ID SIRB1_HUMAN Reviewed; 398 AA. AC O00241; A6NLM2; B2R8V0; Q5TFQ9; Q5TFR0; Q8TB12; Q9H1U5; Q9Y4V0; DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot. DT 02-NOV-2010, sequence version 5. DT 27-MAR-2024, entry version 202. DE RecName: Full=Signal-regulatory protein beta-1; DE Short=SIRP-beta-1; DE AltName: Full=CD172 antigen-like family member B; DE AltName: CD_antigen=CD172b; DE Flags: Precursor; GN Name=SIRPB1; 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 VARIANTS MET-229 AND PRO-363. RC TISSUE=Placenta; RX PubMed=9062191; DOI=10.1038/386181a0; RA Kharitonenkov A., Chen Z., Sures I., Wang H., Schilling J., Ullrich A.; RT "A family of proteins that inhibit signalling through tyrosine kinase RT receptors."; RL Nature 386:181-186(1997). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS MET-229 RP AND PRO-363. RC TISSUE=Neutrophil; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=11780052; DOI=10.1038/414865a; RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.; RT "The DNA sequence and comparative analysis of human chromosome 20."; RL Nature 414:865-871(2001). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT PRO-363. RC TISSUE=Skin; 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 [5] RP INTERACTION WITH TYROBP AND SYK. RX PubMed=10940905; RX DOI=10.1002/1521-4141(2000)30:8<2147::aid-immu2147>3.0.co;2-1; RA Tomasello E., Cant C., Buehring H.-J., Vely F., Andre P., Seiffert M., RA Ullrich A., Vivier E.; RT "Association of signal-regulatory proteins beta with KARAP/DAP-12."; RL Eur. J. Immunol. 30:2147-2156(2000). RN [6] RP FUNCTION, INTERACTION WITH TYROBP, SUBCELLULAR LOCATION, GLYCOSYLATION, AND RP TISSUE SPECIFICITY. RX PubMed=10604985; DOI=10.4049/jimmunol.164.1.9; RA Dietrich J., Cella M., Seiffert M., Buehring H.-J., Colonna M.; RT "Signal-regulatory protein beta 1 is a DAP12-associated activating receptor RT expressed in myeloid cells."; RL J. Immunol. 164:9-12(2000). RN [7] RP SUBUNIT, AND INTERCHAIN DISULFIDE BOND. RX PubMed=16081415; DOI=10.1074/jbc.m506419200; RA Liu Y., Soto I., Tong Q., Chin A., Buhring H.J., Wu T., Zen K., RA Parkos C.A.; RT "SIRPbeta1 is expressed as a disulfide-linked homodimer in leukocytes and RT positively regulates neutrophil transepithelial migration."; RL J. Biol. Chem. 280:36132-36140(2005). RN [8] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-244. RC TISSUE=Plasma; RX PubMed=16335952; DOI=10.1021/pr0502065; RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., RA Smith R.D.; RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, RT hydrazide chemistry, and mass spectrometry."; RL J. Proteome Res. 4:2070-2080(2005). RN [9] RP X-RAY CRYSTALLOGRAPHY (1.19 ANGSTROMS) OF 30-148, AND DISULFIDE BOND. RX PubMed=18657508; DOI=10.1016/j.molcel.2008.05.026; RA Hatherley D., Graham S.C., Turner J., Harlos K., Stuart D.I., Barclay A.N.; RT "Paired receptor specificity explained by structures of signal regulatory RT proteins alone and complexed with CD47."; RL Mol. Cell 31:266-277(2008). RN [10] RP STRUCTURE BY NMR OF 33-155. RG RIKEN structural genomics initiative (RSGI); RT "Solution structure of the first Ig-like domain of signal-regulatory RT protein beta-1 (SIRP-beta-1)."; RL Submitted (DEC-2006) to the PDB data bank. CC -!- FUNCTION: Immunoglobulin-like cell surface receptor involved in the CC negative regulation of receptor tyrosine kinase-coupled signaling CC processes. Participates also in the recruitment of tyrosine kinase SYK. CC Triggers activation of myeloid cells when associated with TYROBP CC (PubMed:10604985). {ECO:0000269|PubMed:10604985}. CC -!- SUBUNIT: Homodimer; disulfide-linked. Interacts with TYROBP. This CC interaction results in the recruitment of SYK. CC {ECO:0000269|PubMed:10604985, ECO:0000269|PubMed:10940905, CC ECO:0000269|PubMed:16081415, ECO:0000269|PubMed:18657508}. CC -!- INTERACTION: CC O00241; O43914: TYROBP; NbExp=4; IntAct=EBI-2615458, EBI-2214794; CC O00241-2; P02654: APOC1; NbExp=3; IntAct=EBI-10179231, EBI-1220105; CC O00241-2; Q9NP55: BPIFA1; NbExp=3; IntAct=EBI-10179231, EBI-953896; CC O00241-2; O75553: DAB1; NbExp=3; IntAct=EBI-10179231, EBI-7875264; CC O00241-2; P50222: MEOX2; NbExp=3; IntAct=EBI-10179231, EBI-748397; CC O00241-2; Q9NWB1-5: RBFOX1; NbExp=3; IntAct=EBI-10179231, EBI-12123390; CC O00241-2; Q93062: RBPMS; NbExp=3; IntAct=EBI-10179231, EBI-740322; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10604985}; CC Single-pass type I membrane protein {ECO:0000255}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=O00241-1; Sequence=Displayed; CC Name=2; CC IsoId=O00241-2; Sequence=VSP_007026; CC Name=3; CC IsoId=Q5TFQ8-1; Sequence=External; CC -!- TISSUE SPECIFICITY: Detected in monocytes and dendritic cells. CC {ECO:0000269|PubMed:10604985}. CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:10604985, CC ECO:0000269|PubMed:16335952}. 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; Y10376; CAA71404.1; -; mRNA. DR EMBL; AK313517; BAG36297.1; -; mRNA. DR EMBL; AL049634; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL138804; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC025286; AAH25286.1; -; mRNA. DR EMBL; BC075835; AAH75835.1; -; mRNA. DR CCDS; CCDS13019.1; -. [O00241-1] DR CCDS; CCDS42850.1; -. [O00241-2] DR RefSeq; NP_001077379.1; NM_001083910.3. [O00241-2] DR RefSeq; NP_001317568.1; NM_001330639.1. DR RefSeq; NP_006056.2; NM_006065.4. [O00241-1] DR RefSeq; XP_016883066.1; XM_017027577.1. DR PDB; 2D9C; NMR; -; A=32-154. DR PDB; 2JJU; X-ray; 1.19 A; A/B=30-148. DR PDBsum; 2D9C; -. DR PDBsum; 2JJU; -. DR AlphaFoldDB; O00241; -. DR SMR; O00241; -. DR BioGRID; 115609; 11. DR IntAct; O00241; 10. DR STRING; 9606.ENSP00000371018; -. DR TCDB; 8.A.23.1.34; the basigin (basigin) family. DR GlyCosmos; O00241; 3 sites, 11 glycans. DR GlyGen; O00241; 6 sites, 11 N-linked glycans (2 sites). DR iPTMnet; O00241; -. DR PhosphoSitePlus; O00241; -. DR BioMuta; SIRPB1; -. DR EPD; O00241; -. DR jPOST; O00241; -. DR MassIVE; O00241; -. DR PaxDb; 9606-ENSP00000371018; -. DR PeptideAtlas; O00241; -. DR ProteomicsDB; 47803; -. [O00241-1] DR ProteomicsDB; 47804; -. [O00241-2] DR Antibodypedia; 23124; 396 antibodies from 34 providers. DR DNASU; 10326; -. DR Ensembl; ENST00000381603.7; ENSP00000371016.3; ENSG00000101307.16. [O00241-2] DR Ensembl; ENST00000381605.9; ENSP00000371018.5; ENSG00000101307.16. [O00241-1] DR GeneID; 10326; -. DR MANE-Select; ENST00000381605.9; ENSP00000371018.5; NM_006065.5; NP_006056.2. DR UCSC; uc002wfk.5; human. [O00241-1] DR AGR; HGNC:15928; -. DR CTD; 10326; -. DR DisGeNET; 10326; -. DR GeneCards; SIRPB1; -. DR HGNC; HGNC:15928; SIRPB1. DR HPA; ENSG00000101307; Tissue enhanced (bone marrow, lung, lymphoid tissue). DR MIM; 603889; gene. DR neXtProt; NX_O00241; -. DR OpenTargets; ENSG00000101307; -. DR PharmGKB; PA38051; -. DR VEuPathDB; HostDB:ENSG00000101307; -. DR eggNOG; ENOG502S1XD; Eukaryota. DR GeneTree; ENSGT00960000186656; -. DR InParanoid; O00241; -. DR OrthoDB; 5401342at2759; -. DR PhylomeDB; O00241; -. DR TreeFam; TF341862; -. DR PathwayCommons; O00241; -. DR Reactome; R-HSA-2172127; DAP12 interactions. DR Reactome; R-HSA-391160; Signal regulatory protein family interactions. DR Reactome; R-HSA-6798695; Neutrophil degranulation. DR SignaLink; O00241; -. DR BioGRID-ORCS; 10326; 10 hits in 1145 CRISPR screens. DR ChiTaRS; SIRPB1; human. DR EvolutionaryTrace; O00241; -. DR GeneWiki; SIRPB1; -. DR GenomeRNAi; 10326; -. DR Pharos; O00241; Tbio. DR Proteomes; UP000005640; Chromosome 20. DR RNAct; O00241; Protein. DR Bgee; ENSG00000101307; Expressed in monocyte and 122 other cell types or tissues. DR ExpressionAtlas; O00241; baseline and differential. DR GO; GO:0009986; C:cell surface; TAS:ARUK-UCL. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0030667; C:secretory granule membrane; TAS:Reactome. DR GO; GO:0007166; P:cell surface receptor signaling pathway; TAS:ProtInc. DR GO; GO:0050766; P:positive regulation of phagocytosis; IBA:GO_Central. DR GO; GO:0050870; P:positive regulation of T cell activation; IBA:GO_Central. DR GO; GO:0007165; P:signal transduction; TAS:ProtInc. DR CDD; cd05772; IgC1_SIRP_domain_2; 1. DR CDD; cd16085; IgC1_SIRP_domain_3; 1. DR CDD; cd16097; IgV_SIRP; 1. DR Gene3D; 2.60.40.10; Immunoglobulins; 3. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR003599; Ig_sub. DR InterPro; IPR013106; Ig_V-set. DR PANTHER; PTHR19971; SIGNAL-REGULATORY PROTEIN BETA; 1. DR PANTHER; PTHR19971:SF37; SIGNAL-REGULATORY PROTEIN BETA-1; 1. DR Pfam; PF07654; C1-set; 2. DR Pfam; PF07686; V-set; 1. DR SMART; SM00409; IG; 2. DR SMART; SM00407; IGc1; 2. DR SUPFAM; SSF48726; Immunoglobulin; 3. DR PROSITE; PS50835; IG_LIKE; 3. DR Genevisible; O00241; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cell membrane; Disulfide bond; KW Glycoprotein; Immunoglobulin domain; Membrane; Reference proteome; Repeat; KW Signal; Transmembrane; Transmembrane helix. FT SIGNAL 1..29 FT /evidence="ECO:0000255" FT CHAIN 30..398 FT /note="Signal-regulatory protein beta-1" FT /id="PRO_0000014956" FT TOPO_DOM 30..371 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 372..392 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 393..398 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT DOMAIN 30..136 FT /note="Ig-like V-type" FT DOMAIN 147..246 FT /note="Ig-like C1-type 1" FT DOMAIN 253..347 FT /note="Ig-like C1-type 2" FT CARBOHYD 244 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:16335952" FT CARBOHYD 269 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 291 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 54..120 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114, FT ECO:0000269|PubMed:18657508" FT DISULFID 169..227 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" FT DISULFID 320 FT /note="Interchain" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114, FT ECO:0000269|PubMed:18657508" FT VAR_SEQ 145..361 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_007026" FT VARIANT 23 FT /note="R -> G (in dbSNP:rs1535882)" FT /id="VAR_028789" FT VARIANT 53 FT /note="R -> H (in dbSNP:rs2746603)" FT /id="VAR_028790" FT VARIANT 229 FT /note="I -> M (in dbSNP:rs2253427)" FT /evidence="ECO:0000269|PubMed:14702039, FT ECO:0000269|PubMed:9062191" FT /id="VAR_028791" FT VARIANT 363 FT /note="A -> P (in dbSNP:rs2243603)" FT /evidence="ECO:0000269|PubMed:14702039, FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:9062191" FT /id="VAR_028792" FT CONFLICT 102 FT /note="D -> N (in Ref. 1; CAA71404)" FT /evidence="ECO:0000305" FT CONFLICT 106 FT /note="S -> R (in Ref. 2; BAG36297)" FT /evidence="ECO:0000305" FT STRAND 40..45 FT /evidence="ECO:0007829|PDB:2JJU" FT STRAND 50..52 FT /evidence="ECO:0007829|PDB:2JJU" FT STRAND 55..57 FT /evidence="ECO:0007829|PDB:2JJU" FT STRAND 65..69 FT /evidence="ECO:0007829|PDB:2JJU" FT STRAND 76..84 FT /evidence="ECO:0007829|PDB:2JJU" FT STRAND 89..91 FT /evidence="ECO:0007829|PDB:2JJU" FT STRAND 95..99 FT /evidence="ECO:0007829|PDB:2D9C" FT STRAND 105..107 FT /evidence="ECO:0007829|PDB:2JJU" FT HELIX 112..114 FT /evidence="ECO:0007829|PDB:2JJU" FT STRAND 116..124 FT /evidence="ECO:0007829|PDB:2JJU" FT STRAND 127..129 FT /evidence="ECO:0007829|PDB:2JJU" FT STRAND 131..135 FT /evidence="ECO:0007829|PDB:2JJU" FT STRAND 139..144 FT /evidence="ECO:0007829|PDB:2JJU" SQ SEQUENCE 398 AA; 43211 MW; C9C5E759514E212E CRC64; MPVPASWPHL PSPFLLMTLL LGRLTGVAGE DELQVIQPEK SVSVAAGESA TLRCAMTSLI PVGPIMWFRG AGAGRELIYN QKEGHFPRVT TVSELTKRNN LDFSISISNI TPADAGTYYC VKFRKGSPDD VEFKSGAGTE LSVRAKPSAP VVSGPAVRAT PEHTVSFTCE SHGFSPRDIT LKWFKNGNEL SDFQTNVDPA GDSVSYSIHS TARVVLTRGD VHSQVICEIA HITLQGDPLR GTANLSEAIR VPPTLEVTQQ PMRAENQANV TCQVSNFYPR GLQLTWLENG NVSRTETAST LIENKDGTYN WMSWLLVNTC AHRDDVVLTC QVEHDGQQAV SKSYALEISA HQKEHGSDIT HEAALAPTAP LLVALLLGPK LLLVVGVSAI YICWKQKA //