SIRB1_HUMAN
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 03-AUG-2022, entry version 193.
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}.
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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 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; 10.
DR IntAct; O00241; 10.
DR STRING; 9606.ENSP00000371018; -.
DR TCDB; 8.A.23.1.34; the basigin (basigin) family.
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 PeptideAtlas; O00241; -.
DR PRIDE; O00241; -.
DR ProteomicsDB; 47803; -. [O00241-1]
DR ProteomicsDB; 47804; -. [O00241-2]
DR Antibodypedia; 23124; 348 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 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; 904196at2759; -.
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 1065 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 121 other tissues.
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: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; 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
