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Protein Page:
TK (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitylation
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
TK cytosolic thymidine kinase. Phosphorylated during mitosis. Its enzymatic activity is high in proliferating cells and peaks during the S-phase of the cell cycle; it is very low in resting cells. Note: This description may include information from UniProtKB.
Protein type: Kinase, other; Xenobiotic Metabolism - drug metabolism - other enzymes; EC 2.7.1.21; Nucleotide Metabolism - pyrimidine
Chromosomal Location of Human Ortholog: 17q23.2-q25.3
Cellular Component: cytosol
Molecular Function: ATP binding; identical protein binding; nucleoside kinase activity; protein binding; thymidine kinase activity; zinc ion binding
Biological Process: deoxyribonucleoside monophosphate biosynthetic process; DNA metabolic process; fetal process involved in parturition; gut development; liver development; nucleobase, nucleoside, nucleotide and nucleic acid metabolic process; nucleotide biosynthetic process; phosphorylation; protein homotetramerization; pyrimidine nucleoside salvage; response to copper ion; response to cortisol stimulus; response to nutrient levels; response to toxin; skeletal muscle cell proliferation; thymidine metabolic process
Reference #:  P04183 (UniProtKB)
Alt. Names/Synonyms: KITH; thymidine kinase 1 soluble isoform; thymidine kinase 1, soluble; Thymidine kinase, cytosolic; thymidine kinase-1; TK1; TK2
Gene Symbols: TK1
Molecular weight: 25,469 Da
Basal Isoelectric point: 8.85  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

TK

Protein Structure Not Found.
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Sites Implicated In
enzymatic activity, induced: S13‑p, S231‑p
enzymatic activity, inhibited: S13‑p
molecular association, regulation: S13‑p
protein degradation: S13‑p

Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 LTP 

LTP: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 HTP 

HTP: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 1 S2‑p ______MsCINLPtV
0 1 T8‑p MsCINLPtVLPGsPs
0 1 G12 NLPtVLPGsPsKTRG
4 11 S13‑p LPtVLPGsPsKTRGQ
0 1 S15‑p tVLPGsPsKTRGQIQ
0 1 K16 VLPGsPsKTRGQIQV
0 1 S30‑p VILGPMFsGkSTELM
0 1 K32‑ac LGPMFsGkSTELMRR
0 1 Y48‑p RRFQIAQyKCLVIKy
0 1 Y55‑p yKCLVIKyAKDTRYs
0 1 S62‑p yAKDTRYsSSFCTHD
0 1 T127 IVAALDGTFQRkPFG
0 5 K131‑ub LDGTFQRkPFGAILN
0 1 K164‑ac FREAAYTkRLGTEkE
0 1 K170‑ub TkRLGTEkEVEVIGG
0 1 K180‑ub EVIGGADkyHsVCRL
0 14 Y181‑p VIGGADkyHsVCRLC
0 2 S183‑p GGADkyHsVCRLCYF
0 3 K203‑ub QPAGPDNkENCPVPG
0 9 K220‑ac GEAVAARkLFAPQQI
0 1 K220‑ub GEAVAARkLFAPQQI
1 23 S231‑p PQQILQCsPAN____
  mouse

 
S2 ______MSYINLPTV
T8 MSYINLPTVLPssPS
S12‑p NLPTVLPssPSkTRG
S13‑p LPTVLPssPSkTRGQ
S15 TVLPssPSkTRGQIQ
K16‑ub VLPssPSkTRGQIQV
S30 VILGPMFSGKSTELM
K32 LGPMFSGKSTELMRR
Y48 RRFQIAQYKCLVIKY
Y55 YKCLVIKYAKDTRYS
S62 YAKDTRYSNSFSTHD
T127‑p IVAALDGtFQRkAFG
K131‑ub LDGtFQRkAFGSILN
K164 FREAAYTKRLGLEKE
K170 TKRLGLEKEVEVIGG
K180 EVIGGADKYHSVCRL
Y181 VIGGADKYHSVCRLC
S183 GGADKYHSVCRLCYF
K203‑ub QTAGSDNkNCLVLGQ
K219 GEALVVRKLFASQQV
K219 GEALVVRKLFASQQV
N230 SQQVLQYNSAN____
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