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HCLS1-binding protein 3 (HS1-binding protein 3) (HSP1BP-3)

 H1BP3_MOUSE             Reviewed;         395 AA.
Q3TC93; E9QLQ4; Q9Z1K1;
15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 2.
23-MAY-2018, entry version 89.
RecName: Full=HCLS1-binding protein 3;
AltName: Full=HS1-binding protein 3;
Short=HSP1BP-3;
Name=Hs1bp3;
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], INTERACTION WITH HCLS1, POSSIBLE FUNCTION,
AND TISSUE SPECIFICITY.
STRAIN=BALB/cJ; TISSUE=Lymphocyte;
PubMed=10590261; DOI=10.1093/intimm/11.12.1957;
Takemoto Y., Furuta M., Sato M., Kubo M., Hashimoto Y.;
"Isolation and characterization of a novel HS1 SH3 domain binding
protein, HS1BP3.";
Int. Immunol. 11:1957-1964(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=NOD;
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 GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[4]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Heart, Lung, Pancreas, and 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 be a modulator of IL-2 signaling.
-!- SUBUNIT: Binds HCLS1. Interacts with the SH3 domain of HCLS1 in
vitro. {ECO:0000269|PubMed:10590261}.
-!- TISSUE SPECIFICITY: Ubiquitously expressed.
{ECO:0000269|PubMed:10590261}.
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EMBL; AJ132192; CAA10600.1; -; mRNA.
EMBL; AK170838; BAE42064.1; -; mRNA.
EMBL; AC122860; -; NOT_ANNOTATED_CDS; Genomic_DNA.
CCDS; CCDS49024.1; -.
RefSeq; NP_067404.2; NM_021429.3.
UniGene; Mm.309954; -.
ProteinModelPortal; Q3TC93; -.
SMR; Q3TC93; -.
BioGrid; 208412; 2.
IntAct; Q3TC93; 2.
MINT; Q3TC93; -.
STRING; 10090.ENSMUSP00000020927; -.
iPTMnet; Q3TC93; -.
PhosphoSitePlus; Q3TC93; -.
EPD; Q3TC93; -.
MaxQB; Q3TC93; -.
PaxDb; Q3TC93; -.
PeptideAtlas; Q3TC93; -.
PRIDE; Q3TC93; -.
DNASU; 58240; -.
Ensembl; ENSMUST00000020927; ENSMUSP00000020927; ENSMUSG00000020605.
GeneID; 58240; -.
KEGG; mmu:58240; -.
UCSC; uc007mzo.2; mouse.
CTD; 64342; -.
MGI; MGI:1913224; Hs1bp3.
eggNOG; ENOG410IGRU; Eukaryota.
eggNOG; ENOG41121IK; LUCA.
GeneTree; ENSGT00390000013092; -.
HOGENOM; HOG000112839; -.
HOVERGEN; HBG098900; -.
InParanoid; Q3TC93; -.
OMA; IRDHDTP; -.
OrthoDB; EOG091G12JB; -.
TreeFam; TF335484; -.
ChiTaRS; Hs1bp3; mouse.
PRO; PR:Q3TC93; -.
Proteomes; UP000000589; Chromosome 12.
Bgee; ENSMUSG00000020605; -.
CleanEx; MM_HS1BP3; -.
ExpressionAtlas; Q3TC93; baseline and differential.
Genevisible; Q3TC93; MM.
GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
GO; GO:0005739; C:mitochondrion; ISO:MGI.
GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
GO; GO:0007166; P:cell surface receptor signaling pathway; TAS:MGI.
GO; GO:0042981; P:regulation of apoptotic process; ISO:MGI.
GO; GO:0030217; P:T cell differentiation; TAS:MGI.
CDD; cd06868; PX_HS1BP3; 1.
Gene3D; 3.30.1520.10; -; 1.
InterPro; IPR037901; HS1BP3_PX.
InterPro; IPR001683; Phox.
InterPro; IPR036871; PX_dom_sf.
Pfam; PF00787; PX; 1.
SMART; SM00312; PX; 1.
SUPFAM; SSF64268; SSF64268; 1.
PROSITE; PS50195; PX; 1.
1: Evidence at protein level;
Acetylation; Complete proteome; Phosphoprotein; Reference proteome.
CHAIN 1 395 HCLS1-binding protein 3.
/FTId=PRO_0000313803.
DOMAIN 19 142 PX. {ECO:0000255|PROSITE-
ProRule:PRU00147}.
COMPBIAS 195 204 Poly-Glu.
COMPBIAS 217 231 Pro-rich.
COMPBIAS 273 300 Pro-rich.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000250|UniProtKB:Q53T59}.
MOD_RES 3 3 Phosphoserine.
{ECO:0000250|UniProtKB:Q53T59}.
MOD_RES 191 191 Phosphoserine.
{ECO:0000250|UniProtKB:Q53T59}.
MOD_RES 254 254 Phosphoserine.
{ECO:0000250|UniProtKB:Q53T59}.
MOD_RES 341 341 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q53T59}.
CONFLICT 299 299 R -> S (in Ref. 2; BAE42064).
{ECO:0000305}.
CONFLICT 392 395 PSLF -> SGFQC (in Ref. 1; CAA10600).
{ECO:0000305}.
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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