WDR3_HUMAN - dbPTM
WDR3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID WDR3_HUMAN
UniProt AC Q9UNX4
Protein Name WD repeat-containing protein 3
Gene Name WDR3
Organism Homo sapiens (Human).
Sequence Length 943
Subcellular Localization Nucleus, nucleolus .
Protein Description
Protein Sequence MGLTKQYLRYVASAVFGVIGSQKGNIVFVTLRGEKGRYVAVPACEHVFIWDLRKGEKILILQGLKQEVTCLCPSPDGLHLAVGYEDGSIRIFSLLSGEGNVTFNGHKAAITTLKYDQLGGRLASGSKDTDIIVWDVINESGLYRLKGHKDAITQALFLREKNLLVTSGKDTMVKWWDLDTQHCFKTMVGHRTEVWGLVLLSEEKRLITGASDSELRVWDIAYLQEIEDPEEPDPKKIKGSSPGIQDTLEAEDGAFETDEAPEDRILSCRKAGSIMREGRDRVVNLAVDKTGRILACHGTDSVLELFCILSKKEIQKKMDKKMKKARKKAKLHSSKGEEEDPEVNVEMSLQDEIQRVTNIKTSAKIKSFDLIHSPHGELKAVFLLQNNLVELYSLNPSLPTPQPVRTSRITIGGHRSDVRTLSFSSDNIAVLSAAADSIKIWNRSTLQCIRTMTCEYALCSFFVPGDRQVVIGTKTGKLQLYDLASGNLLETIDAHDGALWSMSLSPDQRGFVTGGADKSVKFWDFELVKDENSTQKRLSVKQTRTLQLDEDVLCVSYSPNQKLLAVSLLDCTVKIFYVDTLKFFLSLYGHKLPVICMDISHDGALIATGSADRNVKIWGLDFGDCHKSLFAHDDSVMYLQFVPKSHLFFTAGKDHKIKQWDADKFEHIQTLEGHHQEIWCLAVSPSGDYVVSSSHDKSLRLWERTREPLILEEEREMEREAEYEESVAKEDQPAVPGETQGDSYFTGKKTIETVKAAERIMEAIELYREETAKMKEHKAICKAAGKEVPLPSNPILMAYGSISPSAYVLEIFKGIKSSELEESLLVLPFSYVPDILKLFNEFIQLGSDVELICRCLFFLLRIHFGQITSNQMLVPVIEKLRETTISKVSQVRDVIGFNMAGLDYLKRECEAKSEVMFFADATSHLEEKKRKRKKREKLILTLT
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----MGLTKQYLRYV
----CCCCHHHHHHH		15.4620068231
7Phosphorylation-MGLTKQYLRYVASA
-CCCCHHHHHHHHHH		8.4920068231
10PhosphorylationLTKQYLRYVASAVFG
CCHHHHHHHHHHHHH		9.5820068231
13PhosphorylationQYLRYVASAVFGVIG
HHHHHHHHHHHHHHC		18.2120068231
21PhosphorylationAVFGVIGSQKGNIVF
HHHHHHCCCCCCEEE		20.0020068231
57UbiquitinationWDLRKGEKILILQGL
EECCCCCEEEEEECC		52.0221890473
65AcetylationILILQGLKQEVTCLC
EEEEECCCCEEEEEE		51.7621466224
65UbiquitinationILILQGLKQEVTCLC
EEEEECCCCEEEEEE		51.76-
93PhosphorylationDGSIRIFSLLSGEGN
CCCEEEEEEECCCCC		26.4820068231
96PhosphorylationIRIFSLLSGEGNVTF
EEEEEEECCCCCEEE		39.8420068231
102PhosphorylationLSGEGNVTFNGHKAA
ECCCCCEEECCEEEE		18.5120068231
114UbiquitinationKAAITTLKYDQLGGR
EEEEEEEEEHHCCCC		44.69-
1142-HydroxyisobutyrylationKAAITTLKYDQLGGR
EEEEEEEEEHHCCCC		44.69-
114AcetylationKAAITTLKYDQLGGR
EEEEEEEEEHHCCCC		44.6926051181
149UbiquitinationLYRLKGHKDAITQAL
CCCCCCCHHHHHHHH		58.48-
161UbiquitinationQALFLREKNLLVTSG
HHHHHHHCCEEEEEC		46.60-
1612-HydroxyisobutyrylationQALFLREKNLLVTSG
HHHHHHHCCEEEEEC		46.60-
169AcetylationNLLVTSGKDTMVKWW
CEEEEECCCCEEEEE		50.2026051181
211PhosphorylationKRLITGASDSELRVW
HCCCCCCCCCCEEEE		42.9125850435
213PhosphorylationLITGASDSELRVWDI
CCCCCCCCCEEEEEE		35.7125850435
235UbiquitinationDPEEPDPKKIKGSSP
CCCCCCCCCCCCCCC		74.61-
235AcetylationDPEEPDPKKIKGSSP
CCCCCCCCCCCCCCC		74.6124431727
238UbiquitinationEPDPKKIKGSSPGIQ
CCCCCCCCCCCCCHH		62.7121890473
240PhosphorylationDPKKIKGSSPGIQDT
CCCCCCCCCCCHHHH		28.4922167270
241PhosphorylationPKKIKGSSPGIQDTL
CCCCCCCCCCHHHHE		35.5022167270
247PhosphorylationSSPGIQDTLEAEDGA
CCCCHHHHEECCCCC		15.3222167270
257PhosphorylationAEDGAFETDEAPEDR
CCCCCCCCCCCCHHH		32.4623927012
270UbiquitinationDRILSCRKAGSIMRE
HHHHHHHHHHHHHHC		62.52-
2892-HydroxyisobutyrylationVVNLAVDKTGRILAC
EEEEEECCCCCEEEE		46.40-
289UbiquitinationVVNLAVDKTGRILAC
EEEEEECCCCCEEEE		46.40-
289AcetylationVVNLAVDKTGRILAC
EEEEEECCCCCEEEE		46.4025953088
333PhosphorylationRKKAKLHSSKGEEED
HHHHHHCCCCCCCCC		44.1518669648
334PhosphorylationKKAKLHSSKGEEEDP
HHHHHCCCCCCCCCC		33.6529214152
335AcetylationKAKLHSSKGEEEDPE
HHHHCCCCCCCCCCC		73.6626051181
3602-HydroxyisobutyrylationIQRVTNIKTSAKIKS
HHHHHCCCCCCEEEE		38.20-
360UbiquitinationIQRVTNIKTSAKIKS
HHHHHCCCCCCEEEE		38.20-
3662-HydroxyisobutyrylationIKTSAKIKSFDLIHS
CCCCCEEEEEEEECC		44.34-
366AcetylationIKTSAKIKSFDLIHS
CCCCCEEEEEEEECC		44.3426051181
366UbiquitinationIKTSAKIKSFDLIHS
CCCCCEEEEEEEECC		44.34-
373PhosphorylationKSFDLIHSPHGELKA
EEEEEECCCCCHHHE		16.1720873877
456PhosphorylationIRTMTCEYALCSFFV
HHHHCCCEEEECEEC		13.66-
473PhosphorylationDRQVVIGTKTGKLQL
CCEEEEEECCCEEEE		17.8226074081
474UbiquitinationRQVVIGTKTGKLQLY
CEEEEEECCCEEEEE		50.49-
474SumoylationRQVVIGTKTGKLQLY
CEEEEEECCCEEEEE		50.4928112733
475PhosphorylationQVVIGTKTGKLQLYD
EEEEEECCCEEEEEE		39.1126074081
481PhosphorylationKTGKLQLYDLASGNL
CCCEEEEEECCCCCE		8.9226074081
505PhosphorylationALWSMSLSPDQRGFV
CEEEEECCHHHCCCC		21.0820860994
513PhosphorylationPDQRGFVTGGADKSV
HHHCCCCCCCCCCCE		27.8624144214
518UbiquitinationFVTGGADKSVKFWDF
CCCCCCCCCEEEEEE		57.52-
5182-HydroxyisobutyrylationFVTGGADKSVKFWDF
CCCCCCCCCEEEEEE		57.52-
519PhosphorylationVTGGADKSVKFWDFE
CCCCCCCCEEEEEEE		30.9622210691
521UbiquitinationGGADKSVKFWDFELV
CCCCCCEEEEEEEEE		48.0721890473
529AcetylationFWDFELVKDENSTQK
EEEEEEECCCCCCCC		72.4626051181
529UbiquitinationFWDFELVKDENSTQK
EEEEEEECCCCCCCC		72.46-
529SumoylationFWDFELVKDENSTQK
EEEEEEECCCCCCCC		72.4628112733
529SumoylationFWDFELVKDENSTQK
EEEEEEECCCCCCCC		72.46-
536AcetylationKDENSTQKRLSVKQT
CCCCCCCCCCCCEEE		56.2325953088
536UbiquitinationKDENSTQKRLSVKQT
CCCCCCCCCCCCEEE		56.23-
541UbiquitinationTQKRLSVKQTRTLQL
CCCCCCCEEEEEEEC		42.44-
567PhosphorylationNQKLLAVSLLDCTVK
CCCCHHHHHHHCEEE		20.0130576142
572PhosphorylationAVSLLDCTVKIFYVD
HHHHHHCEEEEEEHH		25.2230576142
577PhosphorylationDCTVKIFYVDTLKFF
HCEEEEEEHHHHHHH		10.8220068231
580PhosphorylationVKIFYVDTLKFFLSL
EEEEEHHHHHHHHHH		23.0820068231
586PhosphorylationDTLKFFLSLYGHKLP
HHHHHHHHHHCCCCC		17.87-
588PhosphorylationLKFFLSLYGHKLPVI
HHHHHHHHCCCCCEE		17.51-
616AcetylationGSADRNVKIWGLDFG
CCCCCCCEEEEECCC		35.9725953088
645PhosphorylationYLQFVPKSHLFFTAG
EEEECCHHHEEEECC		21.25-
653AcetylationHLFFTAGKDHKIKQW
HEEEECCCCCCCCCC		54.9523749302
653UbiquitinationHLFFTAGKDHKIKQW
HEEEECCCCCCCCCC		54.95-
6532-HydroxyisobutyrylationHLFFTAGKDHKIKQW
HEEEECCCCCCCCCC		54.95-
656UbiquitinationFTAGKDHKIKQWDAD
EECCCCCCCCCCCHH		62.83-
723PhosphorylationEMEREAEYEESVAKE
HHHHHHHHHHHHCCC		31.8523663014
726PhosphorylationREAEYEESVAKEDQP
HHHHHHHHHCCCCCC		18.5525849741
729UbiquitinationEYEESVAKEDQPAVP
HHHHHHCCCCCCCCC		60.72-
739PhosphorylationQPAVPGETQGDSYFT
CCCCCCCCCCCCCCC		43.7126657352
743PhosphorylationPGETQGDSYFTGKKT
CCCCCCCCCCCCCCH		29.0420068231
744PhosphorylationGETQGDSYFTGKKTI
CCCCCCCCCCCCCHH		15.2020068231
746PhosphorylationTQGDSYFTGKKTIET
CCCCCCCCCCCHHHH		39.6020068231
748AcetylationGDSYFTGKKTIETVK
CCCCCCCCCHHHHHH		43.6225953088
748UbiquitinationGDSYFTGKKTIETVK
CCCCCCCCCHHHHHH		43.62-
749UbiquitinationDSYFTGKKTIETVKA
CCCCCCCCHHHHHHH		56.96-
755UbiquitinationKKTIETVKAAERIME
CCHHHHHHHHHHHHH		49.66-
854MethylationSDVELICRCLFFLLR
CCHHHHHHHHHHHHH		17.1230761541
887UbiquitinationLRETTISKVSQVRDV
HHHCCHHHHHHHHHH		41.89-
887AcetylationLRETTISKVSQVRDV
HHHCCHHHHHHHHHH		41.8926051181
906UbiquitinationMAGLDYLKRECEAKS
CCCHHHHHHHHHCCC		39.66-
906AcetylationMAGLDYLKRECEAKS
CCCHHHHHHHHHCCC		39.6626051181
922PhosphorylationVMFFADATSHLEEKK
EEEHHHHCHHHHHHH		19.7525849741
923PhosphorylationMFFADATSHLEEKKR
EEHHHHCHHHHHHHH		28.0025849741
941PhosphorylationKREKLILTLT-----
HHHHHEEECC-----		22.7420068231
943PhosphorylationEKLILTLT-------
HHHEEECC-------		31.1820068231
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 WDR3_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of WDR3_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 WDR3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NOG1_HUMANGTPBP4physical
26344197
NSUN5_HUMANNSUN5physical
26344197
TRUA_HUMANPUS1physical
26344197
PWP2_HUMANPWP2physical
26344197
U3IP2_HUMANRRP9physical
26344197
TBL3_HUMANTBL3physical
26344197
ZO1_HUMANTJP1physical
26344197
WDR36_HUMANWDR36physical
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 WDR3_HUMAN

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Related Literatures of Post-Translational Modification
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-240 AND SER-241, 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-240, AND MASSSPECTROMETRY.
"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 THR-247, AND MASSSPECTROMETRY.
"Tyrosine phosphorylated Par3 regulates epithelial tight junctionassembly promoted by EGFR signaling.";
Wang Y., Du D., Fang L., Yang G., Zhang C., Zeng R., Ullrich A.,Lottspeich F., Chen Z.;
EMBO J. 25:5058-5070(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-723, AND MASSSPECTROMETRY.

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