TYSY_HUMAN - dbPTM
TYSY_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TYSY_HUMAN
UniProt AC P04818
Protein Name Thymidylate synthase
Gene Name TYMS
Organism Homo sapiens (Human).
Sequence Length 313
Subcellular Localization Nucleus . Cytoplasm . Mitochondrion . Mitochondrion matrix . Mitochondrion inner membrane .
Protein Description Contributes to the de novo mitochondrial thymidylate biosynthesis pathway..
Protein Sequence MPVAGSELPRRPLPPAAQERDAEPRPPHGELQYLGQIQHILRCGVRKDDRTGTGTLSVFGMQARYSLRDEFPLLTTKRVFWKGVLEELLWFIKGSTNAKELSSKGVKIWDANGSRDFLDSLGFSTREEGDLGPVYGFQWRHFGAEYRDMESDYSGQGVDQLQRVIDTIKTNPDDRRIIMCAWNPRDLPLMALPPCHALCQFYVVNSELSCQLYQRSGDMGLGVPFNIASYALLTYMIAHITGLKPGDFIHTLGDAHIYLNHIEPLKIQLQREPRPFPKLRILRKVEKIDDFKAEDFQIEGYNPHPTIKMEMAV
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
6Phosphorylation--MPVAGSELPRRPL
--CCCCCCCCCCCCC		26.6520068231
33NitrationPPHGELQYLGQIQHI
CCCCCHHHHHHHHHH		25.98-
51 (in isoform 3)Phosphorylation-46.2025072903
53PhosphorylationRKDDRTGTGTLSVFG
CCCCCCCCEEEEEEE		26.78-
53 (in isoform 3)Phosphorylation-26.7825072903
55 (in isoform 3)Phosphorylation-18.7225072903
57 (in isoform 3)Phosphorylation-18.4225072903
61SulfoxidationGTLSVFGMQARYSLR
EEEEEEEEEEEEECC		1.5921406390
65PhosphorylationVFGMQARYSLRDEFP
EEEEEEEEECCCCCC		18.3123186163
65 (in isoform 3)Phosphorylation-18.3125072903
65NitrationVFGMQARYSLRDEFP
EEEEEEEEECCCCCC		18.31-
66PhosphorylationFGMQARYSLRDEFPL
EEEEEEEECCCCCCC		16.0424719451
66 (in isoform 3)Phosphorylation-16.0425072903
70 (in isoform 3)Phosphorylation-42.6125072903
71 (in isoform 3)Phosphorylation-6.3925072903
77AcetylationEFPLLTTKRVFWKGV
CCCCCCCCCCCHHHH		41.1325953088
77UbiquitinationEFPLLTTKRVFWKGV
CCCCCCCCCCCHHHH		41.1321890473
77UbiquitinationEFPLLTTKRVFWKGV
CCCCCCCCCCCHHHH		41.1321890473
772-HydroxyisobutyrylationEFPLLTTKRVFWKGV
CCCCCCCCCCCHHHH		41.13-
86UbiquitinationVFWKGVLEELLWFIK
CCHHHHHHHHHHHHH		44.1621890473
93UbiquitinationEELLWFIKGSTNAKE
HHHHHHHHCCCCHHH		37.02-
93UbiquitinationEELLWFIKGSTNAKE
HHHHHHHHCCCCHHH		37.0221890473
99UbiquitinationIKGSTNAKELSSKGV
HHCCCCHHHHHHCCC		62.35-
992-HydroxyisobutyrylationIKGSTNAKELSSKGV
HHCCCCHHHHHHCCC		62.35-
99UbiquitinationIKGSTNAKELSSKGV
HHCCCCHHHHHHCCC		62.3521906983
104UbiquitinationNAKELSSKGVKIWDA
CHHHHHHCCCEEEEC		65.4321890473
104UbiquitinationNAKELSSKGVKIWDA
CHHHHHHCCCEEEEC		65.4321890473
107UbiquitinationELSSKGVKIWDANGS
HHHHCCCEEEECCCC		46.9121890473
107UbiquitinationELSSKGVKIWDANGS
HHHHCCCEEEECCCC		46.9121890473
107AcetylationELSSKGVKIWDANGS
HHHHCCCEEEECCCC		46.9125953088
114PhosphorylationKIWDANGSRDFLDSL
EEEECCCCHHHHHHC		28.6022617229
120PhosphorylationGSRDFLDSLGFSTRE
CCHHHHHHCCCCCCC		32.3221712546
124PhosphorylationFLDSLGFSTREEGDL
HHHHCCCCCCCCCCC		25.4220430630
125PhosphorylationLDSLGFSTREEGDLG
HHHCCCCCCCCCCCC		39.5821712546
135PhosphorylationEGDLGPVYGFQWRHF
CCCCCCCCCEECCCC		18.5029978859
135NitrationEGDLGPVYGFQWRHF
CCCCCCCCCEECCCC		18.50-
146PhosphorylationWRHFGAEYRDMESDY
CCCCCCEECCCCCCC		16.0422210691
149SulfoxidationFGAEYRDMESDYSGQ
CCCEECCCCCCCCCC		3.8228183972
151PhosphorylationAEYRDMESDYSGQGV
CEECCCCCCCCCCCH		34.9028796482
153PhosphorylationYRDMESDYSGQGVDQ
ECCCCCCCCCCCHHH		24.7928796482
154PhosphorylationRDMESDYSGQGVDQL
CCCCCCCCCCCHHHH		29.6328796482
167PhosphorylationQLQRVIDTIKTNPDD
HHHHHHHHHHCCCCC		17.16-
169UbiquitinationQRVIDTIKTNPDDRR
HHHHHHHHCCCCCCE		44.3221890473
209UbiquitinationYVVNSELSCQLYQRS
EEECCHHHEEEHHHC		8.8621890473
213NitrationSELSCQLYQRSGDMG
CHHHEEEHHHCCCCC		3.97-
225UbiquitinationDMGLGVPFNIASYAL
CCCCCCCCHHHHHHH		10.8321890473
230NitrationVPFNIASYALLTYMI
CCCHHHHHHHHHHHH		7.70-
258UbiquitinationTLGDAHIYLNHIEPL
EECCEEEECCCCCCE		7.50-
258NitrationTLGDAHIYLNHIEPL
EECCEEEECCCCCCE		7.50-
274UbiquitinationIQLQREPRPFPKLRI
EEECCCCCCCCCHHH		40.51-
278UbiquitinationREPRPFPKLRILRKV
CCCCCCCCHHHEEEE		51.26-
284UbiquitinationPKLRILRKVEKIDDF
CCHHHEEEEEECCCC		51.83-
287UbiquitinationRILRKVEKIDDFKAE
HHEEEEEECCCCCCH		55.19-
287SumoylationRILRKVEKIDDFKAE
HHEEEEEECCCCCCH		55.19-
287SumoylationRILRKVEKIDDFKAE
HHEEEEEECCCCCCH		55.1928112733
292SumoylationVEKIDDFKAEDFQIE
EEECCCCCCHHCCCC		58.84-
292UbiquitinationVEKIDDFKAEDFQIE
EEECCCCCCHHCCCC		58.8421890473
292SumoylationVEKIDDFKAEDFQIE
EEECCCCCCHHCCCC		58.8428112733
301NitrationEDFQIEGYNPHPTIK
HHCCCCCCCCCCCEE		16.84-
306PhosphorylationEGYNPHPTIKMEMAV
CCCCCCCCEEEEEEC		30.1427050516
308SumoylationYNPHPTIKMEMAV--
CCCCCCEEEEEEC--		31.14-
308UbiquitinationYNPHPTIKMEMAV--
CCCCCCEEEEEEC--		31.1421890473
308SumoylationYNPHPTIKMEMAV--
CCCCCCEEEEEEC--		31.1428112733
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
124SPhosphorylationKinaseCSNK2A1P68400
GPS
124SPhosphorylationKinaseCSNK2A2P19784
GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TYSY_HUMAN !!
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 TYSY_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
WDR1_HUMANWDR1physical
22939629
ANCHR_HUMANZFYVE19physical
22939629
ZFY21_HUMANZFYVE21physical
22939629
UBE2B_HUMANUBE2Bphysical
22939629
UBXN7_HUMANUBXN7physical
22939629
UBQL4_HUMANUBQLN4physical
22939629
ZRAB2_HUMANZRANB2physical
22939629
UBE2A_HUMANUBE2Aphysical
22939629
UNK_HUMANUNKphysical
22939629
VATC1_HUMANATP6V1C1physical
22939629
VATE1_HUMANATP6V1E1physical
22939629
WIPI3_HUMANWDR45Bphysical
22939629
UBE2K_HUMANUBE2Kphysical
22939629
VPS4B_HUMANVPS4Bphysical
22939629
UBE2C_HUMANUBE2Cphysical
22939629
UBC12_HUMANUBE2Mphysical
22939629
UFC1_HUMANUFC1physical
22939629
IF5A1_HUMANEIF5Aphysical
22863883
PDCD6_HUMANPDCD6physical
26344197
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
D00584 Fluorouracil (JP16/USP/INN); 5-FU (TN); Adrucil (TN); Carac (TN); Fluoroplex (TN)
D01064 Raltitrexed (JAN/USAN/INN); Tomudex (TN)
D01223 Capecitabine (JAN/USAN/INN); Xeloda (TN)
D01244 Tegafur (JP16/USAN/INN); Atillon (TN)
D01309 Doxifluridine (JP16/INN); Furtulon (TN)
D01784 Carmofur (JP16/INN); Mifurol (TN)
D03828 Pemetrexed disodium (USAN); Alimta (TN)
D04197 Floxuridine (USP/INN); FUDR (TN)
D04964 Metesind glucuronate (USAN)
D06503 Pemetrexed sodium hydrate (JAN); Pemetrexed disodium heptahydrate; Alimta (TN)
D07472 Pemetrexed (INN); Alimta (TN); Pemetrexed (TN)
D07974 Fluorouracil sodium salt; Fluorouracil (TN)
DrugBank
DB01101Capecitabine
DB00322Floxuridine
DB00544Fluorouracil
DB00441Gemcitabine
DB00650Leucovorin
DB00563Methotrexate
DB00642Pemetrexed
DB06813Pralatrexate
DB00293Raltitrexed
DB00432Trifluridine
DB00440Trimethoprim
Regulatory Network of TYSY_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, AND MASSSPECTROMETRY.

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