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P36507 (MP2K2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 164. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Dual specificity mitogen-activated protein kinase kinase 2

Short name=MAP kinase kinase 2
Short name=MAPKK 2
EC=2.7.12.2
Alternative name(s):
ERK activator kinase 2
MAPK/ERK kinase 2
Short name=MEK 2
Gene names
Name:MAP2K2
Synonyms:MEK2, MKK2, PRKMK2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length400 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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.

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Subunit structure

Interacts with MORG1 By similarity. Interacts with SGK1. Ref.12

Post-translational modification

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. Ref.3 Ref.4

Acetylation of Ser-222 and Ser-226 by Yersinia yopJ prevents phosphorylation and activation, thus blocking the MAPK signaling pathway. Ref.4

Involvement in 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.18 Ref.19 Ref.20

Sequence similarities

Belongs to the protein kinase superfamily. STE Ser/Thr protein kinase family. MAP kinase kinase subfamily.

Contains 1 protein kinase domain.

Ontologies

Keywords
   DiseaseCardiomyopathy
Disease mutation
Ectodermal dysplasia
Mental retardation
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
Tyrosine-protein kinase
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processERK1 and ERK2 cascade

Traceable author statement. Source: Reactome

Fc-epsilon receptor signaling pathway

Traceable author statement. Source: Reactome

MAPK cascade

Traceable author statement. Source: Reactome

MyD88-dependent toll-like receptor signaling pathway

Traceable author statement. Source: Reactome

MyD88-independent toll-like receptor signaling pathway

Traceable author statement. Source: Reactome

Ras protein signal transduction

Traceable author statement. Source: Reactome

TRIF-dependent toll-like receptor signaling pathway

Traceable author statement. Source: Reactome

activation of MAPK activity

Traceable author statement PubMed 19565474. Source: UniProtKB

activation of MAPKK activity

Traceable author statement. Source: Reactome

axon guidance

Traceable author statement. Source: Reactome

epidermal growth factor receptor signaling pathway

Traceable author statement. Source: Reactome

fibroblast growth factor receptor signaling pathway

Traceable author statement. Source: Reactome

innate immune response

Traceable author statement. Source: Reactome

insulin receptor signaling pathway

Traceable author statement. Source: Reactome

neurotrophin TRK receptor signaling pathway

Traceable author statement. Source: Reactome

peptidyl-serine autophosphorylation

Inferred from direct assay Ref.1. Source: UniProtKB

positive regulation of cell motility

Inferred from electronic annotation. Source: Ensembl

positive regulation of protein serine/threonine kinase activity

Inferred from direct assay Ref.1. Source: UniProtKB

regulation of Golgi inheritance

Traceable author statement PubMed 19565474. Source: UniProtKB

regulation of early endosome to late endosome transport

Traceable author statement PubMed 19565474. Source: UniProtKB

regulation of stress-activated MAPK cascade

Traceable author statement PubMed 19565474. Source: UniProtKB

small GTPase mediated signal transduction

Traceable author statement. Source: Reactome

stress-activated MAPK cascade

Traceable author statement. Source: Reactome

toll-like receptor 10 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor 2 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor 3 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor 4 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor 5 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor 9 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor TLR1:TLR2 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor TLR6:TLR2 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor signaling pathway

Traceable author statement. Source: Reactome

   Cellular_componentGolgi apparatus

Inferred from direct assay PubMed 21615688. Source: UniProtKB

cell cortex

Inferred from electronic annotation. Source: Ensembl

cell-cell junction

Inferred from direct assay PubMed 21615688. Source: UniProtKB

cytoplasm

Inferred from direct assay. Source: HPA

cytoplasmic side of plasma membrane

Inferred from direct assay PubMed 21615688. Source: UniProtKB

cytosol

Traceable author statement PubMed 19565474. Source: UniProtKB

early endosome

Traceable author statement PubMed 19565474. Source: UniProtKB

endoplasmic reticulum

Inferred from direct assay PubMed 21615688. Source: UniProtKB

extracellular region

Non-traceable author statement Ref.1. Source: UniProtKB

focal adhesion

Traceable author statement PubMed 19565474. Source: UniProtKB

late endosome

Traceable author statement PubMed 19565474. Source: UniProtKB

microtubule

Inferred from direct assay PubMed 21615688. Source: UniProtKB

mitochondrion

Traceable author statement PubMed 19565474. Source: UniProtKB

nucleus

Traceable author statement PubMed 19565474. Source: UniProtKB

perinuclear region of cytoplasm

Inferred from direct assay PubMed 21615688. Source: UniProtKB

peroxisomal membrane

Inferred from direct assay PubMed 21525035. Source: UniProtKB

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

MAP kinase kinase activity

Inferred from direct assay Ref.1. Source: UniProtKB

PDZ domain binding

Inferred from direct assay PubMed 21615688. Source: UniProtKB

protein serine/threonine kinase activator activity

Inferred from direct assay Ref.1. Source: UniProtKB

protein serine/threonine kinase activity

Traceable author statement. Source: Reactome

protein serine/threonine/tyrosine kinase activity

Traceable author statement PubMed 19565474. Source: UniProtKB

protein tyrosine kinase activity

Inferred from electronic annotation. Source: UniProtKB-KW

scaffold protein binding

Inferred from physical interaction PubMed 21615688. Source: UniProtKB

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 400400Dual specificity mitogen-activated protein kinase kinase 2
PRO_0000086372

Regions

Domain72 – 369298Protein kinase
Nucleotide binding78 – 869ATP By similarity
Compositional bias266 – 31550Pro-rich

Sites

Active site1941Proton acceptor By similarity
Binding site1011ATP By similarity
Site10 – 112Cleavage; by anthrax lethal factor

Amino acid modifications

Modified residue11N-acetylmethionine Ref.11
Modified residue2221O-acetylserine; by Yersinia yopJ; alternate
Modified residue2221Phosphoserine; by RAF; alternate Ref.4
Modified residue2261O-acetylserine; by Yersinia yopJ; alternate
Modified residue2261Phosphoserine; alternate Ref.4
Modified residue2931Phosphoserine Ref.9
Modified residue2951Phosphoserine Ref.9 Ref.15
Modified residue3941Phosphothreonine Ref.3 Ref.10 Ref.15 Ref.17
Modified residue3961Phosphothreonine Ref.10 Ref.17

Natural variations

Natural variant571F → C in CFC4. Ref.18
VAR_035095
Natural variant571F → V in CFC4. Ref.19
VAR_069781
Natural variant1281P → Q in CFC4; results in increased kinase activity. Ref.20
VAR_069782
Natural variant1341Y → H in CFC4. Ref.19
VAR_069783

Secondary structure

.............................................. 400
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P36507 [UniParc].

Last modified June 1, 1994. Version 1.
Checksum: 3401D522515C30A5

FASTA40044,424
        10         20         30         40         50         60 
MLARRKPVLP ALTINPTIAE GPSPTSEGAS EANLVDLQKK LEELELDEQQ KKRLEAFLTQ 

        70         80         90        100        110        120 
KAKVGELKDD DFERISELGA GNGGVVTKVQ HRPSGLIMAR KLIHLEIKPA IRNQIIRELQ 

       130        140        150        160        170        180 
VLHECNSPYI VGFYGAFYSD GEISICMEHM DGGSLDQVLK EAKRIPEEIL GKVSIAVLRG 

       190        200        210        220        230        240 
LAYLREKHQI MHRDVKPSNI LVNSRGEIKL CDFGVSGQLI DSMANSFVGT RSYMAPERLQ 

       250        260        270        280        290        300 
GTHYSVQSDI WSMGLSLVEL AVGRYPIPPP DAKELEAIFG RPVVDGEEGE PHSISPRPRP 

       310        320        330        340        350        360 
PGRPVSGHGM DSRPAMAIFE LLDYIVNEPP PKLPNGVFTP DFQEFVNKCL IKNPAERADL 

       370        380        390        400 
KMLTNHTFIK RSEVEEVDFA GWLCKTLRLN QPGTPTRTAV 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and characterization of two distinct human extracellular signal-regulated kinase activator kinases, MEK1 and MEK2."
Zheng C.-F., Guan K.-L.
J. Biol. Chem. 268:11435-11439(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Muscle and Skin.
[3]Bienvenut W.V., Zebisch A., Kolch W.
Submitted (DEC-2008) to UniProtKB
Cited for: 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, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Colon carcinoma.
[4]"Acetylation of MEK2 and I kappa B kinase (IKK) activation loop residues by YopJ inhibits signaling."
Mittal R., Peak-Chew S.Y., McMahon H.T.
Proc. Natl. Acad. Sci. U.S.A. 103:18574-18579(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 210-231, INACTIVATION BY YERSINIA YOPJ, PHOSPHORYLATION AT SER-222 AND SER-226, ACETYLATION AT SER-222 AND SER-226, IDENTIFICATION BY MASS SPECTROMETRY.
[5]"Proteolytic inactivation of MAP-kinase-kinase by anthrax lethal factor."
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.
Science 280:734-737(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: CLEAVAGE BY ANTHRAX LETHAL FACTOR.
[6]"Susceptibility of mitogen-activated protein kinase kinase family members to proteolysis by anthrax lethal factor."
Vitale G., Bernardi L., Napolitani G., Mock M., Montecucco C.
Biochem. J. 352:739-745(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: CLEAVAGE BY ANTHRAX LETHAL FACTOR.
[7]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[8]"Phosphoproteome of resting human platelets."
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A.
J. Proteome Res. 7:526-534(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Platelet.
[9]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-293 AND SER-295, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-394 AND THR-396, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"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."
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.
J. Hepatol. 51:67-76(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SGK1.
[13]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[15]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
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.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-295 AND THR-394, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[16]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-394 AND THR-396, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]"Germline mutations in genes within the MAPK pathway cause cardio-facio-cutaneous syndrome."
Rodriguez-Viciana P., Tetsu O., Tidyman W.E., Estep A.L., Conger B.A., Cruz M.S., McCormick F., Rauen K.A.
Science 311:1287-1290(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CFC4 CYS-57.
[19]"Mutation and phenotypic spectrum in patients with cardio-facio-cutaneous and Costello syndrome."
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. expand/collapse author list , Schulze A., Seemanova E., Seidel H., Spranger S., Tuysuz B., Uhrig S., Wieczorek D., Kutsche K., Zenker M.
Clin. Genet. 73:62-70(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CFC4 VAL-57 AND HIS-134.
[20]"Molecular and functional analysis of a novel MEK2 mutation in cardio-facio-cutaneous syndrome: transmission through four generations."
Rauen K.A., Tidyman W.E., Estep A.L., Sampath S., Peltier H.M., Bale S.J., Lacassie Y.
Am. J. Med. Genet. A 152:807-814(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CFC4 GLN-128, CHARACTERIZATION OF VARIANT CFC4 GLN-128.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L11285 mRNA. No translation available.
BC000471 mRNA. Translation: AAH00471.1.
BC018645 mRNA. Translation: AAH18645.1.
PIRA46723.
RefSeqNP_109587.1. NM_030662.3.
UniGeneHs.465627.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1S9IX-ray3.20A/B55-400[»]
4H3QX-ray2.20B4-16[»]
ProteinModelPortalP36507.
SMRP36507. Positions 60-393.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111591. 20 interactions.
DIPDIP-29119N.
IntActP36507. 13 interactions.
MINTMINT-99667.
STRING9606.ENSP00000262948.

Chemistry

BindingDBP36507.
ChEMBLCHEMBL2964.
GuidetoPHARMACOLOGY2063.

PTM databases

PhosphoSiteP36507.

Polymorphism databases

DMDM547915.

2D gel databases

REPRODUCTION-2DPAGEIPI00003783.

Proteomic databases

PaxDbP36507.
PeptideAtlasP36507.
PRIDEP36507.

Protocols and materials databases

DNASU5605.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000262948; ENSP00000262948; ENSG00000126934.
GeneID5605.
KEGGhsa:5605.
UCSCuc002lzj.3. human.

Organism-specific databases

CTD5605.
GeneCardsGC19M004090.
H-InvDBHIX0033655.
HGNCHGNC:6842. MAP2K2.
HPACAB003835.
HPA051993.
MIM601263. gene.
615280. phenotype.
neXtProtNX_P36507.
Orphanet1340. Cardiofaciocutaneous syndrome.
PharmGKBPA30587.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000234206.
HOVERGENHBG108518.
InParanoidP36507.
KOK04369.
OMARLKQPST.
OrthoDBEOG7HF1KZ.
PhylomeDBP36507.
TreeFamTF105137.

Enzyme and pathway databases

BRENDA2.7.12.2. 2681.
ReactomeREACT_111045. Developmental Biology.
REACT_111102. Signal Transduction.
REACT_116125. Disease.
REACT_6782. TRAF6 Mediated Induction of proinflammatory cytokines.
REACT_6900. Immune System.
SignaLinkP36507.

Gene expression databases

ArrayExpressP36507.
BgeeP36507.
CleanExHS_MAP2K2.
GenevestigatorP36507.

Family and domain databases

InterProIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSMAP2K2. human.
EvolutionaryTraceP36507.
GeneWikiMAP2K2.
GenomeRNAi5605.
NextBio21780.
PMAP-CutDBP36507.
PROP36507.
SOURCESearch...

Entry information

Entry nameMP2K2_HUMAN
AccessionPrimary (citable) accession number: P36507
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: April 16, 2014
This is version 164 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM