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}.
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; 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