dbPTM

CD83_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	CD83_HUMAN
UniProt AC	Q01151
Protein Name	CD83 antigen
Gene Name	CD83
Organism	Homo sapiens (Human).
Sequence Length	205
Subcellular Localization	Membrane Single-pass type I membrane protein.
Protein Description	May play a significant role in antigen presentation or the cellular interactions that follow lymphocyte activation..
Protein Sequence	MSRGLQLLLLSCAYSLAPATPEVKVACSEDVDLPCTAPWDPQVPYTVSWVKLLEGGEERMETPQEDHLRGQHYHQKGQNGSFDAPNERPYSLKIRNTTSCNSGTYRCTLQDPDGQRNLSGKVILRVTGCPAQRKEETFKKYRAEIVLLLALVIFYLTLIIFTCKFARLQSIFPDFSKAGMERAFLPVTSPNKHLGLVTPHKTELV

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
76	Ubiquitination	RGQHYHQKGQNGSFD CCCCCCCCCCCCCCC	49.50	-
79	N-linked_Glycosylation	HYHQKGQNGSFDAPN CCCCCCCCCCCCCCC	57.66	19349973
79	N-linked_Glycosylation	HYHQKGQNGSFDAPN CCCCCCCCCCCCCCC	57.66	19349973
81	Phosphorylation	HQKGQNGSFDAPNER CCCCCCCCCCCCCCC	27.74	29978859
86	N-linked_Glycosylation	NGSFDAPNERPYSLK CCCCCCCCCCCCEEE	60.68	19349973
86	N-linked_Glycosylation	NGSFDAPNERPYSLK CCCCCCCCCCCCEEE	60.68	19349973
90	Phosphorylation	DAPNERPYSLKIRNT CCCCCCCCEEEEECC	32.62	29978859
91	Phosphorylation	APNERPYSLKIRNTT CCCCCCCEEEEECCC	26.35	24719451
96	N-linked_Glycosylation	PYSLKIRNTTSCNSG CCEEEEECCCCCCCC	51.70	UniProtKB CARBOHYD
97	Phosphorylation	YSLKIRNTTSCNSGT CEEEEECCCCCCCCE	15.38	30576142
99	Phosphorylation	LKIRNTTSCNSGTYR EEEECCCCCCCCEEE	14.84	-
104	Phosphorylation	TTSCNSGTYRCTLQD CCCCCCCEEEEEEEC	13.96	30576142
105	Phosphorylation	TSCNSGTYRCTLQDP CCCCCCEEEEEEECC	13.76	-
117	N-linked_Glycosylation	QDPDGQRNLSGKVIL ECCCCCCCCCCCEEE	30.58	UniProtKB CARBOHYD
177	Ubiquitination	SIFPDFSKAGMERAF HHCCCHHHHCHHCCC	49.29	-
188	Phosphorylation	ERAFLPVTSPNKHLG HCCCCCCCCCCCCCC	36.20	22167270
189	Phosphorylation	RAFLPVTSPNKHLGL CCCCCCCCCCCCCCC	27.06	22167270
192	Ubiquitination	LPVTSPNKHLGLVTP CCCCCCCCCCCCCCC	43.52	-
198	Phosphorylation	NKHLGLVTPHKTELV CCCCCCCCCCCCCCC	25.39	18669648
201	Ubiquitination	LGLVTPHKTELV--- CCCCCCCCCCCC---	44.92	-

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	RNF128	Q8TEB7	PMID:19542455

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of CD83_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 CD83_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
IF4E_HUMAN	EIF4E	physical	21988832
ZNT1_HUMAN	SLC30A1	physical	28514442
NDST1_HUMAN	NDST1	physical	28514442
CTR2_HUMAN	SLC7A2	physical	28514442
CEGT_HUMAN	UGCG	physical	28514442
ATP7A_HUMAN	ATP7A	physical	28514442
CA112_HUMAN	C1orf112	physical	28514442
RADIL_HUMAN	RADIL	physical	28514442
CERS5_HUMAN	CERS5	physical	28514442
BMPR2_HUMAN	BMPR2	physical	28514442
UBP8_HUMAN	USP8	physical	28514442
PTPRD_HUMAN	PTPRD	physical	28514442
XPO6_HUMAN	XPO6	physical	28514442
AT2B2_HUMAN	ATP2B2	physical	28514442
RHBT3_HUMAN	RHOBTB3	physical	28514442
STAG1_HUMAN	STAG1	physical	28514442
CERK1_HUMAN	CERK	physical	28514442
TSC2_HUMAN	TSC2	physical	28514442
CIP2A_HUMAN	KIAA1524	physical	28514442
MTOR_HUMAN	MTOR	physical	28514442
DAB2P_HUMAN	DAB2IP	physical	28514442
TM192_HUMAN	TMEM192	physical	28514442
GRK6_HUMAN	GRK6	physical	28514442
TBRG4_HUMAN	TBRG4	physical	28514442
BMR1A_HUMAN	BMPR1A	physical	28514442
ZNT5_HUMAN	SLC30A5	physical	28514442
STEA3_HUMAN	STEAP3	physical	28514442
PIGA_HUMAN	PIGA	physical	28514442
MYADM_HUMAN	MYADM	physical	28514442
FGFR2_HUMAN	FGFR2	physical	28514442
VANG1_HUMAN	VANGL1	physical	28514442
BTAF1_HUMAN	BTAF1	physical	28514442
ZDH13_HUMAN	ZDHHC13	physical	28514442
CD320_HUMAN	CD320	physical	28514442
UBP32_HUMAN	USP32	physical	28514442
THADA_HUMAN	THADA	physical	28514442
HEAT3_HUMAN	HEATR3	physical	28514442
PDS5A_HUMAN	PDS5A	physical	28514442
NFIP1_HUMAN	NDFIP1	physical	28514442
STAG2_HUMAN	STAG2	physical	28514442
TNPO2_HUMAN	TNPO2	physical	28514442
RN128_HUMAN	RNF128	physical	19542455

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 CD83_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-79 AND ASN-86, AND MASSSPECTROMETRY.	19349973 [Abstract]