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 13-FEB-2019, entry version 172. 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; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS MET-229 AND RP PRO-363. RC TISSUE=Placenta; RX PubMed=9062191; DOI=10.1038/386181a0; RA Kharitonenkov A., Chen Z., Sures I., Wang H., Schilling J., RA 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 RP MET-229 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., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA 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., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., 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., RA Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., RA Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., RA Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., RA Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., RA Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., RA 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., RA Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., RA Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., RA Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., RA Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., RA Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., RA Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., RA 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 RP 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 RT project: 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 INTERACTION WITH TYROBP, GLYCOSYLATION, AND 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 RT receptor 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 RT and 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., RA Moore R.J., 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., RA Barclay A.N.; RT "Paired receptor specificity explained by structures of signal RT regulatory 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 CC the negative regulation of receptor tyrosine kinase-coupled CC signaling processes. Participates also in the recruitment of CC tyrosine kinase SYK. 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 O75553:DAB1; NbExp=3; IntAct=EBI-10179231, EBI-7875264; CC P50222:MEOX2; NbExp=3; IntAct=EBI-10179231, EBI-748397; CC Q93062:RBPMS; NbExp=3; IntAct=EBI-10179231, EBI-740322; CC O43914:TYROBP; NbExp=4; IntAct=EBI-2615458, EBI-2214794; CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane CC protein. 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 Note=No experimental confirmation available.; 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. [O00241-1] DR UniGene; Hs.664861; -. 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 ProteinModelPortal; O00241; -. DR SMR; O00241; -. DR BioGrid; 115609; 5. DR IntAct; O00241; 9. DR iPTMnet; O00241; -. DR PhosphoSitePlus; O00241; -. DR BioMuta; SIRPB1; -. DR EPD; O00241; -. DR jPOST; O00241; -. DR PeptideAtlas; O00241; -. DR PRIDE; O00241; -. DR ProteomicsDB; 47803; -. DR ProteomicsDB; 47804; -. [O00241-2] DR DNASU; 10326; -. DR Ensembl; ENST00000381603; ENSP00000371016; ENSG00000101307. [O00241-2] DR Ensembl; ENST00000381605; ENSP00000371018; ENSG00000101307. [O00241-1] DR GeneID; 10326; -. DR UCSC; uc002wfk.5; human. [O00241-1] DR CTD; 10326; -. DR DisGeNET; 10326; -. DR EuPathDB; HostDB:ENSG00000101307.15; -. DR GeneCards; SIRPB1; -. DR HGNC; HGNC:15928; SIRPB1. DR HPA; HPA047463; -. DR MIM; 603889; gene. DR neXtProt; NX_O00241; -. DR OpenTargets; ENSG00000101307; -. DR PharmGKB; PA38051; -. DR GeneTree; ENSGT00940000163660; -. DR HOVERGEN; HBG056632; -. DR InParanoid; O00241; -. DR OrthoDB; 904196at2759; -. DR PhylomeDB; O00241; -. DR TreeFam; TF341862; -. 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 EvolutionaryTrace; O00241; -. DR GeneWiki; SIRPB1; -. DR GenomeRNAi; 10326; -. DR Proteomes; UP000005640; Chromosome 20. DR Bgee; ENSG00000101307; Expressed in 113 organ(s), highest expression level in blood. DR ExpressionAtlas; O00241; baseline and differential. DR Genevisible; O00241; HS. DR GO; GO:0009986; C:cell surface; TAS:ARUK-UCL. DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc. 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:0045087; P:innate immune response; TAS:Reactome. DR GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome. DR GO; GO:0022409; P:positive regulation of cell-cell adhesion; IBA:GO_Central. 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 Gene3D; 2.60.40.10; -; 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 Pfam; PF07654; C1-set; 2. DR Pfam; PF07686; V-set; 1. DR SMART; SM00409; IG; 2. DR SMART; SM00407; IGc1; 2. DR SUPFAM; SSF48726; SSF48726; 3. DR PROSITE; PS50835; IG_LIKE; 3. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Complete proteome; Disulfide bond; KW Glycoprotein; Immunoglobulin domain; Membrane; Polymorphism; KW Reference proteome; Repeat; Signal; Transmembrane; KW Transmembrane helix. FT SIGNAL 1 29 {ECO:0000255}. FT CHAIN 30 398 Signal-regulatory protein beta-1. FT /FTId=PRO_0000014956. FT TOPO_DOM 30 371 Extracellular. {ECO:0000255}. FT TRANSMEM 372 392 Helical. {ECO:0000255}. FT TOPO_DOM 393 398 Cytoplasmic. {ECO:0000255}. FT DOMAIN 30 136 Ig-like V-type. FT DOMAIN 147 246 Ig-like C1-type 1. FT DOMAIN 253 347 Ig-like C1-type 2. FT CARBOHYD 244 244 N-linked (GlcNAc...) asparagine. FT {ECO:0000269|PubMed:16335952}. FT CARBOHYD 269 269 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 291 291 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT DISULFID 54 120 {ECO:0000255|PROSITE-ProRule:PRU00114, FT ECO:0000269|PubMed:18657508}. FT DISULFID 169 227 {ECO:0000255|PROSITE-ProRule:PRU00114}. FT DISULFID 320 320 Interchain. {ECO:0000255|PROSITE- FT ProRule:PRU00114, FT ECO:0000269|PubMed:18657508}. FT VAR_SEQ 145 361 Missing (in isoform 2). FT {ECO:0000303|PubMed:15489334}. FT /FTId=VSP_007026. FT VARIANT 23 23 R -> G (in dbSNP:rs1535882). FT /FTId=VAR_028789. FT VARIANT 53 53 R -> H (in dbSNP:rs2746603). FT /FTId=VAR_028790. FT VARIANT 229 229 I -> M (in dbSNP:rs2253427). FT {ECO:0000269|PubMed:14702039, FT ECO:0000269|PubMed:9062191}. FT /FTId=VAR_028791. FT VARIANT 363 363 A -> P (in dbSNP:rs2243603). FT {ECO:0000269|PubMed:14702039, FT ECO:0000269|PubMed:15489334, FT ECO:0000269|PubMed:9062191}. FT /FTId=VAR_028792. FT CONFLICT 102 102 D -> N (in Ref. 1; CAA71404). FT {ECO:0000305}. FT CONFLICT 106 106 S -> R (in Ref. 2; BAG36297). FT {ECO:0000305}. FT STRAND 40 45 {ECO:0000244|PDB:2JJU}. FT STRAND 50 52 {ECO:0000244|PDB:2JJU}. FT STRAND 55 57 {ECO:0000244|PDB:2JJU}. FT STRAND 65 69 {ECO:0000244|PDB:2JJU}. FT STRAND 76 84 {ECO:0000244|PDB:2JJU}. FT STRAND 89 91 {ECO:0000244|PDB:2JJU}. FT STRAND 95 99 {ECO:0000244|PDB:2D9C}. FT STRAND 105 107 {ECO:0000244|PDB:2JJU}. FT HELIX 112 114 {ECO:0000244|PDB:2JJU}. FT STRAND 116 124 {ECO:0000244|PDB:2JJU}. FT STRAND 127 129 {ECO:0000244|PDB:2JJU}. FT STRAND 131 135 {ECO:0000244|PDB:2JJU}. FT STRAND 139 144 {ECO:0000244|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 //