SDCG3_HUMAN - dbPTM
SDCG3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SDCG3_HUMAN
UniProt AC Q96C92
Protein Name Serologically defined colon cancer antigen 3
Gene Name SDCCAG3
Organism Homo sapiens (Human).
Sequence Length 435
Subcellular Localization Cytoplasm . Midbody . Early endosome . Recycling endosome . During cytokinesis colocalized with PTPN13 at the midbody (PubMed:23108400). Colocalizes in a WASHC2-dependent manner with the retromer CSC complex at endosomes (PubMed:25278552).
Protein Description May be involved in modulation of TNF response. May be involved in presentation of TNFRSF1A on the cell surface (By similarity). Involved in the endosome-to-plasma membrane trafficking and recycling of SNX27-retromer-dependent cargo proteins, such as GLUT1. [PubMed: 25278552 Involved in the regulation of cytokinesis; the function may involve PTPN13 and GIT1]
Protein Sequence MSGYQRRPGATPLSRARSLAIPDAPAFYERRSCLPQLNCERPHGRDLDSPFFGIRPAFMCYVPSPVLASVGDTDFGYGKGKCSKQSPSGAHGTHFGDDRFEDLEEANPFSFREFLKTKNLGLSKEDPASRIYAKEASRHSLGLDHNSPPSQTGGYGLEYQQPFFEDPTGAGDLLDEEEDEDTGWSGAYLPSAIEQTHPERVPAGTSPCSTYLSFFSTPSELAGPESLPSWALSDTDSRVSPASPAGSPSADFAVHGESLGDRHLRTLQISYDALKDENSKLRRKLNEVQSFSEAQTEMVRTLERKLEAKMIKEESDYHDLESVVQQVEQNLELMTKRAVKAENHVVKLKQEISLLQAQVSNFQRENEALRCGQGASLTVVKQNADVALQNLRVVMNSAQASIKQLVSGAETLNLVAEILKSIDRISEVKDEEEDS
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
66 (in isoform 3)Ubiquitination-9.0521890473
101 (in isoform 2)Ubiquitination-63.6821890473
124 (in isoform 1)Ubiquitination-71.7921890473
222 (in isoform 3)Ubiquitination-27.6921890473
257 (in isoform 2)Ubiquitination-28.1021890473
280 (in isoform 1)Ubiquitination-58.5621890473
291 (in isoform 3)Ubiquitination-4.2321890473
326 (in isoform 2)Ubiquitination-29.1621890473
349 (in isoform 1)Ubiquitination-39.9221890473
371 (in isoform 3)Ubiquitination-5.0621890473
406 (in isoform 2)Ubiquitination-4.6121890473
429 (in isoform 1)Ubiquitination-56.2021890473

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 SDCG3_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SDCG3_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 SDCG3_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CHD3_HUMANCHD3physical
16169070
GIT1_HUMANGIT1physical
16169070
VIME_HUMANVIMphysical
16169070
A4_HUMANAPPphysical
21832049
TFPT_HUMANTFPTphysical
25416956
AP1M1_HUMANAP1M1physical
21516116

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 SDCG3_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-243 AND SER-247, ANDMASS SPECTROMETRY.
"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-243 AND SER-247, ANDMASS SPECTROMETRY.

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