(data stored in ACNUC8465 zone)

HOGENOM: RAT8_PE947

ID   RAT8_PE947                           STANDARD;      PRT;   437 AA.
AC   RAT8_PE947; Q62862; Q62863; Q62864;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   Flags: Fragments;
DE   RecName: Full=Dual specificity mitogen-activated protein kinase kinase 5;
DE   Short=MAP kinase kinase 5; Short=MAPKK 5; EC=2.7.12 2;AltName:
DE   Full=MAPK/ERK kinase 5; Short=MEK 5; (RAT8.PE947).
GN   Name=Map2k5; Synonyms=Mek5, Mkk5, Prkmk5;
OS   RATTUS NORVEGICUS.
OC   Eukaryota; Metazoa; Eumetazoa; Bilateria; Coelomata; Deuterostomia;
OC   Chordata; Craniata; Vertebrata; Gnathostomata; Teleostomi; Euteleostomi;
OC   Sarcopterygii; Tetrapoda; Amniota; Mammalia; Theria; Eutheria;
OC   Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS RAT8.PE947.
CC       Rattus norvegicus chromosome 8 RGSC3.4  sequence 1..129041809 annotated
CC       by Ensembl
CC   -!- ANNOTATIONS ORIGIN:MP2K5_RAT
CC   -!- FUNCTION: Acts as a scaffold for the formation of a ternary
CC       MAP3K2/MAP3K3-MAP3K5-MAPK7 signaling complex. Activation of this
CC       pathway appear to play a critical role in protecting cells from
CC       stress-induced apopotosis, neuronal survival and cardiac
CC       development and angiogenesis (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- COFACTOR: Magnesium.
CC   -!- SUBUNIT: Interacts with PARD6A, MAP3K3 and MAPK7. Forms a complex
CC       with SQSTM1 and PRKCZ or PRKCI (By similarity).
CC   -!- SUBCELLULAR LOCATION: Isoform Beta: Cytoplasm, cytosol.
CC   -!- SUBCELLULAR LOCATION: Isoform Alpha-1: Membrane. Note=The
CC       alternatively spliced exon in alpha isoform resemble conserved
CC       sequences that mediate interactions with the cytoskeleton, thereby
CC       explaining the differential localization.
CC   -!- SUBCELLULAR LOCATION: Isoform Alpha-2: Membrane. Note=The
CC       alternatively spliced exon in alpha isoform resemble conserved
CC       sequences that mediate interactions with the cytoskeleton, thereby
CC       explaining the differential localization.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=Alpha-1;
CC         IsoId=Q62862-1; Sequence=Displayed;
CC       Name=Alpha-2;
CC         IsoId=Q62862-2; Sequence=VSP_004881;
CC       Name=Beta;
CC         IsoId=Q62862-3; Sequence=VSP_004880;
CC   -!- TISSUE SPECIFICITY: MEK5 beta is ubiquitously distributed with
CC       highest levels in the liver, whereas MEK5 alpha is expressed only
CC       in liver and brain.
CC   -!- DOMAIN: Binds MAP3K2/MAP3K3 and MAPK7 via non-overlapping residues
CC       of the OPR domain. This domain also mediates interactions with
CC       SQSTM1 and PARD6A (By similarity).
CC   -!- PTM: Activated by phosphorylation on Ser/Thr by MAP kinase kinase
CC       kinases (By similarity).
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC       protein kinase family. MAP kinase kinase subfamily.
CC   -!- SIMILARITY: Contains 1 OPR domain.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   -!- GENE_FAMILY: HOG000234206 [ FAMILY / ALN / TREE ]
DR   HOGENOM:Rattus_norvegicus;ENSRNOG00000007926;ENSRNOT00000051558;ENSRNOP00000050528.
DR   EMBL; BC078860; - ;
DR   EMBL; U37462; - ;
DR   EMBL; U37463; - ;
DR   EMBL; U37464; - ;
DR   UniProtKB/Swiss-Prot; Q62862; Q62863; Q62864; -.
DR   EMBL; U37462; AAC52320.1; -; mRNA.
DR   EMBL; U37463; AAC52321.1; -; mRNA.
DR   EMBL; U37464; AAC52322.1; -; mRNA.
DR   EMBL; BC078860; AAH78860.1; -; mRNA.
DR   IPI; IPI00209255; -.
DR   IPI; IPI00230846; -.
DR   IPI; IPI00230847; -.
DR   RefSeq; NP_001029159.1; NM_001033987.1.
DR   RefSeq; NP_058942.1; NM_017246.2.
DR   UniGene; Rn.11054; -.
DR   ProteinModelPortal; Q62862; -.
DR   SMR; Q62862; 7-113.
DR   IntAct; Q62862; 1.
DR   STRING; Q62862; -.
DR   PhosphoSite; Q62862; -.
DR   Ensembl; ENSRNOT00000010991; ENSRNOP00000010991; ENSRNOG00000007926.
DR   GeneID; 29568; -.
DR   KEGG; rno:29568; -.
DR   UCSC; U37462; rat.
DR   CTD; 5607; -.
DR   RGD; 61890; Map2k5.
DR   eggNOG; roNOG08615; -.
DR   GeneTree; ENSGT00570000078767; -.
DR   InParanoid; Q62862; -.
DR   OrthoDB; EOG49GKGK; -.
DR   PhylomeDB; Q62862; -.
DR   BRENDA; 2.7.12.2; 5301.
DR   Reactome; REACT_96194; Signalling by NGF.
DR   NextBio; 609644; -.
DR   ArrayExpress; Q62862; -.
DR   Genevestigator; Q62862; -.
DR   GermOnline; ENSRNOG00000007926; Rattus norvegicus.
DR   GO; GO:0005829; C:cytosol; IDA:RGD.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IDA:RGD.
DR   GO; GO:0005524; F:ATP binding; IDA:RGD.
DR   GO; GO:0004707; F:MAP kinase activity; EXP:Reactome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004713; F:protein tyrosine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0070375; P:BMK cascade; IMP:RGD.
DR   GO; GO:0030307; P:positive regulation of cell growth; IMP:RGD.
DR   GO; GO:0050679; P:positive regulation of epithelial cell proliferation; IDA:RGD.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000270; OPR_PB1.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR017442; Se/Thr_kinase-like_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   InterPro; IPR002290; Ser/Thr_kinase_dom.
DR   Pfam; PF00564; PB1; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00666; PB1; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR   HOGENOMDNA; RAT8.PE947; -.
KW   ENSRNOG00000007926820036002503210000011;
KW   Map2k5; MP2K5_RAT; BC078860; U37462; U37463; U37464;
KW   Alternative splicing; ATP-binding; Complete proteome; Cytoplasm;
KW   Kinase; Magnesium; Membrane; Metal-binding; Nucleotide-binding;
KW   Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW   Transferase; Tyrosine-protein kinase.
SQ   SEQUENCE   437 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     XENQVLVIRI KIPNSGAVDW TVHSGPQLLF RDVLDVIGQV LPEATTTAFE YEDEDGDRIT
     VRSDEEMKAM LSYYYSTVME QQVNGQLIEP LQIFPRACKP PGERNIHGLK VNTRAGPSQH
     TSPVVSDSLP SNSLKKSSAE LRKILANGQM NEQDIRYRDT LGHGNGGTVY KAYHVPSGKI
     LAVKVILLDI TLELQKQIMS ELEILYKCDS SYIIGFYGAF FVENRISICT EFMDGGSLDV
     YRKIPEHVLG RIAVAVVKGL TYLWSLKILH RDVKPSNMLV NTSGQVKLCD FGVSTQLVNS
     IAKTYVGTNA YMAPERISGE QYGIHSDVWS LGISFMELAL GRFPYPQIQK NQGSLMPLQL
     LQCIVDEDSP VLPLGEFSEP FVHFITQCMR KQPKERPAPE ELMGHPFIVQ FNDGNATVVS
     MWVCRALEER RSQQGPP
//

If you have problems or comments...

PBIL Back to PBIL home page