Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Poliovirus receptor  

UniProtKB / Swiss-Prot ID :  PVR_HUMAN

Gene Name (Synonyms) : 
PVR, PVS  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Isoform Alpha: Cell membrane; Single-pass type I membrane protein. Isoform Delta: Cell membrane; Single-pass type I membrane protein. Isoform Beta: Secreted. Isoform Gamma: Secreted. 

Protein Function :  Mediates NK cell adhesion and triggers NK cell effector functions. Binds two different NK cell receptors: CD96 and CD226. These interactions accumulates at the cell-cell contact site, leading to the formation of a mature immunological synapse between NK cell and target cell. This may trigger adhesion and secretion of lytic granules and IFN-gamma and activate cytoxicity of activated NK cells. May also promote NK cell-target cell modular exchange, and PVR transfer to the NK cell. This transfer is more important in some tumor cells expressing a lot of PVR, and may trigger fratricide NK cell activation, providing tumors with a mechanism of immunoevasion. Plays a role in mediating tumor cell invasion and migration. Serves as a receptor for poliovirus attachment to target cells. May play a role in axonal transport of poliovirus, by targeting virion-PVR-containing endocytic vesicles to the microtubular network through interaction with DYNLT1. This interaction would drive the virus-containing vesicle to the axonal retrograde transport. 

Transmembrane Topology (topPTM) : PVR_HUMAN 

Protein Sequence MARAMAAAWPLLLVALLVLSWPPPGTGDVVVQAPTQVPGFLGDSVTLPCYLQVPNMEVTHVSQLTWARHG...
Predicted Secondary Structure CCCCCHHHHHHHHHHHHHHCCCCCCCCCEEEECCCEEEEEECCEEEEEEEECCCCCCCCCCEEEEEEECC...
Protein Variant
LocationDescription
67A -> T (in dbSNP:rs1058402). VAR_003952
295A -> T (in dbSNP:rs35365841). VAR_049994
340I -> M (in dbSNP:rs203710). VAR_011736
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
Protein Variant
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
90Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)YSESKRLEF
CCCCCEEEE
57.88Phosphositeplus
Link
105N-linked (Glc...)AELRNASLR
CCCCCEEEE
46.64HPRD
Link
105N-linked (GlcNAc...).AELRNASLR
CCCCCEEEE
46.64UniProtKB
Link
120N-linked (Glc...)EDEGNYTCL
CCCEEEEEE
27.22HPRD
Link
120N-linked (GlcNAc...) (complex).EDEGNYTCL
CCCEEEEEE
27.22UniProtKB
Link
278N-linked (GlcNAc...).PTGYNWSTT
CCEEEEEEC
27.80UniProtKB
Link
307N-linked (GlcNAc...).DKPINTTLI
CHHHCEEEE
35.22UniProtKB
Link
398PhosphotyrosineGHVSYSAVS
EEEEEECCC
10.28PhosphoELM
Link-
398PhosphotyrosineGHVSYSAVS
EEEEEECCC
10.28Phosphositeplus
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
PVR_HUMANin vitroHPRD:01434HPRD12663789
VTNC_HUMANENSP00000187830STRING
CD226_HUMANENSP00000187830STRING
PVRL3_HUMANENSP00000187830STRING
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"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-278, GLYCOSYLATION [LARGESCALE ANALYSIS] AT ASN-360 (ISOFORM BETA), AND MASS SPECTROMETRY.
"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-307, AND MASSSPECTROMETRY.
"Human urinary glycoproteomics; attachment site specific analysis ofN-and O-linked glycosylations by CID and ECD.";
Halim A., Nilsson J., Ruetschi U., Hesse C., Larson G.;
Mol. Cell. Proteomics 0:0-0(2011).
Cited for: GLYCOSYLATION AT ASN-120, STRUCTURE OF CARBOHYDRATES, AND MASSSPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures