WDR43_HUMAN - dbPTM
WDR43_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID WDR43_HUMAN
UniProt AC Q15061
Protein Name WD repeat-containing protein 43
Gene Name WDR43
Organism Homo sapiens (Human).
Sequence Length 677
Subcellular Localization Nucleus, nucleolus . Found predominantly at the fibrillar center.
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 MAAGGGGSCDPLAPAGVPCAFSPHSQAYFALASTDGHLRVWETANNRLHQEYVPSAHLSGTCTCLAWAPARLQAKESPQRKKRKSEAVGMSNQTDLLALGTAVGSILLYSTVKGELHSKLISGGHDNRVNCIQWHQDSGCLYSCSDDKHIVEWNVQTCKVKCKWKGDNSSVSSLCISPDGKMLLSAGRTIKLWVLETKEVYRHFTGHATPVSSLMFTTIRPPNESQPFDGITGLYFLSGAVHDRLLNVWQVRSENKEKSAVMSFTVTDEPVYIDLTLSENKEEPVKLAVVCRDGQVHLFEHILNGYCKKPLTSNCTIQIATPGKGKKSTPKPIPILAAGFCSDKMSLLLVYGSWFQPTIERVALNSREPHMCLVRDISNCWAPKVETAITKVRTPVMNSEAKVLVPGIPGHHAAIKPAPPQTEQVESKRKSGGNEVSIEERLGAMDIDTHKKGKEDLQTNSFPVLLTQGLESNDFEMLNKVLQTRNVNLIKKTVLRMPLHTIIPLLQELTKRLQGHPNSAVLMVQWLKCVLTVHASYLSTLPDLVPQLGTLYQLMESRVKTFQKLSHLHGKLILLITQVTASEKTKGATSPGQKAKLVYEEESSEEESDDEIADKDSEDNWDEDEEESESEKDEDVEEEDEDAEGKDEENGEDRDTASEKELNGDSDLDPENESEEE
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
63PhosphorylationAHLSGTCTCLAWAPA
CHHCCCEEEEEECCH		15.4729457462
75AcetylationAPARLQAKESPQRKK
CCHHHCCCCCHHHHH		45.8526051181
77PhosphorylationARLQAKESPQRKKRK
HHHCCCCCHHHHHHH		26.1522167270
85PhosphorylationPQRKKRKSEAVGMSN
HHHHHHHHHHHCCCC		34.5229496963
91PhosphorylationKSEAVGMSNQTDLLA
HHHHHCCCCHHHHHH		21.6226503514
94PhosphorylationAVGMSNQTDLLALGT
HHCCCCHHHHHHHHH		32.6326307563
101PhosphorylationTDLLALGTAVGSILL
HHHHHHHHHHHHHHH		21.0126307563
105PhosphorylationALGTAVGSILLYSTV
HHHHHHHHHHHHEEC		11.9426307563
109PhosphorylationAVGSILLYSTVKGEL
HHHHHHHHEECCCCH		10.0026307563
110PhosphorylationVGSILLYSTVKGELH
HHHHHHHEECCCCHH		27.0526307563
111PhosphorylationGSILLYSTVKGELHS
HHHHHHEECCCCHHH		16.8126307563
119UbiquitinationVKGELHSKLISGGHD
CCCCHHHHHHHCCCC		38.8121906983
119AcetylationVKGELHSKLISGGHD
CCCCHHHHHHHCCCC		38.8125953088
148AcetylationLYSCSDDKHIVEWNV
EEEECCCCCEEEEEE		39.9726051181
162UbiquitinationVQTCKVKCKWKGDNS
EEEEEEEEEECCCCC		7.7121890473
165UbiquitinationCKVKCKWKGDNSSVS
EEEEEEECCCCCCCC		41.7129967540
165AcetylationCKVKCKWKGDNSSVS
EEEEEEECCCCCCCC		41.7126051181
169PhosphorylationCKWKGDNSSVSSLCI
EEECCCCCCCCEEEE		36.5428674151
170PhosphorylationKWKGDNSSVSSLCIS
EECCCCCCCCEEEEC		32.0728674151
172PhosphorylationKGDNSSVSSLCISPD
CCCCCCCCEEEECCC		21.3820873877
173PhosphorylationGDNSSVSSLCISPDG
CCCCCCCEEEECCCC		25.7120873877
177PhosphorylationSVSSLCISPDGKMLL
CCCEEEECCCCCEEE		18.8820873877
181MethylationLCISPDGKMLLSAGR
EEECCCCCEEECCCC		33.48-
181AcetylationLCISPDGKMLLSAGR
EEECCCCCEEECCCC		33.4826051181
181UbiquitinationLCISPDGKMLLSAGR
EEECCCCCEEECCCC		33.4823000965
185PhosphorylationPDGKMLLSAGRTIKL
CCCCEEECCCCEEEE		25.3920068231
189PhosphorylationMLLSAGRTIKLWVLE
EEECCCCEEEEEEEE		22.8820068231
191UbiquitinationLSAGRTIKLWVLETK
ECCCCEEEEEEEECH		35.3721890473
191AcetylationLSAGRTIKLWVLETK
ECCCCEEEEEEEECH		35.3726051181
198UbiquitinationKLWVLETKEVYRHFT
EEEEEECHHHHHHHC		35.4921906983
198AcetylationKLWVLETKEVYRHFT
EEEEEECHHHHHHHC		35.4923749302
241UbiquitinationLYFLSGAVHDRLLNV
EEEHHHHHHHHHHHH		5.7121890473
286UbiquitinationENKEEPVKLAVVCRD
CCCCCCEEEEEEECC		41.2529967540
309AcetylationILNGYCKKPLTSNCT
HHCCCCCCCCCCCCE		41.5226051181
309UbiquitinationILNGYCKKPLTSNCT
HHCCCCCCCCCCCCE		41.5229967540
309SumoylationILNGYCKKPLTSNCT
HHCCCCCCCCCCCCE		41.5225114211
312PhosphorylationGYCKKPLTSNCTIQI
CCCCCCCCCCCEEEE		26.8120068231
313PhosphorylationYCKKPLTSNCTIQIA
CCCCCCCCCCEEEEC		37.2820068231
316PhosphorylationKPLTSNCTIQIATPG
CCCCCCCEEEECCCC		21.8420068231
321PhosphorylationNCTIQIATPGKGKKS
CCEEEECCCCCCCCC		33.9130266825
324UbiquitinationIQIATPGKGKKSTPK
EEECCCCCCCCCCCC		69.6221963094
324MalonylationIQIATPGKGKKSTPK
EEECCCCCCCCCCCC		69.6232601280
328PhosphorylationTPGKGKKSTPKPIPI
CCCCCCCCCCCCCCE		54.1225627689
329PhosphorylationPGKGKKSTPKPIPIL
CCCCCCCCCCCCCEE		44.1825627689
331UbiquitinationKGKKSTPKPIPILAA
CCCCCCCCCCCEEEE		56.5229967540
331AcetylationKGKKSTPKPIPILAA
CCCCCCCCCCCEEEE		56.5226051181
358PhosphorylationYGSWFQPTIERVALN
CCCCCCHHHHHHHCC		25.37-
378PhosphorylationMCLVRDISNCWAPKV
EEEEEEHHHCCCCCC		30.1730108239
384AcetylationISNCWAPKVETAITK
HHHCCCCCCHHHHEE		44.9826051181
384UbiquitinationISNCWAPKVETAITK
HHHCCCCCCHHHHEE		44.98-
384SumoylationISNCWAPKVETAITK
HHHCCCCCCHHHHEE		44.9825114211
391AcetylationKVETAITKVRTPVMN
CCHHHHEECCCCCCC		24.4925953088
391UbiquitinationKVETAITKVRTPVMN
CCHHHHEECCCCCCC		24.4923000965
394PhosphorylationTAITKVRTPVMNSEA
HHHEECCCCCCCCCC		24.1930266825
399PhosphorylationVRTPVMNSEAKVLVP
CCCCCCCCCCEEECC		22.3424732914
402UbiquitinationPVMNSEAKVLVPGIP
CCCCCCCEEECCCCC		31.8629967540
416UbiquitinationPGHHAAIKPAPPQTE
CCCCCCCCCCCCCCH		30.3333845483
416AcetylationPGHHAAIKPAPPQTE
CCCCCCCCCCCCCCH		30.3325953088
427PhosphorylationPQTEQVESKRKSGGN
CCCHHHHHHHCCCCC		38.6125159151
428UbiquitinationQTEQVESKRKSGGNE
CCHHHHHHHCCCCCC		50.7933845483
430UbiquitinationEQVESKRKSGGNEVS
HHHHHHHCCCCCCCC		58.1333845483
431PhosphorylationQVESKRKSGGNEVSI
HHHHHHCCCCCCCCH		56.8429255136
434UbiquitinationSKRKSGGNEVSIEER
HHHCCCCCCCCHHHH		50.4521890473
437PhosphorylationKSGGNEVSIEERLGA
CCCCCCCCHHHHHCC		20.3625159151
449PhosphorylationLGAMDIDTHKKGKED
HCCCCCCCCCCCHHH		35.6128555341
451UbiquitinationAMDIDTHKKGKEDLQ
CCCCCCCCCCHHHHH		66.3733845483
451AcetylationAMDIDTHKKGKEDLQ
CCCCCCCCCCHHHHH		66.3726051181
4512-HydroxyisobutyrylationAMDIDTHKKGKEDLQ
CCCCCCCCCCHHHHH		66.37-
452UbiquitinationMDIDTHKKGKEDLQT
CCCCCCCCCHHHHHC		68.5523503661
454UbiquitinationIDTHKKGKEDLQTNS
CCCCCCCHHHHHCCC		57.8621963094
480UbiquitinationNDFEMLNKVLQTRNV
CCHHHHHHHHHHCCC		40.1229967540
491UbiquitinationTRNVNLIKKTVLRMP
HCCCHHHHHHHHHCH		45.6233845483
491AcetylationTRNVNLIKKTVLRMP
HCCCHHHHHHHHHCH		45.6225953088
493PhosphorylationNVNLIKKTVLRMPLH
CCHHHHHHHHHCHHH		21.5524719451
501PhosphorylationVLRMPLHTIIPLLQE
HHHCHHHHHHHHHHH		28.4322210691
510PhosphorylationIPLLQELTKRLQGHP
HHHHHHHHHHHCCCC		17.2322210691
511AcetylationPLLQELTKRLQGHPN
HHHHHHHHHHCCCCC		64.8326051181
511UbiquitinationPLLQELTKRLQGHPN
HHHHHHHHHHCCCCC		64.8333845483
554UbiquitinationQLGTLYQLMESRVKT
HHHHHHHHHHHHHHH		2.3121890473
564UbiquitinationSRVKTFQKLSHLHGK
HHHHHHHHHHHHHHH		48.0029967540
577PhosphorylationGKLILLITQVTASEK
HHHHEEEEEECCCCC		19.5621406692
580PhosphorylationILLITQVTASEKTKG
HEEEEEECCCCCCCC		18.0421406692
582PhosphorylationLITQVTASEKTKGAT
EEEEECCCCCCCCCC		30.2021406692
584AcetylationTQVTASEKTKGATSP
EEECCCCCCCCCCCC		53.7126051181
589PhosphorylationSEKTKGATSPGQKAK
CCCCCCCCCCCCEEE		44.0920860994
590PhosphorylationEKTKGATSPGQKAKL
CCCCCCCCCCCEEEE		26.8825849741
599PhosphorylationGQKAKLVYEEESSEE
CCEEEEEEECCCCCC		28.2321406692
603PhosphorylationKLVYEEESSEEESDD
EEEEECCCCCCCCCC		46.4520363803
604PhosphorylationLVYEEESSEEESDDE
EEEECCCCCCCCCCC		52.9220363803
608PhosphorylationEESSEEESDDEIADK
CCCCCCCCCCCCCCC		54.3520363803
628PhosphorylationWDEDEEESESEKDED
CCCCHHHCHHHCCCC		50.1021406692
630PhosphorylationEDEEESESEKDEDVE
CCHHHCHHHCCCCCH		60.2621406692
656PhosphorylationENGEDRDTASEKELN
CCCCCCCCCCHHHHC		32.7429255136
658PhosphorylationGEDRDTASEKELNGD
CCCCCCCCHHHHCCC		51.8229255136
666PhosphorylationEKELNGDSDLDPENE
HHHHCCCCCCCCCCC		41.2828985074
674PhosphorylationDLDPENESEEE----
CCCCCCCCCCC----		62.9928985074
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 WDR43_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of WDR43_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 WDR43_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NP1L1_HUMANNAP1L1physical
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
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of WDR43_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-431, 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-431, AND MASSSPECTROMETRY.
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-77; THR-394; SER-431 ANDSER-437, AND MASS SPECTROMETRY.
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-394 AND SER-431, ANDMASS 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-431, AND MASSSPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-431, AND MASSSPECTROMETRY.
"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-77; SER-603; SER-604 ANDSER-608, AND MASS SPECTROMETRY.

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