MP2K2_CYPCA
ID MP2K2_CYPCA Reviewed; 397 AA.
AC Q90321;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Dual specificity mitogen-activated protein kinase kinase 2;
DE Short=MAP kinase kinase 2;
DE Short=MAPKK 2;
DE EC=2.7.12.2;
DE AltName: Full=ERK activator kinase 2;
DE AltName: Full=MAPK/ERK kinase 2;
DE Short=MEK2;
GN Name=map2k2; Synonyms=mkk;
OS Cyprinus carpio (Common carp).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Cyprinidae; Cyprininae; Cyprinus.
OX NCBI_TaxID=7962;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=8312367; DOI=10.1016/0167-4889(94)90140-6;
RA Huang C.-J., Lee M.-S., Chang G.-D., Huang F.-L., Lo T.-B.;
RT "Molecular cloning and sequencing of a carp cDNA encoding mitogen-activated
RT protein kinase kinase.";
RL Biochim. Biophys. Acta 1220:223-225(1994).
CC -!- FUNCTION: Catalyzes the concomitant phosphorylation of a threonine and
CC a tyrosine residue in a Thr-Glu-Tyr sequence located in MAP kinases.
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.12.2;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.12.2;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.12.2;
CC -!- PTM: Phosphorylation on Ser/Thr by MAP kinase kinase kinases (RAF)
CC regulates positively the kinase activity. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. MAP kinase kinase subfamily. {ECO:0000305}.
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DR EMBL; L23935; AAA19788.1; -; mRNA.
DR PIR; S41054; S41054.
DR AlphaFoldDB; Q90321; -.
DR SMR; Q90321; -.
DR BRENDA; 2.7.12.2; 1195.
DR Proteomes; UP000694384; Unplaced.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004708; F:MAP kinase kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0004713; F:protein tyrosine kinase activity; IEA:UniProtKB-KW.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase;
KW Tyrosine-protein kinase.
FT CHAIN 1..397
FT /note="Dual specificity mitogen-activated protein kinase
FT kinase 2"
FT /id="PRO_0000086376"
FT DOMAIN 69..366
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 284..306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 191
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 75..83
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 98
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 219
FT /note="Phosphoserine; by RAF"
FT /evidence="ECO:0000250"
FT MOD_RES 223
FT /note="Phosphoserine; by RAF"
FT /evidence="ECO:0000250"
SQ SEQUENCE 397 AA; 44147 MW; C510FF921BF65EDF CRC64;
MAPKRRPVPL IIAPTGEGQS TNIDAASEAN LEALQRKLGE LDLDEQQRKR LEAFLTQKAQ
VGELKDEDFD PICELGAGNG GVVHKVRHKP SRLVMARKLI HLEIKPAIRN QIIRELQVLH
ECNSPYIVGF YGAFYSDGEI SICMEHMDGG SLDQVLKEAR RIPEEILGKV SIAVLRGLVY
LREKHQIMHR DVKPSNILVN SRGEIKLCDF GVSGQLIDSM ANSFVGTRSY MSPERLQGTH
YSVQSDVWSM GLSLVELAIG RFPIPPPDAK ELEAIFGRPV LDKGGAEGHS MSPRQRPPGR
PVSGHGMDSR PAMAIFELLD YIVNEPPPKL PHGVFTTDFE EFVMKCLMKN PADRADLKML
MGHTFIKRAE VEEVDFAGWM CKTMGLPQPS TPTHSAE
