(data stored in ACNUC13530 zone)

HOVERGEN: MK01_BOVIN

ID   MK01_BOVIN              Reviewed;         360 AA.
AC   P46196; A2VE60;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   22-SEP-2009, entry version 86.
DE   RecName: Full=Mitogen-activated protein kinase 1;
DE            EC=2.7.11.24;
DE   AltName: Full=Extracellular signal-regulated kinase 2;
DE            Short=ERK-2;
DE   AltName: Full=Mitogen-activated protein kinase 2;
DE            Short=MAP kinase 2;
DE            Short=MAPK 2;
DE   AltName: Full=p42-MAPK;
DE   AltName: Full=ERT1;
GN   Name=MAPK1; Synonyms=ERK2, PRKM1;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC   Pecora; Bovidae; Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Adrenal medulla;
RA   Ely C.M., Cox M.E., Her J., Parsons S.J.;
RT   "Cloning and sequencing of ERK2 from a bovine adrenal medulla cDNA
RT   library.";
RL   Submitted (JUL-1992) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Fetal pons;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in both the initiation and regulation of
CC       meiosis, mitosis, and postmitotic functions in differentiated
CC       cells by phosphorylating a number of transcription factors such as
CC       ELK1. Phosphorylates EIF4EBP1; required for initiation of
CC       translation. Phosphorylates microtubule-associated protein 2
CC       (MAP2). Phosphorylates SPZ1. Phosphorylates heat shock factor
CC       protein 4 (HSF4) and ARHGEF2 (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- COFACTOR: Magnesium (By similarity).
CC   -!- ENZYME REGULATION: Activated by phosphorylation on tyrosine and
CC       threonine in response to insulin and NGF. Both phosphorylations
CC       are required for activity (By similarity).
CC   -!- SUBUNIT: Interacts with ARHGEF2, NISCH, MORG1 and HSF4 (By
CC       similarity). Interacts (phosphorylated form) with CAV2 ('Tyr-19'-
CC       phosphorylated form); the interaction, promoted by insulin, leads
CC       to nuclear location and MAPK1 activation (By similarity).
CC   -!- DOMAIN: The TXY motif contains the threonine and tyrosine residues
CC       whose phosphorylation activates the MAP kinases.
CC   -!- PTM: Dually phosphorylated on Thr-185 and Tyr-187, which activates
CC       the enzyme (By similarity).
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC
CC       Ser/Thr protein kinase family. MAP kinase subfamily.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
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CC   -!- GENE_FAMILY: HBG014652 [ FAMILY / ALN / TREE ]
DR   EMBL; Z14089; CAA78467.1; -; mRNA.
DR   EMBL; BC133588; AAI33589.2; -; mRNA.
DR   IPI; IPI00713672; -.
DR   PIR; S25011; S25011.
DR   RefSeq; NP_786987.1; -.
DR   UniGene; Bt.167; -.
DR   HSSP; P28482; 1PME.
DR   SMR; P46196; 11-355, 12-356.
DR   STRING; P46196; -.
DR   GeneID; 327672; -.
DR   KEGG; bta:327672; -.
DR   CTD; 327672; -.
DR   HOVERGEN; P46196; -.
DR   BRENDA; 2.7.11.24; 251.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004707; F:MAP kinase activity; IEA:EC.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0006468; P:protein amino acid phosphorylation; IEA:InterPro.
DR   InterPro; IPR008349; Erk_1_2_MAPK.
DR   InterPro; IPR003527; MAP_kinase_CS.
DR   InterPro; IPR000719; Prot_kinase_core.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR017442; Se/Thr_pkinase-rel.
DR   InterPro; IPR008271; Ser_thr_pkin_AS.
DR   InterPro; IPR002290; Ser_thr_pkinase.
DR   Pfam; PF00069; Pkinase; 1.
DR   PRINTS; PR01770; ERK1ERK2MAPK.
DR   ProDom; PD000001; Prot_kinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   PROSITE; PS01351; MAPK; 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; P46196.
DR   SWISS-2DPAGE; P46196.
KW   Acetylation; ATP-binding; Cell cycle; Kinase; Nucleotide-binding;
KW   Phosphoprotein; Serine/threonine-protein kinase; Transferase.
FT   DOMAIN       31    230       PRODOM:2005.1:PD000001  8496
FT   DOMAIN      318    354       PRODOM:2005.1:PD054205  105
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    360       Mitogen-activated protein kinase 1.
FT                                /FTId=PRO_0000186246.
FT   DOMAIN       25    313       Protein kinase.
FT   NP_BIND      31     39       ATP (By similarity).
FT   MOTIF       185    187       TXY.
FT   COMPBIAS      2      9       Poly-Ala.
FT   ACT_SITE    149    149       Proton acceptor (By similarity).
FT   BINDING      54     54       ATP (By similarity).
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES     185    185       Phosphothreonine (By similarity).
FT   MOD_RES     187    187       Phosphotyrosine (By similarity).
FT   MOD_RES     190    190       Phosphothreonine (By similarity).
FT   MOD_RES     202    202       Phosphoserine (By similarity).
SQ   SEQUENCE   360 AA;  41376 MW;  E85D0B2A4E9549DE CRC64;
     MAAAAAAGAG PEMVRGQVFD VGPRYTNLSY IGEGAYGMVC SAYDNVNKVR VAIKKISPFE
     HQTYCQRTLR EIKILLRFRH ENIIGINDII RAPTIEQMKD VYIVQDLMET DLYKLLKTQH
     LSNDHICYFL YQILRGLKYI HSANVLHRDL KPSNLLLNTT CDLKICDFGL ARVADPDHDH
     TGFLTEYVAT RWYRAPEIML NSKGYTKSID IWSVGCILAE MLSNRPIFPG KHYLDQLNHI
     LGILGSPSQE DLNCIINLKA RNYLLSLPHK NKVPWNRLFP NADSKALDLL DKMLTFNPHK
     RIEVEQALAH PYLEQYYDPS DEPVAEAPFK FDMELDDLPK EKLKELIFEE TARFQPGYRS
//

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