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Dual specificity mitogen-activated protein kinase kinase 2 (MAP kinase kinase 2) (MAPKK 2) (EC 2.7.12.2) (ERK activator kinase 2) (MAPK/ERK kinase 2) (MEK 2)

 MP2K2_HUMAN             Reviewed;         400 AA.
P36507;
01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
01-JUN-1994, sequence version 1.
22-NOV-2017, entry version 203.
RecName: Full=Dual specificity mitogen-activated protein kinase kinase 2;
Short=MAP kinase kinase 2;
Short=MAPKK 2;
EC=2.7.12.2 {ECO:0000269|PubMed:10409742};
AltName: Full=ERK activator kinase 2;
AltName: Full=MAPK/ERK kinase 2;
Short=MEK 2;
Name=MAP2K2; Synonyms=MEK2, MKK2, PRKMK2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=8388392;
Zheng C.-F., Guan K.-L.;
"Cloning and characterization of two distinct human extracellular
signal-regulated kinase activator kinases, MEK1 and MEK2.";
J. Biol. Chem. 268:11435-11439(1993).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Muscle, and Skin;
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).
[3]
PROTEIN SEQUENCE OF 40-51; 53-61; 64-100; 102-112; 164-172; 194-205;
265-297; 362-371 AND 389-397, PHOSPHORYLATION AT THR-394, AND
IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Colon carcinoma;
Bienvenut W.V., Zebisch A., Kolch W.;
Submitted (DEC-2008) to UniProtKB.
[4]
PROTEIN SEQUENCE OF 210-231, INACTIVATION BY YERSINIA YOPJ,
PHOSPHORYLATION AT SER-222 AND SER-226, ACETYLATION AT SER-222 AND
SER-226, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=17116858; DOI=10.1073/pnas.0608995103;
Mittal R., Peak-Chew S.Y., McMahon H.T.;
"Acetylation of MEK2 and I kappa B kinase (IKK) activation loop
residues by YopJ inhibits signaling.";
Proc. Natl. Acad. Sci. U.S.A. 103:18574-18579(2006).
[5]
CLEAVAGE BY ANTHRAX LETHAL FACTOR.
PubMed=9563949; DOI=10.1126/science.280.5364.734;
Duesbery N.S., Webb C.P., Leppla S.H., Gordon V.M., Klimpel K.R.,
Copeland T.D., Ahn N.G., Oskarsson M.K., Fukasawa K., Paull K.D.,
Vande Woude G.F.;
"Proteolytic inactivation of MAP-kinase-kinase by anthrax lethal
factor.";
Science 280:734-737(1998).
[6]
PROTEIN SEQUENCE OF 39-49; 52-61 AND 352-361, CATALYTIC ACTIVITY,
COFACTOR, INTERACTION WITH KSR1, SUBCELLULAR LOCATION, AND
PHOSPHORYLATION AT SER-222.
PubMed=10409742; DOI=10.1128/MCB.19.8.5523;
Stewart S., Sundaram M., Zhang Y., Lee J., Han M., Guan K.L.;
"Kinase suppressor of Ras forms a multiprotein signaling complex and
modulates MEK localization.";
Mol. Cell. Biol. 19:5523-5534(1999).
[7]
CLEAVAGE BY ANTHRAX LETHAL FACTOR.
PubMed=11104681; DOI=10.1042/bj3520739;
Vitale G., Bernardi L., Napolitani G., Mock M., Montecucco C.;
"Susceptibility of mitogen-activated protein kinase kinase family
members to proteolysis by anthrax lethal factor.";
Biochem. J. 352:739-745(2000).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[9]
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).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-293 AND SER-295, AND
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 THR-394 AND THR-396, 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).
[12]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[13]
INTERACTION WITH SGK1.
PubMed=19447520; DOI=10.1016/j.jhep.2009.02.027;
Won M., Park K.A., Byun H.S., Kim Y.R., Choi B.L., Hong J.H., Park J.,
Seok J.H., Lee Y.H., Cho C.H., Song I.S., Kim Y.K., Shen H.M.,
Hur G.M.;
"Protein kinase SGK1 enhances MEK/ERK complex formation through the
phosphorylation of ERK2: implication for the positive regulatory role
of SGK1 on the ERK function during liver regeneration.";
J. Hepatol. 51:67-76(2009).
[14]
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).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-295 AND THR-394, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-394 AND THR-396, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-394 AND THR-396, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and 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).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23 AND THR-396, AND
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).
[21]
VARIANT CFC4 CYS-57.
PubMed=16439621; DOI=10.1126/science.1124642;
Rodriguez-Viciana P., Tetsu O., Tidyman W.E., Estep A.L., Conger B.A.,
Cruz M.S., McCormick F., Rauen K.A.;
"Germline mutations in genes within the MAPK pathway cause cardio-
facio-cutaneous syndrome.";
Science 311:1287-1290(2006).
[22]
VARIANTS CFC4 VAL-57 AND HIS-134.
PubMed=18042262; DOI=10.1111/j.1399-0004.2007.00931.x;
Schulz A.L., Albrecht B., Arici C., van der Burgt I., Buske A.,
Gillessen-Kaesbach G., Heller R., Horn D., Hubner C.A., Korenke G.C.,
Konig R., Kress W., Kruger G., Meinecke P., Mucke J., Plecko B.,
Rossier E., Schinzel A., Schulze A., Seemanova E., Seidel H.,
Spranger S., Tuysuz B., Uhrig S., Wieczorek D., Kutsche K., Zenker M.;
"Mutation and phenotypic spectrum in patients with cardio-facio-
cutaneous and Costello syndrome.";
Clin. Genet. 73:62-70(2008).
[23]
VARIANT CFC4 GLN-128, AND CHARACTERIZATION OF VARIANT CFC4 GLN-128.
PubMed=20358587; DOI=10.1002/ajmg.a.33342;
Rauen K.A., Tidyman W.E., Estep A.L., Sampath S., Peltier H.M.,
Bale S.J., Lacassie Y.;
"Molecular and functional analysis of a novel MEK2 mutation in cardio-
facio-cutaneous syndrome: transmission through four generations.";
Am. J. Med. Genet. A 152:807-814(2010).
-!- FUNCTION: Catalyzes the concomitant phosphorylation of a threonine
and a tyrosine residue in a Thr-Glu-Tyr sequence located in MAP
kinases. Activates the ERK1 and ERK2 MAP kinases (By similarity).
{ECO:0000250}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
{ECO:0000269|PubMed:10409742}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:10409742};
-!- SUBUNIT: Interacts with MORG1 (By similarity). Interacts with SGK1
(PubMed:19447520). Interacts with KSR1 (PubMed:10409742).
{ECO:0000250|UniProtKB:Q63932, ECO:0000269|PubMed:10409742,
ECO:0000269|PubMed:19447520}.
-!- INTERACTION:
P10398:ARAF; NbExp=6; IntAct=EBI-1056930, EBI-365961;
P15056:BRAF; NbExp=6; IntAct=EBI-1056930, EBI-365980;
O95273:CCNDBP1; NbExp=3; IntAct=EBI-1056930, EBI-748961;
Q12959:DLG1; NbExp=10; IntAct=EBI-1056930, EBI-357481;
Q8IVT5:KSR1; NbExp=6; IntAct=EBI-1056930, EBI-486984;
P04049:RAF1; NbExp=3; IntAct=EBI-1056930, EBI-365996;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10409742}.
Membrane {ECO:0000269|PubMed:10409742}; Peripheral membrane
protein {ECO:0000269|PubMed:10409742}. Note=Membrane localization
is probably regulated by its interaction with KSR1.
{ECO:0000269|PubMed:10409742}.
-!- PTM: MAPKK is itself dependent on Ser/Thr phosphorylation for
activity catalyzed by MAP kinase kinase kinases (RAF or MEKK1).
Phosphorylated by MAP2K1/MEK1 (By similarity). {ECO:0000250}.
-!- PTM: Acetylation of Ser-222 and Ser-226 by Yersinia yopJ prevents
phosphorylation and activation, thus blocking the MAPK signaling
pathway. {ECO:0000269|PubMed:17116858, ECO:0000269|Ref.3}.
-!- DISEASE: Cardiofaciocutaneous syndrome 4 (CFC4) [MIM:615280]: A
form of cardiofaciocutaneous syndrome, a multiple congenital
anomaly disorder characterized by a distinctive facial appearance,
heart defects and mental retardation. Heart defects include
pulmonic stenosis, atrial septal defects and hypertrophic
cardiomyopathy. Some affected individuals present with ectodermal
abnormalities such as sparse, friable hair, hyperkeratotic skin
lesions and a generalized ichthyosis-like condition. Typical
facial features are similar to Noonan syndrome. They include high
forehead with bitemporal constriction, hypoplastic supraorbital
ridges, downslanting palpebral fissures, a depressed nasal bridge,
and posteriorly angulated ears with prominent helices.
{ECO:0000269|PubMed:16439621, ECO:0000269|PubMed:18042262,
ECO:0000269|PubMed:20358587}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
protein kinase family. MAP kinase kinase subfamily. {ECO:0000305}.
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EMBL; L11285; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; BC000471; AAH00471.1; -; mRNA.
EMBL; BC018645; AAH18645.1; -; mRNA.
CCDS; CCDS12120.1; -.
PIR; A46723; A46723.
RefSeq; NP_109587.1; NM_030662.3.
UniGene; Hs.465627; -.
PDB; 1S9I; X-ray; 3.20 A; A/B=55-400.
PDB; 4H3Q; X-ray; 2.20 A; B=4-16.
PDBsum; 1S9I; -.
PDBsum; 4H3Q; -.
ProteinModelPortal; P36507; -.
SMR; P36507; -.
BioGrid; 111591; 43.
CORUM; P36507; -.
DIP; DIP-29119N; -.
IntAct; P36507; 22.
MINT; MINT-99667; -.
STRING; 9606.ENSP00000262948; -.
BindingDB; P36507; -.
ChEMBL; CHEMBL2964; -.
DrugBank; DB06616; Bosutinib.
DrugBank; DB08911; Trametinib.
GuidetoPHARMACOLOGY; 2063; -.
iPTMnet; P36507; -.
PhosphoSitePlus; P36507; -.
SwissPalm; P36507; -.
BioMuta; MAP2K2; -.
DMDM; 547915; -.
REPRODUCTION-2DPAGE; IPI00003783; -.
EPD; P36507; -.
MaxQB; P36507; -.
PaxDb; P36507; -.
PeptideAtlas; P36507; -.
PRIDE; P36507; -.
DNASU; 5605; -.
Ensembl; ENST00000262948; ENSP00000262948; ENSG00000126934.
GeneID; 5605; -.
KEGG; hsa:5605; -.
UCSC; uc002lzk.4; human.
CTD; 5605; -.
DisGeNET; 5605; -.
EuPathDB; HostDB:ENSG00000126934.13; -.
GeneCards; MAP2K2; -.
GeneReviews; MAP2K2; -.
H-InvDB; HIX0033655; -.
HGNC; HGNC:6842; MAP2K2.
HPA; CAB003835; -.
HPA; HPA051993; -.
MalaCards; MAP2K2; -.
MIM; 601263; gene.
MIM; 615280; phenotype.
neXtProt; NX_P36507; -.
OpenTargets; ENSG00000126934; -.
Orphanet; 1340; Cardiofaciocutaneous syndrome.
Orphanet; 638; Neurofibromatosis-Noonan syndrome.
PharmGKB; PA30587; -.
eggNOG; KOG0581; Eukaryota.
eggNOG; ENOG410XQ5A; LUCA.
GeneTree; ENSGT00760000119199; -.
HOGENOM; HOG000234206; -.
HOVERGEN; HBG108518; -.
InParanoid; P36507; -.
KO; K04369; -.
OMA; IAGWVCK; -.
OrthoDB; EOG091G0DEC; -.
PhylomeDB; P36507; -.
TreeFam; TF105137; -.
BRENDA; 2.7.12.2; 2681.
Reactome; R-HSA-112411; MAPK1 (ERK2) activation.
Reactome; R-HSA-445144; Signal transduction by L1.
Reactome; R-HSA-5210891; Uptake and function of anthrax toxins.
Reactome; R-HSA-5673000; RAF activation.
Reactome; R-HSA-5674135; MAP2K and MAPK activation.
Reactome; R-HSA-5674499; Negative feedback regulation of MAPK pathway.
Reactome; R-HSA-6802946; Signaling by moderate kinase activity BRAF mutants.
Reactome; R-HSA-6802948; Signaling by high-kinase activity BRAF mutants.
Reactome; R-HSA-6802949; Signaling by RAS mutants.
Reactome; R-HSA-6802952; Signaling by BRAF and RAF fusions.
Reactome; R-HSA-6802955; Paradoxical activation of RAF signaling by kinase inactive BRAF.
SignaLink; P36507; -.
SIGNOR; P36507; -.
ChiTaRS; MAP2K2; human.
EvolutionaryTrace; P36507; -.
GeneWiki; MAP2K2; -.
GenomeRNAi; 5605; -.
PMAP-CutDB; P36507; -.
PRO; PR:P36507; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000126934; -.
CleanEx; HS_MAP2K2; -.
ExpressionAtlas; P36507; baseline and differential.
Genevisible; P36507; HS.
GO; GO:0005911; C:cell-cell junction; IDA:UniProtKB.
GO; GO:0009898; C:cytoplasmic side of plasma membrane; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005769; C:early endosome; TAS:UniProtKB.
GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; NAS:UniProtKB.
GO; GO:0005925; C:focal adhesion; TAS:UniProtKB.
GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
GO; GO:0005770; C:late endosome; TAS:UniProtKB.
GO; GO:0005874; C:microtubule; IDA:UniProtKB.
GO; GO:0005739; C:mitochondrion; TAS:UniProtKB.
GO; GO:0005634; C:nucleus; TAS:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
GO; GO:0005778; C:peroxisomal membrane; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004708; F:MAP kinase kinase activity; IDA:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0030165; F:PDZ domain binding; IDA:UniProtKB.
GO; GO:0043539; F:protein serine/threonine kinase activator activity; IDA:UniProtKB.
GO; GO:0004674; F:protein serine/threonine kinase activity; TAS:Reactome.
GO; GO:0004712; F:protein serine/threonine/tyrosine kinase activity; TAS:UniProtKB.
GO; GO:0004713; F:protein tyrosine kinase activity; IEA:UniProtKB-KW.
GO; GO:0097110; F:scaffold protein binding; IPI:UniProtKB.
GO; GO:0000187; P:activation of MAPK activity; TAS:UniProtKB.
GO; GO:0070371; P:ERK1 and ERK2 cascade; TAS:Reactome.
GO; GO:0000165; P:MAPK cascade; TAS:Reactome.
GO; GO:0010629; P:negative regulation of gene expression; IGI:UniProtKB.
GO; GO:0036289; P:peptidyl-serine autophosphorylation; IDA:UniProtKB.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IMP:BHF-UCL.
GO; GO:1903800; P:positive regulation of production of miRNAs involved in gene silencing by miRNA; IMP:BHF-UCL.
GO; GO:0071902; P:positive regulation of protein serine/threonine kinase activity; IDA:UniProtKB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:BHF-UCL.
GO; GO:0035897; P:proteolysis in other organism; TAS:Reactome.
GO; GO:0042981; P:regulation of apoptotic process; IBA:GO_Central.
GO; GO:2000641; P:regulation of early endosome to late endosome transport; TAS:UniProtKB.
GO; GO:0090170; P:regulation of Golgi inheritance; TAS:UniProtKB.
GO; GO:0007346; P:regulation of mitotic cell cycle; IBA:GO_Central.
GO; GO:0032872; P:regulation of stress-activated MAPK cascade; TAS:UniProtKB.
InterPro; IPR011009; Kinase-like_dom_sf.
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; 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; ATP-binding; Cardiomyopathy;
Complete proteome; Cytoplasm; Direct protein sequencing;
Disease mutation; Ectodermal dysplasia; Kinase; Magnesium; Membrane;
Mental retardation; Metal-binding; Nucleotide-binding; Phosphoprotein;
Reference proteome; Serine/threonine-protein kinase; Transferase;
Tyrosine-protein kinase.
CHAIN 1 400 Dual specificity mitogen-activated
protein kinase kinase 2.
/FTId=PRO_0000086372.
DOMAIN 72 369 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 78 86 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
COMPBIAS 266 315 Pro-rich.
ACT_SITE 194 194 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 101 101 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
SITE 10 11 Cleavage; by anthrax lethal factor.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000244|PubMed:19413330}.
MOD_RES 23 23 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 222 222 O-acetylserine; by Yersinia yopJ;
alternate. {ECO:0000269|PubMed:17116858}.
MOD_RES 222 222 Phosphoserine; by RAF; alternate.
{ECO:0000269|PubMed:10409742,
ECO:0000269|PubMed:17116858}.
MOD_RES 226 226 O-acetylserine; by Yersinia yopJ;
alternate. {ECO:0000269|PubMed:17116858}.
MOD_RES 226 226 Phosphoserine; alternate.
{ECO:0000269|PubMed:17116858}.
MOD_RES 293 293 Phosphoserine.
{ECO:0000244|PubMed:18691976}.
MOD_RES 295 295 Phosphoserine.
{ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:20068231}.
MOD_RES 306 306 Phosphoserine.
{ECO:0000250|UniProtKB:Q02750}.
MOD_RES 394 394 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000269|Ref.3}.
MOD_RES 396 396 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
VARIANT 57 57 F -> C (in CFC4; dbSNP:rs121434497).
{ECO:0000269|PubMed:16439621}.
/FTId=VAR_035095.
VARIANT 57 57 F -> V (in CFC4; dbSNP:rs121434498).
{ECO:0000269|PubMed:18042262}.
/FTId=VAR_069781.
VARIANT 128 128 P -> Q (in CFC4; results in increased
kinase activity; dbSNP:rs267607230).
{ECO:0000269|PubMed:20358587}.
/FTId=VAR_069782.
VARIANT 134 134 Y -> H (in CFC4; dbSNP:rs121434499).
{ECO:0000269|PubMed:18042262}.
/FTId=VAR_069783.
CONFLICT 56 56 A -> R (in Ref. 6; AA sequence).
{ECO:0000305}.
HELIX 69 71 {ECO:0000244|PDB:1S9I}.
STRAND 72 80 {ECO:0000244|PDB:1S9I}.
STRAND 85 91 {ECO:0000244|PDB:1S9I}.
TURN 92 94 {ECO:0000244|PDB:1S9I}.
STRAND 97 103 {ECO:0000244|PDB:1S9I}.
HELIX 110 119 {ECO:0000244|PDB:1S9I}.
HELIX 120 122 {ECO:0000244|PDB:1S9I}.
STRAND 133 148 {ECO:0000244|PDB:1S9I}.
HELIX 155 161 {ECO:0000244|PDB:1S9I}.
STRAND 162 164 {ECO:0000244|PDB:1S9I}.
HELIX 167 186 {ECO:0000244|PDB:1S9I}.
HELIX 197 199 {ECO:0000244|PDB:1S9I}.
STRAND 200 202 {ECO:0000244|PDB:1S9I}.
STRAND 208 210 {ECO:0000244|PDB:1S9I}.
HELIX 217 222 {ECO:0000244|PDB:1S9I}.
HELIX 236 239 {ECO:0000244|PDB:1S9I}.
HELIX 246 262 {ECO:0000244|PDB:1S9I}.
HELIX 272 279 {ECO:0000244|PDB:1S9I}.
HELIX 318 327 {ECO:0000244|PDB:1S9I}.
TURN 335 337 {ECO:0000244|PDB:1S9I}.
HELIX 340 349 {ECO:0000244|PDB:1S9I}.
TURN 354 356 {ECO:0000244|PDB:1S9I}.
HELIX 360 364 {ECO:0000244|PDB:1S9I}.
HELIX 367 374 {ECO:0000244|PDB:1S9I}.
HELIX 379 386 {ECO:0000244|PDB:1S9I}.
SEQUENCE 400 AA; 44424 MW; 3401D522515C30A5 CRC64;
MLARRKPVLP ALTINPTIAE GPSPTSEGAS EANLVDLQKK LEELELDEQQ KKRLEAFLTQ
KAKVGELKDD DFERISELGA GNGGVVTKVQ HRPSGLIMAR KLIHLEIKPA IRNQIIRELQ
VLHECNSPYI VGFYGAFYSD GEISICMEHM DGGSLDQVLK EAKRIPEEIL GKVSIAVLRG
LAYLREKHQI MHRDVKPSNI LVNSRGEIKL CDFGVSGQLI DSMANSFVGT RSYMAPERLQ
GTHYSVQSDI WSMGLSLVEL AVGRYPIPPP DAKELEAIFG RPVVDGEEGE PHSISPRPRP
PGRPVSGHGM DSRPAMAIFE LLDYIVNEPP PKLPNGVFTP DFQEFVNKCL IKNPAERADL
KMLTNHTFIK RSEVEEVDFA GWLCKTLRLN QPGTPTRTAV


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