dbPTM

CD36_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	CD36_HUMAN
UniProt AC	P16671
Protein Name	Platelet glycoprotein 4
Gene Name	CD36
Organism	Homo sapiens (Human).
Sequence Length	472
Subcellular Localization	Cell membrane Multi-pass membrane protein . Membrane raft . Golgi apparatus . Apical cell membrane . Upon ligand-binding, internalized through dynamin-dependent endocytosis.
Protein Description	Multifunctional glycoprotein that acts as receptor for a broad range of ligands. Ligands can be of proteinaceous nature like thrombospondin, fibronectin, collagen or amyloid-beta as well as of lipidic nature such as oxidized low-density lipoprotein (oxLDL), anionic phospholipids, long-chain fatty acids and bacterial diacylated lipopeptides. They are generally multivalent and can therefore engage multiple receptors simultaneously, the resulting formation of CD36 clusters initiates signal transduction and internalization of receptor-ligand complexes. The dependency on coreceptor signaling is strongly ligand specific. Cellular responses to these ligands are involved in angiogenesis, inflammatory response, fatty acid metabolism, taste and dietary fat processing in the intestine (Probable). Binds long-chain fatty acids and facilitates their transport into cells, thus participating in muscle lipid utilization, adipose energy storage, and gut fat absorption (By similarity). [PubMed: 18353783]
Protein Sequence	MGCDRNCGLIAGAVIGAVLAVFGGILMPVGDLLIQKTIKKQVVLEEGTIAFKNWVKTGTEVYRQFWIFDVQNPQEVMMNSSNIQVKQRGPYTYRVRFLAKENVTQDAEDNTVSFLQPNGAIFEPSLSVGTEADNFTVLNLAVAAASHIYQNQFVQMILNSLINKSKSSMFQVRTLRELLWGYRDPFLSLVPYPVTTTVGLFYPYNNTADGVYKVFNGKDNISKVAIIDTYKGKRNLSYWESHCDMINGTDAASFPPFVEKSQVLQFFSSDICRSIYAVFESDVNLKGIPVYRFVLPSKAFASPVENPDNYCFCTEKIISKNCTSYGVLDISKCKEGRPVYISLPHFLYASPDVSEPIDGLNPNEEEHRTYLDIEPITGFTLQFAKRLQVNLLVKPSEKIQVLKNLKRNYIVPILWLNETGTIGDEKANMFRSQVTGKINLLGLIEMILLSVGVVMFVAFMISYCACRSKTIK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
3	S-palmitoylation	-----MGCDRNCGLI -----CCCCCCHHHH	4.25	8798390
7	S-palmitoylation	-MGCDRNCGLIAGAV -CCCCCCHHHHHHHH	4.96	8798390
57	Phosphorylation	AFKNWVKTGTEVYRQ EEECCCCCCCCCEEE	39.45	21712546
62	Phosphorylation	VKTGTEVYRQFWIFD CCCCCCCEEEEEEEE	7.77	-
79	N-linked_Glycosylation	NPQEVMMNSSNIQVK CHHHEEECCCCEEEE	24.96	17660510
92	Dephosphorylation	VKQRGPYTYRVRFLA EEECCCCEEEEEEEE	14.16	16299313
92	Phosphorylation	VKQRGPYTYRVRFLA EEECCCCEEEEEEEE	14.16	22247259
102	N-linked_Glycosylation	VRFLAKENVTQDAED EEEEEECCCCCCCCC	41.24	UniProtKB CARBOHYD
134	N-linked_Glycosylation	SVGTEADNFTVLNLA CCCCCCCCCCHHHHH	41.35	UniProtKB CARBOHYD
160	Phosphorylation	FVQMILNSLINKSKS HHHHHHHHHHHCCCC	27.47	24719451
163	N-linked_Glycosylation	MILNSLINKSKSSMF HHHHHHHHCCCCCHH	48.09	UniProtKB CARBOHYD
168	Phosphorylation	LINKSKSSMFQVRTL HHHCCCCCHHHHHHH	27.61	23532336
205	N-linked_Glycosylation	VGLFYPYNNTADGVY EEEEECCCCCCCCEE	34.57	19159218
220	N-linked_Glycosylation	KVFNGKDNISKVAII EEECCCCCEEEEEEE	43.87	UniProtKB CARBOHYD
235	N-linked_Glycosylation	DTYKGKRNLSYWESH ECCCCCCCHHHHHHH	36.50	17660510
247	N-linked_Glycosylation	ESHCDMINGTDAASF HHHCCCCCCCCHHHC	40.45	17660510
268	Phosphorylation	SQVLQFFSSDICRSI HHHHHHHCHHHHHHH	28.52	22210691
276	Phosphorylation	SDICRSIYAVFESDV HHHHHHHHHHHHCCC	9.65	22210691
297	Phosphorylation	VYRFVLPSKAFASPV EEEEECCCCCCCCCC	32.24	22210691
298	Acetylation	YRFVLPSKAFASPVE EEEECCCCCCCCCCC	45.65	158665
321	N-linked_Glycosylation	TEKIISKNCTSYGVL CHHHHCCCCCEECEE	27.75	18780401
323	Phosphorylation	KIISKNCTSYGVLDI HHHCCCCCEECEEEH	34.08	-
417	N-linked_Glycosylation	IVPILWLNETGTIGD EEEEEEECCCCCCCH	32.95	16263699
464	S-palmitoylation	VAFMISYCACRSKTI HHHHHHHHHHHCCCC	1.99	8798390
466	S-palmitoylation	FMISYCACRSKTIK- HHHHHHHHHCCCCC-	4.51	8798390
468	O-linked_Glycosylation	ISYCACRSKTIK--- HHHHHHHCCCCC---	33.75	31410220
469	Ubiquitination	SYCACRSKTIK---- HHHHHHCCCCC----	34.61	PubMed
470	O-linked_Glycosylation	YCACRSKTIK----- HHHHHCCCCC-----	34.93	31410220
472	Ubiquitination	ACRSKTIK------- HHHCCCCC-------	60.56	18353783

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
92	T	Phosphorylation	Kinase	PRKCA	P17252	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
469	K	ubiquitylation	18353783
Ubiquitinated at Lys-469 and Lys-472.
472	K	ubiquitylation	18353783
Ubiquitinated at Lys-469 and Lys-472.

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 CD36_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
DHI1_HUMAN	HSD11B1	physical	9555943
LDLR_HUMAN	LDLR	physical	9555943
VLDLR_HUMAN	VLDLR	physical	9555943
FYN_HUMAN	FYN	physical	1715582
LYN_HUMAN	LYN	physical	1715582
YES_HUMAN	YES1	physical	1715582
MATK_HUMAN	MATK	physical	9171348
ITA2B_HUMAN	ITGA2B	physical	11238109
ITB3_HUMAN	ITGB3	physical	11238109
ITA6_HUMAN	ITGA6	physical	11238109
CD9_HUMAN	CD9	physical	11238109
ITB1_HUMAN	ITGB1	physical	11238109
A4_HUMAN	APP	physical	21832049
CHRD_HUMAN	CHRD	physical	21988832
OCTC_HUMAN	CROT	physical	28514442
TTMP_HUMAN	C3orf52	physical	28514442
MBOA7_HUMAN	MBOAT7	physical	28514442

Drug and Disease Associations

Kegg Disease
H01108	CD36 deficiency; Platelet glycoprotein IV deficiency
OMIM Disease
608404	Platelet glycoprotein IV deficiency (PG4D)
610938	Coronary heart disease 7 (CHDS7)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of CD36_HUMAN

Related Literatures of Post-Translational Modification

N-linked Glycosylation
Reference	PubMed
"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-205 AND ASN-417, AND MASSSPECTROMETRY.	19159218 [Abstract]
"Identification of N-linked glycoproteins in human milk by hydrophilicinteraction liquid chromatography and mass spectrometry."; Picariello G., Ferranti P., Mamone G., Roepstorff P., Addeo F.; Proteomics 8:3833-3847(2008). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-321, AND MASSSPECTROMETRY.	18780401 [Abstract]
"Elucidation of N-glycosylation sites on human platelet proteins: aglycoproteomic approach."; Lewandrowski U., Moebius J., Walter U., Sickmann A.; Mol. Cell. Proteomics 5:226-233(2006). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-417, AND MASSSPECTROMETRY.	16263699 [Abstract]
Palmitoylation
Reference	PubMed
"CD36 is palmitoylated on both N- and C-terminal cytoplasmic tails."; Tao N., Wagner S.J., Lublin D.M.; J. Biol. Chem. 271:22315-22320(1996). Cited for: PALMITOYLATION AT CYS-3; CYS-7; CYS-464 AND CYS-466.	8798390 [Abstract]

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