C43BP_HUMAN - dbPTM
C43BP_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID C43BP_HUMAN
UniProt AC Q9Y5P4
Protein Name Collagen type IV alpha-3-binding protein
Gene Name COL4A3BP
Organism Homo sapiens (Human).
Sequence Length 624
Subcellular Localization Cytoplasm . Golgi apparatus . Endoplasmic reticulum . Preferentially localized to the Golgi apparatus.
Protein Description Shelters ceramides and diacylglycerol lipids inside its START domain and mediates the intracellular trafficking of ceramides and diacylglycerol lipids in a non-vesicular manner..
Protein Sequence MSDNQSWNSSGSEEDPETESGPPVERCGVLSKWTNYIHGWQDRWVVLKNNALSYYKSEDETEYGCRGSICLSKAVITPHDFDECRFDISVNDSVWYLRAQDPDHRQQWIDAIEQHKTESGYGSESSLRRHGSMVSLVSGASGYSATSTSSFKKGHSLREKLAEMETFRDILCRQVDTLQKYFDACADAVSKDELQRDKVVEDDEDDFPTTRSDGDFLHSTNGNKEKLFPHVTPKGINGIDFKGEAITFKATTAGILATLSHCIELMVKREDSWQKRLDKETEKKRRTEEAYKNAMTELKKKSHFGGPDYEEGPNSLINEEEFFDAVEAALDRQDKIEEQSQSEKVRLHWPTSLPSGDAFSSVGTHRFVQKPYSRSSSMSSIDLVSASDDVHRFSSQVEEMVQNHMTYSLQDVGGDANWQLVVEEGEMKVYRREVEENGIVLDPLKATHAVKGVTGHEVCNYFWNVDVRNDWETTIENFHVVETLADNAIIIYQTHKRVWPASQRDVLYLSVIRKIPALTENDPETWIVCNFSVDHDSAPLNNRCVRAKINVAMICQTLVSPPEGNQEISRDNILCKITYVANVNPGGWAPASVLRAVAKREYPKFLKRFTSYVQEKTAGKPILF
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
59 (in isoform 3)Phosphorylation-75.1820873877
73MalonylationRGSICLSKAVITPHD
CCEEEEECEEECCCC
33.4526320211
73AcetylationRGSICLSKAVITPHD
CCEEEEECEEECCCC
33.4525953088
119 (in isoform 2)Phosphorylation-42.41-
126 (in isoform 2)Phosphorylation-23.11-
132 (in isoform 2)Phosphorylation-15.19-
150 (in isoform 2)Phosphorylation-40.97-
160AcetylationKGHSLREKLAEMETF
CCCCHHHHHHCHHHH
46.7125953088
191AcetylationACADAVSKDELQRDK
HHHHHCCHHHHHHCC
48.9326822725
251 (in isoform 3)Phosphorylation-20.1227251275
254 (in isoform 3)Phosphorylation-17.2227251275
260 (in isoform 3)Phosphorylation-16.3827251275
263 (in isoform 3)Phosphorylation-3.6927251275
269 (in isoform 3)Phosphorylation-41.3627251275
272 (in isoform 3)Phosphorylation-27.0127251275
275 (in isoform 3)Phosphorylation-48.9827251275
315 (in isoform 2)Phosphorylation-33.49-
344 (in isoform 2)Ubiquitination-37.5921906983
344 (in isoform 1)Ubiquitination-37.5921906983
360 (in isoform 3)Phosphorylation-26.3227251275
437 (in isoform 3)Phosphorylation-31.8027642862
501 (in isoform 3)Phosphorylation-11.5527251275
503 (in isoform 3)Phosphorylation-47.9327251275
504 (in isoform 3)Phosphorylation-33.2527251275
505 (in isoform 3)Phosphorylation-27.4327251275
507 (in isoform 3)Phosphorylation-4.1127251275
738 (in isoform 3)Phosphorylation-27251275

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
132SPhosphorylationKinaseCSNK1G2P78368
GPS
132SPhosphorylationKinasePRKD1Q15139
PSP
132SPhosphorylationKinasePKD-Uniprot

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of C43BP_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 C43BP_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
C43BP_HUMANCOL4A3BPphysical
16189514
RTN3_HUMANRTN3physical
16189514
CENPR_HUMANITGB3BPphysical
16189514
RTN4_HUMANRTN4physical
16189514
CBS_HUMANCBSphysical
19447967
TGM2_HUMANTGM2physical
21988832
PACN2_HUMANPACSIN2physical
22863883
2A5G_HUMANPPP2R5Cphysical
22863883
C43BP_HUMANCOL4A3BPphysical
25416956
AR6P1_HUMANARL6IP1physical
25416956
CENPR_HUMANITGB3BPphysical
25416956
ACTL8_HUMANACTL8physical
25416956
RBP2_HUMANRANBP2physical
26344197
MARK1_HUMANMARK1physical
28514442
MARK2_HUMANMARK2physical
28514442
MARK3_HUMANMARK3physical
28514442
TRAF7_HUMANTRAF7physical
28514442

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
616351Mental retardation, autosomal dominant 34 (MRD34)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of C43BP_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-380, AND MASSSPECTROMETRY.
"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-377, AND MASSSPECTROMETRY.
"Regulation of secretory transport by protein kinase D-mediatedphosphorylation of the ceramide transfer protein.";
Fugmann T., Hausser A., Schoeffler P., Schmid S., Pfizenmaier K.,Olayioye M.A.;
J. Cell Biol. 178:15-22(2007).
Cited for: PHOSPHORYLATION AT SER-132, FUNCTION, AND MUTAGENESIS OF SER-132.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-315, AND MASSSPECTROMETRY.

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