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Signal-transducing adaptor protein 1 (STAP-1) (Stem cell adaptor protein 1)

 STAP1_MOUSE             Reviewed;         297 AA.
Q9JM90; A6H6C6; Q3TRM1; Q6PES6;
12-APR-2005, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 1.
22-NOV-2017, entry version 125.
RecName: Full=Signal-transducing adaptor protein 1;
Short=STAP-1;
AltName: Full=Stem cell adaptor protein 1;
Name=Stap1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, PHOSPHORYLATION,
INTERACTION WITH KIT AND CSF1R, AND TISSUE SPECIFICITY.
PubMed=10679268; DOI=10.1006/bbrc.2000.2223;
Masuhara M., Nagao K., Nishikawa M., Sasaki M., Yoshimura A.,
Osawa M.;
"Molecular cloning of murine STAP-1, the stem-cell-specific adaptor
protein containing PH and SH2 domains.";
Biochem. Biophys. Res. Commun. 268:697-703(2000).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=C57BL/6J; TISSUE=Bone, and Thymus;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
STRAIN=FVB/N; TISSUE=Brain, and Mammary gland;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-170, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Mast cell;
PubMed=17947660; DOI=10.4049/jimmunol.179.9.5864;
Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
Kawakami T., Salomon A.R.;
"Quantitative time-resolved phosphoproteomic analysis of mast cell
signaling.";
J. Immunol. 179:5864-5876(2007).
[5]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Spleen;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: May function as an adapter molecule downstream of KIT in
the proliferation or differentiation of hematopoietic stem cells.
{ECO:0000269|PubMed:10679268}.
-!- SUBUNIT: Interacts with URI1; the interaction is phosphorylation-
dependent occurs in a growth-dependent manner (By similarity).
Interacts with KIT and CSF1R. {ECO:0000250,
ECO:0000269|PubMed:10679268}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm
{ECO:0000305}. Mitochondrion {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9JM90-1; Sequence=Displayed;
Name=2;
IsoId=Q9JM90-2; Sequence=VSP_013399, VSP_013400;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Expression restricted to the bone marrow.
{ECO:0000269|PubMed:10679268}.
-!- PTM: Phosphorylated on tyrosine by TEC. Phosphorylated on tyrosine
by KIT. {ECO:0000250}.
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EMBL; AB036058; BAA92531.1; -; mRNA.
EMBL; AK041474; BAC30953.1; -; mRNA.
EMBL; AK162655; BAE37007.1; -; mRNA.
EMBL; BC057898; AAH57898.1; -; mRNA.
EMBL; BC145828; AAI45829.1; -; mRNA.
EMBL; BC145830; AAI45831.1; -; mRNA.
CCDS; CCDS19377.1; -. [Q9JM90-1]
RefSeq; NP_001297568.1; NM_001310639.1.
RefSeq; NP_064376.1; NM_019992.4. [Q9JM90-1]
RefSeq; XP_006535224.1; XM_006535161.3. [Q9JM90-2]
UniGene; Mm.131237; -.
ProteinModelPortal; Q9JM90; -.
SMR; Q9JM90; -.
BioGrid; 208177; 4.
STRING; 10090.ENSMUSP00000031171; -.
iPTMnet; Q9JM90; -.
PhosphoSitePlus; Q9JM90; -.
EPD; Q9JM90; -.
PaxDb; Q9JM90; -.
PeptideAtlas; Q9JM90; -.
PRIDE; Q9JM90; -.
Ensembl; ENSMUST00000198435; ENSMUSP00000143251; ENSMUSG00000029254. [Q9JM90-1]
GeneID; 56792; -.
KEGG; mmu:56792; -.
UCSC; uc008xxf.1; mouse. [Q9JM90-2]
UCSC; uc008xxg.1; mouse. [Q9JM90-1]
CTD; 26228; -.
MGI; MGI:1926193; Stap1.
eggNOG; ENOG410IGPX; Eukaryota.
eggNOG; ENOG4111PK4; LUCA.
GeneTree; ENSGT00530000063841; -.
HOGENOM; HOG000234375; -.
HOVERGEN; HBG062262; -.
InParanoid; Q9JM90; -.
OMA; YWTELRG; -.
OrthoDB; EOG091G0929; -.
PhylomeDB; Q9JM90; -.
TreeFam; TF332087; -.
PRO; PR:Q9JM90; -.
Proteomes; UP000000589; Chromosome 5.
Bgee; ENSMUSG00000029254; -.
CleanEx; MM_STAP1; -.
ExpressionAtlas; Q9JM90; baseline and differential.
Genevisible; Q9JM90; MM.
GO; GO:0005737; C:cytoplasm; ISO:MGI.
GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
GO; GO:0005739; C:mitochondrion; ISO:MGI.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; ISO:MGI.
GO; GO:0043234; C:protein complex; ISO:MGI.
GO; GO:0005157; F:macrophage colony-stimulating factor receptor binding; IPI:BHF-UCL.
GO; GO:0001784; F:phosphotyrosine residue binding; ISO:MGI.
GO; GO:0019901; F:protein kinase binding; ISO:MGI.
GO; GO:0030971; F:receptor tyrosine kinase binding; IPI:BHF-UCL.
GO; GO:0005070; F:SH3/SH2 adaptor activity; IDA:MGI.
GO; GO:0005068; F:transmembrane receptor protein tyrosine kinase adaptor activity; IDA:BHF-UCL.
GO; GO:0071222; P:cellular response to lipopolysaccharide; IDA:BHF-UCL.
GO; GO:0030099; P:myeloid cell differentiation; TAS:MGI.
GO; GO:0010760; P:negative regulation of macrophage chemotaxis; IMP:BHF-UCL.
GO; GO:1902227; P:negative regulation of macrophage colony-stimulating factor signaling pathway; IMP:BHF-UCL.
GO; GO:1904140; P:negative regulation of microglial cell migration; IMP:BHF-UCL.
GO; GO:0042326; P:negative regulation of phosphorylation; IDA:BHF-UCL.
GO; GO:1900028; P:negative regulation of ruffle assembly; IMP:BHF-UCL.
GO; GO:2000251; P:positive regulation of actin cytoskeleton reorganization; IMP:BHF-UCL.
GO; GO:0050861; P:positive regulation of B cell receptor signaling pathway; ISO:MGI.
GO; GO:0010628; P:positive regulation of gene expression; IDA:BHF-UCL.
GO; GO:1903980; P:positive regulation of microglial cell activation; IMP:BHF-UCL.
GO; GO:1904151; P:positive regulation of microglial cell mediated cytotoxicity; IDA:BHF-UCL.
GO; GO:1903997; P:positive regulation of non-membrane spanning protein tyrosine kinase activity; ISO:MGI.
GO; GO:0060100; P:positive regulation of phagocytosis, engulfment; IDA:BHF-UCL.
GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IDA:BHF-UCL.
CDD; cd10403; SH2_STAP1; 1.
Gene3D; 2.30.29.30; -; 1.
Gene3D; 3.30.505.10; -; 1.
InterPro; IPR011993; PH-like_dom_sf.
InterPro; IPR001849; PH_domain.
InterPro; IPR000980; SH2.
InterPro; IPR036860; SH2_dom_sf.
InterPro; IPR035877; STAP1_SH2.
Pfam; PF00169; PH; 1.
SMART; SM00233; PH; 1.
SMART; SM00252; SH2; 1.
SUPFAM; SSF50729; SSF50729; 1.
SUPFAM; SSF55550; SSF55550; 1.
PROSITE; PS50003; PH_DOMAIN; 1.
PROSITE; PS50001; SH2; 1.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Cytoplasm; Mitochondrion;
Nucleus; Phosphoprotein; Reference proteome; SH2 domain.
CHAIN 1 297 Signal-transducing adaptor protein 1.
/FTId=PRO_0000072238.
DOMAIN 25 121 PH. {ECO:0000255|PROSITE-
ProRule:PRU00145}.
DOMAIN 179 273 SH2. {ECO:0000255|PROSITE-
ProRule:PRU00191}.
MOD_RES 170 170 Phosphotyrosine.
{ECO:0000244|PubMed:17947660}.
VAR_SEQ 122 127 LTVPQH -> VIRFPL (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_013399.
VAR_SEQ 128 297 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_013400.
SEQUENCE 297 AA; 34628 MW; 8033C606990AAA75 CRC64;
MMAKKPPKPA PRRIFQERLK ITALPLYFEG FLLVKRSDHQ EYKHYWTELR GTTLFFYTDK
KSTIYVGKLD IIDLVCLTGQ HSTEKNCAKF TLVLPKEEVH VKTENTESGE EWRGFILTVT
ELTVPQHVSL LPGQVIRLHE VLEREKKRRI ETDQLPLMPP EKEKEPVQDY ADVLNPLPEC
FYAVSRKEAT AMLEKNPSWG NMILRPGSDS KNYSITIRQE IEMPRIKHFK VTRTGNNYTI
ELEKPVTLPN LFSVIDYFVK ETRGNLRPFI HSADDNFGQD PNIEDRSEKF KKNPHNA


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