STAP2_MOUSE
ID STAP2_MOUSE Reviewed; 411 AA.
AC Q8R0L1; Q8BWS2;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Signal-transducing adaptor protein 2;
DE Short=STAP-2;
GN Name=Stap2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH CSF1R, FUNCTION,
RP TISSUE SPECIFICITY, PHOSPHORYLATION, AND SUBCELLULAR LOCATION.
RC TISSUE=Fetal liver;
RX PubMed=12540842; DOI=10.1074/jbc.m211230200;
RA Minoguchi M., Minoguchi S., Aki D., Joo A., Yamamoto T., Yumioka T.,
RA Matsuda T., Yoshimura A.;
RT "STAP-2/BKS, an adaptor/docking protein, modulates STAT3 activation in
RT acute-phase response through its YXXQ motif.";
RL J. Biol. Chem. 278:11182-11189(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Liver;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Colon;
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).
CC -!- FUNCTION: Substrate of protein kinase PTK6 (By similarity). May play a
CC regulatory role in the acute-phase response in systemic inflammation
CC and may modulate STAT3 activity. {ECO:0000250,
CC ECO:0000269|PubMed:12540842}.
CC -!- SUBUNIT: Interacts with PTK6 and CSF1R. {ECO:0000269|PubMed:12540842}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12540842}. Membrane
CC {ECO:0000269|PubMed:12540842}; Peripheral membrane protein
CC {ECO:0000269|PubMed:12540842}. Note=The translocation to the membranes
CC occurs in response to EGF when the protein is overexpressed in
CC fibroblastic cells.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8R0L1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8R0L1-2; Sequence=VSP_013401, VSP_013402;
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:12540842}.
CC -!- PTM: Phosphorylated on tyrosine. Phosphorylated by PTK6 at Tyr-250
CC modulates PTK6-mediated STAT3 activation. {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; AK050131; BAC34083.1; -; mRNA.
DR EMBL; AK050172; BAC34107.1; -; mRNA.
DR EMBL; BC026642; AAH26642.1; -; mRNA.
DR CCDS; CCDS28889.1; -. [Q8R0L1-1]
DR RefSeq; NP_666046.1; NM_145934.2. [Q8R0L1-1]
DR RefSeq; XP_017172690.1; XM_017317201.1.
DR AlphaFoldDB; Q8R0L1; -.
DR SMR; Q8R0L1; -.
DR BioGRID; 223125; 6.
DR STRING; 10090.ENSMUSP00000038130; -.
DR iPTMnet; Q8R0L1; -.
DR PhosphoSitePlus; Q8R0L1; -.
DR MaxQB; Q8R0L1; -.
DR PaxDb; Q8R0L1; -.
DR PeptideAtlas; Q8R0L1; -.
DR PRIDE; Q8R0L1; -.
DR ProteomicsDB; 258638; -. [Q8R0L1-1]
DR ProteomicsDB; 258639; -. [Q8R0L1-2]
DR Antibodypedia; 1197; 312 antibodies from 35 providers.
DR DNASU; 106766; -.
DR Ensembl; ENSMUST00000043785; ENSMUSP00000038130; ENSMUSG00000038781. [Q8R0L1-1]
DR GeneID; 106766; -.
DR KEGG; mmu:106766; -.
DR UCSC; uc008dao.3; mouse. [Q8R0L1-1]
DR CTD; 55620; -.
DR MGI; MGI:2147039; Stap2.
DR VEuPathDB; HostDB:ENSMUSG00000038781; -.
DR eggNOG; ENOG502QURW; Eukaryota.
DR GeneTree; ENSGT00530000063841; -.
DR HOGENOM; CLU_043957_0_0_1; -.
DR InParanoid; Q8R0L1; -.
DR OMA; EMPACYY; -.
DR OrthoDB; 680358at2759; -.
DR PhylomeDB; Q8R0L1; -.
DR TreeFam; TF332087; -.
DR Reactome; R-MMU-8849474; PTK6 Activates STAT3.
DR BioGRID-ORCS; 106766; 1 hit in 71 CRISPR screens.
DR PRO; PR:Q8R0L1; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q8R0L1; protein.
DR Bgee; ENSMUSG00000038781; Expressed in intestinal villus and 237 other tissues.
DR Genevisible; Q8R0L1; MM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0035591; F:signaling adaptor activity; IEA:InterPro.
DR CDD; cd10404; SH2_STAP2; 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; IPR035878; STAP2_SH2.
DR PANTHER; PTHR16186; PTHR16186; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00252; SH2; 1.
DR SUPFAM; SSF55550; SSF55550; 1.
DR PROSITE; PS50001; SH2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Cytoplasm; Membrane; Phosphoprotein;
KW Reference proteome; SH2 domain.
FT CHAIN 1..411
FT /note="Signal-transducing adaptor protein 2"
FT /id="PRO_0000072240"
FT DOMAIN 20..120
FT /note="PH"
FT DOMAIN 152..248
FT /note="SH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT REGION 291..320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 338..364
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 390..410
FT /evidence="ECO:0000255"
FT COMPBIAS 349..363
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 22
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9UGK3"
FT MOD_RES 250
FT /note="Phosphotyrosine; by PTK6"
FT /evidence="ECO:0000250|UniProtKB:Q9UGK3"
FT MOD_RES 318
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9UGK3"
FT MOD_RES 330
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9UGK3"
FT VAR_SEQ 256..272
FT /note="FVDSDRENGESAWAVPS -> VCDVGLPGLDRDTLSGG (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_013401"
FT VAR_SEQ 273..411
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_013402"
SQ SEQUENCE 411 AA; 45802 MW; 485C00B703C470A8 CRC64;
MATALSPPRG PKLKGAPPSH YYESFLEKKG PCDQDYRKFW AGLQGLAICF YNSNRDLQPL
EKLDLRLFSK LRDEALLGSS RDTAYHFSLV LRDQEVKFKV ESLESCEMWK GFILTVVELR
VPSNLTLLPG HLYMMAEVLT KEEVRRAAEV PWCFLQVSRL EAQLLLERYP ECGNLLLRPG
GDGKDSVSVT TRQILNGSPV VKHYKVKRAG SKYVIDVEDP FSCPSLEAVV NYFVTHTKRA
LVPFLLDEDY EKVLGFVDSD RENGESAWAV PSFRASGPAL PANVLKPLPP VPVSVSSQED
KLPQLPPLPQ LPDTDENYVT PIEDSPAAEY MNQDVSLSSQ AVPLKPKKPA RLPAKPPKPS
VVPKPDLKAI TSVWTRKLGG SSSQASSLVT RLGDITAELE EKLQKRRALE H
