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Putative hydrolase RBBP9 (EC 3.-.-.-) (B5T-overexpressed gene protein) (Protein BOG) (Retinoblastoma-binding protein 10) (RBBP-10) (Retinoblastoma-binding protein 9) (RBBP-9)

 RBBP9_HUMAN             Reviewed;         186 AA.
O75884; D3DW31; Q5JPH9; Q9H1D8;
26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
26-SEP-2001, sequence version 2.
20-JUN-2018, entry version 151.
RecName: Full=Putative hydrolase RBBP9;
EC=3.-.-.-;
AltName: Full=B5T-overexpressed gene protein;
Short=Protein BOG;
AltName: Full=Retinoblastoma-binding protein 10;
Short=RBBP-10;
AltName: Full=Retinoblastoma-binding protein 9;
Short=RBBP-9;
Name=RBBP9; Synonyms=BOG, RBBP10;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND MUTAGENESIS OF LEU-63.
PubMed=9697699; DOI=10.1038/1258;
Woitach J.T., Zhang M., Niu C.-H., Thorgeirsson S.S.;
"A retinoblastoma-binding protein that affects cell-cycle control and
confers transforming ability.";
Nat. Genet. 19:371-374(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND SUBCELLULAR LOCATION.
TISSUE=Fetal brain;
PubMed=12296629; DOI=10.1023/A:1019886918029;
Chen J.-Z., Yang Q.-S., Wang S., Meng X.-F., Ying K., Xie Y.,
Mao Y.-M.;
"Cloning and expression of a novel retinoblastoma binding protein
cDNA, RBBP10.";
Biochem. Genet. 40:273-282(2002).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Lymph node;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ISOFORM 1).
PubMed=11780052; DOI=10.1038/414865a;
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M.,
Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J.,
Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P.,
Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M.,
Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R.,
Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M.,
Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H.,
Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S.,
Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E.,
Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A.,
Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M.,
Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A.,
Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S.,
Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 20.";
Nature 414:865-871(2001).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Skin;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
EMETINE INHIBITION.
PubMed=19329999; DOI=10.1038/nbt.1531;
Bachovchin D.A., Brown S.J., Rosen H., Cravatt B.F.;
"Identification of selective inhibitors of uncharacterized enzymes by
high-throughput screening with fluorescent activity-based probes.";
Nat. Biotechnol. 27:387-394(2009).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[10]
X-RAY CRYSTALLOGRAPHY (1.72 ANGSTROMS).
PubMed=19004028; DOI=10.1002/prot.22278;
Vorobiev S.M., Su M., Seetharaman J., Huang Y.J., Chen C.X.,
Maglaqui M., Janjua H., Proudfoot M., Yakunin A., Xiao R., Acton T.B.,
Montelione G.T., Tong L.;
"Crystal structure of human retinoblastoma binding protein 9.";
Proteins 74:526-529(2009).
-!- FUNCTION: May play a role in the transformation process due to its
capacity to confer resistance to the growth-inhibitory effects of
TGF-beta1 through interaction with retinoblastoma and the
subsequent displacement of E2F-1.
-!- INTERACTION:
Q9NYB0:TERF2IP; NbExp=2; IntAct=EBI-11310604, EBI-750109;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12296629}.
Nucleus {ECO:0000269|PubMed:12296629}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=O75884-1; Sequence=Displayed;
Name=2;
IsoId=O75884-2; Sequence=VSP_004374;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Widely expressed. Expressed at higher levels
in tumor tissues than in normal tissues.
-!- MISCELLANEOUS: Interacts with the serine hydrolase-directed
activity-based probe fluorophosphonate-rhodamine (FP-rhodamine).
This interaction is inhibited selectively and reversibly by
emetine, a compound with cytotoxic activity.
-!- SIMILARITY: Belongs to the RBBP9 family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF039564; AAC63498.1; -; mRNA.
EMBL; AF237576; AAL83721.1; -; mRNA.
EMBL; AL832411; CAI46193.1; -; mRNA.
EMBL; AL121893; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471133; EAX10236.1; -; Genomic_DNA.
EMBL; CH471133; EAX10237.1; -; Genomic_DNA.
EMBL; CH471133; EAX10238.1; -; Genomic_DNA.
EMBL; BC015938; AAH15938.1; -; mRNA.
CCDS; CCDS13136.1; -. [O75884-1]
RefSeq; NP_006597.2; NM_006606.2. [O75884-1]
UniGene; Hs.69330; -.
PDB; 2QS9; X-ray; 1.72 A; A/B=1-186.
PDBsum; 2QS9; -.
ProteinModelPortal; O75884; -.
SMR; O75884; -.
BioGrid; 115964; 4.
IntAct; O75884; 2.
STRING; 9606.ENSP00000336866; -.
BindingDB; O75884; -.
ChEMBL; CHEMBL1075121; -.
GuidetoPHARMACOLOGY; 2874; -.
ESTHER; human-RBBP9; Hydrolase_RBBP9_YdeN.
iPTMnet; O75884; -.
PhosphoSitePlus; O75884; -.
BioMuta; RBBP9; -.
EPD; O75884; -.
MaxQB; O75884; -.
PaxDb; O75884; -.
PeptideAtlas; O75884; -.
PRIDE; O75884; -.
ProteomicsDB; 50241; -.
ProteomicsDB; 50242; -. [O75884-2]
DNASU; 10741; -.
Ensembl; ENST00000337227; ENSP00000336866; ENSG00000089050. [O75884-1]
GeneID; 10741; -.
KEGG; hsa:10741; -.
UCSC; uc002wqy.5; human. [O75884-1]
CTD; 10741; -.
DisGeNET; 10741; -.
EuPathDB; HostDB:ENSG00000089050.14; -.
GeneCards; RBBP9; -.
HGNC; HGNC:9892; RBBP9.
HPA; HPA015830; -.
HPA; HPA049005; -.
MIM; 602908; gene.
neXtProt; NX_O75884; -.
OpenTargets; ENSG00000089050; -.
PharmGKB; PA34256; -.
eggNOG; ENOG410IK06; Eukaryota.
eggNOG; ENOG411109T; LUCA.
GeneTree; ENSGT00390000014861; -.
HOGENOM; HOG000231689; -.
HOVERGEN; HBG056175; -.
InParanoid; O75884; -.
KO; K07002; -.
OMA; ANWYGWL; -.
OrthoDB; EOG091G0MJ3; -.
PhylomeDB; O75884; -.
TreeFam; TF106470; -.
EvolutionaryTrace; O75884; -.
GeneWiki; RBBP9; -.
GenomeRNAi; 10741; -.
PRO; PR:O75884; -.
Proteomes; UP000005640; Chromosome 20.
Bgee; ENSG00000089050; -.
CleanEx; HS_RBBP9; -.
Genevisible; O75884; HS.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
GO; GO:0042127; P:regulation of cell proliferation; IEA:Ensembl.
Gene3D; 3.40.50.1820; -; 1.
InterPro; IPR029058; AB_hydrolase.
InterPro; IPR010662; Hydrolase_RBBP9/YdeN.
Pfam; PF06821; Ser_hydrolase; 1.
SUPFAM; SSF53474; SSF53474; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome; Cytoplasm;
Hydrolase; Nucleus; Phosphoprotein; Reference proteome.
CHAIN 1 186 Putative hydrolase RBBP9.
/FTId=PRO_0000097180.
REGION 56 70 Retinoblastoma protein binding.
{ECO:0000255}.
ACT_SITE 75 75 Charge relay system. {ECO:0000255}.
ACT_SITE 138 138 Charge relay system. {ECO:0000255}.
ACT_SITE 165 165 Charge relay system. {ECO:0000255}.
MOD_RES 49 49 Phosphothreonine; by CK2. {ECO:0000255}.
MOD_RES 135 135 Phosphoserine; by CK2. {ECO:0000255}.
VAR_SEQ 152 186 RLETKLHKFTDCGHFQNTEFHELITVVKSLLKVPA -> SW
TPNCTNSLTVVTFRTQSSMN (in isoform 2).
{ECO:0000303|PubMed:9697699}.
/FTId=VSP_004374.
MUTAGEN 63 63 L->Q: Loss of retinoblastoma protein
binding. {ECO:0000269|PubMed:9697699}.
CONFLICT 2 2 A -> V (in Ref. 1; AAC63498).
{ECO:0000305}.
CONFLICT 13 14 NG -> KI (in Ref. 1; AAC63498).
{ECO:0000305}.
CONFLICT 18 18 V -> E (in Ref. 1; AAC63498).
{ECO:0000305}.
CONFLICT 93 94 IV -> LI (in Ref. 1; AAC63498).
{ECO:0000305}.
CONFLICT 102 103 DL -> EF (in Ref. 1; AAC63498).
{ECO:0000305}.
CONFLICT 115 115 T -> S (in Ref. 1; AAC63498).
{ECO:0000305}.
CONFLICT 129 129 Y -> H (in Ref. 1; AAC63498).
{ECO:0000305}.
STRAND 6 10 {ECO:0000244|PDB:2QS9}.
STRAND 13 16 {ECO:0000244|PDB:2QS9}.
TURN 18 20 {ECO:0000244|PDB:2QS9}.
HELIX 24 31 {ECO:0000244|PDB:2QS9}.
STRAND 39 41 {ECO:0000244|PDB:2QS9}.
TURN 47 49 {ECO:0000244|PDB:2QS9}.
HELIX 52 61 {ECO:0000244|PDB:2QS9}.
STRAND 69 74 {ECO:0000244|PDB:2QS9}.
HELIX 76 87 {ECO:0000244|PDB:2QS9}.
STRAND 91 97 {ECO:0000244|PDB:2QS9}.
HELIX 106 110 {ECO:0000244|PDB:2QS9}.
HELIX 120 126 {ECO:0000244|PDB:2QS9}.
STRAND 128 135 {ECO:0000244|PDB:2QS9}.
STRAND 139 141 {ECO:0000244|PDB:2QS9}.
HELIX 143 153 {ECO:0000244|PDB:2QS9}.
STRAND 156 162 {ECO:0000244|PDB:2QS9}.
HELIX 172 182 {ECO:0000244|PDB:2QS9}.
SEQUENCE 186 AA; 21000 MW; F645E159DCB759BF CRC64;
MASPSKAVIV PGNGGGDVTT HGWYGWVKKE LEKIPGFQCL AKNMPDPITA RESIWLPFME
TELHCDEKTI IIGHSSGAIA AMRYAETHRV YAIVLVSAYT SDLGDENERA SGYFTRPWQW
EKIKANCPYI VQFGSTDDPF LPWKEQQEVA DRLETKLHKF TDCGHFQNTE FHELITVVKS
LLKVPA


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