ASGR1_HUMAN - dbPTM
ASGR1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ASGR1_HUMAN
UniProt AC P07306
Protein Name Asialoglycoprotein receptor 1
Gene Name ASGR1
Organism Homo sapiens (Human).
Sequence Length 291
Subcellular Localization Isoform H1a: Membrane
Single-pass type II membrane protein.
Isoform H1b: Secreted .
Protein Description Mediates the endocytosis of plasma glycoproteins to which the terminal sialic acid residue on their complex carbohydrate moieties has been removed. The receptor recognizes terminal galactose and N-acetylgalactosamine units. After ligand binding to the receptor, the resulting complex is internalized and transported to a sorting organelle, where receptor and ligand are disassociated. The receptor then returns to the cell membrane surface..
Protein Sequence MTKEYQDLQHLDNEESDHHQLRKGPPPPQPLLQRLCSGPRLLLLSLGLSLLLLVVVCVIGSQNSQLQEELRGLRETFSNFTASTEAQVKGLSTQGGNVGRKMKSLESQLEKQQKDLSEDHSSLLLHVKQFVSDLRSLSCQMAALQGNGSERTCCPVNWVEHERSCYWFSRSGKAWADADNYCRLEDAHLVVVTSWEEQKFVQHHIGPVNTWMGLHDQNGPWKWVDGTDYETGFKNWRPEQPDDWYGHGLGGGEDCAHFTDDGRWNDDVCQRPYRWVCETELDKASQEPPLL
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
2Phosphorylation------MTKEYQDLQ
------CCHHHHHHH
32.36-
5Phosphorylation---MTKEYQDLQHLD
---CCHHHHHHHCCC
14.6429116813
16PhosphorylationQHLDNEESDHHQLRK
HCCCCCCCCHHHHHC
35.7429116813
36S-palmitoylationQPLLQRLCSGPRLLL
HHHHHHHCCCHHHHH
4.888943311
79N-linked_GlycosylationGLRETFSNFTASTEA
HHHHHHHHCCCCCHH
33.8119159218
81O-linked_GlycosylationRETFSNFTASTEAQV
HHHHHHCCCCCHHHH
24.77-
93O-linked_GlycosylationAQVKGLSTQGGNVGR
HHHCCCCCCCCHHHH
35.95OGP
147N-linked_GlycosylationQMAALQGNGSERTCC
HHHHHCCCCCCCEEE
37.5519159218
149O-linked_GlycosylationAALQGNGSERTCCPV
HHHCCCCCCCEEEEC
28.09-
285PhosphorylationETELDKASQEPPLL-
CHHHHHHHCCCCCC-
40.608943311
285O-linked_GlycosylationETELDKASQEPPLL-
CHHHHHHHCCCCCC-
40.60OGP

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 ASGR1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ASGR1_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 ASGR1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CERS2_HUMANCERS2physical
11543633
A4_HUMANAPPphysical
21832049
EDEM1_HUMANEDEM1physical
23233672
SYVN1_HUMANSYVN1physical
23233672
FBX6_HUMANFBXO6physical
23233672
GRP78_HUMANHSPA5physical
23233672
ZEP1_HUMANHIVEP1physical
21988832
CERS2_HUMANCERS2physical
21988832
PLVAP_HUMANPLVAPphysical
28514442
PTN2_HUMANPTPN2physical
28514442
GABT_HUMANABATphysical
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 ASGR1_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-79 AND ASN-147, AND MASSSPECTROMETRY.
Palmitoylation
ReferencePubMed
"Fatty acylation of the rat and human asialoglycoprotein receptors. Aconserved cytoplasmic cysteine residue is acylated in all receptorsubunits.";
Zeng F.Y., Weigel P.H.;
J. Biol. Chem. 271:32454-32460(1996).
Cited for: PALMITOYLATION AT CYS-36.

TOP