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O75884

- RBBP9_HUMAN

UniProt

O75884 - RBBP9_HUMAN

Protein

Putative hydrolase RBBP9

Gene

RBBP9

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 121 (01 Oct 2014)
      Sequence version 2 (26 Sep 2001)
      Previous versions | rss
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    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 systemSequence Analysis
    Active sitei138 – 1381Charge relay systemSequence Analysis
    Active sitei165 – 1651Charge relay systemSequence Analysis

    GO - Molecular functioni

    1. hydrolase activity Source: UniProtKB-KW

    GO - Biological processi

    1. regulation of cell proliferation Source: Ensembl

    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 1 Publication. Nucleus 1 Publication

    GO - Cellular componenti

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

    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 RBBP9PRO_0000097180Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei49 – 491Phosphothreonine; by CK2Sequence Analysis
    Modified residuei135 – 1351Phosphoserine; by CK2Sequence Analysis

    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

    1
    186
    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO75884.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni56 – 7015Retinoblastoma protein bindingSequence AnalysisAdd
    BLAST

    Sequence similaritiesi

    Belongs to the RBBP9 family.Curated

    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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti2 – 21A → V in AAC63498. (PubMed:9697699)Curated
    Sequence conflicti13 – 142NG → KI in AAC63498. (PubMed:9697699)Curated
    Sequence conflicti18 – 181V → E in AAC63498. (PubMed:9697699)Curated
    Sequence conflicti93 – 942IV → LI in AAC63498. (PubMed:9697699)Curated
    Sequence conflicti102 – 1032DL → EF in AAC63498. (PubMed:9697699)Curated
    Sequence conflicti115 – 1151T → S in AAC63498. (PubMed:9697699)Curated
    Sequence conflicti129 – 1291Y → H in AAC63498. (PubMed:9697699)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei152 – 18635RLETK…LKVPA → SWTPNCTNSLTVVTFRTQSS MN in isoform 2. 1 PublicationVSP_004374Add
    BLAST

    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...
    MobiDBi 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

    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: October 1, 2014
    This is version 121 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