ASGR2_HUMAN - dbPTM
ASGR2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ASGR2_HUMAN
UniProt AC P07307
Protein Name Asialoglycoprotein receptor 2
Gene Name ASGR2
Organism Homo sapiens (Human).
Sequence Length 311
Subcellular Localization Membrane
Single-pass type II membrane protein.
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 MAKDFQDIQQLSSEENDHPFHQGEGPGTRRLNPRRGNPFLKGPPPAQPLAQRLCSMVCFSLLALSFNILLLVVICVTGSQSEGHGGAQLQAELRSLKEAFSNFSSSTLTEVQAISTHGGSVGDKITSLGAKLEKQQQDLKADHDALLFHLKHFPVDLRFVACQMELLHSNGSQRTCCPVNWVEHQGSCYWFSHSGKAWAEAEKYCQLENAHLVVINSWEEQKFIVQHTNPFNTWIGLTDSDGSWKWVDGTDYRHNYKNWAVTQPDNWHGHELGGSEDCVEVQPDGRWNDDFCLQVYRWVCEKRRNATGEVA
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
12PhosphorylationFQDIQQLSSEENDHP
HHHHHHHCCCCCCCC
31.221924301
13PhosphorylationQDIQQLSSEENDHPF
HHHHHHCCCCCCCCC
58.4826422651
54S-palmitoylationQPLAQRLCSMVCFSL
HHHHHHHHHHHHHHH
2.41-
102N-linked_GlycosylationSLKEAFSNFSSSTLT
HHHHHHHCCCCCCCE
34.0716335952
134AcetylationSLGAKLEKQQQDLKA
HHHHHHHHHHHHHHC
64.9423749302
170N-linked_GlycosylationQMELLHSNGSQRTCC
HHHHHHCCCCCCEEE
43.3019159218
305N-linked_GlycosylationWVCEKRRNATGEVA-
HHHHHHHCCCCCCC-
45.98UniProtKB CARBOHYD

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
12SPhosphorylationKinasePKC-FAMILY-GPS
12SPhosphorylationKinasePKC_GROUP-PhosphoELM

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ASGR2_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 ASGR2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CERS2_HUMANCERS2physical
11543633
EDEM1_HUMANEDEM1physical
21062743
ERLEC_HUMANERLEC1physical
21062743
SYVN1_HUMANSYVN1physical
21062743
FBX6_HUMANFBXO6physical
21062743
DERL1_HUMANDERL1physical
21062743
ERLEC_HUMANERLEC1physical
21917589
OS9_HUMANOS9physical
21917589
CERS2_HUMANCERS2physical
21988832
DHE3_HUMANGLUD1physical
21988832
HES1_HUMANHES1physical
21988832
MROH5_HUMANMROH5physical
21988832
TM214_HUMANTMEM214physical
26186194
S38A9_HUMANSLC38A9physical
26186194
TTYH3_HUMANTTYH3physical
26186194
P121A_HUMANPOM121physical
26186194
FKRP_HUMANFKRPphysical
26186194
SENP5_HUMANSENP5physical
26186194
IF1AX_HUMANEIF1AXphysical
26186194
RL23_HUMANRPL23physical
26186194
PARVG_HUMANPARVGphysical
26186194
SOAT1_HUMANSOAT1physical
26186194
TIMP3_HUMANTIMP3physical
26186194
SERC1_HUMANSERINC1physical
26186194
RFT1_HUMANRFT1physical
26186194
LMA2L_HUMANLMAN2Lphysical
26186194
TMPPE_HUMANTMPPEphysical
26186194
GOGA5_HUMANGOLGA5physical
26186194
SBP1_HUMANSELENBP1physical
26186194
PTN1_HUMANPTPN1physical
26186194
LMBR1_HUMANLMBR1physical
26186194
AGRL3_HUMANLPHN3physical
26186194
MANEA_HUMANMANEAphysical
26186194
JMJD8_HUMANJMJD8physical
26186194
COX1_HUMANCOX1physical
26186194
F189B_HUMANFAM189Bphysical
26186194
AG10A_HUMANALG10physical
26186194
MFSD8_HUMANMFSD8physical
26186194
SCAM2_HUMANSCAMP2physical
26186194
EGFL7_HUMANEGFL7physical
26186194
HACD2_HUMANPTPLBphysical
26186194
ZDH18_HUMANZDHHC18physical
26186194
TM214_HUMANTMEM214physical
28514442
SERC1_HUMANSERINC1physical
28514442
PARVG_HUMANPARVGphysical
28514442
MFSD8_HUMANMFSD8physical
28514442
S38A9_HUMANSLC38A9physical
28514442
TIMP3_HUMANTIMP3physical
28514442
JMJD8_HUMANJMJD8physical
28514442
SOAT1_HUMANSOAT1physical
28514442
FKRP_HUMANFKRPphysical
28514442
TTYH3_HUMANTTYH3physical
28514442
AGRL3_HUMANLPHN3physical
28514442
RL23_HUMANRPL23physical
28514442
COX1_HUMANCOX1physical
28514442
LMA2L_HUMANLMAN2Lphysical
28514442
LMBR1_HUMANLMBR1physical
28514442
ZDH18_HUMANZDHHC18physical
28514442
TMPPE_HUMANTMPPEphysical
28514442
GOGA5_HUMANGOLGA5physical
28514442
GRP78_HUMANHSPA5physical
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 ASGR2_HUMAN

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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-102 AND ASN-170, AND MASSSPECTROMETRY.
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,hydrazide chemistry, and mass spectrometry.";
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,Moore R.J., Smith R.D.;
J. Proteome Res. 4:2070-2080(2005).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-102, AND MASSSPECTROMETRY.

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