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Protein

Thymidine kinase, cytosolic

Gene

TK1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Miscellaneous

Two forms have been identified in animal cells, one in cytosol and one in mitochondria. Activity of the cytosolic enzyme is high in proliferating cells and peaks during the S-phase of the cell cycle; it is very low in resting cells.

Catalytic activityi

ATP + thymidine = ADP + thymidine 5'-phosphate.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei98Proton acceptorSequence analysis1
Binding sitei128Substrate; via amide nitrogenCombined sources4 Publications1
Metal bindingi153ZincCombined sources4 Publications1
Metal bindingi156ZincCombined sources4 Publications1
Binding sitei181SubstrateCombined sources4 Publications1
Metal bindingi185ZincCombined sources4 Publications1
Metal bindingi188ZincCombined sources4 Publications1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi26 – 33ATPCombined sources4 Publications8
Nucleotide bindingi58 – 60ATPCombined sources3 Publications3
Nucleotide bindingi97 – 100ATPCombined sources2 Publications4

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • identical protein binding Source: IntAct
  • nucleoside kinase activity Source: Reactome
  • thymidine kinase activity Source: GO_Central
  • zinc ion binding Source: UniProtKB

GO - Biological processi

  • DNA biosynthetic process Source: UniProtKB-KW
  • DNA metabolic process Source: GO_Central
  • nucleobase-containing compound metabolic process Source: ProtInc
  • protein homotetramerization Source: UniProtKB
  • pyrimidine nucleoside salvage Source: Reactome
  • thymidine metabolic process Source: GO_Central

Keywordsi

Molecular functionKinase, Transferase
Biological processDNA synthesis
LigandATP-binding, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

BioCyciMetaCyc:HS09657-MONOMER.
BRENDAi2.7.1.21. 2681.
ReactomeiR-HSA-539107. Activation of E2F1 target genes at G1/S.
R-HSA-73614. Pyrimidine salvage.
SABIO-RKiP04183.
SIGNORiP04183.

Names & Taxonomyi

Protein namesi
Recommended name:
Thymidine kinase, cytosolic (EC:2.7.1.21)
Gene namesi
Name:TK1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 17

Organism-specific databases

EuPathDBiHostDB:ENSG00000167900.11.
HGNCiHGNC:11830. TK1.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi163T → S: 140-fold lower K(m) for AZT. 1 Publication1

Organism-specific databases

DisGeNETi7083.
OpenTargetsiENSG00000167900.
PharmGKBiPA352.

Chemistry databases

ChEMBLiCHEMBL2883.
DrugBankiDB01692. Dithioerythritol.
DB02452. Thymidine-5'-Triphosphate.
DB00432. Trifluridine.
DB00495. Zidovudine.

Polymorphism and mutation databases

BioMutaiTK1.
DMDMi23503074.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00001749482 – 234Thymidine kinase, cytosolicAdd BLAST233

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineCombined sources1
Modified residuei2PhosphoserineCombined sources1
Modified residuei13PhosphoserineCombined sources1 Publication1
Modified residuei231PhosphoserineCombined sources1

Post-translational modificationi

Phosphorylated on Ser-13 in mitosis.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP04183.
MaxQBiP04183.
PaxDbiP04183.
PeptideAtlasiP04183.
PRIDEiP04183.

PTM databases

iPTMnetiP04183.
PhosphoSitePlusiP04183.

Expressioni

Gene expression databases

BgeeiENSG00000167900.
CleanExiHS_TK1.
ExpressionAtlasiP04183. baseline and differential.
GenevisibleiP04183. HS.

Organism-specific databases

HPAiCAB004683.

Interactioni

Subunit structurei

Homotetramer.3 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • identical protein binding Source: IntAct

Protein-protein interaction databases

BioGridi112938. 173 interactors.
IntActiP04183. 160 interactors.
MINTiMINT-200463.
STRINGi9606.ENSP00000301634.

Chemistry databases

BindingDBiP04183.

Structurei

Secondary structure

1234
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi20 – 26Combined sources7
Helixi32 – 45Combined sources14
Beta strandi50 – 55Combined sources6
Helixi61 – 63Combined sources3
Helixi67 – 72Combined sources6
Beta strandi73 – 80Combined sources8
Helixi81 – 84Combined sources4
Helixi85 – 89Combined sources5
Beta strandi92 – 98Combined sources7
Helixi99 – 101Combined sources3
Helixi105 – 114Combined sources10
Beta strandi118 – 126Combined sources9
Beta strandi130 – 132Combined sources3
Helixi136 – 142Combined sources7
Beta strandi144 – 148Combined sources5
Turni154 – 156Combined sources3
Beta strandi158 – 160Combined sources3
Beta strandi162 – 167Combined sources6
Turni178 – 180Combined sources3
Beta strandi181 – 184Combined sources4
Helixi186 – 189Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1W4RX-ray1.83A/B/C/D/E/F/G/H15-194[»]
1XBTX-ray2.40A/B/C/D/E/F/G/H1-193[»]
2ORVX-ray2.30A/B1-234[»]
2WVJX-ray2.20A/B/C/D/E/F/G/H1-193[»]
ProteinModelPortaliP04183.
SMRiP04183.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP04183.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni172 – 176Substrate bindingCombined sources3 Publications5

Sequence similaritiesi

Belongs to the thymidine kinase family.Curated

Phylogenomic databases

eggNOGiKOG3125. Eukaryota.
COG1435. LUCA.
GeneTreeiENSGT00390000011309.
HOGENOMiHOG000076390.
HOVERGENiHBG006215.
InParanoidiP04183.
KOiK00857.
PhylomeDBiP04183.
TreeFamiTF314839.

Family and domain databases

InterProiView protein in InterPro
IPR027417. P-loop_NTPase.
IPR001267. Thymidine_kinase.
IPR020633. Thymidine_kinase_CS.
PANTHERiPTHR11441. PTHR11441. 1 hit.
PfamiView protein in Pfam
PF00265. TK. 1 hit.
PIRSFiPIRSF035805. TK_cell. 1 hit.
SUPFAMiSSF52540. SSF52540. 1 hit.
PROSITEiView protein in PROSITE
PS00603. TK_CELLULAR_TYPE. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P04183-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSCINLPTVL PGSPSKTRGQ IQVILGPMFS GKSTELMRRV RRFQIAQYKC
60 70 80 90 100
LVIKYAKDTR YSSSFCTHDR NTMEALPACL LRDVAQEALG VAVIGIDEGQ
110 120 130 140 150
FFPDIVEFCE AMANAGKTVI VAALDGTFQR KPFGAILNLV PLAESVVKLT
160 170 180 190 200
AVCMECFREA AYTKRLGTEK EVEVIGGADK YHSVCRLCYF KKASGQPAGP
210 220 230
DNKENCPVPG KPGEAVAARK LFAPQQILQC SPAN
Length:234
Mass (Da):25,469
Last modified:September 19, 2002 - v2
Checksum:i76901415C631EF21
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti106V → M in AAA61187 (PubMed:6549046).Curated1
Sequence conflicti106V → M in AAA61191 (PubMed:3301530).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K02581 mRNA. Translation: AAA61187.1.
M15205 Genomic DNA. Translation: AAA61191.1.
AK314950 mRNA. Translation: BAG37455.1.
BT006941 mRNA. Translation: AAP35587.1.
BC006484 mRNA. Translation: AAH06484.1.
BC007872 mRNA. Translation: AAH07872.1.
BC007986 mRNA. Translation: AAH07986.1.
M13643 Genomic DNA. Translation: AAA61189.1.
CCDSiCCDS11754.1.
PIRiA27318. KIHUT.
RefSeqiNP_003249.3. NM_003258.4.
UniGeneiHs.515122.

Genome annotation databases

EnsembliENST00000301634; ENSP00000301634; ENSG00000167900.
GeneIDi7083.
KEGGihsa:7083.
UCSCiuc002juw.3. human.

Similar proteinsi

Entry informationi

Entry nameiKITH_HUMAN
AccessioniPrimary (citable) accession number: P04183
Secondary accession number(s): B2RC58, Q969V0, Q9UMG9
Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 20, 1987
Last sequence update: September 19, 2002
Last modified: September 27, 2017
This is version 187 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families