Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Poliovirus receptor-related protein 1  

UniProtKB / Swiss-Prot ID :  PVRL1_HUMAN

Gene Name (Synonyms) : 
PVRL1, HVEC, PRR1  

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 Gamma: Secreted. 

Protein Function :  Promotes cell-cell contacts by forming homophilic or heterophilic trans-dimers. Heterophilic interactions have been detected between PVRL1/nectin-1 and PVRL3/nectin-3 and between PVRL1/nectin-1 and PVRL4/nectin-4. 

Transmembrane Topology (topPTM) : PVRL1_HUMAN 

Protein Sequence MARMGLAGAAGRWWGLALGLTAFFLPGVHSQVVQVNDSMYGFIGTDVVLHCSFANPLPSVKITQVTWQKS...
Predicted Secondary Structure CCCCCCCCCCCHHHHHHHHHHHHHCCCCEEEEEEECCEEEEEECCCEEEEEEECCCCCCCCCCEEEEEEE...
Protein Variant -
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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
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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
190Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)ETRLKGEAE
EECCCCCCC
51.95Phosphositeplus
Link
202N-linked (Glc...)IRNPNGTVT
EECCCCEEE
63.42HPRD
Link
202N-linked (GlcNAc...).IRNPNGTVT
EECCCCEEE
63.42UniProtKB
Link
286N-linked (Glc...)WTTLNGSLP
EEECCEEEC
35.60HPRD
Link
332N-linked (Glc...)QVEVNITEF
EEEEEEEEC
23.20HPRD
Link
332N-linked (GlcNAc...).QVEVNITEF
EEEEEEEEC
23.20UniProtKB
Link
422PhosphoserineYPDDSDDEK
CCCCCCCEE
55.10HPRD
Link-
422PhosphoserineYPDDSDDEK
CCCCCCCEE
55.10Phosphositeplus
Link-
422PhosphoserineYPDDSDDEK
CCCCCCCEE
55.10SysPTM
Link-
434PhosphoserinePLGGSSYEE
CCCCCCCCC
28.13Phosphositeplus
Link-
435PhosphoserineLGGSSYEEE
CCCCCCCCC
39.58Phosphositeplus
Link-
465Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)DEDAKRPYF
CCCCCCCHH
67.25Phosphositeplus
Link-
468PhosphotyrosineAKRPYFTVD
CCCCHHHHH
18.86HPRD
Link-
468PhosphotyrosineAKRPYFTVD
CCCCHHHHH
18.86Phosphositeplus
Link-
468Phosphotyrosine.AKRPYFTVD
CCCCHHHHH
18.86UniProtKB
Link-
481PhosphotyrosineRQDGYGDRT
CCCCCCCCC
24.92Phosphositeplus
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
PVRL1_HUMANphysical interactionMINT-49750MINT12011057
AFAD_HUMANin vitro
in vivo
yeast 2-hybrid
HPRD:07200HPRD10225955
10617658
PVR_HUMANin vitroHPRD:07200HPRD12011057
PRIO_HUMANin vivoHPRD:07200HPRD15146195
PARD3_HUMANin vitro
in vivo
HPRD:07200HPRD12515806
PVRL1_HUMANin vitroHPRD:07200HPRD12011057
IQGA1_HUMANENSP00000264025STRING
PAEP_HUMANENSP00000264025STRING
PVRL3_HUMANENSP00000264025STRING
DUFFY_HUMANENSP00000264025STRING
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Disease Reference
Kegg disease
H00516 Isolated orofacial clefts, including: Cleft lip with or without cleft palate; Cleft palate
OMIM disease
225060Ectodermal dysplasia, Margarita Island type (EDMI)
225060Non-syndromic orofacial cleft 7 (OFC7)
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins.";
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,Schiess R., Aebersold R., Watts J.D.;
Nat. Biotechnol. 27:378-386(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-332, 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-202, AND MASSSPECTROMETRY.
Phosphorylation
ReferencePubMed
"Multiple reaction monitoring for robust quantitative proteomicanalysis of cellular signaling networks.";
Wolf-Yadlin A., Hautaniemi S., Lauffenburger D.A., White F.M.;
Proc. Natl. Acad. Sci. U.S.A. 104:5860-5865(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-468, AND MASSSPECTROMETRY.
"An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells.";
Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.;
J. Proteome Res. 8:3852-3861(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-468, AND MASSSPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures