CD63_HUMAN - dbPTM
CD63_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CD63_HUMAN
UniProt AC P08962
Protein Name CD63 antigen
Gene Name CD63
Organism Homo sapiens (Human).
Sequence Length 238
Subcellular Localization Cell membrane
Multi-pass membrane protein . Lysosome membrane
Multi-pass membrane protein . Late endosome membrane
Multi-pass membrane protein . Endosome, multivesicular body . Melanosome . Secreted, exosome . Cell surface . Also found in Weibe
Protein Description Functions as cell surface receptor for TIMP1 and plays a role in the activation of cellular signaling cascades. Plays a role in the activation of ITGB1 and integrin signaling, leading to the activation of AKT, FAK/PTK2 and MAP kinases. Promotes cell survival, reorganization of the actin cytoskeleton, cell adhesion, spreading and migration, via its role in the activation of AKT and FAK/PTK2. Plays a role in VEGFA signaling via its role in regulating the internalization of KDR/VEGFR2. Plays a role in intracellular vesicular transport processes, and is required for normal trafficking of the PMEL luminal domain that is essential for the development and maturation of melanocytes. Plays a role in the adhesion of leukocytes onto endothelial cells via its role in the regulation of SELP trafficking. May play a role in mast cell degranulation in response to Ms4a2/FceRI stimulation, but not in mast cell degranulation in response to other stimuli..
Protein Sequence MAVEGGMKCVKFLLYVLLLAFCACAVGLIAVGVGAQLVLSQTIIQGATPGSLLPVVIIAVGVFLFLVAFVGCCGACKENYCLMITFAIFLSLIMLVEVAAAIAGYVFRDKVMSEFNNNFRQQMENYPKNNHTASILDRMQADFKCCGAANYTDWEKIPSMSKNRVPDSCCINVTVGCGINFNEKAIHKEGCVEKIGGWLRKNVLVVAAAALGIAFVEVLGIVFACCLVKSIRSGYEVM
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
87UbiquitinationYCLMITFAIFLSLIM
HHHHHHHHHHHHHHH
5.2921890473
105UbiquitinationVAAAIAGYVFRDKVM
HHHHHHHHHHHHHHH
6.3321890473
1102-HydroxyisobutyrylationAGYVFRDKVMSEFNN
HHHHHHHHHHHHHHH
35.26-
110UbiquitinationAGYVFRDKVMSEFNN
HHHHHHHHHHHHHHH
35.2621890473
113PhosphorylationVFRDKVMSEFNNNFR
HHHHHHHHHHHHHHH
41.8628060719
128UbiquitinationQQMENYPKNNHTASI
HHHHHCCCCCCHHHH
61.0821890473
130N-linked_GlycosylationMENYPKNNHTASILD
HHHCCCCCCHHHHHH
39.7612754519
139UbiquitinationTASILDRMQADFKCC
HHHHHHHHHHHHCCC
3.7321890473
146S-palmitoylationMQADFKCCGAANYTD
HHHHHCCCCCCCCCC
4.2429575903
150N-linked_GlycosylationFKCCGAANYTDWEKI
HCCCCCCCCCCHHHC
39.4417660510
152PhosphorylationCCGAANYTDWEKIPS
CCCCCCCCCHHHCCC
34.1529759185
159PhosphorylationTDWEKIPSMSKNRVP
CCHHHCCCCCCCCCC
38.8821406692
161PhosphorylationWEKIPSMSKNRVPDS
HHHCCCCCCCCCCCC
30.9921406692
162UbiquitinationEKIPSMSKNRVPDSC
HHCCCCCCCCCCCCC
39.8821890473
169S-palmitoylationKNRVPDSCCINVTVG
CCCCCCCCEEEEEEC
3.3529575903
170S-palmitoylationNRVPDSCCINVTVGC
CCCCCCCEEEEEECC
2.6929575903
172N-linked_GlycosylationVPDSCCINVTVGCGI
CCCCCEEEEEECCCC
14.9717660510
177S-palmitoylationCINVTVGCGINFNEK
EEEEEECCCCCCCCH
4.2629575903
1882-HydroxyisobutyrylationFNEKAIHKEGCVEKI
CCCHHHCCCCCHHHH
50.08-
188UbiquitinationFNEKAIHKEGCVEKI
CCCHHHCCCCCHHHH
50.08-
194UbiquitinationHKEGCVEKIGGWLRK
CCCCCHHHHCHHHHH
26.67-

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 CD63_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CD63_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 CD63_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
KIT_HUMANKITphysical
12036870
CD9_HUMANCD9physical
8630057
FPRP_HUMANPTGFRNphysical
11278880
ITB1_HUMANITGB1physical
12175627
DRA_HUMANHLA-DRAphysical
9759843
CD82_HUMANCD82physical
9759843
DMB_HUMANHLA-DMBphysical
9759843
DOB_HUMANHLA-DOBphysical
9759843
GAG_HV1H2gagphysical
10708443
CD81_HUMANCD81physical
16533950
ENV_HV1H2envphysical
10708443
SDC1_HUMANSDC1physical
22660413
SDCB1_HUMANSDCBPphysical
22660413

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 CD63_HUMAN

loading...

Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry.";
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
J. Proteome Res. 8:651-661(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-130, AND MASSSPECTROMETRY.
"Identification and quantification of N-linked glycoproteins usinghydrazide chemistry, stable isotope labeling and mass spectrometry.";
Zhang H., Li X.-J., Martin D.B., Aebersold R.;
Nat. Biotechnol. 21:660-666(2003).
Cited for: GLYCOSYLATION AT ASN-130.

TOP