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Protein

Sialic acid-binding Ig-like lectin 7

Gene

SIGLEC7

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

Functioni

Putative adhesion molecule that mediates sialic-acid dependent binding to cells. Preferentially binds to alpha-2,3- and alpha-2,6-linked sialic acid. Also binds disialogangliosides (disialogalactosyl globoside, disialyl lactotetraosylceramide and disialyl GalNAc lactotetraoslylceramide). The sialic acid recognition site may be masked by cis interactions with sialic acids on the same cell surface. In the immune response, may act as an inhibitory receptor upon ligand induced tyrosine phosphorylation by recruiting cytoplasmic phosphatase(s) via their SH2 domain(s) that block signal transduction through dephosphorylation of signaling molecules. Mediates inhibition of natural killer cells cytotoxicity. May play a role in hemopoiesis. Inhibits differentiation of CD34+ cell precursors towards myelomonocytic cell lineage and proliferation of leukemic myeloid cells (in vitro).1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei124 – 1241Sialic acid2 Publications

GO - Molecular functioni

  • carbohydrate binding Source: ProtInc
  • receptor activity Source: ProtInc

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Keywords - Ligandi

Lectin

Enzyme and pathway databases

ReactomeiR-HSA-198933. Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.

Names & Taxonomyi

Protein namesi
Recommended name:
Sialic acid-binding Ig-like lectin 7
Short name:
Siglec-7
Alternative name(s):
Adhesion inhibitory receptor molecule 1
Short name:
AIRM-1
CDw328
D-siglec
QA79 membrane protein
p75
CD_antigen: CD328
Gene namesi
Name:SIGLEC7
Synonyms:AIRM1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:10876. SIGLEC7.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini19 – 353335ExtracellularSequence analysisAdd
BLAST
Transmembranei354 – 37623HelicalSequence analysisAdd
BLAST
Topological domaini377 – 46791CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • integral component of plasma membrane Source: ProtInc
  • plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA35777.

Polymorphism and mutation databases

DMDMi25009269.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818Sequence analysisAdd
BLAST
Chaini19 – 467449Sialic acid-binding Ig-like lectin 7PRO_0000014947Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi46 ↔ 106PROSITE-ProRule annotation4 Publications
Glycosylationi105 – 1051N-linked (GlcNAc...)2 Publications
Glycosylationi142 – 1421N-linked (GlcNAc...)Sequence analysis
Glycosylationi165 – 1651N-linked (GlcNAc...)Sequence analysis
Disulfide bondi168 ↔ 217PROSITE-ProRule annotation
Glycosylationi229 – 2291N-linked (GlcNAc...)Sequence analysis
Glycosylationi235 – 2351N-linked (GlcNAc...)Sequence analysis
Glycosylationi242 – 2421N-linked (GlcNAc...)Sequence analysis
Glycosylationi260 – 2601N-linked (GlcNAc...)Sequence analysis
Disulfide bondi276 ↔ 320PROSITE-ProRule annotation
Glycosylationi334 – 3341N-linked (GlcNAc...)Sequence analysis
Modified residuei429 – 4291PhosphoserineCombined sources

Post-translational modificationi

Tyrosine phosphorylated.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiQ9Y286.
PRIDEiQ9Y286.

PTM databases

iPTMnetiQ9Y286.
PhosphoSiteiQ9Y286.

Expressioni

Tissue specificityi

Predominantly expressed by resting and activated natural killer cells and at lower levels by granulocytes and monocytes. High expression found in placenta, liver, lung, spleen, and peripheral blood leukocytes.

Gene expression databases

BgeeiQ9Y286.
CleanExiHS_SIGLEC7.
ExpressionAtlasiQ9Y286. baseline and differential.
GenevisibleiQ9Y286. HS.

Organism-specific databases

HPAiCAB025154.

Interactioni

Subunit structurei

Interacts with PTPN6/SHP-1 upon phosphorylation.3 Publications

Protein-protein interaction databases

BioGridi117967. 5 interactions.
IntActiQ9Y286. 1 interaction.
STRINGi9606.ENSP00000323328.

Structurei

Secondary structure

1
467
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi23 – 253Combined sources
Beta strandi27 – 304Combined sources
Beta strandi32 – 376Combined sources
Beta strandi42 – 443Combined sources
Beta strandi46 – 494Combined sources
Turni54 – 585Combined sources
Beta strandi62 – 676Combined sources
Beta strandi69 – 713Combined sources
Helixi72 – 743Combined sources
Beta strandi78 – 814Combined sources
Helixi85 – 884Combined sources
Helixi89 – 913Combined sources
Turni92 – 943Combined sources
Beta strandi95 – 973Combined sources
Helixi101 – 1033Combined sources
Beta strandi108 – 1103Combined sources
Helixi115 – 1173Combined sources
Beta strandi119 – 1279Combined sources
Beta strandi130 – 1334Combined sources
Beta strandi139 – 1446Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1NKOX-ray1.45A19-150[»]
1O7SX-ray1.75A18-144[»]
1O7VX-ray1.90A18-144[»]
2DF3X-ray1.90A18-144[»]
2G5RX-ray1.60A18-144[»]
2HRLX-ray1.85A18-144[»]
ProteinModelPortaliQ9Y286.
SMRiQ9Y286. Positions 18-237, 254-343.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9Y286.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini39 – 12284Ig-like V-typeAdd
BLAST
Domaini150 – 23384Ig-like C2-type 1Add
BLAST
Domaini240 – 33697Ig-like C2-type 2Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni131 – 1355Sialic acid binding3 Publications

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi435 – 4406ITIM motif

Domaini

Sequence similaritiesi

Keywords - Domaini

Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IJT6. Eukaryota.
ENOG410YKZU. LUCA.
GeneTreeiENSGT00760000119139.
HOGENOMiHOG000236324.
HOVERGENiHBG036161.
InParanoidiQ9Y286.
KOiK06739.
OMAiGQEATNN.
OrthoDBiEOG7W6WRM.
PhylomeDBiQ9Y286.
TreeFamiTF332441.

Family and domain databases

Gene3Di2.60.40.10. 3 hits.
InterProiIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR013106. Ig_V-set.
[Graphical view]
PfamiPF13895. Ig_2. 1 hit.
PF07686. V-set. 1 hit.
[Graphical view]
SMARTiSM00409. IG. 3 hits.
SM00408. IGc2. 1 hit.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 3 hits.
PROSITEiPS50835. IG_LIKE. 2 hits.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

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

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9Y286-1) [UniParc]FASTAAdd to basket

Also known as: AIRM-1b

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
MLLLLLLPLL WGRERVEGQK SNRKDYSLTM QSSVTVQEGM CVHVRCSFSY
60 70 80 90 100
PVDSQTDSDP VHGYWFRAGN DISWKAPVAT NNPAWAVQEE TRDRFHLLGD
110 120 130 140 150
PQTKNCTLSI RDARMSDAGR YFFRMEKGNI KWNYKYDQLS VNVTALTHRP
160 170 180 190 200
NILIPGTLES GCFQNLTCSV PWACEQGTPP MISWMGTSVS PLHPSTTRSS
210 220 230 240 250
VLTLIPQPQH HGTSLTCQVT LPGAGVTTNR TIQLNVSYPP QNLTVTVFQG
260 270 280 290 300
EGTASTALGN SSSLSVLEGQ SLRLVCAVDS NPPARLSWTW RSLTLYPSQP
310 320 330 340 350
SNPLVLELQV HLGDEGEFTC RAQNSLGSQH VSLNLSLQQE YTGKMRPVSG
360 370 380 390 400
VLLGAVGGAG ATALVFLSFC VIFIVVRSCR KKSARPAADV GDIGMKDANT
410 420 430 440 450
IRGSASQGNL TESWADDNPR HHGLAAHSSG EEREIQYAPL SFHKGEPQDL
460
SGQEATNNEY SEIKIPK
Length:467
Mass (Da):51,143
Last modified:November 1, 1999 - v1
Checksum:i8AFE44462B001F52
GO
Isoform 2 (identifier: Q9Y286-2) [UniParc]FASTAAdd to basket

Also known as: AIRM-2

The sequence of this isoform differs from the canonical sequence as follows:
     145-238: ALTHRPNILI...NRTIQLNVSY → D

Show »
Length:374
Mass (Da):41,237
Checksum:i4E37C43130E19527
GO
Isoform 3 (identifier: Q9Y286-3) [UniParc]FASTAAdd to basket

Also known as: AIRM-3

The sequence of this isoform differs from the canonical sequence as follows:
     145-145: A → E
     146-467: Missing.

Note: No experimental confirmation available. May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.
Show »
Length:145
Mass (Da):16,812
Checksum:iB2754D9627528108
GO
Isoform 4 (identifier: Q9Y286-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     145-145: A → G
     146-467: Missing.

Note: No experimental confirmation available.
Show »
Length:145
Mass (Da):16,740
Checksum:iB1154D9627528108
GO

Sequence cautioni

The sequence AAF44346.1 differs from that shown. Reason: Frameshift at position 406. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti42 – 421V → A in AAF44346 (PubMed:10764831).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti215 – 2151L → P in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_035523

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei145 – 23894ALTHR…LNVSY → D in isoform 2. 3 PublicationsVSP_002555Add
BLAST
Alternative sequencei145 – 1451A → E in isoform 3. 1 PublicationVSP_002556
Alternative sequencei145 – 1451A → G in isoform 4. 1 PublicationVSP_002557
Alternative sequencei146 – 467322Missing in isoform 3 and isoform 4. 1 PublicationVSP_002558Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF170485 mRNA. Translation: AAF12759.1.
AJ007395 mRNA. Translation: CAB46011.1.
AJ130710 mRNA. Translation: CAB51126.1.
AJ130711 mRNA. Translation: CAB51127.1.
AJ130712 mRNA. Translation: CAB51128.1.
AJ130713 mRNA. Translation: CAB51129.1.
AF178981 mRNA. Translation: AAF44346.1. Frameshift.
AF193441 mRNA. Translation: AAF06790.1.
CCDSiCCDS12826.1. [Q9Y286-1]
CCDS42601.1. [Q9Y286-2]
CCDS62771.1. [Q9Y286-4]
RefSeqiNP_001264130.1. NM_001277201.1. [Q9Y286-4]
NP_055200.1. NM_014385.3. [Q9Y286-1]
NP_057627.2. NM_016543.3. [Q9Y286-2]
UniGeneiHs.655393.

Genome annotation databases

EnsembliENST00000305628; ENSP00000306757; ENSG00000168995. [Q9Y286-2]
ENST00000317643; ENSP00000323328; ENSG00000168995. [Q9Y286-1]
ENST00000536156; ENSP00000437609; ENSG00000168995. [Q9Y286-3]
ENST00000600577; ENSP00000472529; ENSG00000168995. [Q9Y286-4]
GeneIDi27036.
KEGGihsa:27036.
UCSCiuc002pvv.1. human. [Q9Y286-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Functional Glycomics Gateway - Glycan Binding

Siglec-7

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF170485 mRNA. Translation: AAF12759.1.
AJ007395 mRNA. Translation: CAB46011.1.
AJ130710 mRNA. Translation: CAB51126.1.
AJ130711 mRNA. Translation: CAB51127.1.
AJ130712 mRNA. Translation: CAB51128.1.
AJ130713 mRNA. Translation: CAB51129.1.
AF178981 mRNA. Translation: AAF44346.1. Frameshift.
AF193441 mRNA. Translation: AAF06790.1.
CCDSiCCDS12826.1. [Q9Y286-1]
CCDS42601.1. [Q9Y286-2]
CCDS62771.1. [Q9Y286-4]
RefSeqiNP_001264130.1. NM_001277201.1. [Q9Y286-4]
NP_055200.1. NM_014385.3. [Q9Y286-1]
NP_057627.2. NM_016543.3. [Q9Y286-2]
UniGeneiHs.655393.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1NKOX-ray1.45A19-150[»]
1O7SX-ray1.75A18-144[»]
1O7VX-ray1.90A18-144[»]
2DF3X-ray1.90A18-144[»]
2G5RX-ray1.60A18-144[»]
2HRLX-ray1.85A18-144[»]
ProteinModelPortaliQ9Y286.
SMRiQ9Y286. Positions 18-237, 254-343.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi117967. 5 interactions.
IntActiQ9Y286. 1 interaction.
STRINGi9606.ENSP00000323328.

PTM databases

iPTMnetiQ9Y286.
PhosphoSiteiQ9Y286.

Polymorphism and mutation databases

DMDMi25009269.

Proteomic databases

PaxDbiQ9Y286.
PRIDEiQ9Y286.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000305628; ENSP00000306757; ENSG00000168995. [Q9Y286-2]
ENST00000317643; ENSP00000323328; ENSG00000168995. [Q9Y286-1]
ENST00000536156; ENSP00000437609; ENSG00000168995. [Q9Y286-3]
ENST00000600577; ENSP00000472529; ENSG00000168995. [Q9Y286-4]
GeneIDi27036.
KEGGihsa:27036.
UCSCiuc002pvv.1. human. [Q9Y286-1]

Organism-specific databases

CTDi27036.
GeneCardsiSIGLEC7.
H-InvDBHIX0040323.
HGNCiHGNC:10876. SIGLEC7.
HPAiCAB025154.
MIMi604410. gene.
neXtProtiNX_Q9Y286.
PharmGKBiPA35777.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IJT6. Eukaryota.
ENOG410YKZU. LUCA.
GeneTreeiENSGT00760000119139.
HOGENOMiHOG000236324.
HOVERGENiHBG036161.
InParanoidiQ9Y286.
KOiK06739.
OMAiGQEATNN.
OrthoDBiEOG7W6WRM.
PhylomeDBiQ9Y286.
TreeFamiTF332441.

Enzyme and pathway databases

ReactomeiR-HSA-198933. Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.

Miscellaneous databases

EvolutionaryTraceiQ9Y286.
GeneWikiiSIGLEC7.
GenomeRNAii27036.
NextBioi49592.
PROiQ9Y286.
SOURCEiSearch...

Gene expression databases

BgeeiQ9Y286.
CleanExiHS_SIGLEC7.
ExpressionAtlasiQ9Y286. baseline and differential.
GenevisibleiQ9Y286. HS.

Family and domain databases

Gene3Di2.60.40.10. 3 hits.
InterProiIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR013106. Ig_V-set.
[Graphical view]
PfamiPF13895. Ig_2. 1 hit.
PF07686. V-set. 1 hit.
[Graphical view]
SMARTiSM00409. IG. 3 hits.
SM00408. IGc2. 1 hit.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 3 hits.
PROSITEiPS50835. IG_LIKE. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification and characterization of a novel siglec, siglec-7, expressed by human natural killer cells and monocytes."
    Nicoll G., Ni J., Liu D., Klenerman P., Munday J., Dubock S., Mattei M.-G., Crocker P.R.
    J. Biol. Chem. 274:34089-34095(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Dendritic cell.
  2. "Identification and molecular cloning of p75/AIRM1, a novel member of the sialoadhesin family that functions as an inhibitory receptor in human natural killer cells."
    Falco M., Biassoni R., Bottino C., Vitale M., Sivori S., Augugliaro R., Moretta L., Moretta A.
    J. Exp. Med. 190:793-802(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4), PHOSPHORYLATION, INTERACTION WITH PTPN6.
    Tissue: Lymphoid tissue.
  3. "Characterization of a novel siglec from dendritic cells."
    Zhang W., Wan T., Cao X.
    Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    Tissue: Dendritic cell.
  4. "Siglec-7: a sialic acid-binding lectin of the immunoglobulin superfamily."
    Angata T., Varki A.
    Glycobiology 10:431-438(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
  5. "Engagement of p75/AIRM1 or CD33 inhibits the proliferation of normal or leukemic myeloid cells."
    Vitale C., Romagnani C., Falco M., Ponte M., Vitale M., Moretta A., Bacigalupo A., Moretta L., Mingari M.C.
    Proc. Natl. Acad. Sci. U.S.A. 96:15091-15096(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. "Binding specificity of siglec7 to disialogangliosides of renal cell carcinoma: possible role of disialogangliosides in tumor progression."
    Ito A., Handa K., Withers D.A., Satoh M., Hakomori S.
    FEBS Lett. 498:116-120(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISIALOGANGLIOSIDE-BINDING.
  7. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-429, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  8. "High resolution crystal structures of Siglec-7. Insights into ligand specificity in the Siglec family."
    Alphey M.S., Attrill H., Crocker P.R., van Aalten D.M.
    J. Biol. Chem. 278:3372-3377(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 18-144, DISULFIDE BOND, GLYCOSYLATION AT ASN-105.
  9. "Structure of the saccharide-binding domain of the human natural killer cell inhibitory receptor p75/AIRM1."
    Dimasi N., Moretta A., Moretta L., Biassoni R., Mariuzza R.A.
    Acta Crystallogr. D 60:401-403(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 19-150, DISULFIDE BOND.
  10. "The structure of siglec-7 in complex with sialosides: leads for rational structure-based inhibitor design."
    Attrill H., Takazawa H., Witt S., Kelm S., Isecke R., Brossmer R., Ando T., Ishida H., Kiso M., Crocker P.R., van Aalten D.M.
    Biochem. J. 397:271-278(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 18-144 IN COMPLEX WITH SIALYLATED LIGAND, GLYCOSYLATION AT ASN-105, DISULFIDE BOND.
  11. "Siglec-7 undergoes a major conformational change when complexed with the alpha(2,8)-disialylganglioside GT1b."
    Attrill H., Imamura A., Sharma R.S., Kiso M., Crocker P.R., van Aalten D.M.
    J. Biol. Chem. 281:32774-32783(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 18-144 IN COMPLEX WITH ALPHA(2,8)-DISIALYLATED LIGAND GT1B, GLYCOSYLATION AT ASN-105, DISULFIDE BOND.
  12. Cited for: VARIANT [LARGE SCALE ANALYSIS] PRO-215.

Entry informationi

Entry nameiSIGL7_HUMAN
AccessioniPrimary (citable) accession number: Q9Y286
Secondary accession number(s): Q9NZQ1
, Q9UJ86, Q9UJ87, Q9Y502
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 8, 2002
Last sequence update: November 1, 1999
Last modified: May 11, 2016
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. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.