MAP2K2
entrez
5605
canonical
uniprot
P36507
canonical
ensembl
ENSG00000126934
resolver
ensp
ENSP00000262948
resolver
ensp
ENSP00000615919
resolver
enst
ENST00000262948
resolver
genesymbol
MAP2K2
resolver
genesymbol_syn
MEK2
resolver
genesymbol_syn
MKK2
resolver
genesymbol_syn
PRKMK2
resolver
hgnc
HGNC:6842
resolver
uniprot
B3KS97
resolver
uniprot_entry
B3KS97_HUMAN
resolver
uniprot_entry
MP2K2_HUMAN
resolver
amino_acid_sequence
MLARRKPVLPALTINPTIAEGPSPTSEGASEANLVDLQKKLEELELDEQQKKRLEAFLTQKAKVGELKDDDFERISELGAGNGGVVTKVQHRPSGLIMARKLIHLEIKPAIRNQIIRELQVLHECNSPYIVGFYGAFYSDGEISICMEHMDGGSLDQVLKEAKRIPEEILGKVSIAVLRGLAYLREKHQIMHRDVKPSNILVNSRGEIKLCDFGVSGQLIDSMANSFVGTRSYMAPERLQGTHYSVQSDIWSMGLSLVELAVGRYPIPPPDAKELEAIFGRPVVDGEEGEPHSISPRPRPPGRPVSGHGMDSRPAMAIFELLDYIVNEPPPKLPNGVFTPDFQEFVNKCLIKNPAERADLKMLTNHTFIKRSEVEEVDFAGWLCKTLRLNQPGTPTRTAV
uniprot
proteins
disease_involvement
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 intellectual disability. 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 variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
2.7.12.2
uniprot
proteins
function
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). Activates BRAF in a KSR1 or KSR2-dependent manner; by binding to KSR1 or KSR2 releases the inhibitory intramolecular interaction between KSR1 or KSR2 protein kinase and N-terminal domains which promotes KSR1 or KSR2-BRAF dimerization and BRAF activation (PubMed:29433126). {ECO:0000250|UniProtKB:Q63932, ECO:0000269|PubMed:29433126}.
uniprot
proteins
mass_dalton
44424
uniprot
proteins
post_translational_modification
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: (Microbial infection) 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}.
uniprot
proteins
protein_family
MAP kinase kinase subfamily
uniprot
proteins
protein_family
Protein kinase superfamily
uniprot
proteins
protein_family
STE Ser/Thr protein kinase family
uniprot
proteins
pubmed
10409742
uniprot
proteins
pubmed
11104681
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16439621
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
17116858
uniprot
proteins
pubmed
18042262
uniprot
proteins
pubmed
18088087
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
18691976
uniprot
proteins
pubmed
19369195
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19447520
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20358587
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
22538822
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
29433126
uniprot
proteins
pubmed
8388392
uniprot
proteins
pubmed
9563949
uniprot
proteins
sequence_length
400
uniprot
proteins
subcellular_location
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}.
uniprot
proteins