WDR75_HUMAN - dbPTM
WDR75_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID WDR75_HUMAN
UniProt AC Q8IWA0
Protein Name WD repeat-containing protein 75
Gene Name WDR75
Organism Homo sapiens (Human).
Sequence Length 830
Subcellular Localization Nucleus, nucleolus .
Protein Description Ribosome biogenesis factor. Involved in nucleolar processing of pre-18S ribosomal RNA. Required for optimal pre-ribosomal RNA transcription by RNA polymerase I..
Protein Sequence MVEEENIRVVRCGGSELNFRRAVFSADSKYIFCVSGDFVKVYSTVTEECVHILHGHRNLVTGIQLNPNNHLQLYSCSLDGTIKLWDYIDGILIKTFIVGCKLHALFTLAQAEDSVFVIVNKEKPDIFQLVSVKLPKSSSQEVEAKELSFVLDYINQSPKCIAFGNEGVYVAAVREFYLSVYFFKKKTTSRFTLSSSRNKKHAKNNFTCVACHPTEDCIASGHMDGKIRLWRNFYDDKKYTYTCLHWHHDMVMDLAFSVTGTSLLSGGRESVLVEWRDATEKNKEFLPRLGATIEHISVSPAGDLFCTSHSDNKIIIIHRNLEASAVIQGLVKDRSIFTGLMIDPRTKALVLNGKPGHLQFYSLQSDKQLYNLDIIQQEYINDYGLIQIELTKAAFGCFGNWLATVEQRQEKETELELQMKLWMYNKKTQGFILNTKINMPHEDCITALCFCNAEKSEQPTLVTASKDGYFKVWILTDDSDIYKKAVGWTCDFVGSYHKYQATNCCFSEDGSLLAVSFEEIVTIWDSVTWELKCTFCQRAGKIRHLCFGRLTCSKYLLGATENGILCCWNLLSCALEWNAKLNVRVMEPDPNSENIAAISQSSVGSDLFVFKPSEPRPLYIQKGISREKVQWGVFVPRDVPESFTSEAYQWLNRSQFYFLTKSQSLLTFSTKSPEEKLTPTSKQLLAEESLPTTPFYFILGKHRQQQDEKLNETLENELVQLPLTENIPAISELLHTPAHVLPSAAFLCSMFVNSLLLSKETKSAKEIPEDVDMEEEKESEDSDEENDFTEKVQDTSNTGLGEDIIHQLSKSEEKELRKFRKIDYSWIAAL
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
57UbiquitinationVHILHGHRNLVTGIQ
HHHHCCCCCEEEEEE		42.6523000965
59UbiquitinationILHGHRNLVTGIQLN
HHCCCCCEEEEEEEC		3.5323000965
69UbiquitinationGIQLNPNNHLQLYSC
EEEECCCCCEEEEEE		38.2022817900
72UbiquitinationLNPNNHLQLYSCSLD
ECCCCCEEEEEEECC		30.7022817900
81UbiquitinationYSCSLDGTIKLWDYI
EEEECCCCEEHHHHC		18.0122817900
121UbiquitinationSVFVIVNKEKPDIFQ
EEEEEEECCCCCEEE		57.1123000965
123UbiquitinationFVIVNKEKPDIFQLV
EEEEECCCCCEEEEE		49.9923000965
123AcetylationFVIVNKEKPDIFQLV
EEEEECCCCCEEEEE		49.9926051181
123SumoylationFVIVNKEKPDIFQLV
EEEEECCCCCEEEEE		49.9928112733
133UbiquitinationIFQLVSVKLPKSSSQ
EEEEEEEECCCCCCC		52.1222817900
136UbiquitinationLVSVKLPKSSSQEVE
EEEEECCCCCCCCCC		73.7021906983
145UbiquitinationSSQEVEAKELSFVLD
CCCCCCHHHHHHHHH		45.7622817900
148PhosphorylationEVEAKELSFVLDYIN
CCCHHHHHHHHHHHH		17.8828348404
153PhosphorylationELSFVLDYINQSPKC
HHHHHHHHHHCCCCE		9.5228348404
157PhosphorylationVLDYINQSPKCIAFG
HHHHHHCCCCEEEEC		23.10-
192PhosphorylationKKTTSRFTLSSSRNK
CCCCCCEEECCCCCH		25.3120166139
194PhosphorylationTTSRFTLSSSRNKKH
CCCCEEECCCCCHHH		24.1820166139
195PhosphorylationTSRFTLSSSRNKKHA
CCCEEECCCCCHHHC		36.1120166139
196PhosphorylationSRFTLSSSRNKKHAK
CCEEECCCCCHHHCC		36.1723186163
203UbiquitinationSRNKKHAKNNFTCVA
CCCHHHCCCCEEEEE		52.74-
203AcetylationSRNKKHAKNNFTCVA
CCCHHHCCCCEEEEE		52.7426051181
217UbiquitinationACHPTEDCIASGHMD
EEECCHHCCCCCCCC		1.9722817900
219UbiquitinationHPTEDCIASGHMDGK
ECCHHCCCCCCCCCE		18.7822817900
226AcetylationASGHMDGKIRLWRNF
CCCCCCCEEEEEEEE		22.0123749302
226UbiquitinationASGHMDGKIRLWRNF
CCCCCCCEEEEEEEE		22.01-
226MalonylationASGHMDGKIRLWRNF
CCCCCCCEEEEEEEE		22.0126320211
268UbiquitinationTSLLSGGRESVLVEW
CCHHCCCCEEEEEEE		36.2222817900
281UbiquitinationEWRDATEKNKEFLPR
EEECCHHHCHHHHHH		69.8022817900
283UbiquitinationRDATEKNKEFLPRLG
ECCHHHCHHHHHHHC		61.9921906983
283AcetylationRDATEKNKEFLPRLG
ECCHHHCHHHHHHHC		61.9926051181
290UbiquitinationKEFLPRLGATIEHIS
HHHHHHHCCEEEEEE		23.1921890473
313UbiquitinationCTSHSDNKIIIIHRN
EECCCCCEEEEEECC		40.03-
313AcetylationCTSHSDNKIIIIHRN
EECCCCCEEEEEECC		40.0326051181
332UbiquitinationAVIQGLVKDRSIFTG
HHHHHHHCCCCCCCC		53.0921906983
332AcetylationAVIQGLVKDRSIFTG
HHHHHHHCCCCCCCC		53.0926051181
338O-linked_GlycosylationVKDRSIFTGLMIDPR
HCCCCCCCCCEECCC		27.9530379171
347UbiquitinationLMIDPRTKALVLNGK
CEECCCCEEEEECCC		40.79-
354UbiquitinationKALVLNGKPGHLQFY
EEEEECCCCCCEEEE		46.9121906983
363UbiquitinationGHLQFYSLQSDKQLY
CCEEEEECCCCCEEE		3.7329967540
402UbiquitinationFGCFGNWLATVEQRQ
HCHHHHHHHHHHHHH		3.1223000965
402AcetylationFGCFGNWLATVEQRQ
HCHHHHHHHHHHHHH		3.1219608861
404PhosphorylationCFGNWLATVEQRQEK
HHHHHHHHHHHHHHH		23.54-
407UbiquitinationNWLATVEQRQEKETE
HHHHHHHHHHHHHHH		48.2823000965
411UbiquitinationTVEQRQEKETELELQ
HHHHHHHHHHHHHHH		62.69-
411AcetylationTVEQRQEKETELELQ
HHHHHHHHHHHHHHH		62.6925953088
413PhosphorylationEQRQEKETELELQMK
HHHHHHHHHHHHHHH		57.87-
419UbiquitinationETELELQMKLWMYNK
HHHHHHHHHHHHHCC		6.3522817900
420UbiquitinationTELELQMKLWMYNKK
HHHHHHHHHHHHCCC		26.4922817900
426AcetylationMKLWMYNKKTQGFIL
HHHHHHCCCCCCEEE		39.4426051181
427SumoylationKLWMYNKKTQGFILN
HHHHHCCCCCCEEEE		42.30-
427SumoylationKLWMYNKKTQGFILN
HHHHHCCCCCCEEEE		42.3028112733
427UbiquitinationKLWMYNKKTQGFILN
HHHHHCCCCCCEEEE		42.3029967540
455UbiquitinationLCFCNAEKSEQPTLV
HHCCCCCCCCCCEEE		57.81-
455AcetylationLCFCNAEKSEQPTLV
HHCCCCCCCCCCEEE		57.8126051181
456PhosphorylationCFCNAEKSEQPTLVT
HCCCCCCCCCCEEEE		32.7322210691
466AcetylationPTLVTASKDGYFKVW
CEEEEECCCCCEEEE		53.3519608861
466UbiquitinationPTLVTASKDGYFKVW
CEEEEECCCCCEEEE		53.3523000965
466MalonylationPTLVTASKDGYFKVW
CEEEEECCCCCEEEE		53.3526320211
471UbiquitinationASKDGYFKVWILTDD
ECCCCCEEEEEEECC		28.3323000965
479PhosphorylationVWILTDDSDIYKKAV
EEEEECCCHHHHHHH		28.8122210691
482PhosphorylationLTDDSDIYKKAVGWT
EECCCHHHHHHHCCC		16.0722210691
483AcetylationTDDSDIYKKAVGWTC
ECCCHHHHHHHCCCC		34.2926051181
483UbiquitinationTDDSDIYKKAVGWTC
ECCCHHHHHHHCCCC		34.2921906983
484AcetylationDDSDIYKKAVGWTCD
CCCHHHHHHHCCCCC		31.1924471193
484UbiquitinationDDSDIYKKAVGWTCD
CCCHHHHHHHCCCCC		31.1922817900
547UbiquitinationGKIRHLCFGRLTCSK
CCCEEEEECCCHHHH		8.8622817900
551PhosphorylationHLCFGRLTCSKYLLG
EEEECCCHHHHHHCC		17.24-
558UbiquitinationTCSKYLLGATENGIL
HHHHHHCCCCCCCEE		28.0527667366
560PhosphorylationSKYLLGATENGILCC
HHHHCCCCCCCEEHH		28.34-
564UbiquitinationLGATENGILCCWNLL
CCCCCCCEEHHHHHH		3.9222817900
602O-linked_GlycosylationIAAISQSSVGSDLFV
EEEEECCCCCCCEEE		23.9030379171
607UbiquitinationQSSVGSDLFVFKPSE
CCCCCCCEEEECCCC		4.1722817900
611UbiquitinationGSDLFVFKPSEPRPL
CCCEEEECCCCCCCE		42.1921906983
612UbiquitinationSDLFVFKPSEPRPLY
CCEEEECCCCCCCEE		32.2422817900
618UbiquitinationKPSEPRPLYIQKGIS
CCCCCCCEEECCCCC		6.5823503661
619PhosphorylationPSEPRPLYIQKGISR
CCCCCCEEECCCCCH		12.18-
622UbiquitinationPRPLYIQKGISREKV
CCCEEECCCCCHHHC		48.9627667366
628UbiquitinationQKGISREKVQWGVFV
CCCCCHHHCEEEEEC		38.3222817900
628MalonylationQKGISREKVQWGVFV
CCCCCHHHCEEEEEC		38.3226320211
628AcetylationQKGISREKVQWGVFV
CCCCCHHHCEEEEEC		38.3225953088
637UbiquitinationQWGVFVPRDVPESFT
EEEEECCCCCCCCCC		52.8621890473
648PhosphorylationESFTSEAYQWLNRSQ
CCCCHHHHHHHHHHC		9.0027642862
662PhosphorylationQFYFLTKSQSLLTFS
CEEEEECCCEEEEEC		21.5530266825
664PhosphorylationYFLTKSQSLLTFSTK
EEEECCCEEEEECCC		32.2230266825
667PhosphorylationTKSQSLLTFSTKSPE
ECCCEEEEECCCCHH		22.3430266825
669PhosphorylationSQSLLTFSTKSPEEK
CCEEEEECCCCHHHH		29.6823312004
670PhosphorylationQSLLTFSTKSPEEKL
CEEEEECCCCHHHHC		31.2023186163
671UbiquitinationSLLTFSTKSPEEKLT
EEEEECCCCHHHHCC		63.9221906983
671AcetylationSLLTFSTKSPEEKLT
EEEEECCCCHHHHCC		63.9226051181
672PhosphorylationLLTFSTKSPEEKLTP
EEEECCCCHHHHCCC		37.3225159151
676UbiquitinationSTKSPEEKLTPTSKQ
CCCCHHHHCCCCHHH		56.8721906983
676AcetylationSTKSPEEKLTPTSKQ
CCCCHHHHCCCCHHH		56.8726051181
676SumoylationSTKSPEEKLTPTSKQ
CCCCHHHHCCCCHHH		56.8728112733
678PhosphorylationKSPEEKLTPTSKQLL
CCHHHHCCCCHHHHH		35.2725159151
680PhosphorylationPEEKLTPTSKQLLAE
HHHHCCCCHHHHHHH		43.2328985074
681PhosphorylationEEKLTPTSKQLLAEE
HHHCCCCHHHHHHHC		21.4326074081
682UbiquitinationEKLTPTSKQLLAEES
HHCCCCHHHHHHHCC		47.6623503661
692PhosphorylationLAEESLPTTPFYFIL
HHHCCCCCCCEEHHH		53.0121406692
693PhosphorylationAEESLPTTPFYFILG
HHCCCCCCCEEHHHC		14.9527273156
696PhosphorylationSLPTTPFYFILGKHR
CCCCCCEEHHHCCCH		7.3021406692
701UbiquitinationPFYFILGKHRQQQDE
CEEHHHCCCHHHHHH		31.9722817900
718PhosphorylationNETLENELVQLPLTE
HHHHHHHHCCCCCCC		4.4833259812
732PhosphorylationENIPAISELLHTPAH
CCCCHHHHHHCCCCH		49.6032142685
746UbiquitinationHVLPSAAFLCSMFVN
HHHHHHHHHHHHHHH		7.6522817900
750UbiquitinationSAAFLCSMFVNSLLL
HHHHHHHHHHHHHHH		4.1922817900
779PhosphorylationDMEEEKESEDSDEEN
CHHHHHCCCCCHHHC		58.7429255136
782PhosphorylationEEKESEDSDEENDFT
HHHCCCCCHHHCCHH		42.7629255136
789PhosphorylationSDEENDFTEKVQDTS
CHHHCCHHHHHHHCC		37.4523927012
795PhosphorylationFTEKVQDTSNTGLGE
HHHHHHHCCCCCCCH		13.5422167270
796PhosphorylationTEKVQDTSNTGLGED
HHHHHHCCCCCCCHH		40.4622167270
798PhosphorylationKVQDTSNTGLGEDII
HHHHCCCCCCCHHHH		33.2822167270
809PhosphorylationEDIIHQLSKSEEKEL
HHHHHHHCCCHHHHH		27.8022167270
810UbiquitinationDIIHQLSKSEEKELR
HHHHHHCCCHHHHHH		71.1721906983
810AcetylationDIIHQLSKSEEKELR
HHHHHHCCCHHHHHH		71.1726051181
811PhosphorylationIIHQLSKSEEKELRK
HHHHHCCCHHHHHHH		47.8425159151
814UbiquitinationQLSKSEEKELRKFRK
HHCCCHHHHHHHHHC		58.9822817900
821UbiquitinationKELRKFRKIDYSWIA
HHHHHHHCCCHHHHH		42.96-
824PhosphorylationRKFRKIDYSWIAAL-
HHHHCCCHHHHHCC-		14.91-
825PhosphorylationKFRKIDYSWIAAL--
HHHCCCHHHHHCC--		14.30-
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 WDR75_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of WDR75_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 WDR75_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of WDR75_HUMAN !!
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 WDR75_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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-466, AND MASS SPECTROMETRY.
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-779 AND SER-782, ANDMASS SPECTROMETRY.
"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-779 AND SER-782, ANDMASS SPECTROMETRY.
"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-779; SER-782; SER-796AND SER-811, AND MASS SPECTROMETRY.
"Phosphoproteome analysis of the human mitotic spindle.";
Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.;
Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-779 AND SER-796, 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-779 AND SER-782, ANDMASS SPECTROMETRY.

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