UMPS_HUMAN - dbPTM
UMPS_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID UMPS_HUMAN
UniProt AC P11172
Protein Name Uridine 5'-monophosphate synthase
Gene Name UMPS
Organism Homo sapiens (Human).
Sequence Length 480
Subcellular Localization
Protein Description
Protein Sequence MAVARAALGPLVTGLYDVQAFKFGDFVLKSGLSSPIYIDLRGIVSRPRLLSQVADILFQTAQNAGISFDTVCGVPYTALPLATVICSTNQIPMLIRRKETKDYGTKRLVEGTINPGETCLIIEDVVTSGSSVLETVEVLQKEGLKVTDAIVLLDREQGGKDKLQAHGIRLHSVCTLSKMLEILEQQKKVDAETVGRVKRFIQENVFVAANHNGSPLSIKEAPKELSFGARAELPRIHPVASKLLRLMQKKETNLCLSADVSLARELLQLADALGPSICMLKTHVDILNDFTLDVMKELITLAKCHEFLIFEDRKFADIGNTVKKQYEGGIFKIASWADLVNAHVVPGSGVVKGLQEVGLPLHRGCLLIAEMSSTGSLATGDYTRAAVRMAEEHSEFVVGFISGSRVSMKPEFLHLTPGVQLEAGGDNLGQQYNSPQEVIGKRGSDIIIVGRGIISAADRLEAAEMYRKAAWEAYLSRLGV
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
2Acetylation------MAVARAALG
------CHHHHHHHH		12.0419413330
16PhosphorylationGPLVTGLYDVQAFKF
HHHHCCCCCCCCCCC		18.53-
22UbiquitinationLYDVQAFKFGDFVLK
CCCCCCCCCCCCCCC		51.9921906983
22 (in isoform 1)Ubiquitination-51.9921906983
29UbiquitinationKFGDFVLKSGLSSPI
CCCCCCCCCCCCCCE		36.8621906983
29 (in isoform 1)Ubiquitination-36.8621906983
30PhosphorylationFGDFVLKSGLSSPIY
CCCCCCCCCCCCCEE		40.5823186163
33PhosphorylationFVLKSGLSSPIYIDL
CCCCCCCCCCEEEEC		37.2828152594
34PhosphorylationVLKSGLSSPIYIDLR
CCCCCCCCCEEEECC		21.9928152594
37PhosphorylationSGLSSPIYIDLRGIV
CCCCCCEEEECCHHH		7.5527155012
41 (in isoform 2)Ubiquitination-29.1021906983
106AcetylationETKDYGTKRLVEGTI
CCCCCCCCEEEECCC		39.1012654819
136 (in isoform 2)Ubiquitination-3.3221906983
145 (in isoform 2)Ubiquitination-54.6821906983
145UbiquitinationVLQKEGLKVTDAIVL
HHHHCCCCCCEEEEE		54.68-
146 (in isoform 2)Ubiquitination-7.6221906983
160UbiquitinationLDREQGGKDKLQAHG
EEHHHCCHHHHHHCC		59.52-
162AcetylationREQGGKDKLQAHGIR
HHHCCHHHHHHCCCC		46.0823749302
162UbiquitinationREQGGKDKLQAHGIR
HHHCCHHHHHHCCCC		46.0819608861
172PhosphorylationAHGIRLHSVCTLSKM
HCCCCHHHHHHHHHH		24.3928857561
174S-nitrosocysteineGIRLHSVCTLSKMLE
CCCHHHHHHHHHHHH		3.38-
175PhosphorylationIRLHSVCTLSKMLEI
CCHHHHHHHHHHHHH		31.7323312004
178AcetylationHSVCTLSKMLEILEQ
HHHHHHHHHHHHHHH		51.0926051181
178UbiquitinationHSVCTLSKMLEILEQ
HHHHHHHHHHHHHHH		51.09-
1872-HydroxyisobutyrylationLEILEQQKKVDAETV
HHHHHHHCCCCHHHH		55.23-
187UbiquitinationLEILEQQKKVDAETV
HHHHHHHCCCCHHHH		55.23-
188UbiquitinationEILEQQKKVDAETVG
HHHHHHCCCCHHHHH		40.80-
214PhosphorylationVAANHNGSPLSIKEA
EEECCCCCCCCHHCC		28.1622167270
217PhosphorylationNHNGSPLSIKEAPKE
CCCCCCCCHHCCCCC		34.6922167270
219 (in isoform 1)Ubiquitination-44.4321906983
219UbiquitinationNGSPLSIKEAPKELS
CCCCCCHHCCCCCCC		44.4321906983
223UbiquitinationLSIKEAPKELSFGAR
CCHHCCCCCCCCCCC		77.62-
231 (in isoform 2)Ubiquitination-23.3421906983
241PhosphorylationPRIHPVASKLLRLMQ
CCHHHHHHHHHHHHC		24.87-
242AcetylationRIHPVASKLLRLMQK
CHHHHHHHHHHHHCC		41.6325953088
242UbiquitinationRIHPVASKLLRLMQK
CHHHHHHHHHHHHCC		41.63-
252PhosphorylationRLMQKKETNLCLSAD
HHHCCCCCCHHHCCC		42.2322210691
257PhosphorylationKETNLCLSADVSLAR
CCCCHHHCCCHHHHH		22.7922210691
261PhosphorylationLCLSADVSLARELLQ
HHHCCCHHHHHHHHH		19.5022210691
263 (in isoform 2)Ubiquitination-8.7321906983
303UbiquitinationKELITLAKCHEFLIF
HHHHHHHHHCEEEEE		38.96-
314UbiquitinationFLIFEDRKFADIGNT
EEEECCCCCCCCCHH		58.1721906983
314 (in isoform 1)Ubiquitination-58.1721906983
314AcetylationFLIFEDRKFADIGNT
EEEECCCCCCCCCHH		58.1725953088
323AcetylationADIGNTVKKQYEGGI
CCCCHHHHHHHCCCC		31.9225953088
323UbiquitinationADIGNTVKKQYEGGI
CCCCHHHHHHHCCCC		31.9221906983
323 (in isoform 1)Ubiquitination-31.9221906983
324UbiquitinationDIGNTVKKQYEGGIF
CCCHHHHHHHCCCCE		54.5021906983
324MalonylationDIGNTVKKQYEGGIF
CCCHHHHHHHCCCCE		54.5026320211
324 (in isoform 1)Ubiquitination-54.5021906983
332UbiquitinationQYEGGIFKIASWADL
HHCCCCEEECCHHHH		35.13-
335PhosphorylationGGIFKIASWADLVNA
CCCEEECCHHHHHHC		26.6928348404
352UbiquitinationVPGSGVVKGLQEVGL
CCCCCHHCCHHHCCC		52.04-
352AcetylationVPGSGVVKGLQEVGL
CCCCCHHCCHHHCCC		52.0426051181
394PhosphorylationVRMAEEHSEFVVGFI
HHHHHHCCCEEEEEE		35.69-
409UbiquitinationSGSRVSMKPEFLHLT
CCCCCCCCCHHHCCC		33.6121906983
409 (in isoform 1)Ubiquitination-33.6121906983
432PhosphorylationGDNLGQQYNSPQEVI
CCCHHHCCCCHHHHH		15.1022817900
441UbiquitinationSPQEVIGKRGSDIII
CHHHHHCCCCCCEEE		42.322190698
441 (in isoform 1)Ubiquitination-42.3221906983
444PhosphorylationEVIGKRGSDIIIVGR
HHHCCCCCCEEEECC		29.6620068231
455PhosphorylationIVGRGIISAADRLEA
EECCCHHCHHHHHHH		18.58-
459MethylationGIISAADRLEAAEMY
CHHCHHHHHHHHHHH		29.69115919533
465SulfoxidationDRLEAAEMYRKAAWE
HHHHHHHHHHHHHHH		3.1730846556
466PhosphorylationRLEAAEMYRKAAWEA
HHHHHHHHHHHHHHH		10.6425690035
468UbiquitinationEAAEMYRKAAWEAYL
HHHHHHHHHHHHHHH		25.60-
474PhosphorylationRKAAWEAYLSRLGV-
HHHHHHHHHHHHCC-		8.1624850871
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

Oops, there are no upstream regulatory protein records of UMPS_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of UMPS_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 UMPS_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
BORG2_HUMANCDC42EP3physical
16169070
ZN227_HUMANZNF227physical
21988832
ADPPT_HUMANAASDHPPTphysical
26344197
A16A1_HUMANALDH16A1physical
26344197
SSDH_HUMANALDH5A1physical
26344197
APT_HUMANAPRTphysical
26344197
DUT_HUMANDUTphysical
26344197
GLGB_HUMANGBE1physical
26344197
LGUL_HUMANGLO1physical
26344197
GNPI1_HUMANGNPDA1physical
26344197
GNPI2_HUMANGNPDA2physical
26344197
HEM3_HUMANHMBSphysical
26344197
ITPA_HUMANITPAphysical
26344197
PGAM1_HUMANPGAM1physical
26344197
AMPB_HUMANRNPEPphysical
26344197
SPS1_HUMANSEPHS1physical
26344197
SPS2_HUMANSEPHS2physical
26344197
EPHA4_HUMANEPHA4physical
28514442
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
258900Orotic aciduria 1 (ORAC1)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB00544Fluorouracil
Regulatory Network of UMPS_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-162, AND MASS SPECTROMETRY.
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-214, AND MASSSPECTROMETRY.
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer.";
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
Cell 131:1190-1203(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-37, AND MASSSPECTROMETRY.

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