KITH_HUMAN - dbPTM
KITH_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID KITH_HUMAN
UniProt AC P04183
Protein Name Thymidine kinase, cytosolic
Gene Name TK1
Organism Homo sapiens (Human).
Sequence Length 234
Subcellular Localization Cytoplasm.
Protein Description
Protein Sequence MSCINLPTVLPGSPSKTRGQIQVILGPMFSGKSTELMRRVRRFQIAQYKCLVIKYAKDTRYSSSFCTHDRNTMEALPACLLRDVAQEALGVAVIGIDEGQFFPDIVEFCEAMANAGKTVIVAALDGTFQRKPFGAILNLVPLAESVVKLTAVCMECFREAAYTKRLGTEKEVEVIGGADKYHSVCRLCYFKKASGQPAGPDNKENCPVPGKPGEAVAARKLFAPQQILQCSPAN
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
2Phosphorylation------MSCINLPTV
------CCCCCCCCC
24.5730631047
2Acetylation------MSCINLPTV
------CCCCCCCCC
24.5720068231
8PhosphorylationMSCINLPTVLPGSPS
CCCCCCCCCCCCCCC
37.5330631047
13PhosphorylationLPTVLPGSPSKTRGQ
CCCCCCCCCCCCCCC
24.8629255136
15PhosphorylationTVLPGSPSKTRGQIQ
CCCCCCCCCCCCCEE
48.6429255136
16UbiquitinationVLPGSPSKTRGQIQV
CCCCCCCCCCCCEEE
45.70-
17PhosphorylationLPGSPSKTRGQIQVI
CCCCCCCCCCCEEEE
44.3528464451
30PhosphorylationVILGPMFSGKSTELM
EEECCCCCCCCHHHH
38.7721712546
32AcetylationLGPMFSGKSTELMRR
ECCCCCCCCHHHHHH
53.6724846093
48PhosphorylationRRFQIAQYKCLVIKY
HHHHHHHEEEEEEEE
8.47-
49UbiquitinationRFQIAQYKCLVIKYA
HHHHHHEEEEEEEEC
14.71-
54AcetylationQYKCLVIKYAKDTRY
HEEEEEEEECCCCCC
31.5126051181
55PhosphorylationYKCLVIKYAKDTRYS
EEEEEEEECCCCCCC
14.04-
61PhosphorylationKYAKDTRYSSSFCTH
EECCCCCCCCCCCCC
18.2629496907
62PhosphorylationYAKDTRYSSSFCTHD
ECCCCCCCCCCCCCC
19.0625159151
63PhosphorylationAKDTRYSSSFCTHDR
CCCCCCCCCCCCCCC
20.6429214152
64PhosphorylationKDTRYSSSFCTHDRN
CCCCCCCCCCCCCCC
20.5728555341
70MethylationSSFCTHDRNTMEALP
CCCCCCCCCHHHHHH
32.68115918525
131UbiquitinationLDGTFQRKPFGAILN
CCCCCCCCCCCHHHH
33.64-
164AcetylationFREAAYTKRLGTEKE
HHHHHHHHCCCCCCE
32.7119816723
170UbiquitinationTKRLGTEKEVEVIGG
HHCCCCCCEEEEECC
67.8821906983
1702-HydroxyisobutyrylationTKRLGTEKEVEVIGG
HHCCCCCCEEEEECC
67.88-
1802-HydroxyisobutyrylationEVIGGADKYHSVCRL
EEECCCCHHCHHHHH
44.31-
180AcetylationEVIGGADKYHSVCRL
EEECCCCHHCHHHHH
44.3125953088
180UbiquitinationEVIGGADKYHSVCRL
EEECCCCHHCHHHHH
44.31-
181PhosphorylationVIGGADKYHSVCRLC
EECCCCHHCHHHHHH
10.4029978859
183PhosphorylationGGADKYHSVCRLCYF
CCCCHHCHHHHHHHE
21.5929978859
192UbiquitinationCRLCYFKKASGQPAG
HHHHHEEECCCCCCC
37.57-
203AcetylationQPAGPDNKENCPVPG
CCCCCCCCCCCCCCC
58.6526051181
203UbiquitinationQPAGPDNKENCPVPG
CCCCCCCCCCCCCCC
58.65-
211UbiquitinationENCPVPGKPGEAVAA
CCCCCCCCCCCHHHH
43.72-
211AcetylationENCPVPGKPGEAVAA
CCCCCCCCCCCHHHH
43.7226051181
220AcetylationGEAVAARKLFAPQQI
CCHHHHHHHCCCHHH
43.1426051181
220UbiquitinationGEAVAARKLFAPQQI
CCHHHHHHHCCCHHH
43.1421890473
230GlutathionylationAPQQILQCSPAN---
CCHHHHCCCCCC---
4.7622555962
231PhosphorylationPQQILQCSPAN----
CHHHHCCCCCC----
17.6829255136

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
13SPhosphorylationKinaseCDK1P06493
PSP
13SPhosphorylationKinaseCDK2P24941
PSP
-KUbiquitinationE3 ubiquitin ligaseFZR1Q9UM11
PMID:14701726

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
13SPhosphorylation

9575153

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of KITH_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GDF9_HUMANGDF9physical
16169070
CC90B_HUMANCCDC90Bphysical
16169070
PTPRK_HUMANPTPRKphysical
16169070
APLP1_HUMANAPLP1physical
16169070
ERG28_HUMANC14orf1physical
16169070
CSN6_HUMANCOPS6physical
16169070
RBM48_HUMANRBM48physical
16169070
NC2A_HUMANDRAP1physical
16169070
SETB1_HUMANSETDB1physical
16169070
TBB2A_HUMANTUBB2Aphysical
16169070
DPYL1_HUMANCRMP1physical
16169070
G3P_HUMANGAPDHphysical
16169070
LRIF1_HUMANLRIF1physical
16169070
TLE1_HUMANTLE1physical
16169070
P53_HUMANTP53physical
16169070
U119A_HUMANUNC119physical
16169070
CDN1A_HUMANCDKN1Aphysical
11389691
MOFA1_HUMANMRFAP1physical
21900206
ADDA_HUMANADD1physical
21900206
TSC2_HUMANTSC2physical
21900206
KIF5A_HUMANKIF5Aphysical
21900206
HMGX3_HUMANHMGXB3physical
21900206
RXRA_HUMANRXRAphysical
21900206
CSAD_HUMANCSADphysical
21900206
PSME1_HUMANPSME1physical
21900206
ABHD4_HUMANABHD4physical
21900206
ECHB_HUMANHADHBphysical
21900206
WIZ_HUMANWIZphysical
21900206
MAST2_HUMANMAST2physical
21900206
PLXA3_HUMANPLXNA3physical
21900206
SNX1_HUMANSNX1physical
21900206
ITSN1_HUMANITSN1physical
21900206
PTPRK_HUMANPTPRKphysical
21900206
GDF9_HUMANGDF9physical
21900206
RM37_HUMANMRPL37physical
21900206
DEAF1_HUMANDEAF1physical
21900206
SMC5_HUMANSMC5physical
21900206
ZBT16_HUMANZBTB16physical
21900206
ZXDC_HUMANZXDCphysical
21900206
KLH23_HUMANKLHL23physical
21900206
CDK4_HUMANCDK4physical
21900206
GPCP1_HUMANGPCPD1physical
21900206
KI67_HUMANMKI67physical
21900206
SUMO3_HUMANSUMO3physical
21900206
DCOR_HUMANODC1physical
21900206
TYB4_HUMANTMSB4Xphysical
21900206
DDAH2_HUMANDDAH2physical
21900206
CHSP1_HUMANCARHSP1physical
21900206
ATS10_HUMANADAMTS10physical
21900206
HBAP1_HUMANHSPBAP1physical
21900206
HEM1_HUMANALAS1physical
21900206
CS060_HUMANC19orf60physical
21900206
ACTB_HUMANACTBphysical
21900206
CSN6_HUMANCOPS6physical
21900206
DPYL1_HUMANCRMP1physical
21900206
TRI46_HUMANTRIM46physical
21900206
ACTY_HUMANACTR1Bphysical
21900206
UBP4_HUMANUSP4physical
21900206
DALD3_HUMANDALRD3physical
21900206
TAF1C_HUMANTAF1Cphysical
21900206
A2MG_HUMANA2Mphysical
21900206
SP110_HUMANSP110physical
21900206
MED31_HUMANMED31physical
21900206
CENPB_HUMANCENPBphysical
21900206
CC90B_HUMANCCDC90Bphysical
21900206
DC1I1_HUMANDYNC1I1physical
21900206
FBN3_HUMANFBN3physical
21900206
RL13_HUMANRPL13physical
21900206
INP5K_HUMANINPP5Kphysical
21900206
APLP1_HUMANAPLP1physical
21900206
A16L2_HUMANATG16L2physical
21900206
KLHL5_HUMANKLHL5physical
21900206
FA20C_HUMANFAM20Cphysical
21900206
MPPD1_HUMANMPPED1physical
21900206
MSH2_HUMANMSH2physical
21900206
AAMP_HUMANAAMPphysical
21900206
WDR60_HUMANWDR60physical
21900206
NDF2_HUMANNEUROD2physical
21900206
LRIF1_HUMANLRIF1physical
21900206
INT11_HUMANCPSF3Lphysical
21900206
IR3IP_HUMANIER3IP1physical
21900206
ZN431_HUMANZNF431physical
21900206
ACL6B_HUMANACTL6Bphysical
21900206
IF4A2_HUMANEIF4A2physical
21900206
JHD2C_HUMANJMJD1Cphysical
21900206
PP4C_HUMANPPP4Cphysical
21900206
KPYM_HUMANPKMphysical
21900206
AGAP1_HUMANAGAP1physical
21900206
TNR16_HUMANNGFRphysical
21900206
PAAF1_HUMANPAAF1physical
21900206
ST1A3_HUMANSULT1A3physical
21900206
ST1A4_HUMANSULT1A3physical
21900206
NMT2_HUMANNMT2physical
21900206
TTC38_HUMANTTC38physical
21900206
SYQ_HUMANQARSphysical
21900206
RBBP4_HUMANRBBP4physical
21900206
TETN_HUMANCLEC3Bphysical
21900206
NRBP_HUMANNRBP1physical
21900206
SETB1_HUMANSETDB1physical
21900206
DMPK_HUMANDMPKphysical
21900206
ATX3_HUMANATXN3physical
21900206
MIC60_HUMANIMMTphysical
21900206
CO4A2_HUMANCOL4A2physical
21900206
VATA_HUMANATP6V1Aphysical
21900206
P53_HUMANTP53physical
21900206
KI21B_HUMANKIF21Bphysical
21900206
CPNE6_HUMANCPNE6physical
21900206
EXT2_HUMANEXT2physical
21900206
CAB45_HUMANSDF4physical
21900206
TIAM2_HUMANTIAM2physical
21900206
FAD1_HUMANFLAD1physical
21900206
ERG28_HUMANC14orf1physical
21900206
DACT1_HUMANDACT1physical
21900206
SEM5B_HUMANSEMA5Bphysical
21900206
BAG6_HUMANBAG6physical
21900206
RBM48_HUMANRBM48physical
21900206
G3P_HUMANGAPDHphysical
21900206
TBA1A_HUMANTUBA1Aphysical
21900206
SEPT6_HUMANSEPT6physical
21900206
F13A_HUMANF13A1physical
21900206
TYK2_HUMANTYK2physical
21900206
EIF3G_HUMANEIF3Gphysical
21900206
JADE1_HUMANJADE1physical
21900206
RUVB1_HUMANRUVBL1physical
21900206
WDR73_HUMANWDR73physical
21900206
PROC_HUMANPROCphysical
21900206
TRM2A_HUMANTRMT2Aphysical
21900206
TLE1_HUMANTLE1physical
21900206
FST_HUMANFSTphysical
21900206
THOC3_HUMANTHOC3physical
21900206
DCA13_HUMANDCAF13physical
21900206
RS2_HUMANRPS2physical
21900206
TBB2A_HUMANTUBB2Aphysical
21900206
A1BG_HUMANA1BGphysical
21900206
CO4A5_HUMANCOL4A5physical
21900206
ATPB_HUMANATP5Bphysical
21900206
EF1A1_HUMANEEF1A1physical
21900206
CC115_HUMANCCDC115physical
21900206
GDIA_HUMANGDI1physical
21900206
EZH2_HUMANEZH2physical
21900206
HERC3_HUMANHERC3physical
21900206
U119A_HUMANUNC119physical
21900206
IF6_HUMANEIF6physical
21900206
DUS2L_HUMANDUS2physical
21900206
KBRS2_HUMANNKIRAS2physical
21900206
TBB3_HUMANTUBB3physical
21900206
SCG1_HUMANCHGBphysical
21900206
KDM6B_HUMANKDM6Bphysical
21900206
MYOME_HUMANPDE4DIPphysical
21900206
KITH_HUMANTK1physical
21900206
TC1D2_HUMANTCTEX1D2physical
21900206
COBA2_HUMANCOL11A2physical
21900206
EM55_HUMANMPP1physical
21900206
CRIP2_HUMANCRIP2physical
21900206
WDR18_HUMANWDR18physical
21900206
MET23_HUMANMETTL23physical
21900206
RFA1_HUMANRPA1physical
21900206
ARFG1_HUMANARFGAP1physical
21900206
PLD3_HUMANPLD3physical
21900206
DOCK7_HUMANDOCK7physical
21900206
ALBU_HUMANALBphysical
21900206
PTN4_HUMANPTPN4physical
21900206
KMT2B_HUMANKMT2Bphysical
21900206
ASNA_HUMANASNA1physical
21900206
BGAL_HUMANGLB1physical
21900206
FIBB_HUMANFGBphysical
21900206
FAF1_HUMANFAF1physical
21900206
FZR1_HUMANFZR1physical
14701726
CDC20_HUMANCDC20physical
14701726
A4_HUMANAPPphysical
21832049

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB00432Trifluridine
DB00495Zidovudine
Regulatory Network of KITH_HUMAN

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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.
"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.
"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.
"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.
"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.
"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.

TOP