位置:首页 > 蛋白库 > KC1G1_BOVIN
KC1G1_BOVIN
ID   KC1G1_BOVIN             Reviewed;         457 AA.
AC   A7E3X2; Q32KN4;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=Casein kinase I isoform gamma-1;
DE            Short=CKI-gamma 1;
DE            EC=2.7.11.1;
GN   Name=CSNK1G1;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX   PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA   Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA   Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT   "Characterization of 954 bovine full-CDS cDNA sequences.";
RL   BMC Genomics 6:166-166(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=Crossbred X Angus; TISSUE=Liver;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Serine/threonine-protein kinase. Casein kinases are
CC       operationally defined by their preferential utilization of acidic
CC       proteins such as caseins as substrates. It can phosphorylate a large
CC       number of proteins. Participates in Wnt signaling. Regulates fast
CC       synaptic transmission mediated by glutamate. Phosphorylates CLSPN (By
CC       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   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=A7E3X2-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=A7E3X2-2; Sequence=VSP_036439;
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BT030743; ABS45059.1; -; mRNA.
DR   EMBL; BC110009; AAI10010.1; -; mRNA.
DR   RefSeq; NP_001033235.1; NM_001038146.2.
DR   RefSeq; XP_005211737.1; XM_005211680.3. [A7E3X2-1]
DR   RefSeq; XP_010807562.1; XM_010809260.2.
DR   AlphaFoldDB; A7E3X2; -.
DR   SMR; A7E3X2; -.
DR   STRING; 9913.ENSBTAP00000022379; -.
DR   PaxDb; A7E3X2; -.
DR   PRIDE; A7E3X2; -.
DR   Ensembl; ENSBTAT00000022379; ENSBTAP00000022379; ENSBTAG00000016823. [A7E3X2-1]
DR   GeneID; 527889; -.
DR   KEGG; bta:527889; -.
DR   CTD; 53944; -.
DR   VEuPathDB; HostDB:ENSBTAG00000016823; -.
DR   eggNOG; KOG1165; Eukaryota.
DR   GeneTree; ENSGT00940000155628; -.
DR   HOGENOM; CLU_019279_2_0_1; -.
DR   InParanoid; A7E3X2; -.
DR   OrthoDB; 889559at2759; -.
DR   TreeFam; TF313349; -.
DR   Proteomes; UP000009136; Chromosome 10.
DR   Bgee; ENSBTAG00000016823; Expressed in semen and 111 other tissues.
DR   ExpressionAtlas; A7E3X2; 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   Alternative splicing; ATP-binding; Cytoplasm; Kinase; Nucleotide-binding;
KW   Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW   Transferase; Wnt signaling pathway.
FT   CHAIN           1..457
FT                   /note="Casein kinase I isoform gamma-1"
FT                   /id="PRO_0000364341"
FT   DOMAIN          43..314
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          1..36
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          350..384
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..23
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        361..384
FT                   /note="Polar 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"
FT   MOD_RES         343
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HCP0"
FT   VAR_SEQ         368..457
FT                   /note="TASSERRGEWEIQPSRQTNTSYLTSHLAADRHGGSVQVVSSTNGELNVDDPT
FT                   GAHSNAPITAHAEVEVVEEAKCCCFFKRKRKKTTQRHK -> IRKLRHRKSEDLAQGPT
FT                   ATKTFNSRVVCPAGSLFPLPSTHISRNHVQEMKPGDRSSCTSKRSLIGSTLTR (in
FT                   isoform 2)"
FT                   /evidence="ECO:0000303|Ref.2"
FT                   /id="VSP_036439"
FT   CONFLICT        274
FT                   /note="I -> V (in Ref. 2; AAI10010)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   457 AA;  52620 MW;  897F7AB2FB7B88EA CRC64;
     MDHPSREKDE RQRTTKPMAQ RREHCSRPSG STSSGVLMVG PNFRVGKKIG CGNFGELRLG
     KNLYTNEYVA IKLEPIKSRA PQLHLEYRFY KQLGSAGEGL PQVYYFGPCG KYNAMVLELL
     GPSLEDLFDL CDRTFTLKTV LMIAIQLLSR MEYVHSKNLI YRDVKPENFL IGRQGNKKEH
     VIHIIDFGLA KEYIDPETKK HIPYREHKSL TGTARYMSIN THLGKEQSRR DDLEALGHMF
     MYFLRGSLPW QGLKADTLKE RYQKIGDTKR NTPIEVLCEN FPEEMATYLR YVRRLDFFEK
     PDYEYLRTLF TDLFERKGYT FDYAYDWVGR PIPTPVGSVH VDSGASAITR ESHTHRDRPS
     QQPLRNQTAS SERRGEWEIQ PSRQTNTSYL TSHLAADRHG GSVQVVSSTN GELNVDDPTG
     AHSNAPITAH AEVEVVEEAK CCCFFKRKRK KTTQRHK
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024