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P04183

- KITH_HUMAN

UniProt

P04183 - KITH_HUMAN

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Protein

Thymidine kinase, cytosolic

Gene
TK1
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei98 – 981Proton acceptor Reviewed prediction
Binding sitei128 – 1281Substrate; via amide nitrogen
Metal bindingi153 – 1531Zinc
Metal bindingi156 – 1561Zinc
Binding sitei181 – 1811Substrate
Metal bindingi185 – 1851Zinc
Metal bindingi188 – 1881Zinc

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi26 – 338ATP
Nucleotide bindingi58 – 603ATP
Nucleotide bindingi97 – 1004ATP

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. identical protein binding Source: IntAct
  3. nucleoside kinase activity Source: Reactome
  4. thymidine kinase activity Source: ProtInc
  5. zinc ion binding Source: UniProtKB

GO - Biological processi

  1. deoxyribonucleoside monophosphate biosynthetic process Source: GOC
  2. digestive tract development Source: Ensembl
  3. DNA replication Source: UniProtKB-KW
  4. fetal process involved in parturition Source: Ensembl
  5. liver development Source: Ensembl
  6. nucleobase-containing compound metabolic process Source: ProtInc
  7. nucleobase-containing small molecule metabolic process Source: Reactome
  8. nucleotide biosynthetic process Source: GOC
  9. protein homotetramerization Source: UniProtKB
  10. pyrimidine nucleobase metabolic process Source: Reactome
  11. pyrimidine nucleoside salvage Source: Reactome
  12. response to copper ion Source: Ensembl
  13. response to cortisol Source: Ensembl
  14. response to nutrient levels Source: Ensembl
  15. response to toxic substance Source: Ensembl
  16. skeletal muscle cell proliferation Source: Ensembl
  17. small molecule metabolic process Source: Reactome
  18. thymidine metabolic process Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

DNA synthesis

Keywords - Ligandi

ATP-binding, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

BioCyciMetaCyc:HS09657-MONOMER.
BRENDAi2.7.1.21. 2681.
ReactomeiREACT_655. Pyrimidine salvage reactions.
SABIO-RKP04183.

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
ProteomesiUP000005640: Chromosome 17

Organism-specific databases

HGNCiHGNC:11830. TK1.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA352.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 234233Thymidine kinase, cytosolicPRO_0000174948Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine4 Publications
Modified residuei13 – 131Phosphoserine1 Publication
Modified residuei231 – 2311Phosphoserine2 Publications

Post-translational modificationi

Phosphorylated on Ser-13 in mitosis.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP04183.
PaxDbiP04183.
PeptideAtlasiP04183.
PRIDEiP04183.

PTM databases

PhosphoSiteiP04183.

Expressioni

Gene expression databases

ArrayExpressiP04183.
BgeeiP04183.
CleanExiHS_TK1.
GenevestigatoriP04183.

Organism-specific databases

HPAiCAB004683.

Interactioni

Subunit structurei

Homotetramer.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-712550,EBI-712550

Protein-protein interaction databases

BioGridi112938. 160 interactions.
IntActiP04183. 157 interactions.
MINTiMINT-200463.
STRINGi9606.ENSP00000301634.

Structurei

Secondary structure

1
234
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi20 – 267
Helixi32 – 4514
Beta strandi50 – 556
Helixi61 – 633
Helixi67 – 726
Beta strandi73 – 808
Helixi81 – 844
Helixi85 – 895
Beta strandi92 – 987
Helixi99 – 1013
Helixi105 – 11410
Beta strandi118 – 1269
Beta strandi130 – 1323
Helixi136 – 1427
Beta strandi144 – 1485
Turni154 – 1563
Beta strandi158 – 1603
Beta strandi162 – 1676
Turni178 – 1803
Beta strandi181 – 1844
Helixi186 – 1894

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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. Positions 18-191.

Miscellaneous databases

EvolutionaryTraceiP04183.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni172 – 1765Substrate binding

Sequence similaritiesi

Belongs to the thymidine kinase family.

Phylogenomic databases

eggNOGiCOG1435.
HOGENOMiHOG000076390.
HOVERGENiHBG006215.
InParanoidiP04183.
KOiK00857.
OrthoDBiEOG7MSMPX.
PhylomeDBiP04183.
TreeFamiTF314839.

Family and domain databases

InterProiIPR027417. P-loop_NTPase.
IPR001267. Thymidine_kinase.
IPR020633. Thymidine_kinase_CS.
[Graphical view]
PANTHERiPTHR11441. PTHR11441. 1 hit.
PfamiPF00265. TK. 1 hit.
[Graphical view]
PIRSFiPIRSF035805. TK_cell. 1 hit.
SUPFAMiSSF52540. SSF52540. 1 hit.
PROSITEiPS00603. TK_CELLULAR_TYPE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P04183-1 [UniParc]FASTAAdd to Basket

« Hide

MSCINLPTVL PGSPSKTRGQ IQVILGPMFS GKSTELMRRV RRFQIAQYKC    50
LVIKYAKDTR YSSSFCTHDR NTMEALPACL LRDVAQEALG VAVIGIDEGQ 100
FFPDIVEFCE AMANAGKTVI VAALDGTFQR KPFGAILNLV PLAESVVKLT 150
AVCMECFREA AYTKRLGTEK EVEVIGGADK YHSVCRLCYF KKASGQPAGP 200
DNKENCPVPG KPGEAVAARK LFAPQQILQC SPAN 234
Length:234
Mass (Da):25,469
Last modified:September 19, 2002 - v2
Checksum:i76901415C631EF21
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti106 – 1061V → M in AAA61187. 1 Publication
Sequence conflicti106 – 1061V → M in AAA61191. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.
ENST00000405273; ENSP00000384981; ENSG00000167900.
GeneIDi7083.
KEGGihsa:7083.
UCSCiuc002juw.2. human.

Polymorphism databases

DMDMi23503074.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS11754.1.
PIRi A27318. KIHUT.
RefSeqi NP_003249.3. NM_003258.4.
UniGenei Hs.515122.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1W4R X-ray 1.83 A/B/C/D/E/F/G/H 15-194 [» ]
1XBT X-ray 2.40 A/B/C/D/E/F/G/H 1-193 [» ]
2ORV X-ray 2.30 A/B 1-234 [» ]
2WVJ X-ray 2.20 A/B/C/D/E/F/G/H 1-193 [» ]
ProteinModelPortali P04183.
SMRi P04183. Positions 18-191.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 112938. 160 interactions.
IntActi P04183. 157 interactions.
MINTi MINT-200463.
STRINGi 9606.ENSP00000301634.

Chemistry

BindingDBi P04183.
ChEMBLi CHEMBL2883.

PTM databases

PhosphoSitei P04183.

Polymorphism databases

DMDMi 23503074.

Proteomic databases

MaxQBi P04183.
PaxDbi P04183.
PeptideAtlasi P04183.
PRIDEi P04183.

Protocols and materials databases

DNASUi 7083.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000301634 ; ENSP00000301634 ; ENSG00000167900 .
ENST00000405273 ; ENSP00000384981 ; ENSG00000167900 .
GeneIDi 7083.
KEGGi hsa:7083.
UCSCi uc002juw.2. human.

Organism-specific databases

CTDi 7083.
GeneCardsi GC17M076170.
HGNCi HGNC:11830. TK1.
HPAi CAB004683.
MIMi 188300. gene.
neXtProti NX_P04183.
PharmGKBi PA352.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1435.
HOGENOMi HOG000076390.
HOVERGENi HBG006215.
InParanoidi P04183.
KOi K00857.
OrthoDBi EOG7MSMPX.
PhylomeDBi P04183.
TreeFami TF314839.

Enzyme and pathway databases

BioCyci MetaCyc:HS09657-MONOMER.
BRENDAi 2.7.1.21. 2681.
Reactomei REACT_655. Pyrimidine salvage reactions.
SABIO-RK P04183.

Miscellaneous databases

ChiTaRSi TK1. human.
EvolutionaryTracei P04183.
GeneWikii Thymidine_kinase_1.
GenomeRNAii 7083.
NextBioi 27705.
PROi P04183.
SOURCEi Search...

Gene expression databases

ArrayExpressi P04183.
Bgeei P04183.
CleanExi HS_TK1.
Genevestigatori P04183.

Family and domain databases

InterProi IPR027417. P-loop_NTPase.
IPR001267. Thymidine_kinase.
IPR020633. Thymidine_kinase_CS.
[Graphical view ]
PANTHERi PTHR11441. PTHR11441. 1 hit.
Pfami PF00265. TK. 1 hit.
[Graphical view ]
PIRSFi PIRSF035805. TK_cell. 1 hit.
SUPFAMi SSF52540. SSF52540. 1 hit.
PROSITEi PS00603. TK_CELLULAR_TYPE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Human thymidine kinase gene: molecular cloning and nucleotide sequence of a cDNA expressible in mammalian cells."
    Bradshaw H.D. Jr., Deininger P.L.
    Mol. Cell. Biol. 4:2316-2320(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Sequence, structure and promoter characterization of the human thymidine kinase gene."
    Flemington E., Bradshaw H.D. Jr., Traina-Dorge V., Slagel V., Deininger P.L.
    Gene 52:267-277(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  4. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Lymph, Skin and Uterus.
  6. "Genetic analysis of the human thymidine kinase gene promoter."
    Kreidberg J.A., Kelly T.J.
    Mol. Cell. Biol. 6:2903-2909(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-22.
  7. "Serine 13 is the site of mitotic phosphorylation of human thymidine kinase."
    Chang Z.F., Huang D.Y., Chi L.M.
    J. Biol. Chem. 273:12095-12100(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-13.
  8. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
    Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
    Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-231, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  11. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-231, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. Cited for: X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 1-193 IN COMPLEX WITH ZINC IONS AND TTP, SUBUNIT.
  16. Cited for: X-RAY CRYSTALLOGRAPHY (1.83 ANGSTROMS) OF 15-194 IN COMPLEX WITH ZINC IONS AND TTP.
  17. "Binding of ATP to TK1-like enzymes is associated with a conformational change in the quaternary structure."
    Segura-Pena D., Lutz S., Monnerjahn C., Konrad M., Lavie A.
    J. Mol. Biol. 369:129-141(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) IN COMPLEX WITH ZINC IONS; SUBSTRATE AND ATP ANALOG, SUBUNIT.

Entry informationi

Entry nameiKITH_HUMAN
AccessioniPrimary (citable) accession number: P04183
Secondary accession number(s): B2RC58, Q969V0, Q9UMG9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 20, 1987
Last sequence update: September 19, 2002
Last modified: September 3, 2014
This is version 157 of the entry and version 2 of the sequence. [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

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.

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

External Data

Dasty 3

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