WDR20_HUMAN - dbPTM
WDR20_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID WDR20_HUMAN
UniProt AC Q8TBZ3
Protein Name WD repeat-containing protein 20
Gene Name WDR20
Organism Homo sapiens (Human).
Sequence Length 569
Subcellular Localization
Protein Description Regulator of deubiquitinating complexes. Activates deubiquitinating activity of complexes containing USP12. [PubMed: 20147737]
Protein Sequence MATEGGGKEMNEIKTQFTTREGLYKLLPHSEYSRPNRVPFNSQGSNPVRVSFVNLNDQSGNGDRLCFNVGRELYFYIYKGVRKAADLSKPIDKRIYKGTQPTCHDFNHLTATAESVSLLVGFSAGQVQLIDPIKKETSKLFNEERLIDKSRVTCVKWVPGSESLFLVAHSSGNMYLYNVEHTCGTTAPHYQLLKQGESFAVHTCKSKSTRNPLLKWTVGEGALNEFAFSPDGKFLACVSQDGFLRVFNFDSVELHGTMKSYFGGLLCVCWSPDGKYIVTGGEDDLVTVWSFVDCRVIARGHGHKSWVSVVAFDPYTTSVEEGDPMEFSGSDEDFQDLLHFGRDRANSTQSRLSKRNSTDSRPVSVTYRFGSVGQDTQLCLWDLTEDILFPHQPLSRARTHTNVMNATSPPAGSNGNSVTTPGNSVPPPLPRSNSLPHSAVSNAGSKSSVMDGAIASGVSKFATLSLHDRKERHHEKDHKRNHSMGHISSKSSDKLNLVTKTKTDPAKTLGTPLCPRMEDVPLLEPLICKKIAHERLTVLIFLEDCIVTACQEGFICTWGRPGKVVSFNP
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------MATEGGGKE
------CCCCCCCCH		17.8522814378
8UbiquitinationMATEGGGKEMNEIKT
CCCCCCCCHHHHHHC		58.00-
51PhosphorylationGSNPVRVSFVNLNDQ
CCCCEEEEEEECCCC		16.9527732954
59PhosphorylationFVNLNDQSGNGDRLC
EEECCCCCCCCCEEE		36.7727732954
76PhosphorylationVGRELYFYIYKGVRK
CCCCHHHEHHHCHHH		6.9818083107
139AcetylationPIKKETSKLFNEERL
CHHHHHHHHHCHHHH		65.6025953088
150PhosphorylationEERLIDKSRVTCVKW
HHHHCCCCCEEEEEE		28.3821406692
153PhosphorylationLIDKSRVTCVKWVPG
HCCCCCEEEEEECCC		15.5221406692
161PhosphorylationCVKWVPGSESLFLVA
EEEECCCCCEEEEEE		20.2421406692
163PhosphorylationKWVPGSESLFLVAHS
EECCCCCEEEEEEEC		26.5621406692
170PhosphorylationSLFLVAHSSGNMYLY
EEEEEEECCCCEEEE		30.1521406692
171PhosphorylationLFLVAHSSGNMYLYN
EEEEEECCCCEEEEE		25.0721406692
175PhosphorylationAHSSGNMYLYNVEHT
EECCCCEEEEEEEEC		15.2721406692
177PhosphorylationSSGNMYLYNVEHTCG
CCCCEEEEEEEECCC		10.3221406692
182PhosphorylationYLYNVEHTCGTTAPH
EEEEEEECCCCCCCH		10.1021406692
185PhosphorylationNVEHTCGTTAPHYQL
EEEECCCCCCCHHHH		23.1821406692
186PhosphorylationVEHTCGTTAPHYQLL
EEECCCCCCCHHHHH		24.3921406692
190PhosphorylationCGTTAPHYQLLKQGE
CCCCCCHHHHHHCCC		10.3721406692
308PhosphorylationHGHKSWVSVVAFDPY
CCCCCEEEEEEECCC		12.4820068231
328PhosphorylationEGDPMEFSGSDEDFQ
CCCCCCCCCCCHHHH		24.8727251275
330PhosphorylationDPMEFSGSDEDFQDL
CCCCCCCCCHHHHHH		36.3127251275
347PhosphorylationFGRDRANSTQSRLSK
HCHHCCHHHHHHHHH		27.1720363803
348PhosphorylationGRDRANSTQSRLSKR
CHHCCHHHHHHHHHC		30.3021406692
350PhosphorylationDRANSTQSRLSKRNS
HCCHHHHHHHHHCCC		34.9630576142
353PhosphorylationNSTQSRLSKRNSTDS
HHHHHHHHHCCCCCC		28.5820363803
357PhosphorylationSRLSKRNSTDSRPVS
HHHHHCCCCCCCCEE		37.3122167270
358PhosphorylationRLSKRNSTDSRPVSV
HHHHCCCCCCCCEEE		41.3630266825
360PhosphorylationSKRNSTDSRPVSVTY
HHCCCCCCCCEEEEE		38.2730266825
364PhosphorylationSTDSRPVSVTYRFGS
CCCCCCEEEEEECCC		16.0722167270
366PhosphorylationDSRPVSVTYRFGSVG
CCCCEEEEEECCCCC		11.0622167270
367PhosphorylationSRPVSVTYRFGSVGQ
CCCEEEEEECCCCCC		11.2023927012
371PhosphorylationSVTYRFGSVGQDTQL
EEEEECCCCCCCCEE		21.9920068231
407PhosphorylationHTNVMNATSPPAGSN
CCCCCCCCCCCCCCC		36.4424719451
408PhosphorylationTNVMNATSPPAGSNG
CCCCCCCCCCCCCCC		26.8621712546
420PhosphorylationSNGNSVTTPGNSVPP
CCCCCCCCCCCCCCC		27.3521712546
432PhosphorylationVPPPLPRSNSLPHSA
CCCCCCCCCCCCCHH		28.9122167270
434PhosphorylationPPLPRSNSLPHSAVS
CCCCCCCCCCCHHCC		44.5222167270
438PhosphorylationRSNSLPHSAVSNAGS
CCCCCCCHHCCCCCC		28.5530266825
441PhosphorylationSLPHSAVSNAGSKSS
CCCCHHCCCCCCCCH		22.2230266825
445PhosphorylationSAVSNAGSKSSVMDG
HHCCCCCCCCHHHHH		27.2730266825
447PhosphorylationVSNAGSKSSVMDGAI
CCCCCCCCHHHHHHH		29.8425056879
448PhosphorylationSNAGSKSSVMDGAIA
CCCCCCCHHHHHHHH		25.7925056879
463PhosphorylationSGVSKFATLSLHDRK
CCCCCCCCCCCHHHH		21.7330266825
465PhosphorylationVSKFATLSLHDRKER
CCCCCCCCCHHHHHH		21.2123401153
483PhosphorylationKDHKRNHSMGHISSK
HHCCCCCCCCCCCCC		29.9728348404
488PhosphorylationNHSMGHISSKSSDKL
CCCCCCCCCCCCCCC		26.4921406692
489PhosphorylationHSMGHISSKSSDKLN
CCCCCCCCCCCCCCC		35.6321406692
491PhosphorylationMGHISSKSSDKLNLV
CCCCCCCCCCCCCEE		45.8023401153
492PhosphorylationGHISSKSSDKLNLVT
CCCCCCCCCCCCEEE		42.3630266825
499PhosphorylationSDKLNLVTKTKTDPA
CCCCCEEEECCCCHH		35.8426657352
500UbiquitinationDKLNLVTKTKTDPAK
CCCCEEEECCCCHHH		40.31-
505 (in isoform 6)Phosphorylation-40.6727732954
507 (in isoform 6)Phosphorylation-50.0720068231
508 (in isoform 6)Phosphorylation-32.3120068231
510 (in isoform 6)Phosphorylation-30.4420068231
511PhosphorylationDPAKTLGTPLCPRME
CHHHCCCCCCCCCHH		19.0526853621
513 (in isoform 6)Phosphorylation-6.7020068231
514 (in isoform 6)Phosphorylation-1.8020068231
518 (in isoform 6)Phosphorylation-58.0720068231
566 (in isoform 2)Phosphorylation-23.4627732954
568 (in isoform 2)Phosphorylation-33.5920068231
569 (in isoform 2)Phosphorylation-43.5120068231
571 (in isoform 2)Phosphorylation-20068231
574 (in isoform 2)Phosphorylation-20068231
575 (in isoform 2)Phosphorylation-20068231
579 (in isoform 2)Phosphorylation-20068231
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 WDR20_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of WDR20_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 WDR20_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
COBA2_HUMANCOL11A2physical
19615732
ODPA_HUMANPDHA1physical
19615732
PKN2_HUMANPKN2physical
19615732
SURF2_HUMANSURF2physical
19615732
1433B_HUMANYWHABphysical
19615732
1433F_HUMANYWHAHphysical
19615732
RPAC1_HUMANPOLR1Cphysical
19615732
OPTN_HUMANOPTNphysical
19615732
UBXN1_HUMANUBXN1physical
19615732
FBXW5_HUMANFBXW5physical
19615732
WDR48_HUMANWDR48physical
19615732
UBP12_HUMANUSP12physical
19615732
UBP46_HUMANUSP46physical
19615732
WDR48_HUMANWDR48physical
20147737
DAPP1_HUMANDAPP1physical
25814554
UBP12_HUMANUSP12physical
26462181
WDR48_HUMANWDR48physical
26462181
ANDR_HUMANARphysical
26462181
UBP12_HUMANUSP12physical
27373336
FERM2_HUMANFERMT2physical
28514442
FBXW5_HUMANFBXW5physical
28514442
OPTN_HUMANOPTNphysical
28514442
WDR48_HUMANWDR48physical
28514442
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
There are no disease associations of PTM sites.
Regulatory Network of WDR20_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-434, 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-432 AND SER-434, ANDMASS SPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-357, AND MASSSPECTROMETRY.

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