P04184 (KITH_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Thymidine kinase, cytosolic
EC=2.7.1.21

Gene names

Name:	Tk1
Synonyms:	Tk-1

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	233 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level

General annotation (Comments)

Catalytic activity	ATP + thymidine = ADP + thymidine 5'-phosphate.
Subunit structure	Homotetramer By similarity.
Subcellular location	Cytoplasm.
Post-translational modification	Phosphorylated on Ser-13 in mitosis By similarity.
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.
Sequence similarities	Belongs to the thymidine kinase family.
Sequence caution	The sequence AAA40452.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	DNA synthesis
Cellular component	Cytoplasm
Coding sequence diversity	Polymorphism
Ligand	ATP-binding Metal-binding Nucleotide-binding Zinc
Molecular function	Kinase Transferase
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA replication Inferred from electronic annotation. Source: UniProtKB-KW digestive tract development Inferred from electronic annotation. Source: Compara fetal process involved in parturition Inferred from electronic annotation. Source: Compara liver development Inferred from electronic annotation. Source: Compara protein homotetramerization Inferred from electronic annotation. Source: Compara response to copper ion Inferred from electronic annotation. Source: Compara response to cortisol stimulus Inferred from electronic annotation. Source: Compara response to nutrient levels Inferred from electronic annotation. Source: Compara response to toxin Inferred from electronic annotation. Source: Compara skeletal muscle cell proliferation Inferred from electronic annotation. Source: Compara thymidine metabolic process Inferred from electronic annotation. Source: Compara
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW thymidine kinase activity Inferred from direct assay PubMed 204065. Source: MGI zinc ion binding Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 233	232	Thymidine kinase, cytosolic		PRO_0000174949
Regions
	Nucleotide binding	26 – 33	8	ATP Probable
	Nucleotide binding	58 – 60	3	ATP By similarity
	Nucleotide binding	97 – 100	4	ATP By similarity
	Region	172 – 176	5	Substrate binding By similarity
Sites
	Active site	98	1	Proton acceptor Potential
	Metal binding	153	1	Zinc By similarity
	Metal binding	156	1	Zinc By similarity
	Metal binding	185	1	Zinc By similarity
	Metal binding	188	1	Zinc By similarity
	Binding site	128	1	Substrate; via amide nitrogen By similarity
	Binding site	181	1	Substrate By similarity
Amino acid modifications
	Modified residue	2	1	N-acetylserine By similarity
	Modified residue	13	1	Phosphoserine By similarity
Natural variations
	Natural variant	88	1	S → A. Ref.3
Experimental info
	Sequence conflict	27	1	P → L in AAH91758. Ref.6
	Sequence conflict	88	1	S → L in AAA40451. Ref.1
	Sequence conflict	88	1	S → L in AAA40452. Ref.1
	Sequence conflict	185	1	C → G in BAC39384. Ref.5
	Sequence conflict	198	1	A → V in BAC39384. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	P04184 [UniParc]. Last modified February 26, 2008. Version 3. Checksum: 78366623EDED0C6C	FASTA	233	25,776
	10 20 30 40 50 60 MSYINLPTVL PSSPSKTRGQ IQVILGPMFS GKSTELMRRV RRFQIAQYKC LVIKYAKDTR 70 80 90 100 110 120 YSNSFSTHDR NTMDALPACM LRDVTQESLG VAVIGIDEGQ FFPDIVDFCE MMANEGKTVI 130 140 150 160 170 180 VAALDGTFQR KAFGSILNLV PLAESVVKLT AVCMECFREA AYTKRLGLEK EVEVIGGADK 190 200 210 220 230 YHSVCRLCYF KKSSAQTAGS DNKNCLVLGQ PGEALVVRKL FASQQVLQYN SAN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
IPI	IPI00648094.
PIR	KIMST. JC1252.
RefSeq	NP_001258658.1. NM_001271729.1. NP_033413.2. NM_009387.2.
UniGene	Mm.2661.
3D structure databases
ProteinModelPortal	P04184.
SMR	P04184. Positions 18-191.
ModBase	Search...
PTM databases
PhosphoSite	P04184.
Proteomic databases
PaxDb	P04184.
PRIDE	P04184.
Protocols and materials databases
DNASU	21877.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000026661; ENSMUSP00000026661; ENSMUSG00000025574.
GeneID	21877.
KEGG	mmu:21877.
Organism-specific databases
CTD	7083.
MGI	MGI:98763. Tk1.
Phylogenomic databases
eggNOG	COG1435.
GeneTree	ENSGT00390000011309.
HOGENOM	HOG000076390.
HOVERGEN	HBG006215.
InParanoid	P04184.
KO	K00857.
OMA	KVHAICV.
OrthoDB	EOG4VHK7C.
Enzyme and pathway databases
BRENDA	2.7.1.21. 3474.
SABIO-RK	P04184.
Gene expression databases
ArrayExpress	P04184.
Bgee	P04184.
CleanEx	MM_TK1.
Genevestigator	P04184.
GermOnline	ENSMUSG00000025574. Mus musculus.
Family and domain databases
InterPro	IPR001267. Thymidine_kinase. IPR020633. Thymidine_kinase_CS. [Graphical view]
PANTHER	PTHR11441. PTHR11441. 1 hit.
Pfam	PF00265. TK. 1 hit. [Graphical view]
PIRSF	PIRSF035805. TK_cell. 1 hit.
PROSITE	PS00603. TK_CELLULAR_TYPE. 1 hit. [Graphical view]
ProtoNet	Search...
Other
BindingDB	P04184.
ChEMBL	CHEMBL2618.
NextBio	301386.
SOURCE	Search...

Entry information

Entry name

KITH_MOUSE

Accession

Primary (citable) accession number: P04184
Secondary accession number(s): Q58EU0, Q8C3P8, Q921J8

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 20, 1987
Last sequence update:	February 26, 2008
Last modified:	April 3, 2013
This is version 102 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program