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Database: UniProt/SWISS-PROT
Entry: MK06_CHICK
LinkDB: MK06_CHICK
Original site: MK06_CHICK 
ID   MK06_CHICK              Reviewed;         721 AA.
AC   Q5F3W3;
DT   05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   16-JAN-2019, entry version 102.
DE   RecName: Full=Mitogen-activated protein kinase 6;
DE            Short=MAP kinase 6;
DE            Short=MAPK 6;
DE            EC=2.7.11.24;
GN   Name=MAPK6; ORFNames=RCJMB04_5i17;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes;
OC   Phasianidae; Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=CB; TISSUE=Bursa of Fabricius;
RX   PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA   Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J.,
RA   Fiedler P., Kutter S., Blagodatski A., Kostovska D., Koter M.,
RA   Plachy J., Carninci P., Hayashizaki Y., Buerstedde J.-M.;
RT   "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT   function analysis.";
RL   Genome Biol. 6:R6.1-R6.9(2005).
CC   -!- FUNCTION: Phosphorylates microtubule-associated protein 2 (MAP2).
CC       May promote entry in the cell cycle (By similarity).
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC         [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216;
CC         EC=2.7.11.24;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC         threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC         Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC         EC=2.7.11.24;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- ACTIVITY REGULATION: Activated by threonine and tyrosine
CC       phosphorylation. {ECO:0000250}.
CC   -!- DOMAIN: The TXY motif contains the threonine and tyrosine residues
CC       whose phosphorylation activates the MAP kinases.
CC   -!- PTM: Dually phosphorylated on Thr-626 and Tyr-628, which activates
CC       the enzyme. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC
CC       Ser/Thr protein kinase family. MAP kinase subfamily.
CC       {ECO:0000305}.
DR   EMBL; AJ851537; CAH65171.1; -; mRNA.
DR   RefSeq; NP_001025720.1; NM_001030549.1.
DR   RefSeq; XP_015147391.1; XM_015291905.1.
DR   RefSeq; XP_015147392.1; XM_015291906.1.
DR   RefSeq; XP_015147393.1; XM_015291907.1.
DR   RefSeq; XP_015147394.1; XM_015291908.1.
DR   RefSeq; XP_015147395.1; XM_015291909.1.
DR   RefSeq; XP_015147396.1; XM_015291910.1.
DR   RefSeq; XP_015147397.1; XM_015291911.1.
DR   RefSeq; XP_015147399.1; XM_015291913.1.
DR   UniGene; Gga.3411; -.
DR   ProteinModelPortal; Q5F3W3; -.
DR   SMR; Q5F3W3; -.
DR   STRING; 9031.ENSGALP00000007460; -.
DR   PaxDb; Q5F3W3; -.
DR   PRIDE; Q5F3W3; -.
DR   Ensembl; ENSGALT00000061654; ENSGALP00000057521; ENSGALG00000031448.
DR   GeneID; 415419; -.
DR   KEGG; gga:415419; -.
DR   CTD; 5597; -.
DR   eggNOG; KOG0660; Eukaryota.
DR   eggNOG; ENOG410XNY0; LUCA.
DR   GeneTree; ENSGT00940000154351; -.
DR   HOGENOM; HOG000233020; -.
DR   HOVERGEN; HBG104376; -.
DR   InParanoid; Q5F3W3; -.
DR   KO; K06855; -.
DR   OMA; RDSEVNH; -.
DR   OrthoDB; 741207at2759; -.
DR   PhylomeDB; Q5F3W3; -.
DR   TreeFam; TF105098; -.
DR   Reactome; R-GGA-5687128; MAPK6/MAPK4 signaling.
DR   PRO; PR:Q5F3W3; -.
DR   Proteomes; UP000000539; Chromosome 10.
DR   Bgee; ENSGALG00000004690; Expressed in 11 organ(s), highest expression level in brain.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
DR   GO; GO:0032156; C:septin cytoskeleton; IEA:Ensembl.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004707; F:MAP kinase activity; IBA:GO_Central.
DR   GO; GO:0046982; F:protein heterodimerization activity; IEA:Ensembl.
DR   GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0071310; P:cellular response to organic substance; IBA:GO_Central.
DR   GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR   GO; GO:0060999; P:positive regulation of dendritic spine development; IEA:Ensembl.
DR   GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR008350; MAPK_ERK3/4.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   Pfam; PF00069; Pkinase; 1.
DR   PRINTS; PR01771; ERK3ERK4MAPK.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; SSF56112; 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;
KW   ATP-binding; Cell cycle; Complete proteome; Kinase;
KW   Nucleotide-binding; Phosphoprotein; Reference proteome;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN         1    721       Mitogen-activated protein kinase 6.
FT                                /FTId=PRO_0000249010.
FT   DOMAIN       20    316       Protein kinase. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   NP_BIND      26     34       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   MOTIF       626    628       TXY.
FT   ACT_SITE    152    152       Proton acceptor. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159, ECO:0000255|PROSITE-
FT                                ProRule:PRU10027}.
FT   BINDING      49     49       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   MOD_RES     626    626       Phosphothreonine. {ECO:0000250}.
FT   MOD_RES     628    628       Phosphotyrosine. {ECO:0000250}.
SQ   SEQUENCE   721 AA;  82747 MW;  CC605A2282F16E43 CRC64;
     MAEKFESLMN IHGFDLGSRY MDLKPLGCGG NGLVFSAVDN DCDKRVAVKK IVLTDPQSVK
     HALREIKIIR RLDHDNIVKV FEILGPSGSQ LTDDVGSLTE LNCVYIVQEY METDLANLLE
     QGPLLEDHAR LFMYQLLRGL KYIHSANVLH RDLKPANLFI NTEDLVLKIG DFGLARIMDP
     HYSHKGHLSE GLVTKWYRSP RLLLSPNNYT KAIDMWAAGC IFAEMLTGKT LFAGAHELEQ
     MQLILESIPV VHEEDRQELL NVIPVYIRND MTEPHKPLTQ LLPGISPEAL DFLEQILTFS
     PMDRLTAEEA LSHPYMSIYS FPTDEPISSH PFHIEDEVDD ILLMDESHSH IYNWERYHES
     QFSDHDWPIH NNYEADEVQR DPRALSDVTD EEEVQVDPRK YLDGDREKYL EDPAFDTHFS
     TEPCWQYSDH HENKYCDLEC SHTCNYKMRS SSYLDNLVWR DSEVNHYYEP KLIIDLSNWK
     EQSKEKSDKK GKSKCEKNGL VKAQIALEEA SQQLVEKERE KNQGFDFDSF IAETIQLSLQ
     HEPTDVDKLN DLNSSVSQME SKGLISKSVS REKQEKGMAN LAQLGALYQT SWESQFVSNG
     EECFLIDQFC CEVRKDEQVE KENTYTSYLD KFFSKKEDAE MLEPEPVEEG KLGEKERGES
     FLSNSGELFF NKQLEAIGIP QFHSPVGSPL KSIQATLTPS AMKSSPQIPH KTYSSILKHL
     N
//
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