ID TYOBP_HUMAN Reviewed; 113 AA. AC O43914; A8K2X0; F5H389; Q6FGA5; Q9UMT3; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1998, sequence version 1. DT 13-FEB-2019, entry version 159. DE RecName: Full=TYRO protein tyrosine kinase-binding protein; DE AltName: Full=DNAX-activation protein 12; DE AltName: Full=Killer-activating receptor-associated protein; DE Short=KAR-associated protein; DE Flags: Precursor; GN Name=TYROBP; Synonyms=DAP12, KARAP; 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 [GENOMIC DNA / MRNA] (ISOFORM 1). RX PubMed=9490415; DOI=10.1038/35642; RA Lanier L.L., Corliss B.C., Wu J., Leong C., Phillips J.H.; RT "Immunoreceptor DAP12 bearing a tyrosine-based activation motif is RT involved in activating NK cells."; RL Nature 391:703-707(1998). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). RC TISSUE=Lymphoid tissue; RA Cantoni C., Biassoni R.; RT "Killer activating receptor associated protein isoform b."; RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). RA Begum N.A., Seya T.; RT "Dendritic cells express two types of immunoreceptor DAP12 RT transcripts."; RL Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases. 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 RT vector."; RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Umbilical cord blood; 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 [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). RC TISSUE=Macrophage; RX PubMed=16344560; DOI=10.1101/gr.4039406; RA Kimura K., Wakamatsu A., Suzuki Y., Ota T., Nishikawa T., RA Yamashita R., Yamamoto J., Sekine M., Tsuritani K., Wakaguri H., RA Ishii S., Sugiyama T., Saito K., Isono Y., Irie R., Kushida N., RA Yoneyama T., Otsuka R., Kanda K., Yokoi T., Kondo H., Wagatsuma M., RA Murakawa K., Ishida S., Ishibashi T., Takahashi-Fujii A., Tanase T., RA Nagai K., Kikuchi H., Nakai K., Isogai T., Sugano S.; RT "Diversification of transcriptional modulation: large-scale RT identification and characterization of putative alternative promoters RT of human genes."; RL Genome Res. 16:55-65(2006). RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15057824; DOI=10.1038/nature02399; RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., RA Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., RA Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., RA Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M., RA Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., RA Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., RA Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., RA Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., RA Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., RA Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., RA Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., RA Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., RA Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., RA Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., RA Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., RA Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., RA Rubin E.M., Lucas S.M.; RT "The DNA sequence and biology of human chromosome 19."; RL Nature 428:529-535(2004). RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain; 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 [10] RP INTERACTION WITH CLECSF5. RX PubMed=10449773; DOI=10.1073/pnas.96.17.9792; RA Bakker A.B.H., Baker E., Sutherland G.R., Phillips J.H., Lanier L.L.; RT "Myeloid DAP12-associating lectin (MDL)-1 is a cell surface receptor RT involved in the activation of myeloid cells."; RL Proc. Natl. Acad. Sci. U.S.A. 96:9792-9796(1999). RN [11] RP INVOLVEMENT IN PLOSL. RX PubMed=10888890; DOI=10.1038/77153; RA Paloneva J., Kestilae M., Wu J., Salminen A., Boehling T., RA Ruotsalainen V., Hakola P., Bakker A.B.H., Phillips J.H., RA Pekkarinen P., Lanier L.L., Timonen T., Peltonen L.; RT "Loss-of-function mutations in TYROBP (DAP12) result in a presenile RT dementia with bone cysts."; RL Nat. Genet. 25:357-361(2000). RN [12] RP INTERACTION WITH TREM1. RX PubMed=10799849; DOI=10.4049/jimmunol.164.10.4991; RA Bouchon A., Dietrich J., Colonna M.; RT "Inflammatory responses can be triggered by TREM-1, a novel receptor RT expressed on neutrophils and monocytes."; RL J. Immunol. 164:4991-4995(2000). RN [13] RP INVOLVEMENT IN PLOSL. RX PubMed=12370476; DOI=10.1212/WNL.59.7.1105; RA Kondo T., Takahashi K., Kohara N., Takahashi Y., Hayashi S., RA Takahashi H., Matsuo H., Yamazaki M., Inoue K., Miyamoto K., RA Yamamura T.; RT "Heterogeneity of presenile dementia with bone cysts (Nasu-Hakola RT disease): three genetic forms."; RL Neurology 59:1105-1107(2002). RN [14] RP TISSUE SPECIFICITY. RX PubMed=11922939; DOI=10.1016/S0161-5890(02)00004-4; RA Gingras M.-C., Lapillonne H., Margolin J.F.; RT "TREM-1, MDL-1, and DAP12 expression is associated with a mature stage RT of myeloid development."; RL Mol. Immunol. 38:817-824(2002). RN [15] RP INTERACTION WITH CD300E. RX PubMed=15557162; DOI=10.4049/jimmunol.173.11.6703; RA Aguilar H., Alvarez-Errico D., Garcia-Montero A.C., Orfao A., RA Sayos J., Lopez-Botet M.; RT "Molecular characterization of a novel immune receptor restricted to RT the monocytic lineage."; RL J. Immunol. 173:6703-6711(2004). RN [16] RP INTERACTION WITH SIGLEC14. RX PubMed=17012248; DOI=10.1096/fj.06-5800com; RA Angata T., Hayakawa T., Yamanaka M., Varki A., Nakamura M.; RT "Discovery of Siglec-14, a novel sialic acid receptor undergoing RT concerted evolution with Siglec-5 in primates."; RL FASEB J. 20:1964-1973(2006). RN [17] RP INTERACTION WITH CD300LB. RX PubMed=16920917; DOI=10.4049/jimmunol.177.5.2819; RA Martinez-Barriocanal A., Sayos J.; RT "Molecular and functional characterization of CD300b, a new activating RT immunoglobulin receptor able to transduce signals through two RT different pathways."; RL J. Immunol. 177:2819-2830(2006). RN [18] RP INTERACTION WITH CD300LB. RX PubMed=17928527; DOI=10.1182/blood-2007-04-085787; RA Yamanishi Y., Kitaura J., Izawa K., Matsuoka T., Oki T., Lu Y., RA Shibata F., Yamazaki S., Kumagai H., Nakajima H., Maeda-Yamamoto M., RA Tybulewicz V.L.J., Takai T., Kitamura T.; RT "Analysis of mouse LMIR5/CLM-7 as an activating receptor: differential RT regulation of LMIR5/CLM-7 in mouse versus human cells."; RL Blood 111:688-698(2008). RN [19] RP INTERACTION WITH KIR2DS5. RX PubMed=18624290; DOI=10.1002/eji.200838434; RA Della Chiesa M., Romeo E., Falco M., Balsamo M., Augugliaro R., RA Moretta L., Bottino C., Moretta A., Vitale M.; RT "Evidence that the KIR2DS5 gene codes for a surface receptor RT triggering natural killer cell function."; RL Eur. J. Immunol. 38:2284-2289(2008). RN [20] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200; RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., RA Mann M., Daub H.; RT "Large-scale proteomics analysis of the human kinome."; RL Mol. Cell. Proteomics 8:1751-1764(2009). RN [21] RP INTERACTION WITH CD300H. RX PubMed=26221034; DOI=10.1074/jbc.M115.643361; RA Niizuma K., Tahara-Hanaoka S., Noguchi E., Shibuya A.; RT "Identification and Characterization of CD300H, a New Member of the RT Human CD300 Immunoreceptor Family."; RL J. Biol. Chem. 290:22298-22308(2015). RN [22] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., RA Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [23] RP STRUCTURE BY NMR OF 35-67 IN COMPLEX WITH KLRC2, SUBUNIT, DISULFIDE RP BOND, MUTAGENESIS OF THR-54, AND INTERACTION WITH KLRC2 AND KIR2DS3. RX PubMed=20890284; DOI=10.1038/ni.1943; RA Call M.E., Wucherpfennig K.W., Chou J.J.; RT "The structural basis for intramembrane assembly of an activating RT immunoreceptor complex."; RL Nat. Immunol. 11:1023-1029(2010). CC -!- FUNCTION: Non-covalently associates with activating receptors of CC the CD300 family. Cross-linking of CD300-TYROBP complexes results CC in cellular activation. Involved for instance in neutrophil CC activation mediated by integrin. CC -!- SUBUNIT: Homodimer; disulfide-linked (PubMed:20890284). Interacts CC with SIRPB1 and TREM1 (PubMed:10799849). Interacts with CLECSF5 CC (PubMed:10449773). Interacts with SIGLEC14 (PubMed:17012248). CC Interacts with CD300LB and CD300E (PubMed:15557162, CC PubMed:16920917, PubMed:17928527). Interacts with CD300D (By CC similarity). Interacts (via ITAM domain) with SYK (via SH2 CC domains); activates SYK mediating neutrophils and macrophages CC integrin-mediated activation (By similarity). Interacts with CC KLRC2, KIR2DS3 and KIR2DS5 (PubMed:18624290, PubMed:20890284). CC Interacts with CD300H (PubMed:26221034). CC {ECO:0000250|UniProtKB:O54885, ECO:0000269|PubMed:10449773, CC ECO:0000269|PubMed:10799849, ECO:0000269|PubMed:15557162, CC ECO:0000269|PubMed:16920917, ECO:0000269|PubMed:17012248, CC ECO:0000269|PubMed:17928527, ECO:0000269|PubMed:18624290, CC ECO:0000269|PubMed:20890284, ECO:0000269|PubMed:26221034}. CC -!- INTERACTION: CC Self; NbExp=2; IntAct=EBI-2214794, EBI-2214794; CC Q14953:KIR2DS5; NbExp=3; IntAct=EBI-2214794, EBI-16823921; CC O95944:NCR2; NbExp=2; IntAct=EBI-2214794, EBI-14058375; CC O00241:SIRPB1; NbExp=4; IntAct=EBI-2214794, EBI-2615458; CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane CC protein. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; Synonyms=KARAP-a; CC IsoId=O43914-1; Sequence=Displayed; CC Name=2; Synonyms=KARAP-b; CC IsoId=O43914-2; Sequence=VSP_012909; CC Name=3; CC IsoId=O43914-3; Sequence=VSP_046066; CC Note=No experimental confirmation available.; CC -!- TISSUE SPECIFICITY: Expressed at low levels in the early CC development of the hematopoietic system and in the promonocytic CC stage and at high levels in mature monocytes. Expressed in CC hematological cells and tissues such as peripheral blood CC leukocytes and spleen. Also found in bone marrow, lymph nodes, CC placenta, lung and liver. Expressed at lower levels in different CC parts of the brain especially in the basal ganglia and corpus CC callosum. {ECO:0000269|PubMed:11922939}. CC -!- PTM: Tyrosine phosphorylated. CC -!- DISEASE: Polycystic lipomembranous osteodysplasia with sclerosing CC leukoencephalopathy (PLOSL) [MIM:221770]: Recessively inherited CC disease characterized by a combination of psychotic symptoms CC rapidly progressing to presenile dementia and bone cysts CC restricted to wrists and ankles. PLOSL has a global distribution, CC although most of the patients have been diagnosed in Finland and CC Japan, with an estimated population prevalence of 2x10(-6) in the CC Finns. {ECO:0000269|PubMed:10888890, ECO:0000269|PubMed:12370476}. CC Note=The disease is caused by mutations affecting the gene CC represented in this entry. CC -!- SIMILARITY: Belongs to the TYROBP family. {ECO:0000305}. 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; AF019562; AAD09436.1; -; mRNA. DR EMBL; AF019563; AAD09437.1; -; Genomic_DNA. DR EMBL; AJ010098; CAB52288.1; -; mRNA. DR EMBL; AY074782; AAL74017.1; -; mRNA. DR EMBL; BT009851; AAP88853.1; -; mRNA. DR EMBL; AK290385; BAF83074.1; -; mRNA. DR EMBL; CR450342; CAG29338.1; -; mRNA. DR EMBL; CR542202; CAG46999.1; -; mRNA. DR EMBL; BP295666; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; AD000833; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AD000864; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC011175; AAH11175.1; -; mRNA. DR CCDS; CCDS12482.1; -. [O43914-1] DR CCDS; CCDS46058.1; -. [O43914-2] DR CCDS; CCDS54255.1; -. [O43914-3] DR RefSeq; NP_001166985.1; NM_001173514.1. [O43914-3] DR RefSeq; NP_003323.1; NM_003332.3. [O43914-1] DR RefSeq; NP_937758.1; NM_198125.2. [O43914-2] DR UniGene; Hs.515369; -. DR PDB; 2L34; NMR; -; A/B=35-67. DR PDB; 2L35; NMR; -; A=35-67, B=35-66. DR PDB; 4WO1; X-ray; 2.14 A; A/B/C/D=35-67. DR PDB; 4WOL; X-ray; 1.77 A; A/B/C=35-67. DR PDBsum; 2L34; -. DR PDBsum; 2L35; -. DR PDBsum; 4WO1; -. DR PDBsum; 4WOL; -. DR ProteinModelPortal; O43914; -. DR SMR; O43914; -. DR BioGrid; 113155; 19. DR CORUM; O43914; -. DR IntAct; O43914; 14. DR STRING; 9606.ENSP00000262629; -. DR iPTMnet; O43914; -. DR PhosphoSitePlus; O43914; -. DR BioMuta; TYROBP; -. DR EPD; O43914; -. DR jPOST; O43914; -. DR PaxDb; O43914; -. DR PeptideAtlas; O43914; -. DR PRIDE; O43914; -. DR ProteomicsDB; 49229; -. DR ProteomicsDB; 49230; -. [O43914-2] DR DNASU; 7305; -. DR Ensembl; ENST00000262629; ENSP00000262629; ENSG00000011600. [O43914-1] DR Ensembl; ENST00000544690; ENSP00000445332; ENSG00000011600. [O43914-3] DR Ensembl; ENST00000589517; ENSP00000468447; ENSG00000011600. [O43914-2] DR GeneID; 7305; -. DR KEGG; hsa:7305; -. DR UCSC; uc002ocm.4; human. [O43914-1] DR CTD; 7305; -. DR DisGeNET; 7305; -. DR EuPathDB; HostDB:ENSG00000011600.11; -. DR GeneCards; TYROBP; -. DR GeneReviews; TYROBP; -. DR HGNC; HGNC:12449; TYROBP. DR HPA; CAB009493; -. DR HPA; HPA041899; -. DR MalaCards; TYROBP; -. DR MIM; 221770; phenotype. DR MIM; 604142; gene. DR neXtProt; NX_O43914; -. DR OpenTargets; ENSG00000011600; -. DR Orphanet; 2770; Nasu-Hakola disease. DR PharmGKB; PA37100; -. DR eggNOG; ENOG410J1XS; Eukaryota. DR eggNOG; ENOG410Z4TN; LUCA. DR GeneTree; ENSGT00390000016786; -. DR HOGENOM; HOG000056440; -. DR HOVERGEN; HBG061468; -. DR InParanoid; O43914; -. DR KO; K07992; -. DR OrthoDB; 1508977at2759; -. DR PhylomeDB; O43914; -. DR TreeFam; TF336898; -. DR Reactome; R-HSA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell. DR Reactome; R-HSA-2172127; DAP12 interactions. DR Reactome; R-HSA-2424491; DAP12 signaling. DR Reactome; R-HSA-391160; Signal regulatory protein family interactions. DR Reactome; R-HSA-416700; Other semaphorin interactions. DR Reactome; R-HSA-6798695; Neutrophil degranulation. DR SignaLink; O43914; -. DR ChiTaRS; TYROBP; human. DR EvolutionaryTrace; O43914; -. DR GeneWiki; TYROBP; -. DR GenomeRNAi; 7305; -. DR PRO; PR:O43914; -. DR Proteomes; UP000005640; Chromosome 19. DR Bgee; ENSG00000011600; Expressed in 216 organ(s), highest expression level in blood. DR ExpressionAtlas; O43914; baseline and differential. DR Genevisible; O43914; HS. DR GO; GO:0005623; C:cell; ISS:ARUK-UCL. DR GO; GO:0009986; C:cell surface; IDA:UniProtKB. DR GO; GO:0016021; C:integral component of membrane; TAS:ARUK-UCL. DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0030667; C:secretory granule membrane; TAS:Reactome. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0005102; F:signaling receptor binding; IPI:UniProtKB. DR GO; GO:0030036; P:actin cytoskeleton organization; ISS:UniProtKB. DR GO; GO:0097190; P:apoptotic signaling pathway; ISS:ARUK-UCL. DR GO; GO:0006968; P:cellular defense response; TAS:ProtInc. DR GO; GO:0030900; P:forebrain development; ISS:ARUK-UCL. DR GO; GO:0045087; P:innate immune response; TAS:Reactome. DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:Ensembl. DR GO; GO:0035556; P:intracellular signal transduction; TAS:ProtInc. DR GO; GO:0002282; P:microglial cell activation involved in immune response; ISS:UniProtKB. DR GO; GO:0002274; P:myeloid leukocyte activation; IDA:UniProtKB. DR GO; GO:0030889; P:negative regulation of B cell proliferation; IMP:UniProtKB. DR GO; GO:1900272; P:negative regulation of long-term synaptic potentiation; ISS:ARUK-UCL. DR GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome. DR GO; GO:0030316; P:osteoclast differentiation; IMP:MGI. DR GO; GO:0110090; P:positive regulation of hippocampal neuron apoptotic process; ISS:ARUK-UCL. DR GO; GO:0034241; P:positive regulation of macrophage fusion; IMP:UniProtKB. DR GO; GO:1904151; P:positive regulation of microglial cell mediated cytotoxicity; ISS:UniProtKB. DR GO; GO:0032816; P:positive regulation of natural killer cell activation; IEA:Ensembl. DR GO; GO:2001206; P:positive regulation of osteoclast development; ISS:UniProtKB. DR GO; GO:2000010; P:positive regulation of protein localization to cell surface; IMP:UniProtKB. DR GO; GO:1902685; P:positive regulation of receptor localization to synapse; ISS:ARUK-UCL. DR GO; GO:0032930; P:positive regulation of superoxide anion generation; ISS:ARUK-UCL. DR GO; GO:0050821; P:protein stabilization; IDA:UniProtKB. DR GO; GO:0050776; P:regulation of immune response; TAS:Reactome. DR GO; GO:0007165; P:signal transduction; TAS:ProtInc. DR InterPro; IPR026200; Tyrobp. DR PANTHER; PTHR17554; PTHR17554; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Complete proteome; Disulfide bond; KW Membrane; Phosphoprotein; Polymorphism; Reference proteome; Signal; KW Transmembrane; Transmembrane helix. FT SIGNAL 1 21 {ECO:0000255}. FT CHAIN 22 113 TYRO protein tyrosine kinase-binding FT protein. FT /FTId=PRO_0000022603. FT TOPO_DOM 22 40 Extracellular. {ECO:0000255}. FT TRANSMEM 41 61 Helical. {ECO:0000255}. FT TOPO_DOM 62 113 Cytoplasmic. {ECO:0000255}. FT DOMAIN 80 108 ITAM. FT SITE 54 54 Important for interaction with FT transmembrane receptors. FT MOD_RES 91 91 Phosphotyrosine. FT {ECO:0000250|UniProtKB:O54885}. FT MOD_RES 102 102 Phosphotyrosine. FT {ECO:0000250|UniProtKB:O54885}. FT DISULFID 35 35 Interchain. FT {ECO:0000269|PubMed:20890284}. FT VAR_SEQ 20 30 Missing (in isoform 3). FT {ECO:0000303|PubMed:16344560}. FT /FTId=VSP_046066. FT VAR_SEQ 77 77 Missing (in isoform 2). FT {ECO:0000303|PubMed:14702039, FT ECO:0000303|Ref.2, ECO:0000303|Ref.3}. FT /FTId=VSP_012909. FT VARIANT 111 111 Y -> H (in dbSNP:rs14714). FT /FTId=VAR_011985. FT MUTAGEN 54 54 T->A: Reduced interaction with KLRC2 and FT KIR2DS3. {ECO:0000269|PubMed:20890284}. FT HELIX 40 65 {ECO:0000244|PDB:4WOL}. SQ SEQUENCE 113 AA; 12179 MW; 267CB1C1756F89F0 CRC64; MGGLEPCSRL LLLPLLLAVS GLRPVQAQAQ SDCSCSTVSP GVLAGIVMGD LVLTVLIALA VYFLGRLVPR GRGAAEAATR KQRITETESP YQELQGQRSD VYSDLNTQRP YYK //