GenomeNet

Database: UniProt
Entry: O00241
LinkDB: O00241
Original site: O00241 
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   12-AUG-2020, entry version 184.
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}.
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   SMR; O00241; -.
DR   BioGRID; 115609; 5.
DR   IntAct; O00241; 10.
DR   STRING; 9606.ENSP00000371018; -.
DR   GlyGen; O00241; 6 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; 295 antibodies.
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; ENSG00000101307; Tissue enriched (blood).
DR   MIM; 603889; gene.
DR   neXtProt; NX_O00241; -.
DR   OpenTargets; ENSG00000101307; -.
DR   PharmGKB; PA38051; -.
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   BioGRID-ORCS; 10326; 2 hits in 865 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 blood and 136 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: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; Cell membrane; Disulfide bond;
KW   Glycoprotein; Immunoglobulin domain; Membrane; Polymorphism;
KW   Reference proteome; Repeat; 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:0000244|PDB:2JJU"
FT   STRAND          50..52
FT                   /evidence="ECO:0000244|PDB:2JJU"
FT   STRAND          55..57
FT                   /evidence="ECO:0000244|PDB:2JJU"
FT   STRAND          65..69
FT                   /evidence="ECO:0000244|PDB:2JJU"
FT   STRAND          76..84
FT                   /evidence="ECO:0000244|PDB:2JJU"
FT   STRAND          89..91
FT                   /evidence="ECO:0000244|PDB:2JJU"
FT   STRAND          95..99
FT                   /evidence="ECO:0000244|PDB:2D9C"
FT   STRAND          105..107
FT                   /evidence="ECO:0000244|PDB:2JJU"
FT   HELIX           112..114
FT                   /evidence="ECO:0000244|PDB:2JJU"
FT   STRAND          116..124
FT                   /evidence="ECO:0000244|PDB:2JJU"
FT   STRAND          127..129
FT                   /evidence="ECO:0000244|PDB:2JJU"
FT   STRAND          131..135
FT                   /evidence="ECO:0000244|PDB:2JJU"
FT   STRAND          139..144
FT                   /evidence="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
//
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