ID CD48_HUMAN Reviewed; 243 AA. AC P09326; Q5U055; Q8MGR0; DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1991, sequence version 2. DT 27-MAR-2024, entry version 230. DE RecName: Full=CD48 antigen; DE AltName: Full=B-lymphocyte activation marker BLAST-1; DE AltName: Full=BCM1 surface antigen; DE AltName: Full=Leukocyte antigen MEM-102; DE AltName: Full=SLAM family member 2; DE Short=SLAMF2; DE AltName: Full=Signaling lymphocytic activation molecule 2; DE AltName: Full=TCT.1; DE AltName: CD_antigen=CD48; DE Flags: Precursor; GN Name=CD48; Synonyms=BCM1, BLAST1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND SUBCELLULAR LOCATION. RX PubMed=1999351; DOI=10.1007/bf00210824; RA Vaughan H.A., Henning M.M., Purcell D.F.J., McKenzie I.F.C., Sandrin M.S.; RT "The isolation of cDNA clones for CD48."; RL Immunogenetics 33:113-117(1991). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=1999350; DOI=10.1007/bf00210823; RA Korinek V., Stefanova I., Angelisova P., Hilbert I., Horejsi V.; RT "The human leucocyte antigen CD48 (MEM-102) is closely related to the RT activation marker Blast-1."; RL Immunogenetics 33:108-112(1991). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=2828034; DOI=10.1002/j.1460-2075.1987.tb02703.x; RA Staunton D.E., Thorley-Lawson D.A.; RT "Molecular cloning of the lymphocyte activation marker Blast-1."; RL EMBO J. 6:3695-3701(1987). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."; RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=B-cell, and Pancreas; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [8] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-27. RX PubMed=1847502; DOI=10.1128/mcb.11.3.1614-1623.1991; RA Fisher R.C., Thorley-Lawson D.A.; RT "Characterization of the Epstein-Barr virus-inducible gene encoding the RT human leukocyte adhesion and activation antigen BLAST-1 (CD48)."; RL Mol. Cell. Biol. 11:1614-1623(1991). RN [9] RP PARTIAL PROTEIN SEQUENCE. RX PubMed=1827826; DOI=10.1084/jem.173.6.1339; RA del Porto P., Mami-Chouaib F., Bruneau J.-M., Jitsukawa S., Dumas J., RA Harnois M., Hercend T.; RT "TCT.1, a target molecule for gamma/delta T cells, is encoded by an RT immunoglobulin superfamily gene (Blast-1) located in the CD1 region of RT human chromosome 1."; RL J. Exp. Med. 173:1339-1344(1991). RN [10] RP SUBCELLULAR LOCATION. RX PubMed=9418191; DOI=10.1023/a:1027327912204; RA Smith G.M., Biggs J., Norris B., Anderson-Stewart P., Ward R.; RT "Detection of a soluble form of the leukocyte surface antigen CD48 in RT plasma and its elevation in patients with lymphoid leukemias and RT arthritis."; RL J. Clin. Immunol. 17:502-509(1997). RN [11] RP INDUCTION BY INTERFERONS, AND SUBCELLULAR LOCATION. RX PubMed=9041467; DOI=10.1089/jir.1997.17.17; RA Tissot C., Rebouissou C., Klein B., Mechti N.; RT "Both human alpha/beta and gamma interferons upregulate the expression of RT CD48 cell surface molecules."; RL J. Interferon Cytokine Res. 17:17-26(1997). RN [12] RP TISSUE SPECIFICITY. RX PubMed=9893294; DOI=10.1111/j.1442-200x.1998.tb01994.x; RA Katsuura M., Shimizu Y., Akiba K., Kanazawa C., Mitsui T., Sendo D., RA Kawakami T., Hayasaka K., Yokoyama S.; RT "CD48 expression on leukocytes in infectious diseases: flow cytometric RT analysis of surface antigen."; RL Acta Paediatr. Jpn. Overseas Ed. 40:580-585(1998). RN [13] RP FUNCTION, AND INTERACTION WITH CD244. RX PubMed=9841922; DOI=10.1084/jem.188.11.2083; RA Brown M.H., Boles K., van der Merwe P.A., Kumar V., Mathew P.A., RA Barclay A.N.; RT "2B4, the natural killer and T cell immunoglobulin superfamily surface RT protein, is a ligand for CD48."; RL J. Exp. Med. 188:2083-2090(1998). RN [14] RP FUNCTION, AND INTERACTION WITH LCK. RX PubMed=12007789; DOI=10.1016/s0167-4889(02)00165-9; RA Hawash I.Y., Hu X.E., Adal A., Cassady J.M., Geahlen R.L., Harrison M.L.; RT "The oxygen-substituted palmitic acid analogue, 13-oxypalmitic acid, RT inhibits Lck localization to lipid rafts and T cell signaling."; RL Biochim. Biophys. Acta 1589:140-150(2002). RN [15] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-104 AND ASN-189. RC TISSUE=Leukemic T-cell; RX PubMed=19349973; DOI=10.1038/nbt.1532; RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., RA Schiess R., Aebersold R., Watts J.D.; RT "Mass-spectrometric identification and relative quantification of N-linked RT cell surface glycoproteins."; RL Nat. Biotechnol. 27:378-386(2009). RN [16] RP FUNCTION. RX PubMed=19494291; DOI=10.4049/jimmunol.0800691; RA Muhammad A., Schiller H.B., Forster F., Eckerstorfer P., Geyeregger R., RA Leksa V., Zlabinger G.J., Sibilia M., Sonnleitner A., Paster W., RA Stockinger H.; RT "Sequential cooperation of CD2 and CD48 in the buildup of the early TCR RT signalosome."; RL J. Immunol. 182:7672-7680(2009). RN [17] RP FUNCTION, AND INTERACTION WITH CD244. RX PubMed=27249817; DOI=10.1098/rsob.160010; RA Claus M., Wingert S., Watzl C.; RT "Modulation of natural killer cell functions by interactions between 2B4 RT and CD48 in cis and in trans."; RL Open Biol. 6:0-0(2016). RN [18] RP STRUCTURE BY NMR OF 24-140. RG RIKEN structural genomics initiative (RSGI); RT "Solution structure of the first Ig-like domain from human CD48 antigen."; RL Submitted (AUG-2007) to the PDB data bank. CC -!- FUNCTION: Glycosylphosphatidylinositol (GPI)-anchored cell surface CC glycoprotein that interacts via its N-terminal immunoglobulin domain CC with cell surface receptors including 2B4/CD244 or CD2 to regulate CC immune cell function and activation (PubMed:27249817, PubMed:12007789). CC Participates in T-cell signaling transduction by associating with CD2 CC and efficiently bringing the Src family protein kinase LCK and LAT to CC the TCR/CD3 complex (PubMed:19494291). In turn, promotes LCK CC phosphorylation and subsequent activation (PubMed:12007789). Induces CC the phosphorylation of the cytoplasmic immunoreceptortyrosine switch CC motifs (ITSMs) of CD244 initiating a series of signaling events that CC leads to the generation of the immunological synapse and the directed CC release of cytolytic granules containing perforin and granzymes by T- CC lymphocytes and NK-cells (PubMed:9841922, PubMed:27249817). CC {ECO:0000269|PubMed:12007789, ECO:0000269|PubMed:19494291, CC ECO:0000269|PubMed:27249817, ECO:0000269|PubMed:9841922}. CC -!- SUBUNIT: Interacts with CD2. Interacts with CD244 (PubMed:9841922, CC PubMed:27249817). Interacts with LCK (PubMed:12007789). CC {ECO:0000269|PubMed:12007789, ECO:0000269|PubMed:27249817, CC ECO:0000269|PubMed:9841922}. CC -!- INTERACTION: CC P09326; Q9BZW8: CD244; NbExp=4; IntAct=EBI-714770, EBI-1580565; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:1999351, CC ECO:0000269|PubMed:9041467}; Lipid-anchor, GPI-anchor CC {ECO:0000269|PubMed:1999351}. Secreted {ECO:0000269|PubMed:9418191}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P09326-1; Sequence=Displayed; CC Name=2; CC IsoId=P09326-2; Sequence=VSP_055598, VSP_055599; CC -!- TISSUE SPECIFICITY: Widely expressed on all hematopoietic cells. CC {ECO:0000269|PubMed:9893294}. CC -!- INDUCTION: By IFN-alpha/beta and IFN-gamma both at the level of CD48 CC mRNA and cell surface expression. {ECO:0000269|PubMed:9041467}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M59904; AAA62834.1; -; mRNA. DR EMBL; X06341; CAA29647.1; -; mRNA. DR EMBL; M37766; AAA36211.1; -; mRNA. DR EMBL; BT019813; AAV38616.1; -; mRNA. DR EMBL; AL121985; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471121; EAW52705.1; -; Genomic_DNA. DR EMBL; BC016182; AAH16182.1; -; mRNA. DR EMBL; BC030224; AAH30224.1; -; mRNA. DR EMBL; M63911; AAA35602.1; -; Genomic_DNA. DR CCDS; CCDS1208.1; -. [P09326-1] DR PIR; A53244; A53244. DR RefSeq; NP_001769.2; NM_001778.3. [P09326-1] DR PDB; 2EDO; NMR; -; A=27-140. DR PDBsum; 2EDO; -. DR AlphaFoldDB; P09326; -. DR SMR; P09326; -. DR BioGRID; 107400; 47. DR IntAct; P09326; 5. DR STRING; 9606.ENSP00000484431; -. DR TCDB; 8.A.23.1.36; the basigin (basigin) family. DR GlyConnect; 1926; 7 N-Linked glycans (3 sites). DR GlyCosmos; P09326; 7 sites, 7 glycans. DR GlyGen; P09326; 7 sites, 7 N-linked glycans (3 sites). DR iPTMnet; P09326; -. DR PhosphoSitePlus; P09326; -. DR SwissPalm; P09326; -. DR BioMuta; CD48; -. DR DMDM; 114871; -. DR CPTAC; CPTAC-1199; -. DR EPD; P09326; -. DR jPOST; P09326; -. DR MassIVE; P09326; -. DR MaxQB; P09326; -. DR PaxDb; 9606-ENSP00000484431; -. DR PeptideAtlas; P09326; -. DR ProteomicsDB; 52212; -. [P09326-1] DR ProteomicsDB; 71445; -. DR TopDownProteomics; P09326-1; -. [P09326-1] DR Antibodypedia; 3737; 1343 antibodies from 48 providers. DR CPTC; P09326; 1 antibody. DR DNASU; 962; -. DR Ensembl; ENST00000368045.3; ENSP00000357024.3; ENSG00000117091.10. [P09326-2] DR Ensembl; ENST00000368046.8; ENSP00000357025.3; ENSG00000117091.10. [P09326-1] DR GeneID; 962; -. DR KEGG; hsa:962; -. DR MANE-Select; ENST00000368046.8; ENSP00000357025.3; NM_001778.4; NP_001769.2. DR UCSC; uc001fwn.4; human. [P09326-1] DR AGR; HGNC:1683; -. DR CTD; 962; -. DR DisGeNET; 962; -. DR GeneCards; CD48; -. DR HGNC; HGNC:1683; CD48. DR HPA; ENSG00000117091; Group enriched (bone marrow, lymphoid tissue). DR MIM; 109530; gene. DR neXtProt; NX_P09326; -. DR OpenTargets; ENSG00000117091; -. DR PharmGKB; PA26223; -. DR VEuPathDB; HostDB:ENSG00000117091; -. DR eggNOG; ENOG502SB68; Eukaryota. DR GeneTree; ENSGT01030000234540; -. DR HOGENOM; CLU_099885_0_0_1; -. DR InParanoid; P09326; -. DR OMA; YFNTKFK; -. DR OrthoDB; 5265418at2759; -. DR PhylomeDB; P09326; -. DR TreeFam; TF334964; -. DR PathwayCommons; P09326; -. DR Reactome; R-HSA-202733; Cell surface interactions at the vascular wall. DR SignaLink; P09326; -. DR BioGRID-ORCS; 962; 15 hits in 1148 CRISPR screens. DR EvolutionaryTrace; P09326; -. DR GeneWiki; CD48; -. DR GenomeRNAi; 962; -. DR Pharos; P09326; Tbio. DR PRO; PR:P09326; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; P09326; Protein. DR Bgee; ENSG00000117091; Expressed in leukocyte and 138 other cell types or tissues. DR ExpressionAtlas; P09326; baseline and differential. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0045121; C:membrane raft; IDA:UniProtKB. DR GO; GO:0005886; C:plasma membrane; TAS:UniProtKB. DR GO; GO:0098552; C:side of membrane; IEA:UniProtKB-KW. DR GO; GO:0006952; P:defense response; TAS:ProtInc. DR CDD; cd05775; IgV_CD2_like_N; 1. DR Gene3D; 2.60.40.10; Immunoglobulins; 2. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003599; Ig_sub. DR InterPro; IPR013106; Ig_V-set. DR PANTHER; PTHR12080:SF105; CD48 ANTIGEN; 1. DR PANTHER; PTHR12080; SIGNALING LYMPHOCYTIC ACTIVATION MOLECULE; 1. DR Pfam; PF13895; Ig_2; 1. DR Pfam; PF07686; V-set; 1. DR SMART; SM00409; IG; 1. DR SUPFAM; SSF48726; Immunoglobulin; 2. DR PROSITE; PS50835; IG_LIKE; 1. DR Genevisible; P09326; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cell membrane; KW Direct protein sequencing; Disulfide bond; Glycoprotein; GPI-anchor; KW Immunoglobulin domain; Lipoprotein; Membrane; Reference proteome; Repeat; KW Secreted; Signal. FT SIGNAL 1..26 FT /evidence="ECO:0000255" FT CHAIN 27..220 FT /note="CD48 antigen" FT /id="PRO_0000014881" FT PROPEP 221..243 FT /note="Removed in mature form" FT /evidence="ECO:0000250" FT /id="PRO_0000014882" FT DOMAIN 29..127 FT /note="Ig-like C2-type 1" FT DOMAIN 132..212 FT /note="Ig-like C2-type 2" FT LIPID 220 FT /note="GPI-anchor amidated serine" FT /evidence="ECO:0000250|UniProtKB:P10252" FT CARBOHYD 40 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 44 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 104 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19349973" FT CARBOHYD 162 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 189 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19349973" FT DISULFID 154..196 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" FT VAR_SEQ 129..169 FT /note="DPVPKPVIKIEKIEDMDDNCYLKLSCVIPGESVNYTWYGDK -> GESGEPK FT SKSPLQWPQMDHCRASWEAWGTLGEEERKTSGQV (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_055598" FT VAR_SEQ 170..243 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_055599" FT VARIANT 102 FT /note="E -> Q (in dbSNP:rs2295615)" FT /id="VAR_020082" FT VARIANT 241 FT /note="L -> S (in dbSNP:rs16832307)" FT /id="VAR_049909" FT CONFLICT 2 FT /note="C -> W (in Ref. 1; AAA62834)" FT /evidence="ECO:0000305" FT CONFLICT 66 FT /note="I -> N (in Ref. 3; CAA29647)" FT /evidence="ECO:0000305" FT STRAND 34..36 FT /evidence="ECO:0007829|PDB:2EDO" FT STRAND 41..43 FT /evidence="ECO:0007829|PDB:2EDO" FT STRAND 51..61 FT /evidence="ECO:0007829|PDB:2EDO" FT STRAND 64..69 FT /evidence="ECO:0007829|PDB:2EDO" FT STRAND 74..76 FT /evidence="ECO:0007829|PDB:2EDO" FT TURN 80..84 FT /evidence="ECO:0007829|PDB:2EDO" FT TURN 89..91 FT /evidence="ECO:0007829|PDB:2EDO" FT STRAND 94..98 FT /evidence="ECO:0007829|PDB:2EDO" FT HELIX 101..103 FT /evidence="ECO:0007829|PDB:2EDO" FT STRAND 105..113 FT /evidence="ECO:0007829|PDB:2EDO" FT TURN 114..116 FT /evidence="ECO:0007829|PDB:2EDO" FT STRAND 117..120 FT /evidence="ECO:0007829|PDB:2EDO" FT STRAND 126..128 FT /evidence="ECO:0007829|PDB:2EDO" SQ SEQUENCE 243 AA; 27683 MW; 9E46D76FC36A512C CRC64; MCSRGWDSCL ALELLLLPLS LLVTSIQGHL VHMTVVSGSN VTLNISESLP ENYKQLTWFY TFDQKIVEWD SRKSKYFESK FKGRVRLDPQ SGALYISKVQ KEDNSTYIMR VLKKTGNEQE WKIKLQVLDP VPKPVIKIEK IEDMDDNCYL KLSCVIPGES VNYTWYGDKR PFPKELQNSV LETTLMPHNY SRCYTCQVSN SVSSKNGTVC LSPPCTLARS FGVEWIASWL VVTVPTILGL LLT //