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Q96NY8

- PVRL4_HUMAN

UniProt

Q96NY8 - PVRL4_HUMAN

Protein

Nectin-4

Gene

PVRL4

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 117 (01 Oct 2014)
      Sequence version 1 (01 Dec 2001)
      Previous versions | rss
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    Functioni

    Seems to be involved in cell adhesion through trans-homophilic and -heterophilic interactions, the latter including specifically interactions with PVRL2/nectin-1. Does not act as receptor for alpha-herpesvirus entry into cells.

    GO - Molecular functioni

    1. protein binding Source: IntAct

    GO - Biological processi

    1. adherens junction organization Source: Reactome
    2. cell adhesion Source: UniProtKB-KW
    3. cell-cell junction organization Source: Reactome
    4. cell junction assembly Source: Reactome
    5. viral process Source: UniProtKB-KW

    Keywords - Biological processi

    Cell adhesion, Host-virus interaction

    Enzyme and pathway databases

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

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Nectin-4
    Alternative name(s):
    Ig superfamily receptor LNIR
    Poliovirus receptor-related protein 4
    Cleaved into the following chain:
    Gene namesi
    Name:PVRL4
    Synonyms:LNIR, PRR4
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:19688. PVRL4.

    Subcellular locationi

    Cell membrane Curated; Single-pass type I membrane protein Curated. Cell junctionadherens junction 1 Publication
    Note: Colocalizes with MLLT4 at cadherin-based adherens junctions.
    Chain Processed poliovirus receptor-related protein 4 : Secreted
    Note: The secreted form is found in breast tumor patients.

    GO - Cellular componenti

    1. adherens junction Source: UniProtKB-SubCell
    2. extracellular vesicular exosome Source: UniProt
    3. integral component of membrane Source: UniProtKB-KW
    4. plasma membrane Source: Reactome

    Keywords - Cellular componenti

    Cell junction, Cell membrane, Membrane, Secreted

    Pathology & Biotechi

    Involvement in diseasei

    Ectodermal dysplasia-syndactyly syndrome 1 (EDSS1) [MIM:613573]: A form of ectodermal dysplasia, a heterogeneous group of disorders due to abnormal development of two or more ectodermal structures. EDSS1 is characterized by the association of hair and teeth abnormalities with cutaneous syndactyly of the hands and/or feet. Hair morphologic abnormalities include twists at irregular intervals (pilli torti) and swelling along the shafts, particularly associated with areas of breakage. Dental findings consist of abnormally widely spaced teeth, with peg-shaped and conical crowns. Patients have normal sweating.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti185 – 1851T → M in EDSS1. 1 Publication
    VAR_064189

    Keywords - Diseasei

    Disease mutation, Ectodermal dysplasia

    Organism-specific databases

    MIMi613573. phenotype.
    Orphaneti247820. Ectodermal dysplasia - syndactyly syndrome.
    PharmGKBiPA134991624.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 3131Sequence AnalysisAdd
    BLAST
    Chaini32 – 510479Nectin-4PRO_0000297673Add
    BLAST
    Chaini32 – ?Processed poliovirus receptor-related protein 4PRO_0000311086

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi52 ↔ 127
    Disulfide bondi171 ↔ 223
    Disulfide bondi270 ↔ 315PROSITE-ProRule annotation
    Glycosylationi281 – 2811N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

    The soluble form is produced by proteolytic cleavage at the cell surface (shedding), probably by ADAM17/TACE.1 Publication

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    MaxQBiQ96NY8.
    PaxDbiQ96NY8.
    PRIDEiQ96NY8.

    PTM databases

    PhosphoSiteiQ96NY8.

    Expressioni

    Tissue specificityi

    Predominantly expressed in placenta. Not detected in normal breast epithelium but expressed in breast carcinoma.2 Publications

    Gene expression databases

    ArrayExpressiQ96NY8.
    BgeeiQ96NY8.
    CleanExiHS_PRR4.
    HS_PVRL4.
    GenevestigatoriQ96NY8.

    Organism-specific databases

    HPAiHPA010775.

    Interactioni

    Subunit structurei

    Self-associates. Interacts via its Ig-like V-type domain with PVRL1/nectin-1 Ig-like V-type domain. Interacts via its C-terminus with MLLT4. Binds to Measles virus protein H and acts as a receptor for this virus.5 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    HQ786F22EBI-4314784,EBI-5323300From a different organism.
    PVRL1Q152232EBI-4314784,EBI-1771314
    TIGITQ495A12EBI-4314784,EBI-4314807

    Protein-protein interaction databases

    BioGridi123544. 3 interactions.
    DIPiDIP-41492N.
    IntActiQ96NY8. 4 interactions.
    MINTiMINT-237395.
    STRINGi9606.ENSP00000356991.

    Structurei

    Secondary structure

    1
    510
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi38 – 436
    Beta strandi48 – 503
    Beta strandi62 – 698
    Beta strandi72 – 743
    Beta strandi77 – 837
    Turni84 – 863
    Beta strandi87 – 904
    Helixi92 – 943
    Turni95 – 973
    Beta strandi112 – 1143
    Helixi119 – 1213
    Beta strandi123 – 13412
    Beta strandi136 – 14611
    Beta strandi152 – 1554
    Beta strandi165 – 17713
    Beta strandi180 – 1878
    Beta strandi190 – 1978
    Beta strandi199 – 21012
    Helixi214 – 2163
    Beta strandi220 – 2267
    Beta strandi234 – 2396

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4FRWX-ray3.50A/B/C/D/E/F32-243[»]
    4GJTX-ray3.10B/C32-146[»]
    4JJHX-ray2.25A/B32-153[»]
    ProteinModelPortaliQ96NY8.
    SMRiQ96NY8. Positions 32-335.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini32 – 349318ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini371 – 510140CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei350 – 37021HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini32 – 144113Ig-like V-type 1Add
    BLAST
    Domaini148 – 23790Ig-like C2-type 1Add
    BLAST
    Domaini248 – 33184Ig-like C2-type 2Add
    BLAST

    Sequence similaritiesi

    Belongs to the nectin family.Curated

    Keywords - Domaini

    Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG149403.
    HOGENOMiHOG000115806.
    HOVERGENiHBG108310.
    InParanoidiQ96NY8.
    KOiK06593.
    OMAiQDEGIKQ.
    OrthoDBiEOG73RBB5.
    PhylomeDBiQ96NY8.
    TreeFamiTF338610.

    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.
    IPR003598. Ig_sub2.
    IPR013106. Ig_V-set.
    IPR013151. Immunoglobulin.
    [Graphical view]
    PfamiPF08205. C2-set_2. 1 hit.
    PF00047. ig. 1 hit.
    PF07686. V-set. 1 hit.
    [Graphical view]
    SMARTiSM00409. IG. 1 hit.
    SM00408. IGc2. 1 hit.
    [Graphical view]
    PROSITEiPS50835. IG_LIKE. 3 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q96NY8-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPLSLGAEMW GPEAWLLLLL LLASFTGRCP AGELETSDVV TVVLGQDAKL    50
    PCFYRGDSGE QVGQVAWARV DAGEGAQELA LLHSKYGLHV SPAYEGRVEQ 100
    PPPPRNPLDG SVLLRNAVQA DEGEYECRVS TFPAGSFQAR LRLRVLVPPL 150
    PSLNPGPALE EGQGLTLAAS CTAEGSPAPS VTWDTEVKGT TSSRSFKHSR 200
    SAAVTSEFHL VPSRSMNGQP LTCVVSHPGL LQDQRITHIL HVSFLAEASV 250
    RGLEDQNLWH IGREGAMLKC LSEGQPPPSY NWTRLDGPLP SGVRVDGDTL 300
    GFPPLTTEHS GIYVCHVSNE FSSRDSQVTV DVLDPQEDSG KQVDLVSASV 350
    VVVGVIAALL FCLLVVVVVL MSRYHRRKAQ QMTQKYEEEL TLTRENSIRR 400
    LHSHHTDPRS QPEESVGLRA EGHPDSLKDN SSCSVMSEEP EGRSYSTLTT 450
    VREIETQTEL LSPGSGRAEE EEDQDEGIKQ AMNHFVQENG TLRAKPTGNG 500
    IYINGRGHLV 510
    Length:510
    Mass (Da):55,454
    Last modified:December 1, 2001 - v1
    Checksum:iDCF5E1D794F227FA
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti35 – 351E → G in BAB55344. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti53 – 531F → L.
    Corresponds to variant rs3737786 [ dbSNP | Ensembl ].
    VAR_034669
    Natural varianti185 – 1851T → M in EDSS1. 1 Publication
    VAR_064189

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF426163 mRNA. Translation: AAL23958.1.
    AK027753 mRNA. Translation: BAB55344.1.
    AL591806 Genomic DNA. Translation: CAI15376.1.
    CH471121 Genomic DNA. Translation: EAW52665.1.
    BC010423 mRNA. Translation: AAH10423.1.
    CCDSiCCDS1216.1.
    RefSeqiNP_112178.2. NM_030916.2.
    UniGeneiHs.492490.
    Hs.732297.

    Genome annotation databases

    EnsembliENST00000368012; ENSP00000356991; ENSG00000143217.
    GeneIDi81607.
    KEGGihsa:81607.
    UCSCiuc001fxo.2. human.

    Polymorphism databases

    DMDMi74761016.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF426163 mRNA. Translation: AAL23958.1 .
    AK027753 mRNA. Translation: BAB55344.1 .
    AL591806 Genomic DNA. Translation: CAI15376.1 .
    CH471121 Genomic DNA. Translation: EAW52665.1 .
    BC010423 mRNA. Translation: AAH10423.1 .
    CCDSi CCDS1216.1.
    RefSeqi NP_112178.2. NM_030916.2.
    UniGenei Hs.492490.
    Hs.732297.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4FRW X-ray 3.50 A/B/C/D/E/F 32-243 [» ]
    4GJT X-ray 3.10 B/C 32-146 [» ]
    4JJH X-ray 2.25 A/B 32-153 [» ]
    ProteinModelPortali Q96NY8.
    SMRi Q96NY8. Positions 32-335.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 123544. 3 interactions.
    DIPi DIP-41492N.
    IntActi Q96NY8. 4 interactions.
    MINTi MINT-237395.
    STRINGi 9606.ENSP00000356991.

    PTM databases

    PhosphoSitei Q96NY8.

    Polymorphism databases

    DMDMi 74761016.

    Proteomic databases

    MaxQBi Q96NY8.
    PaxDbi Q96NY8.
    PRIDEi Q96NY8.

    Protocols and materials databases

    DNASUi 81607.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000368012 ; ENSP00000356991 ; ENSG00000143217 .
    GeneIDi 81607.
    KEGGi hsa:81607.
    UCSCi uc001fxo.2. human.

    Organism-specific databases

    CTDi 81607.
    GeneCardsi GC01M161040.
    H-InvDB HIX0001228.
    HGNCi HGNC:19688. PVRL4.
    HPAi HPA010775.
    MIMi 609607. gene.
    613573. phenotype.
    neXtProti NX_Q96NY8.
    Orphaneti 247820. Ectodermal dysplasia - syndactyly syndrome.
    PharmGKBi PA134991624.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG149403.
    HOGENOMi HOG000115806.
    HOVERGENi HBG108310.
    InParanoidi Q96NY8.
    KOi K06593.
    OMAi QDEGIKQ.
    OrthoDBi EOG73RBB5.
    PhylomeDBi Q96NY8.
    TreeFami TF338610.

    Enzyme and pathway databases

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

    Miscellaneous databases

    GenomeRNAii 81607.
    NextBioi 71924.
    PROi Q96NY8.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q96NY8.
    Bgeei Q96NY8.
    CleanExi HS_PRR4.
    HS_PVRL4.
    Genevestigatori Q96NY8.

    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.
    IPR003598. Ig_sub2.
    IPR013106. Ig_V-set.
    IPR013151. Immunoglobulin.
    [Graphical view ]
    Pfami PF08205. C2-set_2. 1 hit.
    PF00047. ig. 1 hit.
    PF07686. V-set. 1 hit.
    [Graphical view ]
    SMARTi SM00409. IG. 1 hit.
    SM00408. IGc2. 1 hit.
    [Graphical view ]
    PROSITEi PS50835. IG_LIKE. 3 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "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: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, SUBCELLULAR LOCATION, SUBUNIT, INTERACTION WITH MLLT4 AND PVRL1.
    2. "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].
      Tissue: Placenta.
    3. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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].
      Tissue: Pancreas.
    6. "Prominent role of the Ig-like V domain in trans-interactions of nectins. Nectin3 and nectin 4 bind to the predicted C-C'-C'-D beta-strands of the nectin1 V domain."
      Fabre S., Reymond N., Cocchi F., Menotti L., Dubreuil P., Campadelli-Fiume G., Lopez M.
      J. Biol. Chem. 277:27006-27013(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PVLR1.
    7. "Nectin-4, a new serological breast cancer marker, is a substrate for tumor necrosis factor-alpha-converting enzyme (TACE)/ADAM-17."
      Fabre-Lafay S., Garrido-Urbani S., Reymond N., Goncalves A., Dubreuil P., Lopez M.
      J. Biol. Chem. 280:19543-19550(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEOLYTIC PROCESSING.
    8. Cited for: TISSUE SPECIFICITY.
    9. Cited for: INTERACTION WITH MEASLES VIRUS PROTEIN H.
    10. Cited for: X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) OF 32-243, SUBUNIT, DISULFIDE BONDS, IDENTIFICATION BY MASS SPECTROMETRY.
    11. "Structure of measles virus hemagglutinin bound to its epithelial receptor nectin-4."
      Zhang X., Lu G., Qi J., Li Y., He Y., Xu X., Shi J., Zhang C.W., Yan J., Gao G.F.
      Nat. Struct. Mol. Biol. 20:67-72(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 32-146 IN COMPLEX WITH WITH MEASLES VIRUS HEMAGGLUTININ, SUBUNIT, DISULFIDE BOND.
    12. Cited for: VARIANT EDSS1 MET-185.

    Entry informationi

    Entry nameiPVRL4_HUMAN
    AccessioniPrimary (citable) accession number: Q96NY8
    Secondary accession number(s): Q96K15
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 21, 2007
    Last sequence update: December 1, 2001
    Last modified: October 1, 2014
    This is version 117 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 chromosome 1
      Human chromosome 1: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3