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 03-AUG-2022, entry version 117.
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; Phasianidae;
OC 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., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA 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). May
CC promote entry in the cell cycle (By similarity). {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, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; 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 the
CC enzyme. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC protein kinase family. MAP kinase subfamily. {ECO:0000305}.
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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 AlphaFoldDB; Q5F3W3; -.
DR SMR; Q5F3W3; -.
DR STRING; 9031.ENSGALP00000040749; -.
DR PaxDb; Q5F3W3; -.
DR PRIDE; Q5F3W3; -.
DR Ensembl; ENSGALT00000061654; ENSGALP00000057521; ENSGALG00000031448.
DR Ensembl; ENSGALT00000090669; ENSGALP00000065050; ENSGALG00000031448.
DR GeneID; 415419; -.
DR KEGG; gga:415419; -.
DR CTD; 5596; -.
DR VEuPathDB; HostDB:geneid_415419; -.
DR eggNOG; KOG0660; Eukaryota.
DR GeneTree; ENSGT00940000154351; -.
DR InParanoid; Q5F3W3; -.
DR OMA; EADWQLH; -.
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; ENSGALG00000031448; Expressed in brain and 14 other tissues.
DR ExpressionAtlas; Q5F3W3; baseline and differential.
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:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
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:0006468; P:protein phosphorylation; IEA:Ensembl.
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; Kinase; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..721
FT /note="Mitogen-activated protein kinase 6"
FT /id="PRO_0000249010"
FT DOMAIN 20..316
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOTIF 626..628
FT /note="TXY"
FT ACT_SITE 152
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 26..34
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 49
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 626
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
FT MOD_RES 628
FT /note="Phosphotyrosine"
FT /evidence="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
