EKS-RAN-00225
Eukaryotic Protein Kinase & Protein Phosphatase Database
TagContent
EKPD IDEKS-RAN-00225
Classification
Group/FamilyScoreE-ValueStartEndDomain Length
STE/STE7386.39.0E-11669361293
StatusReviewed
Ensembl ProteinENSRNOP00000013933
UniProt AccessionQ01986; Q5EBD5;
Protein NameDual specificity mitogen-activated protein kinase kinase 1
Protein Synonyms/Alias MAP kinase kinase 1; MAPKK 1; ERK activator kinase 1; MAPK/ERK kinase 1; MEK 1;
Gene NameMap2k1
Gene Synonyms/Alias Map2k1; Mek1, Prkmk1;
Ensembl Information
Ensembl Gene IDEnsembl Protein IDEnsembl Transcript ID
ENSRNOG00000010176ENSRNOP00000013933ENSRNOT00000013933
OrganismRattus norvegicus
Functional DescriptionDual specificity protein kinase which acts as anessential component of the MAP kinase signal transduction pathway. Binding of extracellular ligands such as growth factors, cytokines and hormones to their cell-surface receptors activates RAS and this initiates RAF1 activation. RAF1 then further activates the dual-specificity protein kinases MAP2K1/MEK1 and MAP2K2/MEK2. Both MAP2K1/MEK1 and MAP2K2/MEK2 function specifically in the MAPK/ERK cascade, and catalyze the concomitant phosphorylation of a threonine and a tyrosine residue in a Thr-Glu-Tyr sequence located in the extracellular signal-regulated kinases MAPK3/ERK1 and MAPK1/ERK2, leading to their activation and further transduction of the signal within the MAPK/ERK cascade. Depending on the cellular context, this pathway mediates diverse biological functions such as cell growth, adhesion, survival and differentiation, predominantly through the regulation of transcription, metabolism and cytoskeletal rearrangements. One target of the MAPK/ERK cascade is peroxisome proliferator- activated receptor gamma (PPARG), a nuclear receptor that promotes differentiation and apoptosis. MAP2K1/MEK1 has been shown to export PPARG from the nucleus. The MAPK/ERK cascade is also involved in the regulation of endosomal dynamics, including lysosome processing and endosome cycling through the perinuclear recycling compartment (PNRC), as well as in the fragmentation of the Golgi apparatus during mitosis.
Protein Length393
Protein Sequence
(FASTA)
MPKKKPTPIQ LNPAPDGSAV NGTSSAETNL EALQKKLEEL ELDEQQRKRL EAFLTQKQKV 60
GELKDDDFEK ISELGAGNGG VVFKVSHKPS GLVMARKLIH LEIKPAIRNQ IIRELQVLHE 120
CNSPYIVGFY GAFYSDGEIS ICMEHMDGGS LDQVLKKAGR IPEQILGKVS IAVIKGLTYL 180
REKHKIMHRD VKPSNILVNS RGEIKLCDFG VSGQLIDSMA NSFVGTRSYM SPERLQGTHY 240
SVQSDIWSMG LSLVEMAVGR YPIPPPDAKE LELLFGCQVE GDAAETPPRP RTPGRPLSSY 300
GMDSRPPMAI FELLDYIVNE PPPKLPSGVF SLEFQDFVNK CLIKNPAERA DLKQLMVHAF 360
IKRSDAEEVD FAGWLCSTIG LNQPSTPTHA ASI 393
Nucleotide Sequence
(FASTA)
ATGCCCAAGA AGAAGCCGAC GCCCATCCAG CTGAACCCGG CCCCCGATGG CTCCGCGGTT 60
AACGGGACCA GCTCGGCCGA GACCAACCTG GAGGCCTTGC AGAAGAAGCT GGAGGAGCTG 120
GAGCTGGACG AGCAGCAGCG GAAGCGCCTT GAGGCCTTTC TGACGCAGAA GCAGAAGGTG 180
GGAGAGTTGA AGGATGATGA CTTTGAGAAG ATCAGTGAAC TGGGGGCTGG CAATGGTGGA 240
GTGGTGTTCA AGGTCTCCCA CAAGCCATCT GGCCTGGTTA TGGCTAGGAA GCTAATTCAC 300
CTGGAGATCA AACCCGCAAT CCGGAACCAG ATCATCCGGG AGCTGCAGGT GCTGCATGAG 360
TGCAACTCCC CGTACATAGT GGGCTTCTAC GGGGCCTTCT ACAGTGACGG CGAGATCAGC 420
ATCTGCATGG AGCACATGGA TGGTGGGTCC TTGGATCAAG TGCTGAAGAA AGCTGGAAGA 480
ATTCCTGAGC AAATTTTAGG AAAAGTCAGC ATCGCTGTGA TAAAAGGCCT GACATATCTA 540
CGAGAGAAGC ACAAGATTAT GCACAGAGAT GTCAAGCCTT CCAACATTCT AGTGAACTCA 600
CGTGGGGAGA TCAAACTCTG CGATTTTGGG GTCAGCGGGC AGCTAATTGA CTCCATGGCC 660
AACTCCTTCG TGGGAACAAG GTCCTACATG TCGCCTGAGA GACTCCAGGG GACTCACTAC 720
TCTGTGCAGT CGGACATCTG GAGCATGGGG CTCTCTCTGG TGGAGATGGC AGTTGGAAGA 780
TACCCCATTC CTCCTCCTGA TGCCAAGGAG CTGGAGCTGC TGTTTGGATG CCAGGTGGAA 840
GGAGACGCGG CCGAAACGCC ACCCAGGCCA AGGACCCCTG GGAGGCCCCT CAGCTCATAT 900
GGAATGGATA GCCGACCTCC CATGGCAATT TTTGAGTTGT TGGATTACAT CGTCAATGAG 960
CCTCCTCCAA AACTGCCCAG TGGAGTATTC AGTCTGGAAT TTCAGGATTT TGTGAATAAG 1020
TGCTTAATAA AGAACCCTGC AGAGAGAGCA GATCTGAAGC AGCTCATGGT ACATGCTTTC 1080
ATCAAGAGAT CTGATGCCGA GGAGGTAGAC TTCGCAGGCT GGCTCTGCTC CACCATTGGG 1140
CTTAACCAGC CCAGCACACC AACCCACGCT GCCAGCATCT GA 1182
Domain Profile
S: 2     ekleelGaGnggvVekvlhkksgkilavKtirleikkeeqkqilrelevlkkssnspyiv  61
         ek++elGaGnggvV kv+hk+sg ++a+K i+leik+++++qi+rel+vl+++ nspyiv
Q: 69    EKISELGAGNGGVVFKVSHKPSGLVMARKLIHLEIKPAIRNQIIRELQVLHEC-NSPYIV  127
         799**************************************************.******
S: 62    kfyGafvsegdvsicmelmdgtsldkvlkkvlekkkripekvlgkiavavvkaleylkek  121
         +fyGaf+s+g++sicme+mdg+sld+vlkk    ++ripe++lgk+++av+k+l+yl+ek
Q: 128   GFYGAFYSDGEISICMEHMDGGSLDQVLKK----AGRIPEQILGKVSIAVIKGLTYLREK  183
         *****************************9....8*************************
S: 122   lkiiHRDvKPsNiLvnskGevKlCDFGvsgqlvdsiAksavGtksYmaPEriegkkkYsv  181
         +ki+HRDvKPsNiLvns+Ge+KlCDFGvsgql+ds+A+s+vGt+sYm+PEr++g ++Ysv
Q: 184   HKIMHRDVKPSNILVNSRGEIKLCDFGVSGQLIDSMANSFVGTRSYMSPERLQG-THYSV  242
         ******************************************************.*****
S: 182   ksdvWslGltlvelatgrypyeklke..................................  207
         +sd+Ws+Gl+lve+a+gryp++++++                                  
Q: 243   QSDIWSMGLSLVEMAVGRYPIPPPDAkelellfgcqvegdaaetpprprtpgrplssygm  302
         ************************999*********************************
S: 208   .......ilellkaivneeppklpeeefseefqefvskClkkdekeRpklkellkhafi  259
                i+ell++ivne+ppklp+  fs efq+fv+kCl+k+++eR++lk+l+ hafi
Q: 303   dsrppmaIFELLDYIVNEPPPKLPSGVFSLEFQDFVNKCLIKNPAERADLKQLMVHAFI  361
         *********************************************************97
Domain Sequence
(FASTA)
EKISELGAGN GGVVFKVSHK PSGLVMARKL IHLEIKPAIR NQIIRELQVL HECNSPYIVG 60
FYGAFYSDGE ISICMEHMDG GSLDQVLKKA GRIPEQILGK VSIAVIKGLT YLREKHKIMH 120
RDVKPSNILV NSRGEIKLCD FGVSGQLIDS MANSFVGTRS YMSPERLQGT HYSVQSDIWS 180
MGLSLVEMAV GRYPIPPPDA KELELLFGCQ VEGDAAETPP RPRTPGRPLS SYGMDSRPPM 240
AIFELLDYIV NEPPPKLPSG VFSLEFQDFV NKCLIKNPAE RADLKQLMVH AFI 293
KeywordATP-binding; Complete proteome; Cytoplasm; Cytoskeleton; Direct protein sequencing; Kinase; Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome; Serine/threonine-protein kinase; Transferase; Tyrosine-protein kinase.
Sequence SourceEnsembl
Orthology
Ortholog group
Ailuropoda melanoleuca"; ?>Bos taurus"; ?>Caenorhabditis elegans"; ?>Callithrix jacchus"; ?>Canis familiaris"; ?>Cavia porcellus"; ?>Ciona intestinalis"; ?>Ciona savignyi"; ?>Danio rerio"; ?>Drosophila melanogaster"; ?>Equus caballus"; ?>Felis catus"; ?>Gadus morhua"; ?>Gallus gallus"; ?>Gasterosteus aculeatus"; ?>Gorilla gorilla"; ?>Homo sapiens"; ?>Latimeria chalumnae"; ?>Loxodonta africana"; ?>Macaca mulatta"; ?>Macropus eugenii"; ?>Meleagris gallopavo"; ?>Monodelphis domestica"; ?>Mus musculus"; ?>Mustela putorius furo"; ?>Myotis lucifugus"; ?>Nomascus leucogenys"; ?>Ochotona princeps"; ?>Oreochromis niloticus"; ?>Ornithorhynchus anatinus"; ?>Oryctolagus cuniculus"; ?>Oryzias latipes"; ?>Otolemur garnettii"; ?>Pan troglodytes"; ?>Pelodiscus sinensis"; ?>Pongo abelii"; ?>Pteropus vampyrus"; ?>Taeniopygia guttata"; ?>Tarsius syrichta"; ?>Tetraodon nigroviridis"; ?>Tupaia belangeri"; ?>Xenopus tropicalis"; ?>Xiphophorus maculatus"; ?>Schizosaccharomyces pombe"; ?>
EKS-AIM-00209
EKS-BOT-00227
EKS-CAE-00202
EKS-CAJ-00234
EKS-CAF-00233
EKS-CAP-00253
EKS-CII-00136
EKS-CIS-00012
EKS-DAR-00542
EKS-DRM-00116
EKS-EQC-00219
EKS-FEC-00212
EKS-GAM-00131
EKS-GAG-00189
EKS-GAA-00280
EKS-GOG-00224
EKS-HOS-00234
EKS-LAC-00239
EKS-LOA-00226
EKS-MAM-00229
EKS-MAE-00004
EKS-MEG-00177
EKS-MOD-00225
EKS-MUM-00232
EKS-MUP-00225
EKS-MYL-00228
EKS-NOL-00211
EKS-OCP-00006
EKS-ORN-00296
EKS-ORA-00198
EKS-ORC-00204
EKS-ORL-00274
EKS-OTG-00232
EKS-PAT-00216
EKS-PES-00202
EKS-POA-00220
EKS-PTV-00008
EKS-TAG-00243
EKS-TAS-00005
EKS-TEN-00286
EKS-TUB-00009
EKS-XET-00304
EKS-XIM-00289
EKS-SCP-00009
Gene Ontology
GO:0033267; C:axon part
GO:0005938; C:cell cortex
GO:0005829; C:cytosol
GO:0032839; C:dendrite cytoplasm
GO:0005769; C:early endosome
GO:0005925; C:focal adhesion
GO:0005794; C:Golgi apparatus
GO:0005770; C:late endosome
GO:0005739; C:mitochondrion
GO:0005634; C:nucleus
GO:0043204; C:perikaryon
GO:0048471; C:perinuclear region of cytoplasm
GO:0005886; C:plasma membrane
GO:0005816; C:spindle pole body
GO:0005524; F:ATP binding
GO:0004708; F:MAP kinase kinase activity
GO:0031435; F:mitogen-activated protein kinase kinase kinase binding
GO:0004674; F:protein serine/threonine kinase activity
GO:0004713; F:protein tyrosine kinase activity
GO:0004728; F:receptor signaling protein tyrosine phosphatase activity
GO:0007050; P:cell cycle arrest
GO:0048870; P:cell motility
GO:0008283; P:cell proliferation
GO:0090398; P:cellular senescence
GO:0048313; P:Golgi inheritance
GO:0030216; P:keratinocyte differentiation
GO:0060711; P:labyrinthine layer development
GO:0032402; P:melanosome transport
GO:0007067; P:mitosis
GO:0008285; P:negative regulation of cell proliferation
GO:0034111; P:negative regulation of homotypic cell-cell adhesion
GO:0048812; P:neuron projection morphogenesis
GO:0060674; P:placenta blood vessel development
GO:0045597; P:positive regulation of cell differentiation
GO:0030335; P:positive regulation of cell migration
GO:0032320; P:positive regulation of Ras GTPase activity
GO:0046579; P:positive regulation of Ras protein signal transduction
GO:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter
GO:0051291; P:protein heterooligomerization
GO:2000641; P:regulation of early endosome to late endosome transport
GO:0090170; P:regulation of Golgi inheritance
GO:0032872; P:regulation of stress-activated MAPK cascade
GO:0003056; P:regulation of vascular smooth muscle contraction
GO:0048678; P:response to axon injury
GO:0051384; P:response to glucocorticoid stimulus
GO:0006979; P:response to oxidative stress
GO:0047496; P:vesicle transport along microtubule
KEGG
rno:170851;
InterPros
IPR011009; Kinase-like_dom.
IPR000719; Prot_kinase_cat_dom.
IPR017441; Protein_kinase_ATP_BS.
IPR002290; Ser/Thr_dual-sp_kinase_dom.
IPR008271; Ser/Thr_kinase_AS.
Pfam
PF00069; Pkinase; 1.
SMARTs
SM00220; S_TKc; 1.
Prosites
PS00107; PROTEIN_KINASE_ATP; 1.
PS50011; PROTEIN_KINASE_DOM; 1.
PS00108; PROTEIN_KINASE_ST; 1.
Prints
Created Date20-Feb-2013