RBBP9_MOUSE
ID RBBP9_MOUSE Reviewed; 186 AA.
AC O88851; Q9CYJ9;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 26-SEP-2001, sequence version 2.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Putative hydrolase RBBP9 {ECO:0000250|UniProtKB:O75884};
DE EC=3.-.-.- {ECO:0000250|UniProtKB:O75884};
DE AltName: Full=B5T-overexpressed gene protein {ECO:0000250|UniProtKB:O88350};
DE Short=Protein BOG {ECO:0000250|UniProtKB:O88350};
DE AltName: Full=Retinoblastoma-binding protein 9;
DE Short=RBBP-9;
GN Name=Rbbp9; Synonyms=Bog;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II; TISSUE=Mammary gland;
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).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-174.
RA Woitach J.T.;
RL Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP PROTEIN SEQUENCE OF 164-179, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Hippocampus;
RA Lubec G., Klug S.;
RL Submitted (MAR-2007) to UniProtKB.
RN [5]
RP INDUCTION, AND TISSUE SPECIFICITY.
RX PubMed=16272168; DOI=10.1093/carcin/bgi261;
RA Cassie S., Koturbash I., Hudson D., Baker M., Ilnytskyy Y.,
RA Rodriguez-Juarez R., Weber E., Kovalchuk O.;
RT "Novel retinoblastoma binding protein RBBP9 modulates sex-specific
RT radiation responses in vivo.";
RL Carcinogenesis 27:465-474(2006).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
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: Serine hydrolase whose substrates have not been identified
CC yet. May negatively regulate basal or autocrine TGF-beta signaling by
CC suppressing SMAD2-SMAD3 phosphorylation. May play a role in the
CC transformation process due to its capacity to confer resistance to the
CC growth-inhibitory effects of TGF-beta through interaction with RB1 and
CC the subsequent displacement of E2F1. {ECO:0000250|UniProtKB:O75884}.
CC -!- SUBUNIT: Interacts with RB1; the interaction disrupts RB1 binding to
CC E2F1. Interacts with RBL1 and RBL2. {ECO:0000250|UniProtKB:O88350}.
CC -!- TISSUE SPECIFICITY: Expressed in spleen. {ECO:0000269|PubMed:16272168}.
CC -!- INDUCTION: Following chronic low dose of ionizing radiation, expression
CC is up-regulated in male spleen and down-regulated in female spleen (at
CC protein level). {ECO:0000269|PubMed:16272168}.
CC -!- SIMILARITY: Belongs to the RBBP9 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC63497.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AK017606; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF039563; AAC63497.1; ALT_FRAME; mRNA.
DR EMBL; AK017606; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC011107; AAH11107.1; -; mRNA.
DR CCDS; CCDS16821.1; -.
DR RefSeq; NP_056569.2; NM_015754.2.
DR AlphaFoldDB; O88851; -.
DR SMR; O88851; -.
DR BioGRID; 205000; 1.
DR STRING; 10090.ENSMUSP00000028915; -.
DR ChEMBL; CHEMBL3259487; -.
DR ESTHER; mouse-rbbp9; Hydrolase_RBBP9_YdeN.
DR iPTMnet; O88851; -.
DR PhosphoSitePlus; O88851; -.
DR SwissPalm; O88851; -.
DR REPRODUCTION-2DPAGE; O88851; -.
DR EPD; O88851; -.
DR jPOST; O88851; -.
DR MaxQB; O88851; -.
DR PaxDb; O88851; -.
DR PRIDE; O88851; -.
DR ProteomicsDB; 253179; -.
DR Antibodypedia; 9405; 327 antibodies from 28 providers.
DR DNASU; 26450; -.
DR Ensembl; ENSMUST00000028915; ENSMUSP00000028915; ENSMUSG00000027428.
DR GeneID; 26450; -.
DR KEGG; mmu:26450; -.
DR UCSC; uc008mri.1; mouse.
DR CTD; 10741; -.
DR MGI; MGI:1347074; Rbbp9.
DR VEuPathDB; HostDB:ENSMUSG00000027428; -.
DR eggNOG; ENOG502QVNM; Eukaryota.
DR GeneTree; ENSGT00390000014861; -.
DR HOGENOM; CLU_088863_1_0_1; -.
DR InParanoid; O88851; -.
DR OMA; NHWFPWL; -.
DR OrthoDB; 1320428at2759; -.
DR PhylomeDB; O88851; -.
DR TreeFam; TF106470; -.
DR BioGRID-ORCS; 26450; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Rbbp9; mouse.
DR PRO; PR:O88851; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; O88851; protein.
DR Bgee; ENSMUSG00000027428; Expressed in vestibular epithelium and 257 other tissues.
DR ExpressionAtlas; O88851; baseline and differential.
DR Genevisible; O88851; MM.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0010628; P:positive regulation of gene expression; IDA:MGI.
DR GO; GO:0042127; P:regulation of cell population proliferation; ISO:MGI.
DR GO; GO:0009624; P:response to nematode; IDA:MGI.
DR GO; GO:0060510; P:type II pneumocyte differentiation; IDA:MGI.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR010662; Hydrolase_RBBP9/YdeN.
DR Pfam; PF06821; Ser_hydrolase; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Hydrolase; Reference proteome.
FT CHAIN 1..186
FT /note="Putative hydrolase RBBP9"
FT /id="PRO_0000097181"
FT REGION 56..70
FT /note="Retinoblastoma protein binding"
FT /evidence="ECO:0000255"
FT REGION 63..67
FT /note="Involved in binding to RB1"
FT /evidence="ECO:0000250|UniProtKB:O75884"
FT ACT_SITE 75
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:O75884"
FT ACT_SITE 138
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:O75884"
FT ACT_SITE 165
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:O75884"
FT CONFLICT 131
FT /note="V -> I (in Ref. 3; AAC63497)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 186 AA; 20912 MW; A2351381F228FCCC CRC64;
MASPNKAVIV PGNGGGDVAT HGWYGWVKKG LEQIPGFQCL AKNMPDPITA RESIWLPFME
TELHCDEKTI IIGHSSGAIA AMRYAETHQV YALVLVSAYT SDLGDENERA SGYFSRPWQW
EKIKANCPHI VQFGSTDDPF LPWKEQQEVA DRLDAKLYKF TDRGHFQNTE FHELISVVKS
MLKGPE
