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KITH_CRIGR
ID   KITH_CRIGR              Reviewed;         234 AA.
AC   P09768;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=Thymidine kinase, cytosolic;
DE            EC=2.7.1.21 {ECO:0000250|UniProtKB:P04183};
GN   Name=TK1;
OS   Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Cricetinae; Cricetulus.
OX   NCBI_TaxID=10029;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3453109; DOI=10.1128/mcb.6.6.1998-2010.1986;
RA   Lewis J.A.;
RT   "Structure and expression of the Chinese hamster thymidine kinase gene.";
RL   Mol. Cell. Biol. 6:1998-2010(1986).
CC   -!- FUNCTION: Cell-cycle-regulated enzyme of importance in nucleotide
CC       metabolism. Catalyzes the first enzymatic step in the salvage pathway
CC       converting thymidine into thymidine monophosphate. Transcriptional
CC       regulation limits expression to the S phase of the cell cycle and
CC       transient expression coincides with the oscillation in the
CC       intracellular dTTP concentration. {ECO:0000250|UniProtKB:P04183}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + thymidine = ADP + dTMP + H(+); Xref=Rhea:RHEA:19129,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17748, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:63528, ChEBI:CHEBI:456216; EC=2.7.1.21;
CC         Evidence={ECO:0000250|UniProtKB:P04183};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19130;
CC         Evidence={ECO:0000250|UniProtKB:P04183};
CC   -!- SUBUNIT: Homotetramer. Tetramerization from dimerization is induced by
CC       ATP and increases catalytic efficiency due to a high affinity for
CC       thymidine. Tetramerization is inhibited by phosphorylation at Ser-13.
CC       Interacts (via the KEN box) with FZR1. {ECO:0000250|UniProtKB:P04183}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- DOMAIN: KEN box sequence located in the C-terminal region is required
CC       for its mitotic degradation by the APC/C-FZR1 ubiquitin ligase and
CC       interaction capability with FZR1. {ECO:0000250|UniProtKB:P04183}.
CC   -!- PTM: Phosphorylated on Ser-13 in mitosis. Phosphorylation of Ser-13 by
CC       CDK1 during mitosis reduces homotetramerization and catalytic
CC       efficiency when DNA replication is complete and intracellular TK1 is
CC       still present at a high level. {ECO:0000250|UniProtKB:P04183}.
CC   -!- PTM: Polyubiquitinated. Postmitosis, ubiquitination leads to
CC       proteasomal degradation. The KEN box sequence located at the C-terminal
CC       region targets for degradation by the anaphase promoting complex
CC       (APC/C) activated and rate-limited by FZR1.
CC       {ECO:0000250|UniProtKB:P04183}.
CC   -!- MISCELLANEOUS: Two forms have been identified in animal cells, one in
CC       cytosol and one in mitochondria. Activity of the cytosolic enzyme is
CC       high in proliferating cells and peaks during the S-phase of the cell
CC       cycle; it is very low in resting cells.
CC   -!- SIMILARITY: Belongs to the thymidine kinase family. {ECO:0000305}.
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DR   EMBL; L00369; AAA37022.1; -; Genomic_DNA.
DR   EMBL; L00364; AAA37022.1; JOINED; Genomic_DNA.
DR   EMBL; L00365; AAA37022.1; JOINED; Genomic_DNA.
DR   EMBL; L00366; AAA37022.1; JOINED; Genomic_DNA.
DR   EMBL; L00367; AAA37022.1; JOINED; Genomic_DNA.
DR   EMBL; L00368; AAA37022.1; JOINED; Genomic_DNA.
DR   PIR; A25243; A25243.
DR   RefSeq; NP_001231423.1; NM_001244494.2.
DR   AlphaFoldDB; P09768; -.
DR   SMR; P09768; -.
DR   STRING; 10029.NP_001231423.1; -.
DR   BindingDB; P09768; -.
DR   ChEMBL; CHEMBL3227916; -.
DR   Ensembl; ENSCGRT00001023730; ENSCGRP00001019486; ENSCGRG00001018904.
DR   GeneID; 100689285; -.
DR   KEGG; cge:100689285; -.
DR   CTD; 7083; -.
DR   eggNOG; KOG3125; Eukaryota.
DR   GeneTree; ENSGT00390000011309; -.
DR   OMA; GWLELIC; -.
DR   OrthoDB; 1413914at2759; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR   GO; GO:0004797; F:thymidine kinase activity; ISS:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR   GO; GO:0071897; P:DNA biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0051289; P:protein homotetramerization; ISS:UniProtKB.
DR   GO; GO:0046104; P:thymidine metabolic process; ISS:UniProtKB.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR001267; Thymidine_kinase.
DR   InterPro; IPR020633; Thymidine_kinase_CS.
DR   PANTHER; PTHR11441; PTHR11441; 1.
DR   Pfam; PF00265; TK; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS00603; TK_CELLULAR_TYPE; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; DNA synthesis; Kinase; Metal-binding;
KW   Nucleotide-binding; Phosphoprotein; Transferase; Ubl conjugation; Zinc.
FT   CHAIN           1..234
FT                   /note="Thymidine kinase, cytosolic"
FT                   /id="PRO_0000174947"
FT   MOTIF           203..205
FT                   /note="KEN box"
FT                   /evidence="ECO:0000250|UniProtKB:P04183"
FT   ACT_SITE        98
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255"
FT   BINDING         26..33
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000305"
FT   BINDING         58..60
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P04183"
FT   BINDING         97..100
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P04183"
FT   BINDING         128
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P04183"
FT   BINDING         153
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P04183"
FT   BINDING         156
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P04183"
FT   BINDING         172..176
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P04183"
FT   BINDING         181
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P04183"
FT   BINDING         185
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P04183"
FT   BINDING         188
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P04183"
FT   MOD_RES         13
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P04183"
SQ   SEQUENCE   234 AA;  25622 MW;  8E46DC89FEAF2E9C CRC64;
     MNYINLPTVL PGSPSKTRGQ IQVILGPMFS GKSTELMRRV RRFQIAQNKC LVIKYAKDTR
     YSSSFSTHDR NTMDALPACL LRDVAQEALG AAVIGIDEGQ FFPDIVEFCE VMANAGKTVI
     VAALDGTFQR KAFGSILNLV PLAESVVKLT AVCMECFREA AYTKRLGLEK EVEVIGGADK
     YHSVCRVCYF KKSSVQPAGP DNKENCPVLG QPGEASAVRK LFAPQQVLQH NSTN
 
 
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