dbPTM

CD82_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	CD82_HUMAN
UniProt AC	P27701
Protein Name	CD82 antigen
Gene Name	CD82
Organism	Homo sapiens (Human).
Sequence Length	267
Subcellular Localization	Membrane Multi-pass membrane protein.
Protein Description	Associates with CD4 or CD8 and delivers costimulatory signals for the TCR/CD3 pathway..
Protein Sequence	MGSACIKVTKYFLFLFNLIFFILGAVILGFGVWILADKSSFISVLQTSSSSLRMGAYVFIGVGAVTMLMGFLGCIGAVNEVRCLLGLYFAFLLLILIAQVTAGALFYFNMGKLKQEMGGIVTELIRDYNSSREDSLQDAWDYVQAQVKCCGWVSFYNWTDNAELMNRPEVTYPCSCEVKGEEDNSLSVRKGFCEAPGNRTQSGNHPEDWPVYQEGCMEKVQAWLQENLGIILGVGVGVAIIELLGMVLSICLCRHVHSEDYSKVPKY

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
5	S-palmitoylation	---MGSACIKVTKYF ---CCCHHHHHHHHH	3.11	15492270
74	S-palmitoylation	MLMGFLGCIGAVNEV HHHHHHHHHHHHHHH	2.56	15492270
81	Ubiquitination	CIGAVNEVRCLLGLY HHHHHHHHHHHHHHH	4.40	22817900
83	S-palmitoylation	GAVNEVRCLLGLYFA HHHHHHHHHHHHHHH	4.43	15492270
83	Ubiquitination	GAVNEVRCLLGLYFA HHHHHHHHHHHHHHH	4.43	22817900
112	Ubiquitination	LFYFNMGKLKQEMGG HHHCCHHHHHHHHHH	41.56	22817900
114	Ubiquitination	YFNMGKLKQEMGGIV HCCHHHHHHHHHHHH	47.93	22817900
129	N-linked_Glycosylation	TELIRDYNSSREDSL HHHHHHHCCCCCCHH	37.49	19159218
129	N-linked_Glycosylation	TELIRDYNSSREDSL HHHHHHHCCCCCCHH	37.49	19349973
157	N-linked_Glycosylation	CGWVSFYNWTDNAEL CCEEEECCCCCCHHH	32.91	UniProtKB CARBOHYD
157	N-linked_Glycosylation	CGWVSFYNWTDNAEL CCEEEECCCCCCHHH	32.91	11162423
159	Ubiquitination	WVSFYNWTDNAELMN EEEECCCCCCHHHCC	18.75	22505724
165	Ubiquitination	WTDNAELMNRPEVTY CCCCHHHCCCCCCEE	2.77	22505724
187	Phosphorylation	GEEDNSLSVRKGFCE CCCCCCEEEEECCEE	21.50	24719451
190	Ubiquitination	DNSLSVRKGFCEAPG CCCEEEEECCEECCC	54.93	22505724
198	N-linked_Glycosylation	GFCEAPGNRTQSGNH CCEECCCCCCCCCCC	42.65	11162423
198	N-linked_Glycosylation	GFCEAPGNRTQSGNH CCEECCCCCCCCCCC	42.65	17660510
226	S-palmitoylation	KVQAWLQENLGIILG HHHHHHHHCCCHHHC	52.86	15492270
228	S-palmitoylation	QAWLQENLGIILGVG HHHHHHCCCHHHCHH	5.26	15492270
251	S-palmitoylation	LGMVLSICLCRHVHS HHHHHHHHHHHHHCC	2.36	15492270
253	S-palmitoylation	MVLSICLCRHVHSED HHHHHHHHHHHCCCC	2.16	15492270
258	Phosphorylation	CLCRHVHSEDYSKVP HHHHHHCCCCCCCCC	30.95	28796482
261	Phosphorylation	RHVHSEDYSKVPKY- HHHCCCCCCCCCCC-	13.31	28796482
262	Phosphorylation	HVHSEDYSKVPKY-- HHCCCCCCCCCCC--	39.23	28796482
267	Phosphorylation	DYSKVPKY------- CCCCCCCC-------	20.09	19060867

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
-	K	Ubiquitination	E3 ubiquitin ligase	AMFR	Q9UKV5	PMID:18037895

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of CD82_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 CD82_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CD151_HUMAN	CD151	physical	15492270
CD9_HUMAN	CD9	physical	15492270
ERBB2_HUMAN	ERBB2	physical	14576349
ERBB3_HUMAN	ERBB3	physical	14576349
MCP_HUMAN	CD46	physical	10741407
CD63_HUMAN	CD63	physical	9759843
DRA_HUMAN	HLA-DRA	physical	9759843
DMB_HUMAN	HLA-DMB	physical	9759843
DOB_HUMAN	HLA-DOB	physical	9759843
HBEGF_HUMAN	HBEGF	physical	10749879
ITAL_HUMAN	ITGAL	physical	10602019
EGFR_HUMAN	EGFR	physical	10985391
AMFR_HUMAN	AMFR	physical	18037895
GGT1_HUMAN	GGT1	physical	9862348
CD81_HUMAN	CD81	physical	9862348

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 CD82_HUMAN

Related Literatures of Post-Translational Modification

N-linked Glycosylation
Reference	PubMed
"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."; Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,Schiess R., Aebersold R., Watts J.D.; Nat. Biotechnol. 27:378-386(2009). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-129 AND ASN-198, AND MASSSPECTROMETRY.	19349973 [Abstract]
"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-129, AND MASSSPECTROMETRY.	19159218 [Abstract]