; IGI:BHF-UCL.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IGI:BHF-UCL.
GO; GO:0036003; P:positive regulation of transcription from RNA polymerase II promoter in response to stress; IMP:BHF-UCL.
GO; GO:0045765; P:regulation of angiogenesis; IEA:Ensembl.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
Gene3D; 1.25.10.10; -; 1.
InterPro; IPR011989; ARM-like.
InterPro; IPR011009; Kinase-like_dom.
InterPro; IPR003527; MAP_kinase_CS.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008271; Ser/Thr_kinase_AS.
Pfam; PF00069; Pkinase; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS01351; MAPK; 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;
Cell cycle; Complete proteome; Cytoplasm; Differentiation;
Direct protein sequencing; Kinase; Nucleotide-binding; Nucleus;
Phosphoprotein; Polymorphism; Reference proteome;
Serine/threonine-protein kinase; Transferase.
INIT_MET 1 1 Removed. {ECO:0000269|Ref.7}.
CHAIN 2 816 Mitogen-activated protein kinase 7.
/FTId=PRO_0000186260.
DOMAIN 55 347 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 61 69 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
REGION 2 77 Required for cytoplasmic targeting.
{ECO:0000250}.
REGION 78 139 Required for binding to MAP2K5.
{ECO:0000250}.
REGION 140 406 Necessary for oligomerization.
{ECO:0000250}.
REGION 407 806 May not be required for kinase activity;
required to stimulate MEF2C activity.
{ECO:0000250}.
MOTIF 219 221 TXY.
MOTIF 505 539 Nuclear localization signal.
{ECO:0000250}.
COMPBIAS 338 341 Poly-Ala.
COMPBIAS 403 694 Pro-rich.
COMPBIAS 513 543 Arg-rich.
ACT_SITE 182 182 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 84 84 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 2 2 N-acetylalanine. {ECO:0000269|Ref.7}.
MOD_RES 720 720 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 733 733 Phosphothreonine.
{ECO:0000244|PubMed:18669648}.
VAR_SEQ 1 139 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_035198.
VAR_SEQ 1 133 MAEPLKEEDGEDGSAEPPGPVKAEPAHTAASVAAKNLALLK
ARSFDVTFDVGDEYEIIETIGNGAYGVVSSARRRLTGQQVA
IKKIPNAFDVVTNAKRTLRELKILKHFKHDNIIAIKDILRP
TVPYGEFKSV -> MLFFHTMPSAPMGSQGKAVTCLESEGC
GEDGACPWSVIRPTHASLLPSPSS (in isoform 4).
{ECO:0000303|Ref.4}.
/FTId=VSP_035199.
VAR_SEQ 493 816 DGPSAPLEAPEPRKPVTAQERQREREEKRRRRQERAKEREK
RRQERERKERGAGASGGPSTDPLAGLVLSDNDRSLLERWTR
MARPAAPALTSVPAPAPAPTPTPTPVQPTSPPPGPVAQPTG
PQPQSAGSTSGPVPQPACPPPGPAPHPTGPPGPIPVPAPPQ
IATSTSLLAAQSLVPPPGLPGSSTPGVLPYFPPGLPPPDAG
GAPQSSMSESPDVNLVTQQLSKSQVEDPLPPVFSGTPKGSG
AGYGVGFDLEEFLNQSFDMGVADGPQDGQADSASLSASLLA
DWLEGHGMNPADIESLQREIQMDSPMLLADLPDLQDP ->
GALWAGRVGRGETWTWTRLQAFTFSPAQLPRKWPQRTPGGS
(in isoform 3 and isoform 4).
{ECO:0000303|PubMed:15716121,
ECO:0000303|Ref.4}.
/FTId=VSP_035200.
VARIANT 535 535 R -> H. {ECO:0000269|PubMed:17344846}.
/FTId=VAR_046225.
VARIANT 550 550 G -> A (in dbSNP:rs56388327).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042257.
MUTAGEN 219 221 TEY->AEF: Loss activation by MAP2K5.
{ECO:0000269|PubMed:9384584}.
CONFLICT 610 610 V -> L (in Ref. 1; AAA81381).
{ECO:0000305}.
TURN 45 48 {ECO:0000244|PDB:4IC8}.
STRAND 53 64 {ECO:0000244|PDB:5BYZ}.
STRAND 67 74 {ECO:0000244|PDB:5BYZ}.
TURN 75 77 {ECO:0000244|PDB:5BYZ}.
STRAND 80 86 {ECO:0000244|PDB:5BYZ}.
TURN 87 90 {ECO:0000244|PDB:5BYZ}.
HELIX 93 108 {ECO:0000244|PDB:5BYZ}.
STRAND 117 120 {ECO:0000244|PDB:5BYZ}.
HELIX 127 129 {ECO:0000244|PDB:5BYZ}.
STRAND 133 137 {ECO:0000244|PDB:5BYZ}.
STRAND 141 143 {ECO:0000244|PDB:5BYY}.
HELIX 144 148 {ECO:0000244|PDB:5BYZ}.
STRAND 150 152 {ECO:0000244|PDB:5BYZ}.
HELIX 156 175 {ECO:0000244|PDB:5BYZ}.
HELIX 185 187 {ECO:0000244|PDB:5BYZ}.
STRAND 188 190 {ECO:0000244|PDB:5BYZ}.
STRAND 196 198 {ECO:0000244|PDB:5BYZ}.
HELIX 214 216 {ECO:0000244|PDB:5BYZ}.
HELIX 219 221 {ECO:0000244|PDB:5BYZ}.
HELIX 225 227 {ECO:0000244|PDB:5BYZ}.
HELIX 230 234 {ECO:0000244|PDB:5BYZ}.
HELIX 242 257 {ECO:0000244|PDB:5BYZ}.
HELIX 267 278 {ECO:0000244|PDB:5BYZ}.
HELIX 283 287 {ECO:0000244|PDB:5BYZ}.
STRAND 288 290 {ECO:0000244|PDB:4IC8}.
HELIX 292 300 {ECO:0000244|PDB:5BYZ}.
HELIX 309 312 {ECO:0000244|PDB:5BYZ}.
STRAND 313 316 {ECO:0000244|PDB:5BYY}.
HELIX 318 327 {ECO:0000244|PDB:5BYZ}.
HELIX 332 334 {ECO:0000244|PDB:5BYZ}.
HELIX 338 342 {ECO:0000244|PDB:5BYZ}.
HELIX 345 347 {ECO:0000244|PDB:5BYZ}.
TURN 348 350 {ECO:0000244|PDB:5BYZ}.
HELIX 353 355 {ECO:0000244|PDB:5BYZ}.
HELIX 366 369 {ECO:0000244|PDB:5BYZ}.
STRAND 370 372 {ECO:0000244|PDB:4IC7}.
HELIX 374 393 {ECO:0000244|PDB:5BYZ}.
STRAND 396 398 {ECO:0000244|PDB:4IC7}.
SEQUENCE 816 AA; 88386 MW; 27729FE31658CE3B CRC64;
MAEPLKEEDG EDGSAEPPGP VKAEPAHTAA SVAAKNLALL KARSFDVTFD VGDEYEIIET
IGNGAYGVVS SARRRLTGQQ VAIKKIPNAF DVVTNAKRTL RELKILKHFK HDNIIAIKDI
LRPTVPYGEF KSVYVVLDLM ESDLHQIIHS SQPLTLEHVR YFLYQLLRGL KYMHSAQVIH
RDLKPSNLLV NENCELKIGD FGMARGLCTS PAEHQYFMTE YVATRWYRAP ELMLSLHEYT
QAIDLWSVGC IFGEMLARRQ LFPGKNYVHQ LQLIMMVLGT PSPAVIQAVG AERVRAYIQS
LPPRQPVPWE TVYPGADRQA LSLLGRMLRF EPSARISAAA ALRHPFLAKY HDPDDEPDCA
PPFDFAFDRE ALTRERIKEA IVAEIEDFHA RREGIRQQIR FQPSLQPVAS EPGCPDVEMP
SPWAPSGDCA MESPPPAPPP CPGPAPDTID LTLQPPPPVS EPAPPKKDGA ISDNTKAALK
AALLKSLRSR LRDGPSAPLE APEPRKPVTA QERQREREEK RRRRQERAKE REKRRQERER
KERGAGASGG PSTDPLAGLV LSDNDRSLLE RWTRMARPAA PALTSVPAPA PAPTPTPTPV
QPTSPPPGPV AQPTGPQPQS AGSTSGPVPQ PACPPPGPAP HPTGPPGPIP VPAPPQIATS
TSLLAAQSLV PPPGLPGSST PGVLPYFPPG LPPPDAGGAP QSSMSESPDV NLVTQQLSKS
QVEDPLPPVF SGTPKGSGAG YGVGFDLEEF LNQSFDMGVA DGPQDGQADS ASLSASLLAD
WLEGHGMNPA DIESLQREIQ MDSPMLLADL PDLQDP


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