STAP1_HUMAN
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 03-AUG-2022, entry version 166.
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}.
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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; Q9ULZ2; -.
DR PeptideAtlas; Q9ULZ2; -.
DR PRIDE; Q9ULZ2; -.
DR ProteomicsDB; 85157; -.
DR TopDownProteomics; Q9ULZ2; -.
DR Antibodypedia; 24136; 217 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 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; PACFFDV; -.
DR OrthoDB; 680358at2759; -.
DR PhylomeDB; Q9ULZ2; -.
DR TreeFam; TF332087; -.
DR PathwayCommons; Q9ULZ2; -.
DR SignaLink; Q9ULZ2; -.
DR SIGNOR; Q9ULZ2; -.
DR BioGRID-ORCS; 26228; 14 hits in 1078 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 99 other tissues.
DR ExpressionAtlas; Q9ULZ2; baseline and differential.
DR Genevisible; Q9ULZ2; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; 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:2000251; P:positive regulation of actin cytoskeleton reorganization; 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; cd10403; SH2_STAP1; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 3.30.505.10; -; 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; PTHR16186; 1.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00017; SH2; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00252; SH2; 1.
DR SUPFAM; SSF55550; SSF55550; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50001; SH2; 1.
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
