(data stored in ACNUC13530 zone)

HOVERGEN: MK14A_CYPCA

ID   MK14A_CYPCA             Reviewed;         361 AA.
AC   Q90336;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   16-JUN-2009, entry version 65.
DE   RecName: Full=Mitogen-activated protein kinase 14a;
DE            EC=2.7.11.24;
DE   AltName: Full=Mitogen-activated protein kinase p38a;
DE            Short=MAP kinase p38a;
DE            Short=cp38a;
GN   Name=mapk14a;
OS   Cyprinus carpio (Common carp).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Cyprinidae; Cyprinus.
OX   NCBI_TaxID=7962;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], COFACTOR, TISSUE SPECIFICITY,
RP   PHOSPHORYLATION, AND ENZYME REGULATION.
RC   TISSUE=Ovary;
RX   MEDLINE=20341112; PubMed=10880959;
RX   DOI=10.1046/j.1432-1327.2000.01479.x;
RA   Hashimoto H., Fukuda M., Matsuo Y., Yokoyama Y., Nishida E.,
RA   Toyohara H., Sakaguchi M.;
RT   "Identification of a nuclear export signal in MKK6, an activator of
RT   the carp p38 mitogen-activated protein kinases.";
RL   Eur. J. Biochem. 267:4362-4371(2000).
CC   -!- FUNCTION: Responds to activation by environmental stress, such as
CC       hypertonic stress, and cytokines by phosphorylating downstream
CC       targets.
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- COFACTOR: Magnesium.
CC   -!- ENZYME REGULATION: Activated by threonine and tyrosine
CC       phosphorylation by the dual specificity kinase, MKK6.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By
CC       similarity).
CC   -!- TISSUE SPECIFICITY: Exclusively expressed in the ovary.
CC   -!- DOMAIN: The TXY motif contains the threonine and tyrosine residues
CC       whose phosphorylation activates the MAP kinases.
CC   -!- PTM: Dually phosphorylated on Thr-181 and Tyr-183, which activates
CC       the enzyme.
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; D83274; BAA11881.1; -; mRNA.
DR   HSSP; Q16539; 1KV1.
DR   SMR; Q90336; 5-355.
DR   HOVERGEN; Q90336; -.
DR   BRENDA; 2.7.11.24; 3298.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008339; F:MP kinase activity; IDA:UniProtKB.
DR   GO; GO:0006468; P:protein amino acid phosphorylation; IEA:InterPro.
DR   GO; GO:0007243; P:protein kinase cascade; IDA:UniProtKB.
DR   GO; GO:0006950; P:response to stress; IDA:UniProtKB.
DR   InterPro; IPR003527; MAP_kinase_CS.
DR   InterPro; IPR008352; MAPK_p38.
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; PR01773; P38MAPKINASE.
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; FALSE_NEG.
PE   1: Evidence at protein level;
DR   PRODOM; Q90336.
DR   SWISS-2DPAGE; Q90336.
KW   ATP-binding; Cytoplasm; Kinase; Nucleotide-binding; Nucleus;
KW   Phosphoprotein; Serine/threonine-protein kinase; Transferase.
FT   DOMAIN       27    238       PRODOM:2005.1:PD000001  8496
FT   DOMAIN      310    343       PRODOM:2005.1:PD729355  109
FT   CHAIN         1    361       Mitogen-activated protein kinase 14a.
FT                                /FTId=PRO_0000186296.
FT   DOMAIN       25    309       Protein kinase.
FT   NP_BIND      31     39       ATP (By similarity).
FT   MOTIF       181    183       TXY.
FT   ACT_SITE    151    151       Proton acceptor (By similarity).
FT   BINDING      54     54       ATP (By similarity).
FT   MOD_RES     181    181       Phosphothreonine.
FT   MOD_RES     183    183       Phosphotyrosine.
SQ   SEQUENCE   361 AA;  41660 MW;  D1B023A21964FBDA CRC64;
     MSQKERPTFH RQEVNKTIWE VPVRYQNLSP VGSGAYGTVC SAYDEKTGLK VAVKKLSRPF
     QSIIHAKRTY RELRLLKHMK HENVIGLLDV FTPATSLEEF NDVYLVTHLM GADLNNIVKC
     QKLTDDHVQF LIYQILRGLK YIHSADIIHR DLKPSNLAVN EDCELKILDF GLARHTDDEM
     TGYVATRWYR APEIMLNWMH YNMTVDIWSV GCIMAELLTG RTLFPGTDHI NQLQQIMRLT
     GTPPASLISR MPSHEARTYI NSLPQMPKRN FSEVFIGANP QAVDLLEKML VLDTDKRITA
     AEALAHPYFA QYHDPDDEPE AEPFDQSFES RELDIEEWKR QTYEEVISFE PPVFDGDEME
     S
//

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