(data stored in ACNUC13530 zone)

HOVERGEN: MK10_RAT

ID   MK10_RAT                Reviewed;         464 AA.
AC   P49187;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 2.
DT   13-OCT-2009, entry version 88.
DE   RecName: Full=Mitogen-activated protein kinase 10;
DE            EC=2.7.11.24;
DE   AltName: Full=Stress-activated protein kinase JNK3;
DE   AltName: Full=c-Jun N-terminal kinase 3;
DE   AltName: Full=SAPK-beta;
DE   AltName: Full=p54-beta;
GN   Name=Mapk10; Synonyms=Jnk3, Prkm10;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RX   MEDLINE=94232348; PubMed=8177321; DOI=10.1038/369156a0;
RA   Kyriakis J.M., Banerjee P., Nikolakaki E., Dai T., Rubie E.A.,
RA   Ahmad M.F., Avruch J., Woodgett J.R.;
RT   "The stress-activated protein kinase subfamily of c-Jun kinases.";
RL   Nature 369:156-160(1994).
RN   [2]
RP   IDENTIFICATION OF PROBABLE FRAMESHIFT.
RA   Hulo-Demole C., Braconi-Quintaje S.;
RL   Unpublished observations (MAR-1997).
CC   -!- FUNCTION: Responds to activation by environmental stress and pro-
CC       inflammatory cytokines by phosphorylating a number of
CC       transcription factors, primarily components of AP-1 such as c-Jun
CC       and ATF2 and thus regulates AP-1 transcriptional activity.
CC       Required for stress-induced neuronal apoptosis and the
CC       pathogenesis of glutamate excitotoxicity (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- COFACTOR: Magnesium (By similarity).
CC   -!- ENZYME REGULATION: Activated by threonine and tyrosine
CC       phosphorylation by two dual specificity kinases, MAP2K4 and
CC       MAP2K7. MAP2K7 phosphorylates MAPK10 on Thr-221 causing a
CC       conformational change and a large increase in Vmax for the enzyme.
CC       MAP2K4 then phosphorylates Tyr-223 resulting in a further increase
CC       in Vmax. Inhibited by dual specificity phosphatases, such as
CC       DUSP1. Inhibited by HDAC9 (By similarity).
CC   -!- SUBUNIT: Binds to at least four scaffolding proteins,
CC       MAPK8IP1/JIP-1, MAPK8IP2/JIP-2, MAPK8IP3/JIP-3/JSAP1 and
CC       SPAG9/MAPK8IP4/JIP-4. These proteins also bind other components of
CC       the JNK signaling pathway. Interacts with HDAC9 and MAPKBP1 (By
CC       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-221 and Tyr-223, 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.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA42110.1; Type=Frameshift; Positions=22;
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CC   -!- GENE_FAMILY: HBG014652 [ FAMILY / ALN / TREE ]
DR   EMBL; L27128; AAA42110.1; ALT_FRAME; mRNA.
DR   IPI; IPI00191810; -.
DR   PIR; S43969; S43969.
DR   RefSeq; NP_036938.1; -.
DR   UniGene; Rn.9911; -.
DR   HSSP; P53779; 1JNK.
DR   SMR; P49187; 46-400.
DR   STRING; P49187; -.
DR   PhosphoSite; P49187; -.
DR   Ensembl; ENSRNOT00000002855; ENSRNOP00000002855; ENSRNOG00000002079; Rattus norvegicus.
DR   GeneID; 25272; -.
DR   KEGG; rno:25272; -.
DR   UCSC; NM_012806; rat.
DR   CTD; 25272; -.
DR   RGD; 3663; Mapk10.
DR   HOVERGEN; P49187; -.
DR   BRENDA; 2.7.11.24; 248.
DR   NextBio; 605961; -.
DR   ArrayExpress; P49187; -.
DR   Genevestigator; P49187; -.
DR   GermOnline; ENSRNOG00000002079; Rattus norvegicus.
DR   GO; GO:0005524; F:ATP binding; IDA:RGD.
DR   GO; GO:0004705; F:JUN kinase activity; ISS:UniProtKB.
DR   GO; GO:0007254; P:JNK cascade; ISS:UniProtKB.
DR   GO; GO:0006468; P:protein amino acid phosphorylation; IDA:RGD.
DR   InterPro; IPR008351; JNK_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; PR01772; JNKMAPKINASE.
DR   ProDom; PD000001; Prot_kinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   PROSITE; PS01351; MAPK; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; FALSE_NEG.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   2: Evidence at transcript level;
DR   PRODOM; P49187.
DR   SWISS-2DPAGE; P49187.
KW   ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein;
KW   Serine/threonine-protein kinase; Transferase.
FT   DOMAIN        1     62       PRODOM:2005.1:PD019247  7
FT   DOMAIN       67    290       PRODOM:2005.1:PD000001  8496
FT   DOMAIN      291    333       PRODOM:2005.1:PD904258  25
FT   DOMAIN      364    400       PRODOM:2005.1:PD729355  109
FT   DOMAIN      402    448       PRODOM:2005.1:PD007140  16
FT   CHAIN         1    464       Mitogen-activated protein kinase 10.
FT                                /FTId=PRO_0000186279.
FT   DOMAIN       64    359       Protein kinase.
FT   NP_BIND      70     78       ATP (By similarity).
FT   MOTIF       221    223       TXY.
FT   ACT_SITE    189    189       Proton acceptor (By similarity).
FT   BINDING      93     93       ATP (By similarity).
FT   MOD_RES     221    221       Phosphothreonine (By similarity).
FT   MOD_RES     223    223       Phosphotyrosine (By similarity).
SQ   SEQUENCE   464 AA;  52530 MW;  6D6279D7C3E68AF9 CRC64;
     MSLHFLYYCS EPTLDVKIAF CQGFDKHVDV SSVVKHYNMS KSKVDNQFYS VEVGDSTFTV
     LKRYQNLKPI GSGAQGIVCA AYDAVLDRNV AIKKLSRPFQ NQTHAKRAYR ELVLMKCVNH
     KNIISLLNVF TPQKTLEEFQ DVYLVMELMD ANLCQVIQME LDHERMSYLL YQMLSAIKHL
     HSAGIIHRDL KPSNIVVKSD CTLKILDFGL ARTAGTSFMM TPYVVTRYYR APEVILGMGY
     KENVDIWSVG CIMGEMVRHK ILFPGRDYID QWNKVIEQLG TPCPEFMKKL QPTVRNYVEN
     RPKYAGLTFP KLFPDSLFPA DSEHNKLKAS QARDLLSKML VIDPAKRISV DDALQHPYIN
     VWYDPAEVEA PPPQIYDKQL DEREHTIEEW KELIYKEVMN SEEKTKNGVV KGQPSPSGAA
     VNSSESLPPS SSVNDISSMS TDQTLASDTD SSLEASAGPL GCCR
//

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