WDR18_HUMAN - dbPTM
WDR18_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID WDR18_HUMAN
UniProt AC Q9BV38
Protein Name WD repeat-containing protein 18
Gene Name WDR18
Organism Homo sapiens (Human).
Sequence Length 432
Subcellular Localization Nucleus, nucleolus . Nucleus, nucleoplasm . Cytoplasm . Mainly found in the nucleoplasm, with low levels detected in the cytoplasmic and chromatin fractions.
Protein Description Functions as a component of the Five Friends of Methylated CHTOP (5FMC) complex; the 5FMC complex is recruited to ZNF148 by methylated CHTOP, leading to desumoylation of ZNF148 and subsequent transactivation of ZNF148 target genes. [PubMed: 22872859 Component of the PELP1 complex involved in the nucleolar steps of 28S rRNA maturation and the subsequent nucleoplasmic transit of the pre-60S ribosomal subunit]
Protein Sequence MAAPMEVAVCTDSAAPMWSCIVWELHSGANLLTYRGGQAGPRGLALLNGEYLLAAQLGKNYISAWELQRKDQLQQKIMCPGPVTCLTASPNGLYVLAGVAESIHLWEVSTGNLLVILSRHYQDVSCLQFTGDSSHFISGGKDCLVLVWSLCSVLQADPSRIPAPRHVWSHHALPITDLHCGFGGPLARVATSSLDQTVKLWEVSSGELLLSVLFDVSIMAVTMDLAEHHMFCGGSEGSIFQVDLFTWPGQRERSFHPEQDAGKVFKGHRNQVTCLSVSTDGSVLLSGSHDETVRLWDVQSKQCIRTVALKGPVTNAAILLAPVSMLSSDFRPSLPLPHFNKHLLGAEHGDEPRHGGLTLRLGLHQQGSEPSYLDRTEQLQAVLCSTMEKSVLGGQDQLRVRVTELEDEVRNLRKINRDLFDFSTRFITRPAK
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
51PhosphorylationLALLNGEYLLAAQLG
HHEECCCCHHHHHHC		14.39-
61PhosphorylationAAQLGKNYISAWELQ
HHHHCCCHHCHHHHH		10.3525159151
63PhosphorylationQLGKNYISAWELQRK
HHCCCHHCHHHHHCH		19.5728152594
70UbiquitinationSAWELQRKDQLQQKI
CHHHHHCHHHHHHHH		36.5429967540
121PhosphorylationLVILSRHYQDVSCLQ
EEEECCCCCCCEEEE		12.80-
133PhosphorylationCLQFTGDSSHFISGG
EEEEECCCHHHHCCC		27.36-
191PhosphorylationGPLARVATSSLDQTV
CHHHHHHCCCHHHCE		18.9121406692
192PhosphorylationPLARVATSSLDQTVK
HHHHHHCCCHHHCEE		21.1121406692
193PhosphorylationLARVATSSLDQTVKL
HHHHHCCCHHHCEEE		31.4521406692
197PhosphorylationATSSLDQTVKLWEVS
HCCCHHHCEEEEEEC		21.1921406692
263AcetylationHPEQDAGKVFKGHRN
CCCCCCCCEECCCCC		46.3426051181
263UbiquitinationHPEQDAGKVFKGHRN
CCCCCCCCEECCCCC		46.3421906983
266UbiquitinationQDAGKVFKGHRNQVT
CCCCCEECCCCCCEE		57.7122817900
275UbiquitinationHRNQVTCLSVSTDGS
CCCCEEEEEEECCCC		4.0722817900
276PhosphorylationRNQVTCLSVSTDGSV
CCCEEEEEEECCCCE		19.03-
278UbiquitinationQVTCLSVSTDGSVLL
CEEEEEEECCCCEEE		19.8722817900
301AcetylationRLWDVQSKQCIRTVA
EEEECCCCCEEEEEE		31.9026051181
301UbiquitinationRLWDVQSKQCIRTVA
EEEECCCCCEEEEEE		31.9022505724
313UbiquitinationTVALKGPVTNAAILL
EEECCCCCCHHHHHH		9.8122505724
314PhosphorylationVALKGPVTNAAILLA
EECCCCCCHHHHHHH		23.4420068231
324PhosphorylationAILLAPVSMLSSDFR
HHHHHHHHHHCCCCC		16.9720068231
327PhosphorylationLAPVSMLSSDFRPSL
HHHHHHHCCCCCCCC		21.1520068231
368PhosphorylationLGLHQQGSEPSYLDR
EEEECCCCCCCHHCH		41.8328985074
371PhosphorylationHQQGSEPSYLDRTEQ
ECCCCCCCHHCHHHH		33.9920873877
372PhosphorylationQQGSEPSYLDRTEQL
CCCCCCCHHCHHHHH		24.2820873877
375MethylationSEPSYLDRTEQLQAV
CCCCHHCHHHHHHHH		37.25115919925
376PhosphorylationEPSYLDRTEQLQAVL
CCCHHCHHHHHHHHH		27.9620068231
385PhosphorylationQLQAVLCSTMEKSVL
HHHHHHHHHHHHHHH		26.9920068231
389UbiquitinationVLCSTMEKSVLGGQD
HHHHHHHHHHHCCCC		34.7321963094
401UbiquitinationGQDQLRVRVTELEDE
CCCCEEEEEEHHHHH		24.1721963094
423PhosphorylationNRDLFDFSTRFITRP
CHHHHHCCCCCCCCC		22.1021712546
424PhosphorylationRDLFDFSTRFITRPA
HHHHHCCCCCCCCCC		29.5921712546
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 WDR18_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of WDR18_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 WDR18_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SENP3_HUMANSENP3physical
26186194
ISCA1_HUMANISCA1physical
26186194
NOL9_HUMANNOL9physical
26186194
TEX10_HUMANTEX10physical
26186194
ACOT2_HUMANACOT2physical
26186194
PELP1_HUMANPELP1physical
26186194
CHD8_HUMANCHD8physical
26344197
NOL9_HUMANNOL9physical
26344197
PELP1_HUMANPELP1physical
26344197
SENP3_HUMANSENP3physical
26344197
TEX10_HUMANTEX10physical
26344197
ISCA1_HUMANISCA1physical
28514442
TEX10_HUMANTEX10physical
28514442
SENP3_HUMANSENP3physical
28514442
PELP1_HUMANPELP1physical
28514442
NOL9_HUMANNOL9physical
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 WDR18_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer.";
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
Cell 131:1190-1203(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-61, AND MASSSPECTROMETRY.

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