WDR89_HUMAN - dbPTM
WDR89_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID WDR89_HUMAN
UniProt AC Q96FK6
Protein Name WD repeat-containing protein 89
Gene Name WDR89
Organism Homo sapiens (Human).
Sequence Length 387
Subcellular Localization
Protein Description
Protein Sequence MEKIEEQFANLHIVKCSLGTKEPTYLLGIDTSKTVQAGKENLVAVLCSNGSIRIYDKERLNVLREFSGYPGLLNGVRFANSCDSVYSACTDGTVKCWDARVAREKPVQLFKGYPSNIFISFDINCNDHIICAGTEKVDDDALLVFWDARMNSQNLSTTKDSLGAYSETHSDDVTQVRFHPSNPNMVVSGSSDGLVNVFDINIDNEEDALVTTCNSISSVSCIGWSGKGYKQIYCMTHDEGFYWWDLNHLDTDEPVTRLNIQDVREVVNMKEDALDYLIGGLYHEKTDTLHVIGGTNKGRIHLMNCSMSGLTHVTSLQGGHAATVRSFCWNVQDDSLLTGGEDAQLLLWKPGAIEKTFTKKESMKIASSVHQRVRVHSNDSYKRRKKQ
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
15UbiquitinationFANLHIVKCSLGTKE
HHCCEEEECCCCCCC
19.94-
17PhosphorylationNLHIVKCSLGTKEPT
CCEEEECCCCCCCCE
24.9026074081
20PhosphorylationIVKCSLGTKEPTYLL
EEECCCCCCCCEEEE
37.2126074081
21AcetylationVKCSLGTKEPTYLLG
EECCCCCCCCEEEEE
60.9526051181
21UbiquitinationVKCSLGTKEPTYLLG
EECCCCCCCCEEEEE
60.95-
24PhosphorylationSLGTKEPTYLLGIDT
CCCCCCCEEEEEEEC
28.0826074081
25PhosphorylationLGTKEPTYLLGIDTS
CCCCCCEEEEEEECC
15.6226074081
31PhosphorylationTYLLGIDTSKTVQAG
EEEEEEECCCCCCCC
30.1526074081
32PhosphorylationYLLGIDTSKTVQAGK
EEEEEECCCCCCCCC
23.6826074081
33UbiquitinationLLGIDTSKTVQAGKE
EEEEECCCCCCCCCC
55.60-
34PhosphorylationLGIDTSKTVQAGKEN
EEEECCCCCCCCCCC
20.0226074081
39AcetylationSKTVQAGKENLVAVL
CCCCCCCCCCEEEEE
46.5826051181
67PhosphorylationLNVLREFSGYPGLLN
HHHHHHHCCCCCHHC
32.4422817900
69PhosphorylationVLREFSGYPGLLNGV
HHHHHCCCCCHHCCE
7.9122817900
95AcetylationACTDGTVKCWDARVA
HCCCCCCCEECCHHH
29.4626051181
95UbiquitinationACTDGTVKCWDARVA
HCCCCCCCEECCHHH
29.46-
105UbiquitinationDARVAREKPVQLFKG
CCHHHCCCCEEEECC
44.96-
156PhosphorylationRMNSQNLSTTKDSLG
CCCCCCCCCCHHHCC
41.3922817900
157PhosphorylationMNSQNLSTTKDSLGA
CCCCCCCCCHHHCCC
40.82-
158PhosphorylationNSQNLSTTKDSLGAY
CCCCCCCCHHHCCCC
29.49-
159UbiquitinationSQNLSTTKDSLGAYS
CCCCCCCHHHCCCCC
45.4621906983
161PhosphorylationNLSTTKDSLGAYSET
CCCCCHHHCCCCCCC
30.2018452278
166PhosphorylationKDSLGAYSETHSDDV
HHHCCCCCCCCCCCC
35.1718452278
256PhosphorylationLDTDEPVTRLNIQDV
CCCCCCCEECCHHHH
39.91-
270UbiquitinationVREVVNMKEDALDYL
HHHHHCCCHHHHHHH
47.4321906983
285UbiquitinationIGGLYHEKTDTLHVI
HHHCCCCCCCEEEEE
38.09-
297UbiquitinationHVIGGTNKGRIHLMN
EEECCCCCCCEEEEE
49.78-
356PhosphorylationKPGAIEKTFTKKESM
CCCCEEEEECHHHHH
24.60-
358PhosphorylationGAIEKTFTKKESMKI
CCEEEEECHHHHHHH
46.57-
362PhosphorylationKTFTKKESMKIASSV
EEECHHHHHHHHHHH
33.97-
364MethylationFTKKESMKIASSVHQ
ECHHHHHHHHHHHHH
44.38115978601
377PhosphorylationHQRVRVHSNDSYKRR
HHHHCCCCCCHHHHH
39.2028258704
380PhosphorylationVRVHSNDSYKRRKKQ
HCCCCCCHHHHHCCC
36.4827282143
381PhosphorylationRVHSNDSYKRRKKQ-
CCCCCCHHHHHCCC-
16.0428258704

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 WDR89_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of WDR89_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 WDR89_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049

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 WDR89_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-67 AND TYR-69, AND MASSSPECTROMETRY.

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