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Q13291

- SLAF1_HUMAN

UniProt

Q13291 - SLAF1_HUMAN

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Protein

Signaling lymphocytic activation molecule

Gene

SLAMF1

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

Functioni

High-affinity self-ligand important in bidirectional T-cell to B-cell stimulation. SLAM-induced signal-transduction events in T-lymphocytes are different from those in B-cells. Two modes of SLAM signaling are likely to exist: one in which the inhibitor SH2D1A acts as a negative regulator and another in which protein-tyrosine phosphatase 2C (PTPN11)-dependent signal transduction operates.

GO - Molecular functioni

  1. antigen binding Source: ProtInc
  2. transmembrane signaling receptor activity Source: ProtInc

GO - Biological processi

  1. lymphocyte activation Source: InterPro
  2. positive regulation of cell proliferation Source: ProtInc
  3. regulation of catalytic activity Source: Ensembl
  4. regulation of vesicle fusion Source: Ensembl
  5. signal transduction Source: GOC
  6. viral process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Biological processi

Host-virus interaction

Names & Taxonomyi

Protein namesi
Recommended name:
Signaling lymphocytic activation molecule
Alternative name(s):
CDw150
IPO-3
CD_antigen: CD150
Gene namesi
Name:SLAMF1
Synonyms:SLAM
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:10903. SLAMF1.

Subcellular locationi

Cell membrane; Single-pass type I membrane protein
Note: Present on the surface of B-cells and T-cells.

GO - Cellular componenti

  1. external side of plasma membrane Source: Ensembl
  2. extracellular vesicular exosome Source: UniProt
  3. integral component of membrane Source: UniProtKB-KW
  4. phagocytic vesicle Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA35803.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020Sequence AnalysisAdd
BLAST
Chaini21 – 335315Signaling lymphocytic activation moleculePRO_0000014959Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi53 – 531N-linked (GlcNAc...)Sequence Analysis
Glycosylationi57 – 571N-linked (GlcNAc...)Sequence Analysis
Glycosylationi102 – 1021N-linked (GlcNAc...)Sequence Analysis
Glycosylationi125 – 1251N-linked (GlcNAc...)Sequence Analysis
Glycosylationi150 – 1501N-linked (GlcNAc...)Sequence Analysis
Glycosylationi155 – 1551N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi158 ↔ 228PROSITE-ProRule annotation
Disulfide bondi164 ↔ 209PROSITE-ProRule annotation
Glycosylationi189 – 1891N-linked (GlcNAc...)Sequence Analysis
Glycosylationi217 – 2171N-linked (GlcNAc...)Sequence Analysis

Post-translational modificationi

Phosphorylated by FYN.

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiQ13291.
PRIDEiQ13291.

PTM databases

PhosphoSiteiQ13291.

Expressioni

Tissue specificityi

Constitutively expressed on peripheral blood memory T-cells, T-cell clones, immature thymocytes and a proportion of B-cells, and is rapidly induced on naive T-cells after activation.

Gene expression databases

BgeeiQ13291.
CleanExiHS_SLAMF1.
ExpressionAtlasiQ13291. baseline and differential.
GenevestigatoriQ13291.

Organism-specific databases

HPAiCAB002438.

Interactioni

Subunit structurei

Interacts (via cytoplasmic domain) with SH2D1A, SH2D1B and with PTPN11. Interacts with INPP5D/SHIP1. Binds to Measles virus H protein and acts as a receptor for this virus.6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
HQ786F22EBI-4315002,EBI-5323300From a different organism.
SH2D1AO6088011EBI-4315002,EBI-6983382

Protein-protein interaction databases

BioGridi112395. 63 interactions.
DIPiDIP-40767N.
IntActiQ13291. 5 interactions.
MINTiMINT-113752.
STRINGi9606.ENSP00000306190.

Structurei

Secondary structure

1
335
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi278 – 2814

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1D4TX-ray1.10B276-286[»]
1D4WX-ray1.80C/D276-286[»]
1I3ZX-ray2.15B273-286[»]
1KA6NMR-B276-282[»]
1KA7NMR-B275-286[»]
1M27X-ray2.50B276-286[»]
2DZFmodel-@1-335[»]
2IE9model-@1-335[»]
2IFLmodel-@3-335[»]
2IG5model-@1-335[»]
ProteinModelPortaliQ13291.
SMRiQ13291. Positions 32-140, 142-219.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ13291.

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini21 – 237217ExtracellularSequence AnalysisAdd
BLAST
Topological domaini259 – 33577CytoplasmicSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei238 – 25821HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini29 – 138110Ig-like V-typeAdd
BLAST
Domaini144 – 22380Ig-like C2-typeAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi281 – 2866SH2-bindingSequence Analysis
Motifi307 – 3126SH2-bindingSequence Analysis
Motifi327 – 3326SH2-bindingSequence Analysis

Domaini

The most membrane-proximal SH2-binding motif interacts with SH2 domain of SH2D1A and does not need to be phosphorylated on tyrosine residues.

Sequence similaritiesi

Keywords - Domaini

Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG40451.
GeneTreeiENSGT00510000048858.
HOGENOMiHOG000125310.
HOVERGENiHBG054224.
InParanoidiQ13291.
KOiK06536.
OMAiLYEQVST.
OrthoDBiEOG7Q8CQJ.
PhylomeDBiQ13291.
TreeFamiTF334964.

Family and domain databases

InterProiIPR007110. Ig-like_dom.
IPR010407. Sig_lymph_act_molc_N.
IPR015631. SLAM_fam_rcpts.
[Graphical view]
PANTHERiPTHR12080. PTHR12080. 1 hit.
PfamiPF06214. SLAM. 1 hit.
[Graphical view]
ProDomiPD090491. Sig_lymph_act_molc_N. 1 hit.
[Graphical view] [Entries sharing at least one domain]
PROSITEiPS50835. IG_LIKE. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

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

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q13291-1) [UniParc]FASTAAdd to Basket

Also known as: Long

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
MDPKGLLSLT FVLFLSLAFG ASYGTGGRMM NCPKILRQLG SKVLLPLTYE
60 70 80 90 100
RINKSMNKSI HIVVTMAKSL ENSVENKIVS LDPSEAGPPR YLGDRYKFYL
110 120 130 140 150
ENLTLGIRES RKEDEGWYLM TLEKNVSVQR FCLQLRLYEQ VSTPEIKVLN
160 170 180 190 200
KTQENGTCTL ILGCTVEKGD HVAYSWSEKA GTHPLNPANS SHLLSLTLGP
210 220 230 240 250
QHADNIYICT VSNPISNNSQ TFSPWPGCRT DPSETKPWAV YAGLLGGVIM
260 270 280 290 300
ILIMVVILQL RRRGKTNHYQ TTVEKKSLTI YAQVQKPGPL QKKLDSFPAQ
310 320 330
DPCTTIYVAA TEPVPESVQE TNSITVYASV TLPES
Length:335
Mass (Da):37,231
Last modified:November 1, 1996 - v1
Checksum:iBFB0F27EA31D8C04
GO
Isoform 2 (identifier: Q13291-2) [UniParc]FASTAAdd to Basket

Also known as: Short

The sequence of this isoform differs from the canonical sequence as follows:
     289-298: PLQKKLDSFP → DTHHQTSDLF
     299-335: Missing.

Show »
Length:298
Mass (Da):33,365
Checksum:iDCE97AC03ACDC045
GO
Isoform 3 (identifier: Q13291-3) [UniParc]FASTAAdd to Basket

Also known as: Secreted

The sequence of this isoform differs from the canonical sequence as follows:
     234-263: Missing.

Show »
Length:305
Mass (Da):33,839
Checksum:iF5CBDC25B2E19967
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti11 – 111F → L.
Corresponds to variant rs2295612 [ dbSNP | Ensembl ].
VAR_021924
Natural varianti81 – 811L → F in a breast cancer sample; somatic mutation. 1 Publication
VAR_035524
Natural varianti333 – 3331P → T.
Corresponds to variant rs3796504 [ dbSNP | Ensembl ].
VAR_021925

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei234 – 26330Missing in isoform 3. 1 PublicationVSP_002567Add
BLAST
Alternative sequencei289 – 29810PLQKKLDSFP → DTHHQTSDLF in isoform 2. 1 PublicationVSP_002568
Alternative sequencei299 – 33537Missing in isoform 2. 1 PublicationVSP_002569Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U33017 mRNA. Translation: AAA75380.1.
AL121985, AL138930 Genomic DNA. Translation: CAH73505.1.
AL138930, AL121985 Genomic DNA. Translation: CAI15154.1.
CH471121 Genomic DNA. Translation: EAW52706.1.
BC132792 mRNA. Translation: AAI32793.1.
AF252305 Genomic DNA. Translation: AAG10434.1.
CCDSiCCDS1207.1. [Q13291-1]
PIRiS58892.
RefSeqiNP_003028.1. NM_003037.3. [Q13291-1]
XP_005245513.1. XM_005245456.1. [Q13291-3]
UniGeneiHs.523660.

Genome annotation databases

EnsembliENST00000302035; ENSP00000306190; ENSG00000117090. [Q13291-1]
GeneIDi6504.
KEGGihsa:6504.
UCSCiuc001fwl.4. human. [Q13291-1]

Polymorphism databases

DMDMi9297047.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U33017 mRNA. Translation: AAA75380.1 .
AL121985 , AL138930 Genomic DNA. Translation: CAH73505.1 .
AL138930 , AL121985 Genomic DNA. Translation: CAI15154.1 .
CH471121 Genomic DNA. Translation: EAW52706.1 .
BC132792 mRNA. Translation: AAI32793.1 .
AF252305 Genomic DNA. Translation: AAG10434.1 .
CCDSi CCDS1207.1. [Q13291-1 ]
PIRi S58892.
RefSeqi NP_003028.1. NM_003037.3. [Q13291-1 ]
XP_005245513.1. XM_005245456.1. [Q13291-3 ]
UniGenei Hs.523660.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1D4T X-ray 1.10 B 276-286 [» ]
1D4W X-ray 1.80 C/D 276-286 [» ]
1I3Z X-ray 2.15 B 273-286 [» ]
1KA6 NMR - B 276-282 [» ]
1KA7 NMR - B 275-286 [» ]
1M27 X-ray 2.50 B 276-286 [» ]
2DZF model - @ 1-335 [» ]
2IE9 model - @ 1-335 [» ]
2IFL model - @ 3-335 [» ]
2IG5 model - @ 1-335 [» ]
ProteinModelPortali Q13291.
SMRi Q13291. Positions 32-140, 142-219.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 112395. 63 interactions.
DIPi DIP-40767N.
IntActi Q13291. 5 interactions.
MINTi MINT-113752.
STRINGi 9606.ENSP00000306190.

PTM databases

PhosphoSitei Q13291.

Polymorphism databases

DMDMi 9297047.

Proteomic databases

PaxDbi Q13291.
PRIDEi Q13291.

Protocols and materials databases

DNASUi 6504.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000302035 ; ENSP00000306190 ; ENSG00000117090 . [Q13291-1 ]
GeneIDi 6504.
KEGGi hsa:6504.
UCSCi uc001fwl.4. human. [Q13291-1 ]

Organism-specific databases

CTDi 6504.
GeneCardsi GC01M160577.
HGNCi HGNC:10903. SLAMF1.
HPAi CAB002438.
MIMi 603492. gene.
neXtProti NX_Q13291.
PharmGKBi PA35803.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG40451.
GeneTreei ENSGT00510000048858.
HOGENOMi HOG000125310.
HOVERGENi HBG054224.
InParanoidi Q13291.
KOi K06536.
OMAi LYEQVST.
OrthoDBi EOG7Q8CQJ.
PhylomeDBi Q13291.
TreeFami TF334964.

Miscellaneous databases

EvolutionaryTracei Q13291.
GeneWikii SLAMF1.
GenomeRNAii 6504.
NextBioi 25289.
PROi Q13291.
SOURCEi Search...

Gene expression databases

Bgeei Q13291.
CleanExi HS_SLAMF1.
ExpressionAtlasi Q13291. baseline and differential.
Genevestigatori Q13291.

Family and domain databases

InterProi IPR007110. Ig-like_dom.
IPR010407. Sig_lymph_act_molc_N.
IPR015631. SLAM_fam_rcpts.
[Graphical view ]
PANTHERi PTHR12080. PTHR12080. 1 hit.
Pfami PF06214. SLAM. 1 hit.
[Graphical view ]
ProDomi PD090491. Sig_lymph_act_molc_N. 1 hit.
[Graphical view ] [Entries sharing at least one domain ]
PROSITEi PS50835. IG_LIKE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3).
    Tissue: T-cell.
  2. "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].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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 1).
    Tissue: Testis.
  5. "Absence of SLAM mutations in EBV-associated lymphoproliferative disease patients."
    Ferrand V., Li C., Romeo G., Yin L.
    J. Med. Virol. 70:131-136(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 265-288.
  6. "CDw150 associates with src-homology 2-containing inositol phosphatase and modulates CD95-mediated apoptosis."
    Mikhalap S.V., Shlapatska L.M., Berdova A.G., Law C.L., Clark E.A., Sidorenko S.P.
    J. Immunol. 162:5719-5727(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH INPP5D.
  7. "SLAM (CDw150) is a cellular receptor for measles virus."
    Tatsuo H., Ono N., Tanaka K., Yanagi Y.
    Nature 406:893-897(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MEASLES VIRUS HN PROTEIN, DOMAIN IG-LIKE V-TYPE.
  8. "The X-linked lymphoproliferative-disease gene product SAP regulates signals induced through the co-receptor SLAM."
    Sayos J., Wu C., Morra M., Wang N., Zhang X., Allen D., van Schaik S., Notarangelo L., Geha R., Roncarolo M.G., Oettgen H., de Vries J.E., Aversa G., Terhorst C.
    Nature 395:462-469(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.1 ANGSTROMS) OF 276-286 IN COMPLEX WITH SH2D1A.
  9. "Structural basis for the interaction of the free SH2 domain EAT-2 with SLAM receptors in hematopoietic cells."
    Morra M., Lu J., Poy F., Martin M., Sayos J., Calpe S., Gullo C., Howie D., Rietdijk S., Thompson A., Coyle A.J., Denny C., Yaffe M.B., Engel P., Eck M.J., Terhorst C.
    EMBO J. 20:5840-5852(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 273-286 IN COMPLEX WITH SH2D1B, INTERACTION WITH SH2D1B.
  10. "A 'three-pronged' binding mechanism for the SAP/SH2D1A SH2 domain: structural basis and relevance to the XLP syndrome."
    Hwang P.M., Li C., Morra M., Lillywhite J., Muhandiram D.R., Gertler F., Terhorst C., Kay L.E., Pawson T., Forman-Kay J.D., Li S.-C.
    EMBO J. 21:314-323(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 276-282 IN COMPLEX WITH SH2D1A.
  11. Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 276-286 IN COMPLEX WITH SH2D1A AND FYN.
  12. Cited for: VARIANT [LARGE SCALE ANALYSIS] PHE-81.

Entry informationi

Entry nameiSLAF1_HUMAN
AccessioniPrimary (citable) accession number: Q13291
Secondary accession number(s): Q5W172, Q9HBE8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: November 1, 1996
Last modified: October 29, 2014
This is version 138 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 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3