dbPTM

GPC1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	GPC1_HUMAN
UniProt AC	P35052
Protein Name	Glypican-1
Gene Name	GPC1
Organism	Homo sapiens (Human).
Sequence Length	558
Subcellular Localization	Cell membrane Lipid-anchor, GPI-anchor Extracellular side. Endosome. S-nitrosylated form recycled in endosomes. Localizes to CAV1-containing vesicles close to the cell surface. Cleavage of heparan sulfate side chains takes place mainly in late endo
Protein Description	Cell surface proteoglycan that bears heparan sulfate. Binds, via the heparan sulfate side chains, alpha-4 (V) collagen and participates in Schwann cell myelination (By similarity). May act as a catalyst in increasing the rate of conversion of prion protein PRPN(C) to PRNP(Sc) via associating (via the heparan sulfate side chains) with both forms of PRPN, targeting them to lipid rafts and facilitating their interaction. Required for proper skeletal muscle differentiation by sequestering FGF2 in lipid rafts preventing its binding to receptors (FGFRs) and inhibiting the FGF-mediated signaling..
Protein Sequence	MELRARGWWLLCAAAALVACARGDPASKSRSCGEVRQIYGAKGFSLSDVPQAEISGEHLRICPQGYTCCTSEMEENLANRSHAELETALRDSSRVLQAMLATQLRSFDDHFQHLLNDSERTLQATFPGAFGELYTQNARAFRDLYSELRLYYRGANLHLEETLAEFWARLLERLFKQLHPQLLLPDDYLDCLGKQAEALRPFGEAPRELRLRATRAFVAARSFVQGLGVASDVVRKVAQVPLGPECSRAVMKLVYCAHCLGVPGARPCPDYCRNVLKGCLANQADLDAEWRNLLDSMVLITDKFWGTSGVESVIGSVHTWLAEAINALQDNRDTLTAKVIQGCGNPKVNPQGPGPEEKRRRGKLAPRERPPSGTLEKLVSEAKAQLRDVQDFWISLPGTLCSEKMALSTASDDRCWNGMARGRYLPEVMGDGLANQINNPEVEVDITKPDMTIRQQIMQLKIMTNRLRSAYNGNDVDFQDASDDGSGSGSGDGCLDDLCSRKVSRKSSSSRTPLTHALPGLSEQEGQKTSAASCPQPPTFLLPLLLFLALTVARPRWR

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
29	Phosphorylation	RGDPASKSRSCGEVR HCCCCCCCCCHHHHH	27.25	-
39	Phosphorylation	CGEVRQIYGAKGFSL HHHHHHHHCCCCCCH	11.59	-
79	N-linked_Glycosylation	EMEENLANRSHAELE HHHHHHHCCCHHHHH	49.51	22351761
116	N-linked_Glycosylation	DHFQHLLNDSERTLQ HHHHHHHCCHHHHHH	58.06	22351761
145	Phosphorylation	ARAFRDLYSELRLYY HHHHHHHHHHHHHHH	12.37	-
222	Phosphorylation	RAFVAARSFVQGLGV HHHHHHHHHHHHHCC	25.66	22210691
247	Phosphorylation	VPLGPECSRAVMKLV CCCCHHHHHHHHHHH	22.93	22210691
372	Phosphorylation	APRERPPSGTLEKLV CCCCCCCCCHHHHHH	47.28	-
409	O-linked_Glycosylation	SEKMALSTASDDRCW CHHHHHCCCCCCCCC	30.91	OGP
447	Phosphorylation	PEVEVDITKPDMTIR CCCEEECCCCCCCHH	31.87	27251275
452	Phosphorylation	DITKPDMTIRQQIMQ ECCCCCCCHHHHHHH	22.01	27251275
461	Acetylation	RQQIMQLKIMTNRLR HHHHHHHHHHHHHHH	17.34	24468093
486	O-linked_Glycosylation	QDASDDGSGSGSGDG CCCCCCCCCCCCCCC	36.46	-
488	O-linked_Glycosylation	ASDDGSGSGSGDGCL CCCCCCCCCCCCCHH	31.33	-
490	O-linked_Glycosylation	DDGSGSGSGDGCLDD CCCCCCCCCCCHHHH	35.09	-
512	O-linked_Glycosylation	RKSSSSRTPLTHALP CCCCCCCCCCCHHCC	25.29	55834061
515	O-linked_Glycosylation	SSSRTPLTHALPGLS CCCCCCCCHHCCCCC	13.30	55834067
530	GPI-anchor	EQEGQKTSAASCPQP CCCCCCCCHHHCCCC	28.95	2148568

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 GPC1_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of GPC1_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 GPC1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
UBP3_HUMAN	USP3	physical	28514442
FANCE_HUMAN	FANCE	physical	28514442
AT2B4_HUMAN	ATP2B4	physical	28514442
TM245_HUMAN	TMEM245	physical	28514442
XYLT2_HUMAN	XYLT2	physical	28514442
TM214_HUMAN	TMEM214	physical	28514442
SPCS2_HUMAN	SPCS2	physical	28514442
SC11A_HUMAN	SEC11A	physical	28514442

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 GPC1_HUMAN

Related Literatures of Post-Translational Modification

N-linked Glycosylation
Reference	PubMed
"Crystal structure of N-glycosylated human glypican-1 core protein:Structure of two loops evolutionarily conserved in vertebrateglypican-1."; Svensson G., Awad W., Hakansson M., Mani K., Logan D.T.; J. Biol. Chem. 287:14040-14051(2012). Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), DISULFIDE BONDS, LACK OFGLYCOSYLATION AT SER-55, AND GLYCOSYLATION AT ASN-79 AND ASN-116.	22351761 [Abstract]
"The structural role of N-linked glycans on human glypican-1."; Svensson G., Hyrenius Wittsten A., Linse S., Mani K.; Biochemistry 50:9377-9387(2011). Cited for: GLYCOSYLATION AT ASN-79 AND ASN-116, AND MUTAGENESIS OF ASN-79 ANDASN-116.	21932778 [Abstract]
"Molecular cloning of a phosphatidylinositol-anchored membrane heparansulfate proteoglycan from human lung fibroblasts."; David G., Lories V., Decock B., Marynen P., Cassiman J.-J.,van den Berghe H.; J. Cell Biol. 111:3165-3176(1990). Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 24-53; 100-118 AND298-317, GPI-ANCHOR, GLYCOSYLATION AT ASN-116, AND VARIANT GLY-500.	2148568 [Abstract]