(data stored in ACNUC8465 zone)

SWISSPROT: 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   11-DEC-2019, entry version 121.
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}.
DR   EMBL; L28703; AAA75576.1; -; mRNA.
DR   RefSeq; NP_990719.1; NM_205388.1.
DR   SMR; Q90891; -.
DR   BioGrid; 676605; 1.
DR   STRING; 9031.ENSGALP00000001932; -.
DR   iPTMnet; Q90891; -.
DR   PaxDb; Q90891; -.
DR   PRIDE; Q90891; -.
DR   GeneID; 396349; -.
DR   KEGG; gga:396349; -.
DR   CTD; 5605; -.
DR   eggNOG; KOG0581; Eukaryota.
DR   eggNOG; ENOG410XQ5A; LUCA.
DR   HOGENOM; HOG000234206; -.
DR   InParanoid; Q90891; -.
DR   KO; K04369; -.
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: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;
DR   PRODOM; Q90891.
DR   SWISS-2DPAGE; Q90891.
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   NP_BIND         76..84
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   COMPBIAS        264..313
FT                   /note="Pro-rich"
FT   ACT_SITE        192
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         99
FT                   /note="ATP"
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
//

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