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Q92692

- PVRL2_HUMAN

UniProt

Q92692 - PVRL2_HUMAN

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Protein

Nectin-2

Gene
PVRL2, HVEB, PRR2
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Probable cell adhesion protein.1 Publication

GO - Molecular functioni

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

GO - Biological processi

  1. acrosome assembly Source: Ensembl
  2. adherens junction organization Source: Reactome
  3. adhesion of symbiont to host Source: BHF-UCL
  4. cell-cell junction organization Source: Reactome
  5. cell junction assembly Source: Reactome
  6. cell part morphogenesis Source: Ensembl
  7. cilium organization Source: Ensembl
  8. coreceptor-mediated virion attachment to host cell Source: BHF-UCL
  9. cytoskeleton organization Source: Ensembl
  10. establishment of mitochondrion localization Source: Ensembl
  11. fertilization Source: Ensembl
  12. fusion of virus membrane with host plasma membrane Source: BHF-UCL
  13. homophilic cell adhesion Source: BHF-UCL
  14. positive regulation of immunoglobulin mediated immune response Source: BHF-UCL
  15. positive regulation of mast cell activation Source: BHF-UCL
  16. positive regulation of natural killer cell mediated cytotoxicity Source: BHF-UCL
  17. positive regulation of natural killer cell mediated cytotoxicity directed against tumor cell target Source: BHF-UCL
  18. regulation of immune response Source: Reactome
  19. signal transduction Source: GOC
  20. spermatid development Source: BHF-UCL
  21. spermatid nucleus differentiation Source: Ensembl
  22. sperm mitochondrion organization Source: Ensembl
  23. susceptibility to natural killer cell mediated cytotoxicity Source: BHF-UCL
  24. susceptibility to T cell mediated cytotoxicity Source: BHF-UCL
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_11152. Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
REACT_19195. Adherens junctions interactions.
REACT_19268. Nectin/Necl trans heterodimerization.

Names & Taxonomyi

Protein namesi
Recommended name:
Nectin-2
Alternative name(s):
Herpes virus entry mediator B
Short name:
Herpesvirus entry mediator B
Short name:
HveB
Poliovirus receptor-related protein 2
CD_antigen: CD112
Gene namesi
Name:PVRL2
Synonyms:HVEB, PRR2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 19

Organism-specific databases

HGNCiHGNC:9707. PVRL2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini32 – 360329Extracellular Reviewed predictionAdd
BLAST
Transmembranei361 – 38121Helical; Reviewed predictionAdd
BLAST
Topological domaini382 – 538157Cytoplasmic Reviewed predictionAdd
BLAST

GO - Cellular componenti

  1. cell-cell junction Source: BHF-UCL
  2. cell surface Source: BHF-UCL
  3. extracellular vesicular exosome Source: UniProt
  4. integral component of membrane Source: BHF-UCL
  5. plasma membrane Source: Reactome
  6. zonula adherens Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi81 – 811N → A: Abolishes homodimerization. 1 Publication
Mutagenesisi89 – 891M → F: Loss of entry of HHV-1/Rid1 and HSV-2. No effect on PRV entry. 1 Publication
Mutagenesisi89 – 891M → I: Increased entry of HHV-1/Rid1 and HSV-2. 1 Publication

Organism-specific databases

PharmGKBiPA34052.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3131 Reviewed predictionAdd
BLAST
Chaini32 – 538507Nectin-2PRO_0000015136Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi54 ↔ 1401 Publication
Glycosylationi137 – 1371N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi183 ↔ 238 By similarity
Disulfide bondi283 ↔ 329 By similarity
Glycosylationi324 – 3241N-linked (GlcNAc...) Reviewed prediction
Modified residuei433 – 4331Phosphoserine2 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiQ92692.
PaxDbiQ92692.
PRIDEiQ92692.

PTM databases

PhosphoSiteiQ92692.

Expressioni

Tissue specificityi

Ubiquitous.

Gene expression databases

ArrayExpressiQ92692.
BgeeiQ92692.
CleanExiHS_PVRL2.
GenevestigatoriQ92692.

Organism-specific databases

HPAiCAB026138.
HPA012759.

Interactioni

Subunit structurei

Can form trans-heterodimers with PVRL3/nectin-3 By similarity. Interacts with CD226. Binds with low affinity to TIGIT. Interacts with herpes simplex virus 1 (HHV-1) mutant Rid1, herpes simplex virus 1 (HHV-2) and pseudorabies virus (PRV) envelope glycoprotein D; functions as an entry receptor for these viruses.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-718419,EBI-718419
CD226Q157622EBI-718419,EBI-4314442
MLLT4P551962EBI-718419,EBI-365875
PVRL3Q9NQS33EBI-718419,EBI-2826725

Protein-protein interaction databases

BioGridi111777. 14 interactions.
DIPiDIP-41043N.
IntActiQ92692. 14 interactions.
MINTiMINT-90946.
STRINGi9606.ENSP00000252483.

Structurei

Secondary structure

1
538
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi35 – 373
Beta strandi40 – 434
Beta strandi50 – 523
Beta strandi55 – 584
Beta strandi64 – 718
Helixi77 – 793
Beta strandi81 – 866
Turni87 – 893
Beta strandi90 – 923
Beta strandi95 – 984
Helixi100 – 1023
Beta strandi103 – 1075
Turni113 – 1153
Beta strandi125 – 1273
Helixi132 – 1343
Beta strandi136 – 14510
Beta strandi148 – 15710

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3R0NX-ray1.30A32-158[»]
4DFHX-ray1.85A/B32-158[»]
4DFIX-ray1.80A32-158[»]
4HZAX-ray1.70A/B32-158[»]
ProteinModelPortaliQ92692.
SMRiQ92692. Positions 32-350.

Miscellaneous databases

EvolutionaryTraceiQ92692.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini32 – 156125Ig-like V-typeAdd
BLAST
Domaini162 – 25695Ig-like C2-type 1Add
BLAST
Domaini261 – 34585Ig-like C2-type 2Add
BLAST

Sequence similaritiesi

Belongs to the nectin family.

Keywords - Domaini

Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG149530.
HOGENOMiHOG000237277.
HOVERGENiHBG019169.
InParanoidiQ92692.
KOiK06531.
OMAiREVTWLR.
OrthoDBiEOG7D59N6.
PhylomeDBiQ92692.
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.
[Graphical view]
PfamiPF08205. C2-set_2. 1 hit.
PF07686. V-set. 1 hit.
[Graphical view]
SMARTiSM00409. IG. 1 hit.
[Graphical view]
PROSITEiPS50835. IG_LIKE. 3 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform Delta (identifier: Q92692-1) [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

MARAAALLPS RSPPTPLLWP LLLLLLLETG AQDVRVQVLP EVRGQLGGTV    50
ELPCHLLPPV PGLYISLVTW QRPDAPANHQ NVAAFHPKMG PSFPSPKPGS 100
ERLSFVSAKQ STGQDTEAEL QDATLALHGL TVEDEGNYTC EFATFPKGSV 150
RGMTWLRVIA KPKNQAEAQK VTFSQDPTTV ALCISKEGRP PARISWLSSL 200
DWEAKETQVS GTLAGTVTVT SRFTLVPSGR ADGVTVTCKV EHESFEEPAL 250
IPVTLSVRYP PEVSISGYDD NWYLGRTDAT LSCDVRSNPE PTGYDWSTTS 300
GTFPTSAVAQ GSQLVIHAVD SLFNTTFVCT VTNAVGMGRA EQVIFVRETP 350
NTAGAGATGG IIGGIIAAII ATAVAATGIL ICRQQRKEQT LQGAEEDEDL 400
EGPPSYKPPT PKAKLEAQEM PSQLFTLGAS EHSPLKTPYF DAGASCTEQE 450
MPRYHELPTL EERSGPLHPG ATSLGSPIPV PPGPPAVEDV SLDLEDEEGE 500
EEEEYLDKIN PIYDALSYSS PSDSYQGKGF VMSRAMYV 538
Length:538
Mass (Da):57,742
Last modified:February 1, 1997 - v1
Checksum:i3AE4F83E92F6F624
GO
Isoform Alpha (identifier: Q92692-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     351-479: NTAGAGATGG...GATSLGSPIP → RASPRDVGPL...SLISRRAVYV
     480-538: Missing.

Show »
Length:479
Mass (Da):51,359
Checksum:i870F08D7B9D896F2
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei351 – 479129NTAGA…GSPIP → RASPRDVGPLVWGAVGGTLL VLLLLAGGSLAFILLRVRRR RKSPGGAGGGASGDGGFYDP KAQVLGNGDPVFWTPVVPGP MEPDGKDEEEEEEEEKAEKG LMLPPPPALEDDMESQLDGS LISRRAVYV in isoform Alpha. VSP_002628Add
BLAST
Alternative sequencei480 – 53859Missing in isoform Alpha. VSP_002629Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Isoform Alpha (identifier: Q92692-2)
Sequence conflicti410 – 4101P → L in BAF84019. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X80038 mRNA. Translation: CAA56342.1.
AF058448 mRNA. Translation: AAC23797.1.
AK291330 mRNA. Translation: BAF84019.1.
CR456818 mRNA. Translation: CAG33099.1.
CH471126 Genomic DNA. Translation: EAW57298.1.
BC003091 mRNA. Translation: AAH03091.1.
AF044968
, AF044962, AF044963, AF044964, AF044966, AF044967 Genomic DNA. Translation: AAC82348.1.
AF050154 Genomic DNA. Translation: AAD02503.1.
CCDSiCCDS12645.1. [Q92692-2]
CCDS42576.1. [Q92692-1]
PIRiI68093.
RefSeqiNP_001036189.1. NM_001042724.1. [Q92692-1]
NP_002847.1. NM_002856.2. [Q92692-2]
UniGeneiHs.655455.

Genome annotation databases

EnsembliENST00000252483; ENSP00000252483; ENSG00000130202. [Q92692-1]
ENST00000252485; ENSP00000252485; ENSG00000130202. [Q92692-2]
GeneIDi5819.
KEGGihsa:5819.
UCSCiuc002ozv.3. human. [Q92692-2]
uc002ozw.1. human. [Q92692-1]

Polymorphism databases

DMDMi12643789.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X80038 mRNA. Translation: CAA56342.1 .
AF058448 mRNA. Translation: AAC23797.1 .
AK291330 mRNA. Translation: BAF84019.1 .
CR456818 mRNA. Translation: CAG33099.1 .
CH471126 Genomic DNA. Translation: EAW57298.1 .
BC003091 mRNA. Translation: AAH03091.1 .
AF044968
, AF044962 , AF044963 , AF044964 , AF044966 , AF044967 Genomic DNA. Translation: AAC82348.1 .
AF050154 Genomic DNA. Translation: AAD02503.1 .
CCDSi CCDS12645.1. [Q92692-2 ]
CCDS42576.1. [Q92692-1 ]
PIRi I68093.
RefSeqi NP_001036189.1. NM_001042724.1. [Q92692-1 ]
NP_002847.1. NM_002856.2. [Q92692-2 ]
UniGenei Hs.655455.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3R0N X-ray 1.30 A 32-158 [» ]
4DFH X-ray 1.85 A/B 32-158 [» ]
4DFI X-ray 1.80 A 32-158 [» ]
4HZA X-ray 1.70 A/B 32-158 [» ]
ProteinModelPortali Q92692.
SMRi Q92692. Positions 32-350.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111777. 14 interactions.
DIPi DIP-41043N.
IntActi Q92692. 14 interactions.
MINTi MINT-90946.
STRINGi 9606.ENSP00000252483.

PTM databases

PhosphoSitei Q92692.

Polymorphism databases

DMDMi 12643789.

Proteomic databases

MaxQBi Q92692.
PaxDbi Q92692.
PRIDEi Q92692.

Protocols and materials databases

DNASUi 5819.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000252483 ; ENSP00000252483 ; ENSG00000130202 . [Q92692-1 ]
ENST00000252485 ; ENSP00000252485 ; ENSG00000130202 . [Q92692-2 ]
GeneIDi 5819.
KEGGi hsa:5819.
UCSCi uc002ozv.3. human. [Q92692-2 ]
uc002ozw.1. human. [Q92692-1 ]

Organism-specific databases

CTDi 5819.
GeneCardsi GC19P045349.
HGNCi HGNC:9707. PVRL2.
HPAi CAB026138.
HPA012759.
MIMi 600798. gene.
neXtProti NX_Q92692.
PharmGKBi PA34052.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG149530.
HOGENOMi HOG000237277.
HOVERGENi HBG019169.
InParanoidi Q92692.
KOi K06531.
OMAi REVTWLR.
OrthoDBi EOG7D59N6.
PhylomeDBi Q92692.
TreeFami TF331051.

Enzyme and pathway databases

Reactomei REACT_11152. Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
REACT_19195. Adherens junctions interactions.
REACT_19268. Nectin/Necl trans heterodimerization.

Miscellaneous databases

ChiTaRSi PVRL2. human.
EvolutionaryTracei Q92692.
GeneWikii PVRL2.
GenomeRNAii 5819.
NextBioi 22666.
PROi Q92692.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q92692.
Bgeei Q92692.
CleanExi HS_PVRL2.
Genevestigatori Q92692.

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.
[Graphical view ]
Pfami PF08205. C2-set_2. 1 hit.
PF07686. V-set. 1 hit.
[Graphical view ]
SMARTi SM00409. IG. 1 hit.
[Graphical view ]
PROSITEi PS50835. IG_LIKE. 3 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The human PRR2 gene, related to the human poliovirus receptor gene (PVR), is the true homolog of the murine MPH gene."
    Eberle F., Dubreuil P., Mattei M.-G., Devilard E., Lopez M.
    Gene 159:267-272(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM DELTA).
  2. "A cell surface protein with herpesvirus entry activity (HveB) confers susceptibility to infection by mutants of herpes simplex virus type 1, herpes simplex virus type 2, and pseudorabies virus."
    Warner M.S., Geraghty R.J., Martinez W.M., Montgomery R.I., Whitbeck J.C., Xu R., Eisenberg R.J., Cohen G.H., Spear P.G.
    Virology 246:179-189(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA), FUNCTION AS A RECEPTOR FOR MUTANTS OF HHV-1; HHV-2 AND PRV.
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA).
    Tissue: Tongue.
  4. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA).
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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 ALPHA).
    Tissue: Brain.
  7. "A transcriptional map in the region of 19q13 derived using direct sequencing and exon trapping."
    Yoshiura K., Murray J.C.
    Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 31-538.
  8. "Sequencing of 42kb of the APO E-C2 gene cluster reveals a new gene: PEREC1."
    Freitas E.M., Zhang W.J., Lalonde J.P., Tay G.K., Gaudieri S., Ashworth L.K., Van Bockxmeer F.M., Dawkins R.L.
    DNA Seq. 9:89-100(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 449-538.
  9. "Structural features of nectin-2 (HveB) required for herpes simplex virus entry."
    Martinez W.M., Spear P.G.
    J. Virol. 75:11185-11195(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HHV-1 MUTANT RID1; HHV-2 AND PRV GLYCOPROTEIN D, MUTAGENESIS OF MET-89.
  10. "PVR (CD155) and Nectin-2 (CD112) as ligands of the human DNAM-1 (CD226) activating receptor: involvement in tumor cell lysis."
    Pende D., Bottino C., Castriconi R., Cantoni C., Marcenaro S., Rivera P., Spaggiari G.M., Dondero A., Carnemolla B., Reymond N., Mingari M.C., Lopez M., Moretta L., Moretta A.
    Mol. Immunol. 42:463-469(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CD226.
  11. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-433, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "The surface protein TIGIT suppresses T cell activation by promoting the generation of mature immunoregulatory dendritic cells."
    Yu X., Harden K., Gonzalez L.C., Francesco M., Chiang E., Irving B., Tom I., Ivelja S., Refino C.J., Clark H., Eaton D., Grogan J.L.
    Nat. Immunol. 10:48-57(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TIGIT.
  14. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-433, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. "Structure of Nectin-2 reveals determinants of homophilic and heterophilic interactions that control cell-cell adhesion."
    Samanta D., Ramagopal U.A., Rubinstein R., Vigdorovich V., Nathenson S.G., Almo S.C.
    Proc. Natl. Acad. Sci. U.S.A. 109:14836-14840(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) OF 32-158, SUBUNIT, DISULFIDE BOND, MUTAGENESIS OF ASN-81.

Entry informationi

Entry nameiPVRL2_HUMAN
AccessioniPrimary (citable) accession number: Q92692
Secondary accession number(s): A8K5L5
, O75455, Q6IBI6, Q96J29
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: February 1, 1997
Last modified: September 3, 2014
This is version 150 of the entry and version 1 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 19
    Human chromosome 19: 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

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