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Protein

Thymidine kinase, cytosolic

Gene

Tk1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei98 – 981Proton acceptorSequence Analysis
Binding sitei128 – 1281Substrate; via amide nitrogenBy similarity
Metal bindingi153 – 1531ZincBy similarity
Metal bindingi156 – 1561ZincBy similarity
Binding sitei181 – 1811SubstrateBy similarity
Metal bindingi185 – 1851ZincBy similarity
Metal bindingi188 – 1881ZincBy similarity

Regions

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

GO - Molecular functioni

GO - Biological processi

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

BRENDAi2.7.1.21. 3474.
ReactomeiREACT_295314. Pyrimidine salvage reactions.
SABIO-RKP04184.

Names & Taxonomyi

Protein namesi
Recommended name:
Thymidine kinase, cytosolic (EC:2.7.1.21)
Gene namesi
Name:Tk1
Synonyms:Tk-1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:98763. Tk1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 233232Thymidine kinase, cytosolicPRO_0000174949Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity
Modified residuei13 – 131PhosphoserineBy similarity

Post-translational modificationi

Phosphorylated on Ser-13 in mitosis.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP04184.
PaxDbiP04184.
PRIDEiP04184.

PTM databases

PhosphoSiteiP04184.

Expressioni

Gene expression databases

BgeeiP04184.
CleanExiMM_TK1.
ExpressionAtlasiP04184. baseline and differential.
GenevisibleiP04184. MM.

Interactioni

Subunit structurei

Homotetramer.By similarity

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000026661.

Structurei

3D structure databases

ProteinModelPortaliP04184.
SMRiP04184. Positions 18-191.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

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

Sequence similaritiesi

Belongs to the thymidine kinase family.Curated

Phylogenomic databases

eggNOGiCOG1435.
GeneTreeiENSGT00390000011309.
HOGENOMiHOG000076390.
HOVERGENiHBG006215.
InParanoidiP04184.
KOiK00857.
OMAiVITGPMY.
OrthoDBiEOG7MSMPX.
PhylomeDBiP04184.
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]
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.

P04184-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSYINLPTVL PSSPSKTRGQ IQVILGPMFS GKSTELMRRV RRFQIAQYKC
60 70 80 90 100
LVIKYAKDTR YSNSFSTHDR NTMDALPACM LRDVTQESLG VAVIGIDEGQ
110 120 130 140 150
FFPDIVDFCE MMANEGKTVI VAALDGTFQR KAFGSILNLV PLAESVVKLT
160 170 180 190 200
AVCMECFREA AYTKRLGLEK EVEVIGGADK YHSVCRLCYF KKSSAQTAGS
210 220 230
DNKNCLVLGQ PGEALVVRKL FASQQVLQYN SAN
Length:233
Mass (Da):25,776
Last modified:February 26, 2008 - v3
Checksum:i78366623EDED0C6C
GO

Sequence cautioni

The sequence AAA40452.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti27 – 271P → L in AAH91758 (PubMed:15489334).Curated
Sequence conflicti88 – 881S → L in AAA40451 (PubMed:3018504).Curated
Sequence conflicti88 – 881S → L in AAA40452 (PubMed:3018504).Curated
Sequence conflicti185 – 1851C → G in BAC39384 (PubMed:16141072).Curated
Sequence conflicti198 – 1981A → V in BAC39384 (PubMed:16141072).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti88 – 881S → A.1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M11945 mRNA. Translation: AAA40451.1.
M19438 mRNA. Translation: AAA40452.1. Different initiation.
M68489 Genomic DNA. Translation: AAA40454.1.
S57244 mRNA. Translation: AAB26001.1.
AK085188 mRNA. Translation: BAC39384.1.
AK087988 mRNA. Translation: BAC40077.1.
AK139244 mRNA. Translation: BAE23931.1.
BC012215 mRNA. Translation: AAH12215.1.
BC091758 mRNA. Translation: AAH91758.1.
X60980 Genomic DNA. Translation: CAA43296.1.
M22581 Genomic DNA. Translation: AAA40450.1.
CCDSiCCDS25692.1.
PIRiJC1252. KIMST.
RefSeqiNP_001258658.1. NM_001271729.1.
NP_033413.2. NM_009387.2.
UniGeneiMm.2661.

Genome annotation databases

EnsembliENSMUST00000026661; ENSMUSP00000026661; ENSMUSG00000025574.
GeneIDi21877.
KEGGimmu:21877.
UCSCiuc007mnz.2. mouse.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M11945 mRNA. Translation: AAA40451.1.
M19438 mRNA. Translation: AAA40452.1. Different initiation.
M68489 Genomic DNA. Translation: AAA40454.1.
S57244 mRNA. Translation: AAB26001.1.
AK085188 mRNA. Translation: BAC39384.1.
AK087988 mRNA. Translation: BAC40077.1.
AK139244 mRNA. Translation: BAE23931.1.
BC012215 mRNA. Translation: AAH12215.1.
BC091758 mRNA. Translation: AAH91758.1.
X60980 Genomic DNA. Translation: CAA43296.1.
M22581 Genomic DNA. Translation: AAA40450.1.
CCDSiCCDS25692.1.
PIRiJC1252. KIMST.
RefSeqiNP_001258658.1. NM_001271729.1.
NP_033413.2. NM_009387.2.
UniGeneiMm.2661.

3D structure databases

ProteinModelPortaliP04184.
SMRiP04184. Positions 18-191.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000026661.

Chemistry

BindingDBiP04184.
ChEMBLiCHEMBL2618.

PTM databases

PhosphoSiteiP04184.

Proteomic databases

MaxQBiP04184.
PaxDbiP04184.
PRIDEiP04184.

Protocols and materials databases

DNASUi21877.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000026661; ENSMUSP00000026661; ENSMUSG00000025574.
GeneIDi21877.
KEGGimmu:21877.
UCSCiuc007mnz.2. mouse.

Organism-specific databases

CTDi7083.
MGIiMGI:98763. Tk1.

Phylogenomic databases

eggNOGiCOG1435.
GeneTreeiENSGT00390000011309.
HOGENOMiHOG000076390.
HOVERGENiHBG006215.
InParanoidiP04184.
KOiK00857.
OMAiVITGPMY.
OrthoDBiEOG7MSMPX.
PhylomeDBiP04184.
TreeFamiTF314839.

Enzyme and pathway databases

BRENDAi2.7.1.21. 3474.
ReactomeiREACT_295314. Pyrimidine salvage reactions.
SABIO-RKP04184.

Miscellaneous databases

NextBioi301386.
PROiP04184.
SOURCEiSearch...

Gene expression databases

BgeeiP04184.
CleanExiMM_TK1.
ExpressionAtlasiP04184. baseline and differential.
GenevisibleiP04184. MM.

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]
SUPFAMiSSF52540. SSF52540. 1 hit.
PROSITEiPS00603. TK_CELLULAR_TYPE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning and structural analysis of murine thymidine kinase genomic and cDNA sequences."
    Lin P.-F., Lieberman H.B., Yeh D.-B., Xu T., Zhao S.-Y., Ruddle F.H.
    Mol. Cell. Biol. 5:3149-3156(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Regulation of thymidine kinase during growth, cell cycle and differentiation."
    Wintersberger E., Rotheneder H., Grabner M., Beck G., Seiser C.
    Adv. Enzyme Regul. 32:241-254(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
  3. "Characterization of the murine thymidine kinase-encoding gene and analysis of transcription start point heterogeneity."
    Gudas J.M., Fridovich-Keil J.L., Datta M.W., Bryan J., Pardee A.B.
    Gene 118:205-216(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ALA-88.
  4. "Sequence analysis of tka(-)-1 and tkb(+)-1 alleles in L5178Y tk+/-mouse-lymphoma cells and spontaneous tk-/-mutants."
    Liechty M.C., Rauchfuss H.S., Lugo M.H., Hozier J.C.
    Mutat. Res. 286:299-307(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  5. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J and NOD.
    Tissue: Cerebellum, Stomach and Thymus.
  6. "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].
    Strain: FVB/N and NMRI.
    Tissue: Mammary tumor.
  7. "Presence of regulatory sequences within intron 2 of the mouse thymidine kinase gene."
    Rotheneder H., Grabner M., Wintersberger E.
    Nucleic Acids Res. 19:6805-6809(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-32.
    Tissue: Liver.
  8. "Transcriptional and posttranscriptional mechanisms regulate murine thymidine kinase gene expression in serum-stimulated cells."
    Lieberman H.B., Lin P.F., Yeh D.B., Ruddle F.H.
    Mol. Cell. Biol. 8:5280-5291(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-27.

Entry informationi

Entry nameiKITH_MOUSE
AccessioniPrimary (citable) accession number: P04184
Secondary accession number(s): Q58EU0, Q8C3P8, Q921J8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 20, 1987
Last sequence update: February 26, 2008
Last modified: June 24, 2015
This is version 120 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

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

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.