(data stored in ACNUC8465 zone)

HOGENOM: CANFA20_60_PE34

ID   CANFA20_60_PE34                      STANDARD;      PRT;   403 AA.
AC   CANFA20_60_PE34; Q1HG70;
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   RecName: Full=Dual specificity mitogen-activated protein kinase kinase 2;
DE   Short=MAP kinase kinase 2; Short=MAPKK 2; EC=2.7.12 2;AltName: Full=ERK
DE   activator kinase 2;AltName: Full=MAPK/ERK kinase 2; Short=MEK 2;
DE   (CANFA20_60.PE34).
GN   Name=MAP2K2; Synonyms=MEK2;
OS   CANIS LUPUS FAMILIARIS.
OC   Eukaryota; Metazoa; Eumetazoa; Bilateria; Coelomata; Deuterostomia;
OC   Chordata; Craniata; Vertebrata; Gnathostomata; Teleostomi; Euteleostomi;
OC   Sarcopterygii; Tetrapoda; Amniota; Mammalia; Theria; Eutheria;
OC   Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX   NCBI_TaxID=9615;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS CANFA20_60.PE34.
CC       Canis familiaris chromosome 20 BROADD2 partial sequence 57659320..58654
CC       annotated by Ensembl
CC   -!- ANNOTATIONS ORIGIN:MP2K2_CANFA
CC   -!- FUNCTION: Catalyzes the concomitant phosphorylation of a threonine
CC       and a tyrosine residue in a Thr-Glu-Tyr sequence located in MAP
CC       kinases. Activates the ERK1 and ERK2 MAP kinases (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- SUBUNIT: Interacts with MORG1 (By similarity).
CC   -!- PTM: MAPKK is itself dependent on Ser/Thr phosphorylation for
CC       activity catalyzed by MAP kinase kinase kinases (RAF or MEKK1) (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC       protein kinase family. MAP kinase kinase subfamily.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   -!- GENE_FAMILY: HOG000234206 [ FAMILY / ALN / TREE ]
DR   HOGENOM:Canis_familiaris;ENSCAFG00000019138;ENSCAFT00000030400;ENSCAFP00000028245.
DR   EMBL; DQ489531; - ;
DR   UniProtKB/Swiss-Prot; Q1HG70; -.
DR   EMBL; DQ489531; ABF47220.1; -; mRNA.
DR   RefSeq; NP_001041601.1; NM_001048136.1.
DR   UniGene; Cfa.21225; -.
DR   ProteinModelPortal; Q1HG70; -.
DR   SMR; Q1HG70; 60-392.
DR   STRING; Q1HG70; -.
DR   GeneID; 611939; -.
DR   KEGG; cfa:611939; -.
DR   CTD; 5605; -.
DR   eggNOG; maNOG18868; -.
DR   GeneTree; ENSGT00570000078767; -.
DR   InParanoid; Q1HG70; -.
DR   OrthoDB; EOG4SF965; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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.
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; PF00069; Pkinase; 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; CANFA20_60.PE34; -.
KW   ENSCAFG00000019138fold_1320000031; ENSCAFP00000028245fold_1320000031;
KW   DQ489531;
KW   Acetylation; ATP-binding; Complete proteome; Kinase;
KW   Nucleotide-binding; Phosphoprotein; Reference proteome;
KW   Serine/threonine-protein kinase; Transferase; Tyrosine-protein kinase.
SQ   SEQUENCE   403 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MLARRKPVLP ALTINPAIAE GPSPTSEGAS EANLVDLQKK LAELELDEQQ KKRLEAFLTQ
     KAKVGELKDD DFERISELGA GNGGVVTKVQ HRPSGLIMAR KLIHLEIKPA IRNQIIRELQ
     VLHECNSPYI VGFYGAFYSD GEISICMEHM DGGSLDQVLK EAKRIPEEIL GKVSIAVLRG
     LAYLREKHQI MHRDVKPSNI LVNSRGEIKL CDFGVSGQLI DSMANSFVGT RSYMSPERLQ
     GTHYSVQSDI WSMGLSLVEL SIGRYPIPPP DAKELEAIFG RPMVDGIEGE PHSISPRPRP
     PGRPISALAG HGTDSRPAMA IFELLDYIVN EPPPKLPNGV FTQDFQEFVN KCLIKNPAER
     ADLKMLMSHT FIKRSEVEEV DFAGWLCKTL RLNQPSTPTR TAV
//

If you have problems or comments...

PBIL Back to PBIL home page