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O75884

- RBBP9_HUMAN

UniProt

O75884 - RBBP9_HUMAN

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Protein
Putative hydrolase RBBP9
Gene
RBBP9, BOG, RBBP10
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei75 – 751Charge relay system Reviewed prediction
Active sitei138 – 1381Charge relay system Reviewed prediction
Active sitei165 – 1651Charge relay system Reviewed prediction

GO - Molecular functioni

  1. hydrolase activity Source: UniProtKB-KW
Complete GO annotation...

GO - Biological processi

  1. regulation of cell proliferation Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Names & Taxonomyi

Protein namesi
Recommended name:
Putative hydrolase RBBP9 (EC:3.-.-.-)
Alternative name(s):
B5T-overexpressed gene protein
Short name:
Protein BOG
Retinoblastoma-binding protein 10
Short name:
RBBP-10
Retinoblastoma-binding protein 9
Short name:
RBBP-9
Gene namesi
Name:RBBP9
Synonyms:BOG, RBBP10
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 20

Organism-specific databases

HGNCiHGNC:9892. RBBP9.

Subcellular locationi

Cytoplasm. Nucleus 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. extracellular vesicular exosome Source: UniProt
  3. nucleolus Source: HPA
  4. nucleus Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi63 – 631L → Q: Loss of retinoblastoma protein binding. 1 Publication

Organism-specific databases

PharmGKBiPA34256.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 186186Putative hydrolase RBBP9
PRO_0000097180Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei49 – 491Phosphothreonine; by CK2 Reviewed prediction
Modified residuei135 – 1351Phosphoserine; by CK2 Reviewed prediction

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiO75884.
PaxDbiO75884.
PeptideAtlasiO75884.
PRIDEiO75884.

PTM databases

PhosphoSiteiO75884.

Expressioni

Tissue specificityi

Widely expressed. Expressed at higher levels in tumor tissues than in normal tissues.

Gene expression databases

BgeeiO75884.
CleanExiHS_RBBP9.
GenevestigatoriO75884.

Organism-specific databases

HPAiHPA015830.
HPA049005.

Interactioni

Protein-protein interaction databases

BioGridi115964. 5 interactions.
STRINGi9606.ENSP00000336866.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi6 – 105
Beta strandi13 – 164
Turni18 – 203
Helixi24 – 318
Beta strandi39 – 413
Turni47 – 493
Helixi52 – 6110
Beta strandi69 – 746
Helixi76 – 8712
Beta strandi91 – 977
Helixi106 – 1105
Helixi120 – 1267
Beta strandi128 – 1358
Beta strandi139 – 1413
Helixi143 – 15311
Beta strandi156 – 1627
Helixi172 – 18211

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2QS9X-ray1.72A/B1-186[»]
ProteinModelPortaliO75884.
SMRiO75884. Positions 3-186.

Miscellaneous databases

EvolutionaryTraceiO75884.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni56 – 7015Retinoblastoma protein binding Reviewed prediction
Add
BLAST

Sequence similaritiesi

Belongs to the RBBP9 family.

Phylogenomic databases

eggNOGiNOG79530.
HOGENOMiHOG000231689.
HOVERGENiHBG056175.
InParanoidiO75884.
KOiK07002.
OMAiHCDERTI.
OrthoDBiEOG7XWPPP.
PhylomeDBiO75884.
TreeFamiTF106470.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR010662. Hydrolase_RBBP9/YdeN.
[Graphical view]
PfamiPF06821. Ser_hydrolase. 1 hit.
[Graphical view]
SUPFAMiSSF53474. SSF53474. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: O75884-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

MASPSKAVIV PGNGGGDVTT HGWYGWVKKE LEKIPGFQCL AKNMPDPITA    50
RESIWLPFME TELHCDEKTI IIGHSSGAIA AMRYAETHRV YAIVLVSAYT 100
SDLGDENERA SGYFTRPWQW EKIKANCPYI VQFGSTDDPF LPWKEQQEVA 150
DRLETKLHKF TDCGHFQNTE FHELITVVKS LLKVPA 186
Length:186
Mass (Da):21,000
Last modified:September 26, 2001 - v2
Checksum:iF645E159DCB759BF
GO
Isoform 2 (identifier: O75884-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     152-186: RLETKLHKFTDCGHFQNTEFHELITVVKSLLKVPA → SWTPNCTNSLTVVTFRTQSSMN

Note: No experimental confirmation available.

Show »
Length:173
Mass (Da):19,394
Checksum:i4BA65444A2BD291D
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei152 – 18635RLETK…LKVPA → SWTPNCTNSLTVVTFRTQSS MN in isoform 2.
VSP_004374Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti2 – 21A → V in AAC63498. 1 Publication
Sequence conflicti13 – 142NG → KI in AAC63498. 1 Publication
Sequence conflicti18 – 181V → E in AAC63498. 1 Publication
Sequence conflicti93 – 942IV → LI in AAC63498. 1 Publication
Sequence conflicti102 – 1032DL → EF in AAC63498. 1 Publication
Sequence conflicti115 – 1151T → S in AAC63498. 1 Publication
Sequence conflicti129 – 1291Y → H in AAC63498. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF039564 mRNA. Translation: AAC63498.1.
AF237576 mRNA. Translation: AAL83721.1.
AL832411 mRNA. Translation: CAI46193.1.
AL121893 Genomic DNA. Translation: CAC11112.1.
CH471133 Genomic DNA. Translation: EAX10236.1.
CH471133 Genomic DNA. Translation: EAX10237.1.
CH471133 Genomic DNA. Translation: EAX10238.1.
BC015938 mRNA. Translation: AAH15938.1.
CCDSiCCDS13136.1. [O75884-1]
RefSeqiNP_006597.2. NM_006606.2. [O75884-1]
UniGeneiHs.69330.

Genome annotation databases

EnsembliENST00000337227; ENSP00000336866; ENSG00000089050. [O75884-1]
GeneIDi10741.
KEGGihsa:10741.
UCSCiuc002wqy.3. human. [O75884-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF039564 mRNA. Translation: AAC63498.1 .
AF237576 mRNA. Translation: AAL83721.1 .
AL832411 mRNA. Translation: CAI46193.1 .
AL121893 Genomic DNA. Translation: CAC11112.1 .
CH471133 Genomic DNA. Translation: EAX10236.1 .
CH471133 Genomic DNA. Translation: EAX10237.1 .
CH471133 Genomic DNA. Translation: EAX10238.1 .
BC015938 mRNA. Translation: AAH15938.1 .
CCDSi CCDS13136.1. [O75884-1 ]
RefSeqi NP_006597.2. NM_006606.2. [O75884-1 ]
UniGenei Hs.69330.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2QS9 X-ray 1.72 A/B 1-186 [» ]
ProteinModelPortali O75884.
SMRi O75884. Positions 3-186.
ModBasei Search...

Protein-protein interaction databases

BioGridi 115964. 5 interactions.
STRINGi 9606.ENSP00000336866.

Chemistry

BindingDBi O75884.
ChEMBLi CHEMBL1075121.

PTM databases

PhosphoSitei O75884.

Proteomic databases

MaxQBi O75884.
PaxDbi O75884.
PeptideAtlasi O75884.
PRIDEi O75884.

Protocols and materials databases

DNASUi 10741.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000337227 ; ENSP00000336866 ; ENSG00000089050 . [O75884-1 ]
GeneIDi 10741.
KEGGi hsa:10741.
UCSCi uc002wqy.3. human. [O75884-1 ]

Organism-specific databases

CTDi 10741.
GeneCardsi GC20M018415.
HGNCi HGNC:9892. RBBP9.
HPAi HPA015830.
HPA049005.
MIMi 602908. gene.
neXtProti NX_O75884.
PharmGKBi PA34256.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG79530.
HOGENOMi HOG000231689.
HOVERGENi HBG056175.
InParanoidi O75884.
KOi K07002.
OMAi HCDERTI.
OrthoDBi EOG7XWPPP.
PhylomeDBi O75884.
TreeFami TF106470.

Miscellaneous databases

EvolutionaryTracei O75884.
GeneWikii RBBP9.
GenomeRNAii 10741.
NextBioi 40785.
PROi O75884.
SOURCEi Search...

Gene expression databases

Bgeei O75884.
CleanExi HS_RBBP9.
Genevestigatori O75884.

Family and domain databases

Gene3Di 3.40.50.1820. 1 hit.
InterProi IPR029058. AB_hydrolase.
IPR010662. Hydrolase_RBBP9/YdeN.
[Graphical view ]
Pfami PF06821. Ser_hydrolase. 1 hit.
[Graphical view ]
SUPFAMi SSF53474. SSF53474. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "A retinoblastoma-binding protein that affects cell-cycle control and confers transforming ability."
    Woitach J.T., Zhang M., Niu C.-H., Thorgeirsson S.S.
    Nat. Genet. 19:371-374(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), MUTAGENESIS OF LEU-63.
  2. "Cloning and expression of a novel retinoblastoma binding protein cDNA, RBBP10."
    Chen J.-Z., Yang Q.-S., Wang S., Meng X.-F., Ying K., Xie Y., Mao Y.-M.
    Biochem. Genet. 40:273-282(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION.
    Tissue: Fetal brain.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Lymph node.
  4. "The DNA sequence and comparative analysis of human chromosome 20."
    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.
    Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ISOFORM 1).
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Skin.
  7. "Identification of selective inhibitors of uncharacterized enzymes by high-throughput screening with fluorescent activity-based probes."
    Bachovchin D.A., Brown S.J., Rosen H., Cravatt B.F.
    Nat. Biotechnol. 27:387-394(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: EMETINE INHIBITION.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. Cited for: X-RAY CRYSTALLOGRAPHY (1.72 ANGSTROMS).

Entry informationi

Entry nameiRBBP9_HUMAN
AccessioniPrimary (citable) accession number: O75884
Secondary accession number(s): D3DW31, Q5JPH9, Q9H1D8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: September 26, 2001
Last modified: September 3, 2014
This is version 120 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

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.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 20
    Human chromosome 20: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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