PDCL3_HUMAN - dbPTM
PDCL3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PDCL3_HUMAN
UniProt AC Q9H2J4
Protein Name Phosducin-like protein 3
Gene Name PDCL3
Organism Homo sapiens (Human).
Sequence Length 239
Subcellular Localization Cytoplasm .
Protein Description Acts as a chaperone for the angiogenic VEGF receptor KDR/VEGFR2, controlling its abundance and inhibiting its ubiquitination and degradation. Modulates the activation of caspases during apoptosis. Is a substrate for Orgyia pseudotsugata multicapsid polyhedrosis virus (OpMNPV) IAP-mediated ubiquitination..
Protein Sequence MQDPNADTEWNDILRKKGILPPKESLKELEEEAEEEQRILQQSVVKTYEDMTLEELEDHEDEFNEEDERAIEMYRRRRLAEWKATKLKNKFGEVLEISGKDYVQEVTKAGEGLWVILHLYKQGIPLCALINQHLSGLARKFPDVKFIKAISTTCIPNYPDRNLPTIFVYLEGDIKAQFIGPLVFGGMNLTRDELEWKLSESGAIMTDLEENPKKPIEDVLLSSVRRSVLMKRDSDSEGD
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
1Acetylation-------MQDPNADT
-------CCCCCCCC
10.3326059764
17UbiquitinationWNDILRKKGILPPKE
HHHHHHHCCCCCCHH
44.7624816145
25PhosphorylationGILPPKESLKELEEE
CCCCCHHHHHHHHHH
51.3624719451
27UbiquitinationLPPKESLKELEEEAE
CCCHHHHHHHHHHHH
70.3232015554
33PhosphorylationLKELEEEAEEEQRIL
HHHHHHHHHHHHHHH
32.5532645325
40UbiquitinationAEEEQRILQQSVVKT
HHHHHHHHHHHHHHH
4.0621890473
43PhosphorylationEQRILQQSVVKTYED
HHHHHHHHHHHHHHC
18.8625159151
47PhosphorylationLQQSVVKTYEDMTLE
HHHHHHHHHHCCCHH
22.1228796482
48PhosphorylationQQSVVKTYEDMTLEE
HHHHHHHHHCCCHHH
12.2928796482
52PhosphorylationVKTYEDMTLEELEDH
HHHHHCCCHHHHHHC
43.2529978859
83UbiquitinationRRRLAEWKATKLKNK
HHHHHHHHHHHHHHH
37.3732015554
90AcetylationKATKLKNKFGEVLEI
HHHHHHHHHCCEEEE
53.8327452117
90UbiquitinationKATKLKNKFGEVLEI
HHHHHHHHHCCEEEE
53.8321890473
205SulfoxidationLSESGAIMTDLEENP
HCCCCCCCCCCHHCC
2.0621406390
206PhosphorylationSESGAIMTDLEENPK
CCCCCCCCCCHHCCC
31.18-
222PhosphorylationPIEDVLLSSVRRSVL
CHHHHHHHHHHHHHH
23.7224719451
223PhosphorylationIEDVLLSSVRRSVLM
HHHHHHHHHHHHHHH
21.4428857561
227PhosphorylationLLSSVRRSVLMKRDS
HHHHHHHHHHHCCCC
14.7223403867
231AcetylationVRRSVLMKRDSDSEG
HHHHHHHCCCCCCCC
49.2230591189
234PhosphorylationSVLMKRDSDSEGD--
HHHHCCCCCCCCC--
47.2528355574
236PhosphorylationLMKRDSDSEGD----
HHCCCCCCCCC----
47.6423927012

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 PDCL3_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PDCL3_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 PDCL3_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TCPG_HUMANCCT3physical
26344197
TCPZ_HUMANCCT6Aphysical
26344197
TCPH_HUMANCCT7physical
26344197
TCPQ_HUMANCCT8physical
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 PDCL3_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
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-43; SER-234 AND SER-236,AND MASS SPECTROMETRY.
"Global phosphoproteome of HT-29 human colon adenocarcinoma cells.";
Kim J.-E., Tannenbaum S.R., White F.M.;
J. Proteome Res. 4:1339-1346(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-234 AND SER-236, ANDMASS SPECTROMETRY.

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