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Q15223

- PVRL1_HUMAN

UniProt

Q15223 - PVRL1_HUMAN

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Protein

Nectin-1

Gene

PVRL1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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. Functions as an entry receptor for herpes simplex virus and pseudorabies virus. Has some neurite outgrowth-promoting activity.2 Publications

GO - Molecular functioni

  1. carbohydrate binding Source: Ensembl
  2. cell adhesion molecule binding Source: BHF-UCL
  3. coreceptor activity Source: ProtInc
  4. protein homodimerization activity Source: HGNC
  5. virion binding Source: Ensembl
  6. virus receptor activity Source: UniProtKB-KW

GO - Biological processi

  1. adherens junction organization Source: Reactome
  2. axon guidance Source: Ensembl
  3. cell adhesion Source: UniProtKB
  4. cell-cell junction organization Source: Reactome
  5. cell junction assembly Source: Reactome
  6. desmosome organization Source: Ensembl
  7. enamel mineralization Source: Ensembl
  8. heterophilic cell-cell adhesion Source: HGNC
  9. homophilic cell adhesion Source: HGNC
  10. immune response Source: UniProtKB
  11. iron ion transport Source: Ensembl
  12. lens morphogenesis in camera-type eye Source: Ensembl
  13. regulation of synapse assembly Source: Ensembl
  14. retina development in camera-type eye Source: Ensembl
  15. signal transduction Source: GOC
  16. single organismal cell-cell adhesion Source: UniProtKB
  17. viral entry into host cell Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Host cell receptor for virus entry, Receptor

Keywords - Biological processi

Cell adhesion, Host-virus interaction

Enzyme and pathway databases

ReactomeiREACT_19195. Adherens junctions interactions.
REACT_19268. Nectin/Necl trans heterodimerization.

Protein family/group databases

MEROPSiI43.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Nectin-1
Alternative name(s):
Herpes virus entry mediator C
Short name:
Herpesvirus entry mediator C
Short name:
HveC
Herpesvirus Ig-like receptor
Short name:
HIgR
Poliovirus receptor-related protein 1
CD_antigen: CD111
Gene namesi
Name:PVRL1
Synonyms:HVEC, PRR1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 11

Organism-specific databases

HGNCiHGNC:9706. PVRL1.

Subcellular locationi

GO - Cellular componenti

  1. adherens junction Source: UniProtKB
  2. axon Source: Ensembl
  3. cell-cell adherens junction Source: BHF-UCL
  4. extracellular region Source: UniProtKB-KW
  5. growth cone membrane Source: Ensembl
  6. integral component of membrane Source: UniProtKB
  7. intracellular membrane-bounded organelle Source: Ensembl
  8. membrane Source: ProtInc
  9. plasma membrane Source: Reactome
  10. synapse Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Membrane, Secreted, Synapse

Pathology & Biotechi

Involvement in diseasei

Ectodermal dysplasia, Margarita Island type (EDMI) [MIM:225060]: An autosomal recessive form of ectodermal dysplasia, a heterogeneous group of disorders due to abnormal development of two or more ectodermal structures. It is a syndrome characterized by the association of cleft lip/palate, ectodermal dysplasia (sparse short and dry scalp hair, sparse eyebrows and eyelashes), and partial syndactyly of the fingers and/or toes. Two thirds of the patients do not manifest oral cleft but present with abnormal teeth and nails.
Note: The disease is caused by mutations affecting the gene represented in this entry.
Non-syndromic orofacial cleft 7 (OFC7) [MIM:225060]: A birth defect consisting of cleft lips with or without cleft palate. Cleft lips are associated with cleft palate in two-third of cases. A cleft lip can occur on one or both sides and range in severity from a simple notch in the upper lip to a complete opening in the lip extending into the floor of the nostril and involving the upper gum.
Note: The disease is caused by mutations affecting the gene represented in this entry.

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi82 – 821N → Y: Impairs interaction with herpes simplex glycoprotein D. Decreases susceptibility to infection by herpes simplex virus. 1 Publication
Mutagenesisi84 – 841S → Y: Impairs interaction with herpes simplex glycoprotein D. Decreases susceptibility to infection by herpes simplex virus. 1 Publication
Mutagenesisi129 – 1291F → A or S: Impairs interaction with herpes simplex glycoprotein D. Decreases susceptibility to infection by herpes simplex virus. 1 Publication

Keywords - Diseasei

Ectodermal dysplasia

Organism-specific databases

MIMi225060. phenotype.
Orphaneti1991. Cleft lip with or without cleft palate.
3253. Zlotogora-Ogur syndrome.
PharmGKBiPA34051.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3030Sequence AnalysisAdd
BLAST
Chaini31 – 517487Nectin-1PRO_0000015133Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi36 – 361N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi51 ↔ 124
Glycosylationi72 – 721N-linked (GlcNAc...)1 Publication
Glycosylationi139 – 1391N-linked (GlcNAc...)1 Publication
Disulfide bondi172 ↔ 226
Glycosylationi202 – 2021N-linked (GlcNAc...) (complex)4 Publications
Disulfide bondi269 ↔ 316
Glycosylationi286 – 2861N-linked (GlcNAc...)Sequence Analysis
Glycosylationi297 – 2971N-linked (GlcNAc...)Sequence Analysis
Glycosylationi307 – 3071N-linked (GlcNAc...)Sequence Analysis
Glycosylationi332 – 3321N-linked (GlcNAc...)1 Publication
Modified residuei422 – 4221Phosphoserine1 Publication
Modified residuei434 – 4341Phosphoserine1 Publication
Modified residuei435 – 4351PhosphoserineBy similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiQ15223.
PaxDbiQ15223.
PeptideAtlasiQ15223.
PRIDEiQ15223.

PTM databases

PhosphoSiteiQ15223.

Miscellaneous databases

PMAP-CutDBQ15223.

Expressioni

Gene expression databases

BgeeiQ15223.
CleanExiHS_PVRL1.
ExpressionAtlasiQ15223. baseline and differential.
GenevestigatoriQ15223.

Organism-specific databases

HPAiCAB016135.
HPA026846.

Interactioni

Subunit structurei

Interacts (via Ig-like C2-type domain 2) with FGFR1, FGFR2 and FGFR3 By similarity. Cis- and trans-homodimer. Can form trans-heterodimers with PVRL3/nectin-3 and with PVRL4/nectin-4. Interaction between PVRL1 and PVRL3 on the pre- and postsynaptic sites, respectively, initiates the formation of puncta adherentia junctions between axons and dendrites. Interacts (via cytoplasmic domain) with MLLT4/afadin (via PDZ domain); this interaction recruits PVRL1 to cadherin-based adherens junctions and provides a connection with the actin cytoskeleton. Interacts with integrin alphaV/beta3. Interacts with herpes simplex virus 1 (HHV-1), herpes simplex virus 2 (HHV-2), and pseudorabies virus (PRV) envelope glycoprotein D; functions as an entry receptor for these viruses.By similarity7 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
PVRL3Q9NQS32EBI-1771314,EBI-2826725
PVRL4Q96NY82EBI-1771314,EBI-4314784

Protein-protein interaction databases

BioGridi111776. 6 interactions.
DIPiDIP-40302N.
IntActiQ15223. 2 interactions.
MINTiMINT-90873.
STRINGi9606.ENSP00000264025.

Structurei

Secondary structure

1
517
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi37 – 426
Beta strandi47 – 493
Beta strandi61 – 7111
Beta strandi74 – 829
Turni83 – 853
Beta strandi86 – 894
Turni94 – 963
Beta strandi97 – 1015
Beta strandi103 – 1064
Beta strandi109 – 1113
Helixi116 – 1183
Beta strandi120 – 12910
Beta strandi132 – 14413
Beta strandi147 – 1526
Beta strandi157 – 1593
Beta strandi167 – 17913
Beta strandi182 – 1898
Beta strandi192 – 1998
Beta strandi205 – 2139
Helixi217 – 2193
Beta strandi223 – 2308
Beta strandi233 – 2408
Beta strandi243 – 25210
Beta strandi265 – 27511
Beta strandi279 – 2846
Beta strandi293 – 2964
Beta strandi299 – 3024
Helixi308 – 3103
Beta strandi312 – 3209
Beta strandi323 – 3319

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3ALPX-ray2.80A/B30-335[»]
3SKUX-ray4.00D/E/F31-345[»]
3U82X-ray3.16B30-335[»]
3U83X-ray2.50A30-335[»]
4FMFX-ray3.20A/B/C/D31-337[»]
ProteinModelPortaliQ15223.
SMRiQ15223. Positions 33-335.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ15223.

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini31 – 355325ExtracellularSequence AnalysisAdd
BLAST
Topological domaini377 – 517141CytoplasmicSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei356 – 37621HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini31 – 141111Ig-like V-typeAdd
BLAST
Domaini149 – 23890Ig-like C2-type 1Add
BLAST
Domaini247 – 33488Ig-like C2-type 2Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni282 – 29918Interaction with FGFRBy similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi437 – 4448Poly-Glu
Compositional biasi445 – 4495Poly-Gly

Domaini

Ig-like C2-type 2 mediates neurite outgrowth through binding, induction of phosphorylation, and activation of FGFR.By similarity

Sequence similaritiesi

Belongs to the nectin family.Curated

Keywords - Domaini

Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG147558.
GeneTreeiENSGT00760000119054.
HOGENOMiHOG000115804.
HOVERGENiHBG100542.
InParanoidiQ15223.
KOiK06081.
OMAiMARMGHA.
OrthoDBiEOG73RBB5.
PhylomeDBiQ15223.
TreeFamiTF331051.

Family and domain databases

Gene3Di2.60.40.10. 3 hits.
InterProiIPR013162. CD80_C2-set.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR013106. Ig_V-set.
IPR003596. Ig_V-set_subgr.
[Graphical view]
PfamiPF08205. C2-set_2. 1 hit.
PF07686. V-set. 1 hit.
[Graphical view]
SMARTiSM00409. IG. 1 hit.
SM00406. IGv. 1 hit.
[Graphical view]
PROSITEiPS50835. IG_LIKE. 2 hits.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform Delta (identifier: Q15223-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MARMGLAGAA GRWWGLALGL TAFFLPGVHS QVVQVNDSMY GFIGTDVVLH
60 70 80 90 100
CSFANPLPSV KITQVTWQKS TNGSKQNVAI YNPSMGVSVL APYRERVEFL
110 120 130 140 150
RPSFTDGTIR LSRLELEDEG VYICEFATFP TGNRESQLNL TVMAKPTNWI
160 170 180 190 200
EGTQAVLRAK KGQDDKVLVA TCTSANGKPP SVVSWETRLK GEAEYQEIRN
210 220 230 240 250
PNGTVTVISR YRLVPSREAH QQSLACIVNY HMDRFKESLT LNVQYEPEVT
260 270 280 290 300
IEGFDGNWYL QRMDVKLTCK ADANPPATEY HWTTLNGSLP KGVEAQNRTL
310 320 330 340 350
FFKGPINYSL AGTYICEATN PIGTRSGQVE VNITEFPYTP SPPEHGRRAG
360 370 380 390 400
PVPTAIIGGV AGSILLVLIV VGGIVVALRR RRHTFKGDYS TKKHVYGNGY
410 420 430 440 450
SKAGIPQHHP PMAQNLQYPD DSDDEKKAGP LGGSSYEEEE EEEEGGGGGE
460 470 480 490 500
RKVGGPHPKY DEDAKRPYFT VDEAEARQDG YGDRTLGYQY DPEQLDLAEN
510
MVSQNDGSFI SKKEWYV
Length:517
Mass (Da):57,158
Last modified:September 26, 2001 - v3
Checksum:iDF34C8AEC893EE6D
GO
Isoform Alpha (identifier: Q15223-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     336-458: FPYTPSPPEH...GERKVGGPHP → KPRPQRGLGS...RTTEPRGECP
     459-517: Missing.

Show »
Length:458
Mass (Da):50,721
Checksum:iAB507515F86D7B45
GO
Isoform Gamma (identifier: Q15223-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     335-352: EFPYTPSPPEHGRRAGPV → AFCQLIYPGKGRTRARMF
     353-517: Missing.

Show »
Length:352
Mass (Da):39,150
Checksum:i2FB60588FA752D99
GO

Sequence cautioni

The sequence CAA53980.2 differs from that shown. Reason: Erroneous initiation.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei335 – 35218EFPYT…RAGPV → AFCQLIYPGKGRTRARMF in isoform Gamma. 1 PublicationVSP_002624Add
BLAST
Alternative sequencei336 – 458123FPYTP…GGPHP → KPRPQRGLGSAARLLAGTVA VFLILVAVLTVFFLYNRQQK SPPETDGAGTDQPLSQKPEP SPSRQSSLVPEDIQVVHLDP GRQQQQEEEDLQKLSLQPPY YDLGVSPSYHPSVRTTEPRG ECP in isoform Alpha. CuratedVSP_002626Add
BLAST
Alternative sequencei353 – 517165Missing in isoform Gamma. 1 PublicationVSP_002625Add
BLAST
Alternative sequencei459 – 51759Missing in isoform Alpha. CuratedVSP_002627Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X76400 mRNA. Translation: CAA53980.2. Different initiation.
AF060231 mRNA. Translation: AAC23798.1.
AY029539 mRNA. Translation: AAK33124.1.
BC104948 mRNA. Translation: AAI04949.1.
BC113471 mRNA. Translation: AAI13472.1.
AF252867
, AF196768, AF196769, AF196770, AF196771 Genomic DNA. Translation: AAG16648.1.
AF196774
, AF196768, AF196769, AF196770, AF196771, AF196772, AF196773 Genomic DNA. Translation: AAG16649.1.
CCDSiCCDS8425.1. [Q15223-2]
CCDS8426.1. [Q15223-1]
CCDS8427.1. [Q15223-3]
PIRiJC4024.
RefSeqiNP_002846.3. NM_002855.4. [Q15223-1]
NP_976030.1. NM_203285.1. [Q15223-2]
NP_976031.1. NM_203286.1. [Q15223-3]
UniGeneiHs.334846.

Genome annotation databases

EnsembliENST00000264025; ENSP00000264025; ENSG00000110400. [Q15223-1]
ENST00000340882; ENSP00000345289; ENSG00000110400. [Q15223-3]
ENST00000341398; ENSP00000344974; ENSG00000110400. [Q15223-2]
GeneIDi5818.
KEGGihsa:5818.
UCSCiuc001pwu.1. human. [Q15223-2]
uc001pwv.3. human. [Q15223-1]
uc001pww.3. human. [Q15223-3]

Polymorphism databases

DMDMi18202503.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X76400 mRNA. Translation: CAA53980.2 . Different initiation.
AF060231 mRNA. Translation: AAC23798.1 .
AY029539 mRNA. Translation: AAK33124.1 .
BC104948 mRNA. Translation: AAI04949.1 .
BC113471 mRNA. Translation: AAI13472.1 .
AF252867
, AF196768 , AF196769 , AF196770 , AF196771 Genomic DNA. Translation: AAG16648.1 .
AF196774
, AF196768 , AF196769 , AF196770 , AF196771 , AF196772 , AF196773 Genomic DNA. Translation: AAG16649.1 .
CCDSi CCDS8425.1. [Q15223-2 ]
CCDS8426.1. [Q15223-1 ]
CCDS8427.1. [Q15223-3 ]
PIRi JC4024.
RefSeqi NP_002846.3. NM_002855.4. [Q15223-1 ]
NP_976030.1. NM_203285.1. [Q15223-2 ]
NP_976031.1. NM_203286.1. [Q15223-3 ]
UniGenei Hs.334846.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3ALP X-ray 2.80 A/B 30-335 [» ]
3SKU X-ray 4.00 D/E/F 31-345 [» ]
3U82 X-ray 3.16 B 30-335 [» ]
3U83 X-ray 2.50 A 30-335 [» ]
4FMF X-ray 3.20 A/B/C/D 31-337 [» ]
ProteinModelPortali Q15223.
SMRi Q15223. Positions 33-335.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111776. 6 interactions.
DIPi DIP-40302N.
IntActi Q15223. 2 interactions.
MINTi MINT-90873.
STRINGi 9606.ENSP00000264025.

Protein family/group databases

MEROPSi I43.001.

PTM databases

PhosphoSitei Q15223.

Polymorphism databases

DMDMi 18202503.

Proteomic databases

MaxQBi Q15223.
PaxDbi Q15223.
PeptideAtlasi Q15223.
PRIDEi Q15223.

Protocols and materials databases

DNASUi 5818.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000264025 ; ENSP00000264025 ; ENSG00000110400 . [Q15223-1 ]
ENST00000340882 ; ENSP00000345289 ; ENSG00000110400 . [Q15223-3 ]
ENST00000341398 ; ENSP00000344974 ; ENSG00000110400 . [Q15223-2 ]
GeneIDi 5818.
KEGGi hsa:5818.
UCSCi uc001pwu.1. human. [Q15223-2 ]
uc001pwv.3. human. [Q15223-1 ]
uc001pww.3. human. [Q15223-3 ]

Organism-specific databases

CTDi 5818.
GeneCardsi GC11M119542.
HGNCi HGNC:9706. PVRL1.
HPAi CAB016135.
HPA026846.
MIMi 225060. phenotype.
600644. gene.
neXtProti NX_Q15223.
Orphaneti 1991. Cleft lip with or without cleft palate.
3253. Zlotogora-Ogur syndrome.
PharmGKBi PA34051.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG147558.
GeneTreei ENSGT00760000119054.
HOGENOMi HOG000115804.
HOVERGENi HBG100542.
InParanoidi Q15223.
KOi K06081.
OMAi MARMGHA.
OrthoDBi EOG73RBB5.
PhylomeDBi Q15223.
TreeFami TF331051.

Enzyme and pathway databases

Reactomei REACT_19195. Adherens junctions interactions.
REACT_19268. Nectin/Necl trans heterodimerization.

Miscellaneous databases

ChiTaRSi PVRL1. human.
EvolutionaryTracei Q15223.
GeneWikii PVRL1.
GenomeRNAii 5818.
NextBioi 22658.
PMAP-CutDB Q15223.
PROi Q15223.
SOURCEi Search...

Gene expression databases

Bgeei Q15223.
CleanExi HS_PVRL1.
ExpressionAtlasi Q15223. baseline and differential.
Genevestigatori Q15223.

Family and domain databases

Gene3Di 2.60.40.10. 3 hits.
InterProi IPR013162. CD80_C2-set.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR013106. Ig_V-set.
IPR003596. Ig_V-set_subgr.
[Graphical view ]
Pfami PF08205. C2-set_2. 1 hit.
PF07686. V-set. 1 hit.
[Graphical view ]
SMARTi SM00409. IG. 1 hit.
SM00406. IGv. 1 hit.
[Graphical view ]
PROSITEi PS50835. IG_LIKE. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "cDNA characterization and chromosomal localization of a gene related to the poliovirus receptor gene."
    Lopez M., Eberle F., Mattei M.-G., Gabert J., Bardin F., Maroc C., Dubreuil P.
    Gene 155:261-265(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM DELTA), FUNCTION AS A RECEPTOR FOR HHV-1; HHV-2 AND PRV.
  2. "Entry of alphaherpesviruses mediated by poliovirus receptor-related protein 1 and poliovirus receptor."
    Geraghty R.J., Krummenacher C., Cohen G.H., Eisenberg R.J., Spear P.G.
    Science 280:1618-1620(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM DELTA).
  3. "Novel, soluble isoform of the herpes simplex virus (HSV) receptor nectin1 (or prr1-HIgR-Hvec) modulates positively and negatively susceptibility to hsv infection."
    Lopez M., Cocchi F., Avitabile E., Leclerc A., Adelaide J., Campadelli-Fjume G., Dubreuil P.
    J. Virol. 75:5684-5691(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM GAMMA).
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM DELTA).
    Tissue: Brain.
  5. "Mutations of PVRL1, encoding a cell-cell adhesion molecule/herpesvirus receptor, in cleft lip/palate-ectodermal dysplasia."
    Suzuki K., Hu D., Bustos T., Zlotogora J., Richieri-Costa A., Helms J.A., Spritz R.A.
    Nat. Genet. 25:427-430(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 28-517 (ISOFORMS ALPHA AND DELTA), DISEASE.
  6. "Herpes simplex virus glycoprotein D can bind to poliovirus receptor-related protein 1 or herpesvirus entry mediator, two structurally unrelated mediators of virus entry."
    Krummenacher C., Nicola A.V., Whitbeck J.C., Lou H., Hou W., Lambris J.D., Geraghty R.J., Spear P.G., Cohen G.H., Eisenberg R.J.
    J. Virol. 72:7064-7074(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HHV-1 AND HHV-2 GLYCOPROTEIN D.
  7. "Nectin/PRR: an immunoglobulin-like cell adhesion molecule recruited to cadherin-based adherens junctions through interaction with Afadin, a PDZ domain-containing protein."
    Takahashi K., Nakanishi H., Miyahara M., Mandai K., Satoh K., Satoh A., Nishioka H., Aoki J., Nomoto A., Mizoguchi A., Takai Y.
    J. Cell Biol. 145:539-549(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH AFADIN.
  8. "Nectin4/PRR4, a new afadin-associated member of the nectin family that trans-interacts with nectin1/PRR1 through V domain interaction."
    Reymond N., Fabre S., Lecocq E., Adelaide J., Dubreuil P., Lopez M.
    J. Biol. Chem. 276:43205-43215(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PVRL3 AND PVRL4.
  9. "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) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-202.
    Tissue: Plasma.
  10. "Interaction of integrin alpha(v)beta3 with nectin. Implication in cross-talk between cell-matrix and cell-cell junctions."
    Sakamoto Y., Ogita H., Hirota T., Kawakatsu T., Fukuyama T., Yasumi M., Kanzaki N., Ozaki M., Takai Y.
    J. Biol. Chem. 281:19631-19644(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH INTEGRIN ITGAV/ITGB3.
  11. Cited for: GLYCOSYLATION AT ASN-202.
  12. "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) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-332.
    Tissue: Leukemic T-cell.
  13. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  14. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-422 AND SER-434, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "Binding of herpes simplex virus glycoprotein D to nectin-1 exploits host cell adhesion."
    Zhang N., Yan J., Lu G., Guo Z., Fan Z., Wang J., Shi Y., Qi J., Gao G.F.
    Nat. Commun. 2:577-577(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 30-335 IN COMPLEX WITH HERPES SIMPLEX VIRUS GLYCOPROTEIN D, SUBUNIT, DISULFIDE BONDS.
  16. "Structure of herpes simplex virus glycoprotein D bound to the human receptor nectin-1."
    Di Giovine P., Settembre E.C., Bhargava A.K., Luftig M.A., Lou H., Cohen G.H., Eisenberg R.J., Krummenacher C., Carfi A.
    PLoS Pathog. 7:E1002277-E1002277(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (4.0 ANGSTROMS) OF 31-345 IN COMPLEX WITH HERPES SIMPLEX VIRUS GLYCOPROTEIN D, FUNCTION, SUBUNIT, MUTAGENESIS OF ASN-82; SER-84 AND PHE-129, DISULFIDE BONDS, GLYCOSYLATION AT ASN-72; ASN-139 AND ASN-202.
  17. Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 31-337, SUBUNIT, GLYCOSYLATION AT ASN-202, DISULFIDE BONDS, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiPVRL1_HUMAN
AccessioniPrimary (citable) accession number: Q15223
Secondary accession number(s): O75465
, Q2M3D3, Q9HBE6, Q9HBW2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: September 26, 2001
Last modified: October 29, 2014
This is version 142 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human cell differentiation molecules
    CD nomenclature of surface proteins of human leucocytes and list of entries
  2. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  3. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3