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KC1D_XENTR
ID   KC1D_XENTR              Reviewed;         415 AA.
AC   Q6P647;
DT   25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 118.
DE   RecName: Full=Casein kinase I isoform delta;
DE            Short=CKI-delta;
DE            Short=CKId;
DE            EC=2.7.11.1 {ECO:0000250|UniProtKB:Q5BP74};
DE   AltName: Full=Tau-protein kinase CSNK1D;
DE            EC=2.7.11.26 {ECO:0000250|UniProtKB:P48730};
GN   Name=csnk1d; ORFNames=TEgg020f01.1;
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Egg;
RG   Sanger Xenopus tropicalis EST/cDNA project;
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Casein kinases are operationally defined by their
CC       preferential utilization of acidic proteins such as caseins as
CC       substrates. Central component of the circadian clock. May act as a
CC       negative regulator of circadian rhythmicity by phosphorylating per1 and
CC       per2, which may lead to their degradation. Participates in wnt
CC       signaling (By similarity). {ECO:0000250|UniProtKB:P48730,
CC       ECO:0000250|UniProtKB:Q5BP74}.
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         Evidence={ECO:0000250|UniProtKB:Q5BP74};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17990;
CC         Evidence={ECO:0000250|UniProtKB:Q5BP74};
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; Evidence={ECO:0000250|UniProtKB:Q5BP74};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46609;
CC         Evidence={ECO:0000250|UniProtKB:Q5BP74};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-seryl-[tau protein] = ADP + H(+) + O-phospho-L-seryl-
CC         [tau protein]; Xref=Rhea:RHEA:12801, Rhea:RHEA-COMP:13701, Rhea:RHEA-
CC         COMP:13702, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.26;
CC         Evidence={ECO:0000250|UniProtKB:P48730};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12802;
CC         Evidence={ECO:0000250|UniProtKB:P48730};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonyl-[tau protein] = ADP + H(+) + O-phospho-L-
CC         threonyl-[tau protein]; Xref=Rhea:RHEA:53904, Rhea:RHEA-COMP:13703,
CC         Rhea:RHEA-COMP:13704, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC         EC=2.7.11.26; Evidence={ECO:0000250|UniProtKB:P48730};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53905;
CC         Evidence={ECO:0000250|UniProtKB:P48730};
CC   -!- ACTIVITY REGULATION: Exhibits substrate-dependent heparin activation.
CC       {ECO:0000250|UniProtKB:P48730}.
CC   -!- SUBUNIT: Monomer (By similarity). Interacts with per1 and per2.
CC       Component of the circadian core oscillator (By similarity).
CC       {ECO:0000250|UniProtKB:P48730, ECO:0000250|UniProtKB:Q9DC28}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q5BP74}. Nucleus
CC       {ECO:0000250|UniProtKB:Q5BP74}.
CC   -!- PTM: Autophosphorylated on serine and threonine residues.
CC       {ECO:0000250|UniProtKB:Q5BP74}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. {ECO:0000305}.
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DR   EMBL; CR942537; CAJ81900.1; -; mRNA.
DR   EMBL; BC062487; AAH62487.1; -; mRNA.
DR   RefSeq; NP_989089.1; NM_203758.1.
DR   AlphaFoldDB; Q6P647; -.
DR   SMR; Q6P647; -.
DR   STRING; 8364.ENSXETP00000013928; -.
DR   PaxDb; Q6P647; -.
DR   DNASU; 394689; -.
DR   Ensembl; ENSXETT00000013928; ENSXETP00000013928; ENSXETG00000001288.
DR   GeneID; 394689; -.
DR   KEGG; xtr:394689; -.
DR   CTD; 1453; -.
DR   Xenbase; XB-GENE-5733929; csnk1d.
DR   eggNOG; KOG1164; Eukaryota.
DR   HOGENOM; CLU_019279_2_2_1; -.
DR   InParanoid; Q6P647; -.
DR   OrthoDB; 1097975at2759; -.
DR   Reactome; R-XTR-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR   Reactome; R-XTR-380259; Loss of Nlp from mitotic centrosomes.
DR   Reactome; R-XTR-380270; Recruitment of mitotic centrosome proteins and complexes.
DR   Reactome; R-XTR-380284; Loss of proteins required for interphase microtubule organization from the centrosome.
DR   Reactome; R-XTR-380320; Recruitment of NuMA to mitotic centrosomes.
DR   Reactome; R-XTR-5620912; Anchoring of the basal body to the plasma membrane.
DR   Reactome; R-XTR-8854518; AURKA Activation by TPX2.
DR   Proteomes; UP000008143; Chromosome 10.
DR   Proteomes; UP000790000; Unplaced.
DR   Bgee; ENSXETG00000001288; Expressed in 4-cell stage embryo and 25 other tissues.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0005876; C:spindle microtubule; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004672; F:protein kinase activity; ISS:UniProtKB.
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:1905515; P:non-motile cilium assembly; 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:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR   GO; GO:0042752; P:regulation of circadian rhythm; IBA:GO_Central.
DR   GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR   GO; GO:0051225; P:spindle assembly; IBA:GO_Central.
DR   GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
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; 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; Nucleus;
KW   Reference proteome; Serine/threonine-protein kinase; Transferase;
KW   Wnt signaling pathway.
FT   CHAIN           1..415
FT                   /note="Casein kinase I isoform delta"
FT                   /id="PRO_0000354090"
FT   DOMAIN          9..277
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          301..415
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          317..342
FT                   /note="Autoinhibitory"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        301..320
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        331..359
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        380..415
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        128
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         15..23
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         38
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   415 AA;  47372 MW;  597C9984282650D1 CRC64;
     MELRVGNRYR LGRKIGSGSF GDIYLGTDIA AAEEVAIKLE CVKTKHPQLH IESKIYKMMQ
     GGVGIPTIKW CGAEGDYNVM VMELLGPSLE DLFNFCSRKF SLKTVLLLAD QMISRIEYIH
     SKNFIHRDVK PDNFLMGLGK KGNLVYIIDF GLAKKYRDAR THQHIPYREN KNLTGTARYA
     SINTHLGIEQ SRRDDLESLG YVLMYFNLGS LPWQGLKAAT KRQKYERISE KKMSTPIEVL
     CKGYPSEFAT YLNFCRSLRF DDKPDYSYLR QLFRNLFHRQ GFSYDYVFDW NMLKFGANRA
     AEDAERERRE REERLRHPRN PAARGLPSTA SGRLRGTQEV TPSTPLTPTS HTANTSPRPV
     SGMERERKVS MRLHRGAPVN VSSSDLTGRQ ETSRMSTSQI PSRVASSGLP STVHR
 
 
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