SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q96NY8

- PVRL4_HUMAN

UniProt

Q96NY8 - PVRL4_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Nectin-4
Gene
PVRL4, LNIR, PRR4
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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 junction assembly Source: Reactome
  4. cell-cell junction organization Source: Reactome
  5. viral process Source: UniProtKB-KW
Complete GO annotation...

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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini32 – 349318Extracellular Reviewed prediction
Add
BLAST
Transmembranei350 – 37021Helical; Reviewed prediction
Add
BLAST
Topological domaini371 – 510140Cytoplasmic Reviewed prediction
Add
BLAST

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
Complete GO annotation...

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.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication
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 – 3131 Reviewed prediction
Add
BLAST
Chaini32 – 510479Nectin-4
PRO_0000297673Add
BLAST
Chaini32 – ?Processed poliovirus receptor-related protein 4PRO_0000311086

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi52 ↔ 1272 Publications
Disulfide bondi171 ↔ 2232 Publications
Disulfide bondi270 ↔ 315 By similarity
Glycosylationi281 – 2811N-linked (GlcNAc...) Reviewed prediction

Post-translational modificationi

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

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

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.

Family & Domainsi

Domains and Repeats

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

Sequence similaritiesi

Belongs to the nectin family.

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

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 conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti35 – 351E → G in BAB55344. 1 Publication

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 116 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

Similar proteinsi