MP2K2_CHICK
ID MP2K2_CHICK Reviewed; 398 AA.
AC Q90891;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 131.
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=MEK2, MKK2, PRKMK2;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=White leghorn; TISSUE=Liver;
RX PubMed=9398267; DOI=10.1021/bi971946x;
RA Wang H., Meury L., Morais R.;
RT "Cloning and characterization of cDNAs encoding chicken mitogen-activated
RT protein kinase kinase type 2, MEK2: downregulation of MEK2 in response to
RT inhibition of mitochondrial DNA expression.";
RL Biochemistry 36:15371-15380(1997).
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 Activates the ERK1 and ERK2 MAP kinases (By similarity). {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: Activated by phosphorylation on Ser/Thr catalyzed by MAP kinase
CC kinase kinases (RAF). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. MAP kinase kinase subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; L28703; AAA75576.1; -; mRNA.
DR RefSeq; NP_990719.1; NM_205388.1.
DR AlphaFoldDB; Q90891; -.
DR SMR; Q90891; -.
DR BioGRID; 676605; 1.
DR STRING; 9031.ENSGALP00000001932; -.
DR iPTMnet; Q90891; -.
DR PaxDb; Q90891; -.
DR GeneID; 396349; -.
DR KEGG; gga:396349; -.
DR CTD; 5605; -.
DR VEuPathDB; HostDB:geneid_396349; -.
DR eggNOG; KOG0581; Eukaryota.
DR InParanoid; Q90891; -.
DR OrthoDB; 688282at2759; -.
DR PhylomeDB; Q90891; -.
DR BRENDA; 2.7.12.2; 1306.
DR Reactome; R-GGA-451478; ERK activation.
DR PRO; PR:Q90891; -.
DR Proteomes; UP000000539; 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..398
FT /note="Dual specificity mitogen-activated protein kinase
FT kinase 2"
FT /id="PRO_0000086375"
FT DOMAIN 70..367
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 192
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 76..84
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 99
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 220
FT /note="Phosphoserine; by RAF"
FT /evidence="ECO:0000250"
FT MOD_RES 224
FT /note="Phosphoserine; by RAF"
FT /evidence="ECO:0000250"
SQ SEQUENCE 398 AA; 44078 MW; 84BDD4C9797D62D1 CRC64;
MPAKRKPVLP ALTITPSPAE GPGPGGSAEA NLVDLQKKLE ELELDEQQKK RLEAFLTQKA
KVGELKDDDF ERISELGAGN GGVVTKVQHK PSGLIMARKL IHLEIKPAIR NQIIRELQVL
HECNSPYIVG FYGAFYSDGE ISICMEHMDG GSLDQVLKEA KRIPEEILGK VSIAVLRGLA
YLREKHQIMH RDVKPSNILV NSRGEIKLCD FGVSGQLIDS MANSFVGTRS YMSPERLQGT
HYSVQSDIWS MGLSLVELSI GRYPIPPPDS KELEAIFGRP VVDGAEGESH SVSPWARPPG
RPISGHGMDS RPAMAIFELL DYIVNEPPPK LPNGVFTQDF QEFVNKCLIK NPAERADLKM
LMNHTFIKRS EVEEVDFAGW LCKTLRLNQP STPTRAAV
