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Protein

T-lymphocyte surface antigen Ly-9

Gene

LY9

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

Functioni

Self-ligand receptor of the signaling lymphocytic activation molecule (SLAM) family. SLAM receptors triggered by homo- or heterotypic cell-cell interactions are modulating the activation and differentiation of a wide variety of immune cells and thus are involved in the regulation and interconnection of both innate and adaptive immune response. Activities are controlled by presence or absence of small cytoplasmic adapter proteins, SH2D1A/SAP and/or SH2D1B/EAT-2. May participate in adhesion reactions between T lymphocytes and accessory cells by homophilic interaction. Promotes T-cell differentiation into a helper T-cell Th17 phenotype leading to increased IL-17 secretion; the costimulatory activity requires SH2D1A (PubMed:22184727). Promotes recruitment of RORC to the IL-17 promoter (PubMed:22989874). May be involved in the maintenance of peripheral cell tolerance by serving as a negative regulator of the immune response. May disable autoantibody responses and inhibit IFN-gamma secretion by CD4+ T-cells. May negatively regulate the size of thymic innate CD8+ T-cells and the development of invariant natural killer T (iNKT) cells (By similarity).By similarity2 Publications

GO - Biological processi

  • innate immune response Source: UniProtKB-KW
  • positive regulation of interleukin-17 production Source: UniProtKB
  • T-helper 17 cell lineage commitment Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Adaptive immunity, Cell adhesion, Immunity, Innate immunity

Names & Taxonomyi

Protein namesi
Recommended name:
T-lymphocyte surface antigen Ly-9
Alternative name(s):
Cell surface molecule Ly-9
Lymphocyte antigen 9
SLAM family member 3
Short name:
SLAMF3
Signaling lymphocytic activation molecule 3
CD_antigen: CD229
Gene namesi
Name:LY9
ORF Names:CDABP0070
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:6730. LY9.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini48 – 454407ExtracellularSequence analysisAdd
BLAST
Transmembranei455 – 47622HelicalSequence analysisAdd
BLAST
Topological domaini477 – 655179CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • cell surface Source: Ensembl
  • integral component of membrane Source: UniProtKB-KW
  • plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA30494.

Polymorphism and mutation databases

BioMutaiLY9.
DMDMi71152965.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 4747Sequence analysisAdd
BLAST
Chaini48 – 655608T-lymphocyte surface antigen Ly-9PRO_0000014851Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi68 – 681N-linked (GlcNAc...)Sequence analysis
Glycosylationi95 – 951N-linked (GlcNAc...)Sequence analysis
Glycosylationi120 – 1201N-linked (GlcNAc...)Sequence analysis
Glycosylationi169 – 1691N-linked (GlcNAc...)Sequence analysis
Disulfide bondi172 ↔ 242PROSITE-ProRule annotation
Glycosylationi173 – 1731N-linked (GlcNAc...)Sequence analysis
Disulfide bondi178 ↔ 222PROSITE-ProRule annotation
Glycosylationi285 – 2851N-linked (GlcNAc...)1 Publication
Disulfide bondi377 ↔ 446PROSITE-ProRule annotation
Disulfide bondi383 ↔ 427PROSITE-ProRule annotation
Glycosylationi413 – 4131N-linked (GlcNAc...)Sequence analysis
Glycosylationi424 – 4241N-linked (GlcNAc...)Sequence analysis
Modified residuei603 – 6031Phosphotyrosine Probable2 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiQ9HBG7.
PaxDbiQ9HBG7.
PRIDEiQ9HBG7.

PTM databases

iPTMnetiQ9HBG7.
PhosphoSiteiQ9HBG7.
SwissPalmiQ9HBG7.

Expressioni

Tissue specificityi

Increased surface expression on T-cells of systemic lupus erythematosus (SLE) patients.1 Publication

Gene expression databases

BgeeiQ9HBG7.
CleanExiHS_LY9.
ExpressionAtlasiQ9HBG7. baseline and differential.
GenevisibleiQ9HBG7. HS.

Organism-specific databases

HPAiHPA050917.

Interactioni

Subunit structurei

Interacts with SH2D1A, SH2D1B and INPP5D. Interacts (via phosphorylated cytoplasmic domain) with PTPN11; the interaction is blocked by SH2D1A.3 Publications

Protein-protein interaction databases

BioGridi110241. 4 interactions.
IntActiQ9HBG7. 3 interactions.
STRINGi9606.ENSP00000357020.

Structurei

3D structure databases

ProteinModelPortaliQ9HBG7.
SMRiQ9HBG7. Positions 49-229, 257-446.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini48 – 158111Ig-like V-type 1Add
BLAST
Domaini159 – 23577Ig-like C2-type 1Add
BLAST
Domaini251 – 363113Ig-like V-type 2Add
BLAST
Domaini364 – 45289Ig-like C2-type 2Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi601 – 6066ITSM 1By similarity
Motifi624 – 6296ITSM 2By similarity

Domaini

The ITSMs (immunoreceptor tyrosine-based switch motifs) with the consensus sequence T-X-Y-X-X-[VI] present in SLAM family receptors have overlapping specificity for activating and inhibitory SH2 domain-containing binding partners. Especially they mediate the interaction with the SH2 domain of SH2D1A and SH2D1B. A 'three-pronged' mechanism is proposed involving threonine (position -2), phosphorylated tyrosine (position 0) and valine/isoleucine (position +3).By similarity1 Publication

Sequence similaritiesi

Keywords - Domaini

Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410JJ3F. Eukaryota.
ENOG410ZAYK. LUCA.
GeneTreeiENSGT00530000063114.
HOGENOMiHOG000143391.
HOVERGENiHBG030765.
InParanoidiQ9HBG7.
KOiK06570.
OMAiYHAYVCS.
OrthoDBiEOG77HDFC.
PhylomeDBiQ9HBG7.
TreeFamiTF334964.

Family and domain databases

Gene3Di2.60.40.10. 4 hits.
InterProiIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
[Graphical view]
SMARTiSM00409. IG. 2 hits.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 4 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

Note: Experimental confirmation may be lacking for some isoforms.

Isoform 1 (identifier: Q9HBG7-1) [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
MVAPKSHTDD WAPGPFSSKP QRSQLQIFSS VLQTSLLFLL MGLRASGKDS
60 70 80 90 100
APTVVSGILG GSVTLPLNIS VDTEIENVIW IGPKNALAFA RPKENVTIMV
110 120 130 140 150
KSYLGRLDIT KWSYSLCISN LTLNDAGSYK AQINQRNFEV TTEEEFTLFV
160 170 180 190 200
YEQLQEPQVT MKSVKVSENF SCNITLMCSV KGAEKSVLYS WTPREPHASE
210 220 230 240 250
SNGGSILTVS RTPCDPDLPY ICTAQNPVSQ RSSLPVHVGQ FCTDPGASRG
260 270 280 290 300
GTTGETVVGV LGEPVTLPLA LPACRDTEKV VWLFNTSIIS KEREEAATAD
310 320 330 340 350
PLIKSRDPYK NRVWVSSQDC SLKISQLKIE DAGPYHAYVC SEASSVTSMT
360 370 380 390 400
HVTLLIYRRL RKPKITWSLR HSEDGICRIS LTCSVEDGGN TVMYTWTPLQ
410 420 430 440 450
KEAVVSQGES HLNVSWRSSE NHPNLTCTAS NPVSRSSHQF LSENICSGPE
460 470 480 490 500
RNTKLWIGLF LMVCLLCVGI FSWCIWKRKG RCSVPAFCSS QAEAPADTPE
510 520 530 540 550
PTAGHTLYSV LSQGYEKLDT PLRPARQQPT PTSDSSSDSN LTTEEDEDRP
560 570 580 590 600
EVHKPISGRY EVFDQVTQEG AGHDPAPEGQ ADYDPVTPYV TEVESVVGEN
610 620 630 640 650
TMYAQVFNLQ GKTPVSQKEE SSATIYCSIR KPQVVPPPQQ NDLEIPESPT

YENFT
Length:655
Mass (Da):72,139
Last modified:July 19, 2005 - v3
Checksum:i84ABA3056D69E80A
GO
Isoform 2 (identifier: Q9HBG7-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     500-513: Missing.

Show »
Length:641
Mass (Da):70,655
Checksum:i8649951FCE64465C
GO
Isoform 3 (identifier: Q9HBG7-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     359-448: Missing.
     500-513: Missing.
     524-554: PARQQPTPTSDSSSDSNLTTEEDEDRPEVHK → Q

Show »
Length:521
Mass (Da):57,320
Checksum:i615B60DC9AB6766E
GO
Isoform 4 (identifier: Q9HBG7-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     152-193: EQLQEPQVTM...EKSVLYSWTP → APFIEKLSVH...AEPRVSVREG

Note: No experimental confirmation available.
Show »
Length:655
Mass (Da):71,961
Checksum:iB096694A12285C5C
GO

Sequence cautioni

The sequence CAH72360.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence CAH73509.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti171 – 1711Missing in AAG14995 (PubMed:10970093).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti602 – 6021M → V Decreases interaction with SH2D1A and INPP5D 2-fold, reduced T-cell response. 3 Publications
Corresponds to variant rs509749 [ dbSNP | Ensembl ].
VAR_033612

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei152 – 19342EQLQE…YSWTP → APFIEKLSVHVIEGDHRTLL EGSGLESIISTLAEPRVSVR EG in isoform 4. 1 PublicationVSP_043328Add
BLAST
Alternative sequencei359 – 44890Missing in isoform 3. 1 PublicationVSP_002524Add
BLAST
Alternative sequencei500 – 51314Missing in isoform 2 and isoform 3. 2 PublicationsVSP_002525Add
BLAST
Alternative sequencei524 – 55431PARQQ…PEVHK → Q in isoform 3. 1 PublicationVSP_002526Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF244129 mRNA. Translation: AAG14995.1.
AK292048 mRNA. Translation: BAF84737.1.
AL354714, AL121985 Genomic DNA. Translation: CAH72360.1. Sequence problems.
AL121985, AL354714 Genomic DNA. Translation: CAH73509.1. Sequence problems.
AL121985 Genomic DNA. Translation: CAH73510.1.
CH471121 Genomic DNA. Translation: EAW52699.1.
BC064485 mRNA. Translation: AAH64485.1.
L42621 mRNA. Translation: AAA92623.1.
AY007142 mRNA. Translation: AAG02002.1.
CCDSiCCDS30916.1. [Q9HBG7-1]
CCDS65695.1. [Q9HBG7-2]
RefSeqiNP_001028839.1. NM_001033667.2.
NP_001248385.1. NM_001261456.1. [Q9HBG7-2]
NP_002339.2. NM_002348.3. [Q9HBG7-1]
UniGeneiHs.403857.

Genome annotation databases

EnsembliENST00000263285; ENSP00000263285; ENSG00000122224. [Q9HBG7-1]
ENST00000368037; ENSP00000357016; ENSG00000122224. [Q9HBG7-2]
GeneIDi4063.
KEGGihsa:4063.
UCSCiuc001fwt.5. human. [Q9HBG7-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF244129 mRNA. Translation: AAG14995.1.
AK292048 mRNA. Translation: BAF84737.1.
AL354714, AL121985 Genomic DNA. Translation: CAH72360.1. Sequence problems.
AL121985, AL354714 Genomic DNA. Translation: CAH73509.1. Sequence problems.
AL121985 Genomic DNA. Translation: CAH73510.1.
CH471121 Genomic DNA. Translation: EAW52699.1.
BC064485 mRNA. Translation: AAH64485.1.
L42621 mRNA. Translation: AAA92623.1.
AY007142 mRNA. Translation: AAG02002.1.
CCDSiCCDS30916.1. [Q9HBG7-1]
CCDS65695.1. [Q9HBG7-2]
RefSeqiNP_001028839.1. NM_001033667.2.
NP_001248385.1. NM_001261456.1. [Q9HBG7-2]
NP_002339.2. NM_002348.3. [Q9HBG7-1]
UniGeneiHs.403857.

3D structure databases

ProteinModelPortaliQ9HBG7.
SMRiQ9HBG7. Positions 49-229, 257-446.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110241. 4 interactions.
IntActiQ9HBG7. 3 interactions.
STRINGi9606.ENSP00000357020.

PTM databases

iPTMnetiQ9HBG7.
PhosphoSiteiQ9HBG7.
SwissPalmiQ9HBG7.

Polymorphism and mutation databases

BioMutaiLY9.
DMDMi71152965.

Proteomic databases

MaxQBiQ9HBG7.
PaxDbiQ9HBG7.
PRIDEiQ9HBG7.

Protocols and materials databases

DNASUi4063.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000263285; ENSP00000263285; ENSG00000122224. [Q9HBG7-1]
ENST00000368037; ENSP00000357016; ENSG00000122224. [Q9HBG7-2]
GeneIDi4063.
KEGGihsa:4063.
UCSCiuc001fwt.5. human. [Q9HBG7-1]

Organism-specific databases

CTDi4063.
GeneCardsiLY9.
HGNCiHGNC:6730. LY9.
HPAiHPA050917.
MIMi600684. gene.
neXtProtiNX_Q9HBG7.
PharmGKBiPA30494.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410JJ3F. Eukaryota.
ENOG410ZAYK. LUCA.
GeneTreeiENSGT00530000063114.
HOGENOMiHOG000143391.
HOVERGENiHBG030765.
InParanoidiQ9HBG7.
KOiK06570.
OMAiYHAYVCS.
OrthoDBiEOG77HDFC.
PhylomeDBiQ9HBG7.
TreeFamiTF334964.

Miscellaneous databases

GeneWikiiLY9.
GenomeRNAii4063.
NextBioi15926.
PROiQ9HBG7.
SOURCEiSearch...

Gene expression databases

BgeeiQ9HBG7.
CleanExiHS_LY9.
ExpressionAtlasiQ9HBG7. baseline and differential.
GenevisibleiQ9HBG7. HS.

Family and domain databases

Gene3Di2.60.40.10. 4 hits.
InterProiIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
[Graphical view]
SMARTiSM00409. IG. 2 hits.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 4 hits.
PROSITEiPS50835. IG_LIKE. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Gene structure of the mouse leukocyte cell surface molecule Ly9."
    Tovar V., de la Fuente M.A., Pizcueta P., Bosch J., Engel P.
    Immunogenetics 51:788-793(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT VAL-602.
  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] (ISOFORM 1).
    Tissue: Spleen.
  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] (ISOFORM 4).
    Tissue: Blood.
  6. "Isolation and characterization of cDNA clones for Humly9: the human homologue of mouse Ly9."
    Sandrin M.S., Henning M.M., Lo M.F., Baker E., Sutherland G.R., McKenzie I.F.
    Immunogenetics 43:13-19(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 32-654 (ISOFORM 2), VARIANT VAL-602.
  7. "Pediatric leukemia cDNA sequencing project."
    Zhou J., Yu W., Tang H., Mei G., Tsang Y.T.M., Bouck J., Gibbs R.A., Margolin J.F.
    Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 99-655 (ISOFORM 3).
    Tissue: Leukemia.
  8. "Cell surface receptors Ly-9 and CD84 recruit the X-linked lymphoproliferative disease gene product SAP."
    Sayos J., Martin M., Chen A., Simarro M., Howie D., Morra M., Engel P., Terhorst C.
    Blood 97:3867-3874(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SH2D1A AND PTPN11, PHOSPHORYLATION.
  9. "Dual functional roles for the X-linked lymphoproliferative syndrome gene product SAP/SH2D1A in signaling through the signaling lymphocyte activation molecule (SLAM) family of immune receptors."
    Li C., Iosef C., Jia C.Y., Han V.K., Li S.S.
    J. Biol. Chem. 278:3852-3859(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SH2D1A; SH2D1B AND INPP5D, PHOSPHORYLATION AT TYR-603.
  10. "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-285.
    Tissue: Leukemic T-cell.
  11. "CD3-T cell receptor co-stimulation through SLAMF3 and SLAMF6 receptors enhances RORgammat recruitment to the IL17A promoter in human T lymphocytes."
    Chatterjee M., Hedrich C.M., Rauen T., Ioannidis C., Terhorst C., Tsokos G.C.
    J. Biol. Chem. 287:38168-38177(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  12. "Increased expression of SLAM receptors SLAMF3 and SLAMF6 in systemic lupus erythematosus T lymphocytes promotes Th17 differentiation."
    Chatterjee M., Rauen T., Kis-Toth K., Kyttaris V.C., Hedrich C.M., Terhorst C., Tsokos G.C.
    J. Immunol. 188:1206-1212(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY.
  13. "A polymorphism in a phosphotyrosine signalling motif of CD229 (Ly9, SLAMF3) alters SH2 domain binding and T-cell activation."
    Margraf S., Garner L.I., Wilson T.J., Brown M.H.
    Immunology 146:392-400(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SH2D1A AND INPP5D, CHARACTERIZATION OF VARIANT VAL-602, DOMAIN, PHOSPHORYLATION AT TYR-603.

Entry informationi

Entry nameiLY9_HUMAN
AccessioniPrimary (citable) accession number: Q9HBG7
Secondary accession number(s): A8K7N3
, Q14775, Q5VYI3, Q6P2J4, Q9H4N5, Q9NQ24
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 20, 2002
Last sequence update: July 19, 2005
Last modified: March 16, 2016
This is version 128 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

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 1
    Human chromosome 1: 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. 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.