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Q13291 (SLAF1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 136. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Signaling lymphocytic activation molecule
Alternative name(s):
CDw150
IPO-3
CD_antigen=CD150
Gene names
Name:SLAMF1
Synonyms:SLAM
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length335 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subunit structure

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. Ref.6 Ref.7 Ref.9

Subcellular location

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

Tissue specificity

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.

Domain

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

Post-translational modification

Phosphorylated by FYN.

Sequence similarities

Contains 1 Ig-like C2-type (immunoglobulin-like) domain.

Contains 1 Ig-like V-type (immunoglobulin-like) domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

HQ786F22EBI-4315002,EBI-5323300From a different organism.
SH2D1AO6088011EBI-4315002,EBI-6983382

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q13291-1)

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.
Isoform 2 (identifier: Q13291-2)

Also known as: Short;

The sequence of this isoform differs from the canonical sequence as follows:
     289-298: PLQKKLDSFP → DTHHQTSDLF
     299-335: Missing.
Isoform 3 (identifier: Q13291-3)

Also known as: Secreted;

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Potential
Chain21 – 335315Signaling lymphocytic activation molecule
PRO_0000014959

Regions

Topological domain21 – 237217Extracellular Potential
Transmembrane238 – 25821Helical; Potential
Topological domain259 – 33577Cytoplasmic Potential
Domain144 – 22380Ig-like C2-type
Domain? – 152Ig-like V-type
Motif281 – 2866SH2-binding Potential
Motif307 – 3126SH2-binding Potential
Motif327 – 3326SH2-binding Potential

Amino acid modifications

Glycosylation531N-linked (GlcNAc...) Potential
Glycosylation571N-linked (GlcNAc...) Potential
Glycosylation1021N-linked (GlcNAc...) Potential
Glycosylation1251N-linked (GlcNAc...) Potential
Glycosylation1501N-linked (GlcNAc...) Potential
Glycosylation1551N-linked (GlcNAc...) Potential
Glycosylation1891N-linked (GlcNAc...) Potential
Glycosylation2171N-linked (GlcNAc...) Potential
Disulfide bond158 ↔ 228 By similarity
Disulfide bond164 ↔ 209 By similarity

Natural variations

Alternative sequence234 – 26330Missing in isoform 3.
VSP_002567
Alternative sequence289 – 29810PLQKKLDSFP → DTHHQTSDLF in isoform 2.
VSP_002568
Alternative sequence299 – 33537Missing in isoform 2.
VSP_002569
Natural variant111F → L.
Corresponds to variant rs2295612 [ dbSNP | Ensembl ].
VAR_021924
Natural variant811L → F in a breast cancer sample; somatic mutation. Ref.12
VAR_035524
Natural variant3331P → T.
Corresponds to variant rs3796504 [ dbSNP | Ensembl ].
VAR_021925

Secondary structure

... 335
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (Long) [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: BFB0F27EA31D8C04

FASTA33537,231
        10         20         30         40         50         60 
MDPKGLLSLT FVLFLSLAFG ASYGTGGRMM NCPKILRQLG SKVLLPLTYE RINKSMNKSI 

        70         80         90        100        110        120 
HIVVTMAKSL ENSVENKIVS LDPSEAGPPR YLGDRYKFYL ENLTLGIRES RKEDEGWYLM 

       130        140        150        160        170        180 
TLEKNVSVQR FCLQLRLYEQ VSTPEIKVLN KTQENGTCTL ILGCTVEKGD HVAYSWSEKA 

       190        200        210        220        230        240 
GTHPLNPANS SHLLSLTLGP QHADNIYICT VSNPISNNSQ TFSPWPGCRT DPSETKPWAV 

       250        260        270        280        290        300 
YAGLLGGVIM ILIMVVILQL RRRGKTNHYQ TTVEKKSLTI YAQVQKPGPL QKKLDSFPAQ 

       310        320        330 
DPCTTIYVAA TEPVPESVQE TNSITVYASV TLPES 

« Hide

Isoform 2 (Short) [UniParc].

Checksum: DCE97AC03ACDC045
Show »

FASTA29833,365
Isoform 3 (Secreted) [UniParc].

Checksum: F5CBDC25B2E19967
Show »

FASTA30533,839

References

« Hide 'large scale' references
[1]"A novel receptor involved in T-cell activation."
Cocks B.G., Chang C.-C.J., Carballido J.M., Yssel H., de Vries J.E., Aversa G.
Nature 376:260-263(1995) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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.
[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]"SAP couples Fyn to SLAM immune receptors."
Chan B., Lanyi A., Song H.K., Griesbach J., Simarro-Grande M., Poy F., Howie D., Sumegi J., Terhorst C., Eck M.J.
Nat. Cell Biol. 5:155-160(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 276-286 IN COMPLEX WITH SH2D1A AND FYN.
[12]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] PHE-81.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS1207.1. [Q13291-1]
PIRS58892.
RefSeqNP_003028.1. NM_003037.3. [Q13291-1]
XP_005245513.1. XM_005245456.1. [Q13291-3]
UniGeneHs.523660.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalQ13291.
SMRQ13291. Positions 32-140.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112395. 9 interactions.
DIPDIP-40767N.
IntActQ13291. 5 interactions.
MINTMINT-113752.
STRING9606.ENSP00000306190.

PTM databases

PhosphoSiteQ13291.

Polymorphism databases

DMDM9297047.

Proteomic databases

PaxDbQ13291.
PRIDEQ13291.

Protocols and materials databases

DNASU6504.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000235739; ENSP00000235739; ENSG00000117090. [Q13291-3]
ENST00000302035; ENSP00000306190; ENSG00000117090. [Q13291-1]
GeneID6504.
KEGGhsa:6504.
UCSCuc001fwl.4. human. [Q13291-1]

Organism-specific databases

CTD6504.
GeneCardsGC01M160577.
HGNCHGNC:10903. SLAMF1.
HPACAB002438.
MIM603492. gene.
neXtProtNX_Q13291.
PharmGKBPA35803.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG40451.
HOGENOMHOG000125310.
HOVERGENHBG054224.
InParanoidQ13291.
KOK06536.
OMALYEQVST.
OrthoDBEOG7Q8CQJ.
PhylomeDBQ13291.
TreeFamTF334964.

Gene expression databases

ArrayExpressQ13291.
BgeeQ13291.
CleanExHS_SLAMF1.
GenevestigatorQ13291.

Family and domain databases

InterProIPR007110. Ig-like_dom.
IPR010407. Sig_lymph_act_molc_N.
IPR015631. SLAM_fam_rcpts.
[Graphical view]
PANTHERPTHR12080. PTHR12080. 1 hit.
PfamPF06214. SLAM. 1 hit.
[Graphical view]
ProDomPD090491. Sig_lymph_act_molc_N. 1 hit.
[Graphical view] [Entries sharing at least one domain]
PROSITEPS50835. IG_LIKE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ13291.
GeneWikiSLAMF1.
GenomeRNAi6504.
NextBio25289.
PROQ13291.
SOURCESearch...

Entry information

Entry nameSLAF1_HUMAN
AccessionPrimary (citable) accession number: Q13291
Secondary accession number(s): Q5W172, Q9HBE8
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: November 1, 1996
Last modified: July 9, 2014
This is version 136 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM

Human cell differentiation molecules

CD nomenclature of surface proteins of human leucocytes and list of entries