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KC1G1_CHICK
ID   KC1G1_CHICK             Reviewed;         456 AA.
AC   Q5ZJS0;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 124.
DE   RecName: Full=Casein kinase I isoform gamma-1;
DE            Short=CKI-gamma 1;
DE            EC=2.7.11.1;
GN   Name=CSNK1G1; ORFNames=RCJMB04_16d5;
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: Casein kinases are operationally defined by their
CC       preferential utilization of acidic proteins such as caseins as
CC       substrates. It can phosphorylate a large number of proteins.
CC       Participates in Wnt signaling (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=2.7.11.1;
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=2.7.11.1;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- PTM: Autophosphorylated. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CK1 Ser/Thr
CC       protein kinase family. Casein kinase I subfamily. {ECO:0000305}.
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DR   EMBL; AJ720364; CAG32023.1; -; mRNA.
DR   RefSeq; NP_001005800.1; NM_001005800.1.
DR   RefSeq; XP_015134345.1; XM_015278859.1.
DR   AlphaFoldDB; Q5ZJS0; -.
DR   SMR; Q5ZJS0; -.
DR   STRING; 9031.ENSGALP00000003568; -.
DR   PaxDb; Q5ZJS0; -.
DR   Ensembl; ENSGALT00000050537; ENSGALP00000046476; ENSGALG00000030812.
DR   Ensembl; ENSGALT00000063644; ENSGALP00000056919; ENSGALG00000030812.
DR   Ensembl; ENSGALT00000093350; ENSGALP00000068344; ENSGALG00000030812.
DR   Ensembl; ENSGALT00000094686; ENSGALP00000069416; ENSGALG00000030812.
DR   GeneID; 415328; -.
DR   KEGG; gga:415328; -.
DR   CTD; 53944; -.
DR   VEuPathDB; HostDB:geneid_415328; -.
DR   eggNOG; KOG1165; Eukaryota.
DR   GeneTree; ENSGT00940000155628; -.
DR   HOGENOM; CLU_019279_2_0_1; -.
DR   InParanoid; Q5ZJS0; -.
DR   PhylomeDB; Q5ZJS0; -.
DR   TreeFam; TF313349; -.
DR   PRO; PR:Q5ZJS0; -.
DR   Proteomes; UP000000539; Chromosome 10.
DR   Bgee; ENSGALG00000030812; Expressed in testis and 12 other tissues.
DR   ExpressionAtlas; Q5ZJS0; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:0006897; P:endocytosis; IBA:GO_Central.
DR   GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR   GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IBA:GO_Central.
DR   GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR   GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR   InterPro; IPR022247; Casein_kinase-1_gamma_C.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   Pfam; PF12605; CK1gamma_C; 1.
DR   Pfam; PF00069; Pkinase; 1.
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; Cytoplasm; Kinase; Nucleotide-binding; Phosphoprotein;
KW   Reference proteome; Serine/threonine-protein kinase; Transferase;
KW   Wnt signaling pathway.
FT   CHAIN           1..456
FT                   /note="Casein kinase I isoform gamma-1"
FT                   /id="PRO_0000364343"
FT   DOMAIN          43..314
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          1..35
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          338..382
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..17
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        163
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         49..57
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         72
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   456 AA;  52194 MW;  0868BB8491361FFC CRC64;
     MDHPNREKDE RQRTTKGMPG RSGHGSRPSS SASSGVLMVG PNFRVGKKIG CGNFGELRLG
     KNLYTNEYVA IKLEPIKSRA PQLHLEYRFY KQLGSAAEGL PQVYYFGPCG KYNAMVLELL
     GPSLEDLFDL CDRTFTLKTV LMIAIQLISR MEYVHSKNLI YRDVKPENFL IGRQGNKKDH
     VIHIIDFGLA KEYIDPETKK HIPYREHKSL TGTARYMSIN THLGKEQSRR DDLEALGHMF
     MYFLRGSLPW QGLKADTLKE RYQKIGDTKR NTPVEVLCEN FPEEMATYLR YVRRLDFFER
     PDYDYLRTIF TELFEKKGYT FDYAYDWVGR PIPTPVGSVH VDSGTSAITR DSHVHRDRPS
     QQALRNQASS DRRGEWEIQP SRQTNTSYLT SHLAADRHGG SVQVVSSTNG ELNVDDPTGA
     HSNAPITAQA EVEVVEEAKC CCFFKRKRKK TAQRHK
 
 
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