Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

O88851

- RBBP9_MOUSE

UniProt

O88851 - RBBP9_MOUSE

Protein

Putative hydrolase RBBP9

Gene

Rbbp9

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 110 (01 Oct 2014)
      Sequence version 2 (26 Sep 2001)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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.By similarity

    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 9
    Short name:
    RBBP-9
    Gene namesi
    Name:Rbbp9
    Synonyms:Bog
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 2

    Organism-specific databases

    MGIiMGI:1347074. Rbbp9.

    Subcellular locationi

    Cytoplasm By similarity. Nucleus By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 186186Putative hydrolase RBBP9PRO_0000097181Add
    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

    MaxQBiO88851.
    PaxDbiO88851.
    PRIDEiO88851.

    2D gel databases

    REPRODUCTION-2DPAGEO88851.

    PTM databases

    PhosphoSiteiO88851.

    Expressioni

    Gene expression databases

    ArrayExpressiO88851.
    BgeeiO88851.
    CleanExiMM_RBBP9.
    GenevestigatoriO88851.

    Interactioni

    Protein-protein interaction databases

    IntActiO88851. 4 interactions.
    MINTiMINT-4131919.

    Structurei

    3D structure databases

    ProteinModelPortaliO88851.
    SMRiO88851. Positions 3-185.
    ModBaseiSearch...
    MobiDBiSearch...

    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.
    GeneTreeiENSGT00390000014861.
    HOGENOMiHOG000231689.
    HOVERGENiHBG056175.
    InParanoidiO88851.
    KOiK07002.
    OMAiHCDERTI.
    OrthoDBiEOG7XWPPP.
    PhylomeDBiO88851.
    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.

    Sequencei

    Sequence statusi: Complete.

    O88851-1 [UniParc]FASTAAdd to Basket

    « Hide

    MASPNKAVIV PGNGGGDVAT HGWYGWVKKG LEQIPGFQCL AKNMPDPITA    50
    RESIWLPFME TELHCDEKTI IIGHSSGAIA AMRYAETHQV YALVLVSAYT 100
    SDLGDENERA SGYFSRPWQW EKIKANCPHI VQFGSTDDPF LPWKEQQEVA 150
    DRLDAKLYKF TDRGHFQNTE FHELISVVKS MLKGPE 186
    Length:186
    Mass (Da):20,912
    Last modified:September 26, 2001 - v2
    Checksum:iA2351381F228FCCC
    GO

    Sequence cautioni

    The sequence AAC63497.1 differs from that shown. Reason: Frameshift at position 152.
    The sequence AK017606 differs from that shown. Reason: Frameshift at position 20.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti131 – 1311V → I in AAC63497. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF039563 mRNA. Translation: AAC63497.1. Frameshift.
    AK017606 mRNA. No translation available.
    BC011107 mRNA. Translation: AAH11107.1.
    CCDSiCCDS16821.1.
    RefSeqiNP_056569.2. NM_015754.2.
    UniGeneiMm.440564.

    Genome annotation databases

    EnsembliENSMUST00000028915; ENSMUSP00000028915; ENSMUSG00000027428.
    GeneIDi26450.
    KEGGimmu:26450.
    UCSCiuc008mri.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF039563 mRNA. Translation: AAC63497.1 . Frameshift.
    AK017606 mRNA. No translation available.
    BC011107 mRNA. Translation: AAH11107.1 .
    CCDSi CCDS16821.1.
    RefSeqi NP_056569.2. NM_015754.2.
    UniGenei Mm.440564.

    3D structure databases

    ProteinModelPortali O88851.
    SMRi O88851. Positions 3-185.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi O88851. 4 interactions.
    MINTi MINT-4131919.

    PTM databases

    PhosphoSitei O88851.

    2D gel databases

    REPRODUCTION-2DPAGE O88851.

    Proteomic databases

    MaxQBi O88851.
    PaxDbi O88851.
    PRIDEi O88851.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000028915 ; ENSMUSP00000028915 ; ENSMUSG00000027428 .
    GeneIDi 26450.
    KEGGi mmu:26450.
    UCSCi uc008mri.1. mouse.

    Organism-specific databases

    CTDi 10741.
    MGIi MGI:1347074. Rbbp9.

    Phylogenomic databases

    eggNOGi NOG79530.
    GeneTreei ENSGT00390000014861.
    HOGENOMi HOG000231689.
    HOVERGENi HBG056175.
    InParanoidi O88851.
    KOi K07002.
    OMAi HCDERTI.
    OrthoDBi EOG7XWPPP.
    PhylomeDBi O88851.
    TreeFami TF106470.

    Miscellaneous databases

    NextBioi 304553.
    PROi O88851.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O88851.
    Bgeei O88851.
    CleanExi MM_RBBP9.
    Genevestigatori O88851.

    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. "The transcriptional landscape of the mammalian genome."
      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.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
      Tissue: Embryo.
    2. "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].
      Strain: Czech II.
      Tissue: Mammary gland.
    3. Woitach J.T.
      Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-174.
    4. Lubec G., Klug S.
      Submitted (MAR-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 164-179, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Hippocampus.

    Entry informationi

    Entry nameiRBBP9_MOUSE
    AccessioniPrimary (citable) accession number: O88851
    Secondary accession number(s): Q9CYJ9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 26, 2001
    Last sequence update: September 26, 2001
    Last modified: October 1, 2014
    This is version 110 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3