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MP2K3_XENLA
ID   MP2K3_XENLA             Reviewed;          62 AA.
AC   P39746;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   25-MAY-2022, entry version 82.
DE   RecName: Full=Dual specificity mitogen-activated protein kinase kinase 3;
DE            Short=MAP kinase kinase 3;
DE            Short=MAPKK 3;
DE            EC=2.7.12.2;
DE   AltName: Full=MAPK-ERK kinase 3;
DE   Flags: Fragment;
GN   Name=map2k3; Synonyms=mek3;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Embryo;
RX   PubMed=8395011; DOI=10.1128/mcb.13.9.5738-5748.1993;
RA   Yashar B.M., Kelley C., Yee K., Errede B., Zon L.I.;
RT   "Novel members of the mitogen-activated protein kinase activator family in
RT   Xenopus laevis.";
RL   Mol. Cell. Biol. 13:5738-5748(1993).
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   -!- 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.
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   AlphaFoldDB; P39746; -.
DR   SMR; P39746; -.
DR   Proteomes; UP000186698; Genome assembly.
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; IPR008271; Ser/Thr_kinase_AS.
DR   Pfam; PF00069; Pkinase; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein;
KW   Reference proteome; Serine/threonine-protein kinase; Transferase;
KW   Tyrosine-protein kinase.
FT   CHAIN           <1..>62
FT                   /note="Dual specificity mitogen-activated protein kinase
FT                   kinase 3"
FT                   /id="PRO_0000086380"
FT   DOMAIN          <1..>62
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   NON_TER         1
FT   NON_TER         62
SQ   SEQUENCE   62 AA;  6666 MW;  81A0D7CFF8F5F62D CRC64;
     GKIAVSIVKA LEHLHSKLSV IHRDVKPSNV LINKEGQVNM CDFGISGYLV DSVAKTMDAG
     CK
 
 
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