Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Thymidine kinase, cytosolic  

UniProtKB / Swiss-Prot ID :  KITH_HUMAN

Gene Name (Synonyms) : 
TK1  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Cytoplasm. 

Protein Function :   

Protein Sequence MSCINLPTVLPGSPSKTRGQIQVILGPMFSGKSTELMRRVRRFQIAQYKCLVIKYAKDTRYSSSFCTHDR...
Predicted Secondary Structure CCEEECCCCCCCCCCCCCEEEEEEEECCCCCHHHHHHHHHHHHHHCCCCEEEEEECCCCCCCCEEEEECC...
Protein Variant -
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
2N-acetylserine---MSCINL
---CCEEEC
24.57HPRD
Link-
13PhosphoserineVLPGSPSKT
CCCCCCCCC
24.86Phosphositeplus
Link-
13Phosphoserine (CDK1)VLPGSPSKT
CCCCCCCCC
24.86HPRD
Link-
13Phosphoserine (CDK1;CDK2)VLPGSPSKT
CCCCCCCCC
24.86PhosphoELM
Link-
13Phosphoserine.VLPGSPSKT
CCCCCCCCC
24.86UniProtKB
Link-
15PhosphoserinePGSPSKTRG
CCCCCCCCE
48.64HPRD
Link-
15Phosphoserine.PGSPSKTRG
CCCCCCCCE
48.64UniProtKB
Link-
170Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)LGTEKEVEV
EECCCCEEE
67.88Phosphositeplus
Link
181PhosphotyrosineGADKYHSVC
CCCEEEEEC
10.40Phosphositeplus
Link
220Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)VAARKLFAP
HHHHHHHCC
43.14Phosphositeplus
Link-
231PhosphoserineILQCSPAN
HHCCCCCC
17.68HPRD
Link-
231PhosphoserineILQCSPAN
HHCCCCCC
17.68PhosphoELM
Link-
231PhosphoserineILQCSPAN
HHCCCCCC
17.68Phosphositeplus
Link-
231PhosphoserineILQCSPAN
HHCCCCCC
17.68SysPTM
Link-
231Phosphoserine.ILQCSPAN
HHCCCCCC
17.68UniProtKB
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
GDF9_HUMANphysical interactionMINT-63363MINT16169070
CDN1A_HUMANphysical interactionMINT-18464MINT11389691
TLE1_HUMANphysical interactionMINT-63367MINT16169070
UN119_HUMANphysical interactionMINT-63368MINT16169070
DPYL1_HUMANphysical interactionMINT-63369MINT16169070
DRAP1_HUMANphysical interactionMINT-63370MINT16169070
SETB1_HUMANphysical interactionMINT-63371MINT16169070
CSN6_HUMANphysical interactionMINT-63374MINT16169070
Q9P078_HUMANphysical interactionMINT-63377MINT16169070
ERG28_HUMANphysical interactionMINT-63378MINT16169070
GDF9_HUMANphysical interactionEBI-733553
intact16169070
CC90B_HUMANphysical interactionEBI-733556
intact16169070
PTPRK_HUMANphysical interactionEBI-733559
intact16169070
DPYL1_HUMANphysical interactionEBI-729372
intact16169070
G3P_HUMANphysical interactionEBI-729375
intact16169070
RIF1_HUMANphysical interactionEBI-729378
intact16169070
TLE1_HUMANphysical interactionEBI-729381
intact16169070
P53_HUMANphysical interactionEBI-729384
intact16169070
UN119_HUMANphysical interactionEBI-729387
intact16169070
APLP1_HUMANphysical interactionEBI-730975
intact16169070
ERG28_HUMANphysical interactionEBI-730978
intact16169070
CSN6_HUMANphysical interactionEBI-730981
intact16169070
YG012_HUMANphysical interactionEBI-730984
intact16169070
Q5RL73_HUMANphysical interactionEBI-730984
intact16169070
DRAP1_HUMANphysical interactionEBI-730987
intact16169070
SETB1_HUMANphysical interactionEBI-730990
intact16169070
TBB2A_HUMANphysical interactionEBI-730993
intact16169070
CDN1A_HUMANin vitro
in vivo
HPRD:01771HPRD11389691
P53_HUMANyeast 2-hybridHPRD:01771HPRD16169070
TLE1_HUMANyeast 2-hybridHPRD:01771HPRD16169070
DRAP1_HUMANyeast 2-hybridHPRD:01771HPRD16169070
DPYL1_HUMANyeast 2-hybridHPRD:01771HPRD16169070
UN119_HUMANyeast 2-hybridHPRD:01771HPRD16169070
ERG28_HUMANyeast 2-hybridHPRD:01771HPRD16169070
SETB1_HUMANyeast 2-hybridHPRD:01771HPRD16169070
CSN6_HUMANyeast 2-hybridHPRD:01771HPRD16169070
CA103_HUMANyeast 2-hybridHPRD:01771HPRD16169070
GALK1_HUMANENSP00000301634STRING
AICDA_HUMANENSP00000301634STRING
DUT_HUMANENSP00000301634STRING
VGFR1_HUMANENSP00000301634STRING
KITM_HUMANENSP00000301634STRING
ENTP3_HUMANENSP00000301634STRING
CANT1_HUMANENSP00000301634STRING
TYSY_HUMANENSP00000301634STRING
DCTD_HUMANENSP00000301634STRING
ENTP8_HUMANENSP00000301634STRING
ENTP8_HUMANENSP00000301634STRING
MADCA_HUMANENSP00000301634STRING
PNPH_HUMANENSP00000301634STRING
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
DrugBank
DB00432Trifluridine
DB00495Zidovudine
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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-231, AND MASSSPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13 AND SER-15, AND MASSSPECTROMETRY.
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13, AND MASSSPECTROMETRY.
"Serine 13 is the site of mitotic phosphorylation of human thymidinekinase.";
Chang Z.F., Huang D.Y., Chi L.M.;
J. Biol. Chem. 273:12095-12100(1998).
Cited for: PHOSPHORYLATION AT SER-13.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-231, AND MASSSPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-231, AND MASSSPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures