WDR55_HUMAN - dbPTM
WDR55_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID WDR55_HUMAN
UniProt AC Q9H6Y2
Protein Name WD repeat-containing protein 55
Gene Name WDR55
Organism Homo sapiens (Human).
Sequence Length 383
Subcellular Localization Nucleus, nucleolus. Cytoplasm.
Protein Description Nucleolar protein that acts as a modulator of rRNA synthesis. Plays a central role during organogenesis (By similarity)..
Protein Sequence MDRTCEERPAEDGSDEEDPDSMEAPTRIRDTPEDIVLEAPASGLAFHPARDLLAAGDVDGDVFVFSYSCQEGETKELWSSGHHLKACRAVAFSEDGQKLITVSKDKAIHVLDVEQGQLERRVSKAHGAPINSLLLVDENVLATGDDTGGICLWDQRKEGPLMDMRQHEEYIADMALDPAKKLLLTASGDGCLGIFNIKRRRFELLSEPQSGDLTSVTLMKWGKKVACGSSEGTIYLFNWNGFGATSDRFALRAESIDCMVPVTESLLCTGSTDGVIRAVNILPNRVVGSVGQHTGEPVEELALSHCGRFLASSGHDQRLKFWDMAQLRAVVVDDYRRRKKKGGPLRALSSKTWSTDDFFAGLREEGEDSMAQEEKEETGDDSD
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
4Phosphorylation----MDRTCEERPAE
----CCCCCCCCCCC		21.7223927012
14PhosphorylationERPAEDGSDEEDPDS
CCCCCCCCCCCCCCC		54.9222167270
21PhosphorylationSDEEDPDSMEAPTRI
CCCCCCCCCCCCCCC		24.7430278072
26PhosphorylationPDSMEAPTRIRDTPE
CCCCCCCCCCCCCCC		45.8623927012
31PhosphorylationAPTRIRDTPEDIVLE
CCCCCCCCCCCEEEE		20.8030108239
85UbiquitinationWSSGHHLKACRAVAF
HHCCCHHHHEEEEEE		40.87-
93PhosphorylationACRAVAFSEDGQKLI
HEEEEEECCCCCEEE		25.6620068231
98UbiquitinationAFSEDGQKLITVSKD
EECCCCCEEEEEECC		47.59-
102 (in isoform 2)Ubiquitination-5.4721890473
104UbiquitinationQKLITVSKDKAIHVL
CEEEEEECCCEEEEE		59.93-
1042-HydroxyisobutyrylationQKLITVSKDKAIHVL
CEEEEEECCCEEEEE		59.93-
1062-HydroxyisobutyrylationLITVSKDKAIHVLDV
EEEEECCCEEEEEEC		53.64-
106UbiquitinationLITVSKDKAIHVLDV
EEEEECCCEEEEEEC		53.64-
157UbiquitinationICLWDQRKEGPLMDM
EECEECCCCCCCCCH		62.48-
180UbiquitinationDMALDPAKKLLLTAS
HHHCCHHHHHHHEEC		49.71-
255PhosphorylationRFALRAESIDCMVPV
CCHHHHHHCCEEEEC		23.8127251275
289PhosphorylationLPNRVVGSVGQHTGE
CCCCEEEECCCCCCC		16.0927080861
294PhosphorylationVGSVGQHTGEPVEEL
EEECCCCCCCCHHHH		35.0427080861
304PhosphorylationPVEELALSHCGRFLA
CHHHHHHHHHHHHHH		15.8927080861
320UbiquitinationSGHDQRLKFWDMAQL
CCCCHHHHHHHHHHH		46.7421890473
320 (in isoform 1)Ubiquitination-46.7421890473
351UbiquitinationPLRALSSKTWSTDDF
CCHHHCCCCCCCCCC		51.11-
352PhosphorylationLRALSSKTWSTDDFF
CHHHCCCCCCCCCCH		26.9627080861
354PhosphorylationALSSKTWSTDDFFAG
HHCCCCCCCCCCHHH		27.4727732954
355PhosphorylationLSSKTWSTDDFFAGL
HCCCCCCCCCCHHHH		31.0227080861
369PhosphorylationLREEGEDSMAQEEKE
HHHCCCCCCCHHHHH		16.2418669648
378PhosphorylationAQEEKEETGDDSD--
CHHHHHHHCCCCC--		47.1830278072
382PhosphorylationKEETGDDSD------
HHHHCCCCC------		50.3830278072
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 WDR55_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of WDR55_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 WDR55_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PP4R2_HUMANPPP4R2physical
26344197
MCMBP_HUMANMCMBPphysical
28514442
BOP1_HUMANBOP1physical
28514442
RL7L_HUMANRPL7L1physical
28514442
KLDC3_HUMANKLHDC3physical
28514442
LENG8_HUMANLENG8physical
28514442
WDR12_HUMANWDR12physical
28514442
SPB1_HUMANFTSJ3physical
28514442
REXO5_HUMANLOC81691physical
28514442
RL3_HUMANRPL3physical
28514442
CNDH2_HUMANNCAPH2physical
28514442
PESC_HUMANPES1physical
28514442
JPH1_HUMANJPH1physical
28514442
NOC3L_HUMANNOC3Lphysical
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 WDR55_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-14, 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-14; THR-378 AND SER-382,AND MASS SPECTROMETRY.

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