ID STAP1_HUMAN Reviewed; 295 AA. AC Q9ULZ2; B2R980; DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 24-JAN-2024, entry version 174. DE RecName: Full=Signal-transducing adaptor protein 1; DE Short=STAP-1; DE AltName: Full=BCR downstream-signaling protein 1; DE AltName: Full=Docking protein BRDG1; DE AltName: Full=Stem cell adaptor protein 1; GN Name=STAP1; Synonyms=BRDG1; 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], FUNCTION, AND PHOSPHORYLATION BY TEC. RC TISSUE=Hematopoietic; RX PubMed=10518561; DOI=10.1073/pnas.96.21.11976; RA Ohya K., Kajigaya S., Kitanaka A., Yoshida K., Miyazato A., Yamashita Y., RA Yamanaka T., Ikeda U., Shimada K., Ozawa K., Mano H.; RT "Molecular cloning of a docking protein, BRDG1, that acts downstream of the RT Tec tyrosine kinase."; RL Proc. Natl. Acad. Sci. U.S.A. 96:11976-11981(1999). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Thalamus; 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]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=B-cell; 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 URI1, AND SUBCELLULAR LOCATION. RX PubMed=17936702; DOI=10.1016/j.molcel.2007.08.010; RA Djouder N., Metzler S.C., Schmidt A., Wirbelauer C., Gstaiger M., RA Aebersold R., Hess D., Krek W.; RT "S6K1-mediated disassembly of mitochondrial URI/PP1gamma complexes RT activates a negative feedback program that counters S6K1 survival RT signaling."; RL Mol. Cell 28:28-40(2007). RN [6] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [7] RP STRUCTURE BY NMR OF 16-151. RG RIKEN structural genomics initiative (RSGI); RT "Solution structure of the PH domain of human docking protein BRDG1."; RL Submitted (OCT-2005) to the PDB data bank. CC -!- FUNCTION: In BCR signaling, appears to function as a docking protein CC acting downstream of TEC and participates in a positive feedback loop CC by increasing the activity of TEC. {ECO:0000269|PubMed:10518561}. CC -!- SUBUNIT: Interacts with KIT and CSF1R (By similarity). Interacts with CC URI1; the interaction is phosphorylation-dependent and occurs in a CC growth-dependent manner. {ECO:0000250, ECO:0000269|PubMed:17936702}. CC -!- INTERACTION: CC Q9ULZ2; P10275: AR; NbExp=2; IntAct=EBI-6083058, EBI-608057; CC Q9ULZ2; Q13480: GAB1; NbExp=3; IntAct=EBI-6083058, EBI-517684; CC Q9ULZ2; Q4V328: GRIPAP1; NbExp=3; IntAct=EBI-6083058, EBI-717919; CC Q9ULZ2; P10721: KIT; NbExp=3; IntAct=EBI-6083058, EBI-1379503; CC Q9ULZ2; P08581: MET; NbExp=3; IntAct=EBI-6083058, EBI-1039152; CC Q9ULZ2; Q86VR2: RETREG3; NbExp=8; IntAct=EBI-6083058, EBI-10192441; CC Q9ULZ2; Q96B97: SH3KBP1; NbExp=5; IntAct=EBI-6083058, EBI-346595; CC Q9ULZ2; Q5JPT6; NbExp=5; IntAct=EBI-6083058, EBI-10244213; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17936702}. Cytoplasm CC {ECO:0000269|PubMed:17936702}. Mitochondrion CC {ECO:0000269|PubMed:17936702}. CC -!- PTM: Phosphorylated on tyrosine by TEC. Phosphorylated on tyrosine by CC KIT (By similarity). {ECO:0000250}. 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; AB023483; BAA85311.1; -; mRNA. DR EMBL; AK313676; BAG36427.1; -; mRNA. DR EMBL; CH471057; EAX05547.1; -; Genomic_DNA. DR EMBL; BC014958; AAH14958.1; -; mRNA. DR CCDS; CCDS3515.1; -. DR RefSeq; NP_001304698.1; NM_001317769.1. DR RefSeq; NP_036240.1; NM_012108.3. DR PDB; 1X1F; NMR; -; A=16-151. DR PDB; 3MAZ; X-ray; 1.90 A; A=167-285. DR PDBsum; 1X1F; -. DR PDBsum; 3MAZ; -. DR AlphaFoldDB; Q9ULZ2; -. DR SMR; Q9ULZ2; -. DR BioGRID; 117619; 21. DR CORUM; Q9ULZ2; -. DR IntAct; Q9ULZ2; 45. DR MINT; Q9ULZ2; -. DR STRING; 9606.ENSP00000265404; -. DR iPTMnet; Q9ULZ2; -. DR PhosphoSitePlus; Q9ULZ2; -. DR BioMuta; STAP1; -. DR DMDM; 62511239; -. DR EPD; Q9ULZ2; -. DR MassIVE; Q9ULZ2; -. DR MaxQB; Q9ULZ2; -. DR PaxDb; 9606-ENSP00000265404; -. DR PeptideAtlas; Q9ULZ2; -. DR ProteomicsDB; 85157; -. DR TopDownProteomics; Q9ULZ2; -. DR Antibodypedia; 24136; 228 antibodies from 22 providers. DR DNASU; 26228; -. DR Ensembl; ENST00000265404.7; ENSP00000265404.2; ENSG00000035720.8. DR Ensembl; ENST00000396225.1; ENSP00000379527.1; ENSG00000035720.8. DR GeneID; 26228; -. DR KEGG; hsa:26228; -. DR MANE-Select; ENST00000265404.7; ENSP00000265404.2; NM_012108.4; NP_036240.1. DR UCSC; uc003hde.4; human. DR AGR; HGNC:24133; -. DR CTD; 26228; -. DR DisGeNET; 26228; -. DR GeneCards; STAP1; -. DR HGNC; HGNC:24133; STAP1. DR HPA; ENSG00000035720; Tissue enriched (lymphoid). DR MIM; 604298; gene. DR neXtProt; NX_Q9ULZ2; -. DR OpenTargets; ENSG00000035720; -. DR Orphanet; 406; NON RARE IN EUROPE: Heterozygous familial hypercholesterolemia. DR PharmGKB; PA162404948; -. DR VEuPathDB; HostDB:ENSG00000035720; -. DR eggNOG; ENOG502RZ9C; Eukaryota. DR GeneTree; ENSGT00530000063841; -. DR HOGENOM; CLU_043957_1_0_1; -. DR InParanoid; Q9ULZ2; -. DR OMA; PLYFQGY; -. DR OrthoDB; 4259410at2759; -. DR PhylomeDB; Q9ULZ2; -. DR TreeFam; TF332087; -. DR PathwayCommons; Q9ULZ2; -. DR SignaLink; Q9ULZ2; -. DR SIGNOR; Q9ULZ2; -. DR BioGRID-ORCS; 26228; 15 hits in 1156 CRISPR screens. DR ChiTaRS; STAP1; human. DR EvolutionaryTrace; Q9ULZ2; -. DR GeneWiki; STAP1; -. DR GenomeRNAi; 26228; -. DR Pharos; Q9ULZ2; Tbio. DR PRO; PR:Q9ULZ2; -. DR Proteomes; UP000005640; Chromosome 4. DR RNAct; Q9ULZ2; Protein. DR Bgee; ENSG00000035720; Expressed in lymph node and 101 other cell types or tissues. DR ExpressionAtlas; Q9ULZ2; baseline and differential. DR GO; GO:0034451; C:centriolar satellite; IDA:HPA. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0032991; C:protein-containing complex; IDA:MGI. DR GO; GO:0005157; F:macrophage colony-stimulating factor receptor binding; IEA:Ensembl. DR GO; GO:0005543; F:phospholipid binding; NAS:BHF-UCL. DR GO; GO:0001784; F:phosphotyrosine residue binding; IPI:BHF-UCL. DR GO; GO:0019901; F:protein kinase binding; IPI:BHF-UCL. DR GO; GO:0030296; F:protein tyrosine kinase activator activity; IDA:BHF-UCL. DR GO; GO:0035591; F:signaling adaptor activity; IPI:BHF-UCL. DR GO; GO:0005068; F:transmembrane receptor protein tyrosine kinase adaptor activity; ISS:BHF-UCL. DR GO; GO:0071222; P:cellular response to lipopolysaccharide; ISS:BHF-UCL. DR GO; GO:0010760; P:negative regulation of macrophage chemotaxis; ISS:BHF-UCL. DR GO; GO:1902227; P:negative regulation of macrophage colony-stimulating factor signaling pathway; ISS:BHF-UCL. DR GO; GO:1904140; P:negative regulation of microglial cell migration; IEA:Ensembl. DR GO; GO:0042326; P:negative regulation of phosphorylation; ISS:BHF-UCL. DR GO; GO:1900028; P:negative regulation of ruffle assembly; ISS:BHF-UCL. DR GO; GO:0050861; P:positive regulation of B cell receptor signaling pathway; IDA:BHF-UCL. DR GO; GO:0010628; P:positive regulation of gene expression; ISS:BHF-UCL. DR GO; GO:1903980; P:positive regulation of microglial cell activation; ISS:BHF-UCL. DR GO; GO:1904151; P:positive regulation of microglial cell mediated cytotoxicity; ISS:BHF-UCL. DR GO; GO:0060100; P:positive regulation of phagocytosis, engulfment; ISS:BHF-UCL. DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; ISS:BHF-UCL. DR CDD; cd13268; PH_Brdg1; 1. DR CDD; cd10403; SH2_STAP1; 1. DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1. DR Gene3D; 3.30.505.10; SH2 domain; 1. DR InterPro; IPR011993; PH-like_dom_sf. DR InterPro; IPR001849; PH_domain. DR InterPro; IPR000980; SH2. DR InterPro; IPR036860; SH2_dom_sf. DR InterPro; IPR039111; STAP1/STAP2. DR InterPro; IPR035877; STAP1_SH2. DR PANTHER; PTHR16186:SF10; SIGNAL-TRANSDUCING ADAPTOR PROTEIN 1; 1. DR PANTHER; PTHR16186; SIGNAL-TRANSDUCING ADAPTOR PROTEIN-RELATED; 1. DR Pfam; PF00169; PH; 1. DR Pfam; PF00017; SH2; 1. DR SMART; SM00233; PH; 1. DR SMART; SM00252; SH2; 1. DR SUPFAM; SSF50729; PH domain-like; 1. DR SUPFAM; SSF55550; SH2 domain; 1. DR PROSITE; PS50003; PH_DOMAIN; 1. DR PROSITE; PS50001; SH2; 1. DR Genevisible; Q9ULZ2; HS. PE 1: Evidence at protein level; KW 3D-structure; Cytoplasm; Mitochondrion; Nucleus; Phosphoprotein; KW Reference proteome; SH2 domain. FT CHAIN 1..295 FT /note="Signal-transducing adaptor protein 1" FT /id="PRO_0000072237" FT DOMAIN 25..121 FT /note="PH" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145" FT DOMAIN 177..280 FT /note="SH2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191" FT REGION 270..295 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 279..295 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 168 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:Q9JM90" FT STRAND 22..24 FT /evidence="ECO:0007829|PDB:1X1F" FT STRAND 26..35 FT /evidence="ECO:0007829|PDB:1X1F" FT STRAND 43..50 FT /evidence="ECO:0007829|PDB:1X1F" FT STRAND 53..58 FT /evidence="ECO:0007829|PDB:1X1F" FT STRAND 66..68 FT /evidence="ECO:0007829|PDB:1X1F" FT STRAND 76..79 FT /evidence="ECO:0007829|PDB:1X1F" FT STRAND 89..93 FT /evidence="ECO:0007829|PDB:1X1F" FT STRAND 99..102 FT /evidence="ECO:0007829|PDB:1X1F" FT HELIX 106..121 FT /evidence="ECO:0007829|PDB:1X1F" FT HELIX 132..149 FT /evidence="ECO:0007829|PDB:1X1F" FT HELIX 184..193 FT /evidence="ECO:0007829|PDB:3MAZ" FT HELIX 195..197 FT /evidence="ECO:0007829|PDB:3MAZ" FT STRAND 199..204 FT /evidence="ECO:0007829|PDB:3MAZ" FT STRAND 208..217 FT /evidence="ECO:0007829|PDB:3MAZ" FT STRAND 219..221 FT /evidence="ECO:0007829|PDB:3MAZ" FT STRAND 223..232 FT /evidence="ECO:0007829|PDB:3MAZ" FT STRAND 235..238 FT /evidence="ECO:0007829|PDB:3MAZ" FT STRAND 240..242 FT /evidence="ECO:0007829|PDB:3MAZ" FT STRAND 244..248 FT /evidence="ECO:0007829|PDB:3MAZ" FT HELIX 249..259 FT /evidence="ECO:0007829|PDB:3MAZ" FT TURN 260..262 FT /evidence="ECO:0007829|PDB:3MAZ" SQ SEQUENCE 295 AA; 34291 MW; 8C242AC5C61038E0 CRC64; MMAKKPPKPA PRRIFQERLK ITALPLYFEG FLLIKRSGYR EYEHYWTELR GTTLFFYTDK KSIIYVDKLD IVDLTCLTEQ NSTEKNCAKF TLVLPKEEVQ LKTENTESGE EWRGFILTVT ELSVPQNVSL LPGQVIKLHE VLEREKKRRI ETEQSTSVEK EKEPTEDYVD VLNPMPACFY TVSRKEATEM LQKNPSLGNM ILRPGSDSRN YSITIRQEID IPRIKHYKVM SVGQNYTIEL EKPVTLPNLF SVIDYFVKET RGNLRPFICS TDENTGQEPS MEGRSEKLKK NPHIA //