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H1BP3_MOUSE
ID   H1BP3_MOUSE             Reviewed;         395 AA.
AC   Q3TC93; E9QLQ4; Q9Z1K1;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 2.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=HCLS1-binding protein 3;
DE   AltName: Full=HS1-binding protein 3;
DE            Short=HSP1BP-3;
GN   Name=Hs1bp3;
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], INTERACTION WITH HCLS1, POSSIBLE FUNCTION, AND
RP   TISSUE SPECIFICITY.
RC   STRAIN=BALB/cJ; TISSUE=Lymphocyte;
RX   PubMed=10590261; DOI=10.1093/intimm/11.12.1957;
RA   Takemoto Y., Furuta M., Sato M., Kubo M., Hashimoto Y.;
RT   "Isolation and characterization of a novel HS1 SH3 domain binding protein,
RT   HS1BP3.";
RL   Int. Immunol. 11:1957-1964(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=NOD;
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 GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Heart, Lung, Pancreas, and Spleen;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: May be a modulator of IL-2 signaling.
CC   -!- SUBUNIT: Binds HCLS1. Interacts with the SH3 domain of HCLS1 in vitro.
CC       {ECO:0000269|PubMed:10590261}.
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC       {ECO:0000269|PubMed:10590261}.
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DR   EMBL; AJ132192; CAA10600.1; -; mRNA.
DR   EMBL; AK170838; BAE42064.1; -; mRNA.
DR   EMBL; AC122860; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   CCDS; CCDS49024.1; -.
DR   RefSeq; NP_067404.2; NM_021429.3.
DR   AlphaFoldDB; Q3TC93; -.
DR   SMR; Q3TC93; -.
DR   BioGRID; 208412; 2.
DR   MINT; Q3TC93; -.
DR   STRING; 10090.ENSMUSP00000020927; -.
DR   iPTMnet; Q3TC93; -.
DR   PhosphoSitePlus; Q3TC93; -.
DR   EPD; Q3TC93; -.
DR   MaxQB; Q3TC93; -.
DR   PaxDb; Q3TC93; -.
DR   PeptideAtlas; Q3TC93; -.
DR   PRIDE; Q3TC93; -.
DR   ProteomicsDB; 271374; -.
DR   Antibodypedia; 27299; 163 antibodies from 27 providers.
DR   DNASU; 58240; -.
DR   Ensembl; ENSMUST00000020927; ENSMUSP00000020927; ENSMUSG00000020605.
DR   GeneID; 58240; -.
DR   KEGG; mmu:58240; -.
DR   UCSC; uc007mzo.2; mouse.
DR   CTD; 64342; -.
DR   MGI; MGI:1913224; Hs1bp3.
DR   VEuPathDB; HostDB:ENSMUSG00000020605; -.
DR   eggNOG; ENOG502QSUW; Eukaryota.
DR   GeneTree; ENSGT00390000013092; -.
DR   HOGENOM; CLU_057345_1_0_1; -.
DR   InParanoid; Q3TC93; -.
DR   OMA; KHKPGDV; -.
DR   OrthoDB; 1256753at2759; -.
DR   PhylomeDB; Q3TC93; -.
DR   TreeFam; TF335484; -.
DR   BioGRID-ORCS; 58240; 2 hits in 72 CRISPR screens.
DR   ChiTaRS; Hs1bp3; mouse.
DR   PRO; PR:Q3TC93; -.
DR   Proteomes; UP000000589; Chromosome 12.
DR   RNAct; Q3TC93; protein.
DR   Bgee; ENSMUSG00000020605; Expressed in ectoplacental cone and 203 other tissues.
DR   ExpressionAtlas; Q3TC93; baseline and differential.
DR   Genevisible; Q3TC93; MM.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR   GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR   GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR   GO; GO:0007166; P:cell surface receptor signaling pathway; TAS:MGI.
DR   GO; GO:0042981; P:regulation of apoptotic process; ISO:MGI.
DR   GO; GO:0030217; P:T cell differentiation; TAS:MGI.
DR   CDD; cd06868; PX_HS1BP3; 1.
DR   Gene3D; 3.30.1520.10; -; 1.
DR   InterPro; IPR039701; HS1BP3.
DR   InterPro; IPR037901; HS1BP3_PX.
DR   InterPro; IPR001683; PX_dom.
DR   InterPro; IPR036871; PX_dom_sf.
DR   PANTHER; PTHR14431; PTHR14431; 1.
DR   Pfam; PF00787; PX; 1.
DR   SMART; SM00312; PX; 1.
DR   SUPFAM; SSF64268; SSF64268; 1.
DR   PROSITE; PS50195; PX; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Phosphoprotein; Reference proteome.
FT   CHAIN           1..395
FT                   /note="HCLS1-binding protein 3"
FT                   /id="PRO_0000313803"
FT   DOMAIN          19..142
FT                   /note="PX"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00147"
FT   REGION          143..310
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          322..374
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        207..268
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        329..346
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        359..373
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:Q53T59"
FT   MOD_RES         3
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q53T59"
FT   MOD_RES         191
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q53T59"
FT   MOD_RES         254
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q53T59"
FT   MOD_RES         341
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q53T59"
FT   CONFLICT        299
FT                   /note="R -> S (in Ref. 2; BAE42064)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        392..395
FT                   /note="PSLF -> SGFQC (in Ref. 1; CAA10600)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   395 AA;  43691 MW;  5FB38580320FF456 CRC64;
     MQSPAVLRTS RQVQNAHTGL DLSVPQHQEV RGKMMSGHVE YQILVVTRLA VFKSAKHRPE
     DVVQFLVSKK YSEIEEFYQK LYSCYPAASL PPLPRKVLFV GESDIRERRA MFDEILRCVS
     KDAQLAGSPE LLEFLGTRAP GATGLATRDP SVLDDTASQP GDSDEAFDFF EQQDEVQPPT
     LGLSSKDVEK SLVGEEEEEE EEEEVLDPLG IMRSKKPKKR PEVAVRPKPA PRLTIFDEEV
     DPDAGLFSSD KKVSETRRPL ETTQDSLKLF DDPDLGGAVS LGDPLLLPAA SESRGPTSRP
     EHGDASKELF RVEEDLDLIL NLGSEPKPKP QTKPKPLVPA KPALPRKPTL PASVGPSEPG
     SGPQKQQQIQ AMDEMDILQY IRDHDTLAQD SPSLF
 
 
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