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Protein

Putative hydrolase RBBP9

Gene

Rbbp9

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 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.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
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 9
Short name:
RBBP-9
Gene namesi
Name:Rbbp9
Synonyms:Bog
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:1347074. Rbbp9.

Subcellular locationi

  1. Cytoplasm By similarity
  2. Nucleus By similarity

GO - Cellular componenti

  1. cytoplasm Source: MGI
  2. extracellular vesicular exosome Source: MGI
  3. nucleolus Source: MGI
  4. nucleoplasm Source: MGI
  5. nucleus Source: MGI
Complete GO annotation...

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

BgeeiO88851.
CleanExiMM_RBBP9.
ExpressionAtlasiO88851. baseline and differential.
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

        10         20         30         40         50
MASPNKAVIV PGNGGGDVAT HGWYGWVKKG LEQIPGFQCL AKNMPDPITA
60 70 80 90 100
RESIWLPFME TELHCDEKTI IIGHSSGAIA AMRYAETHQV YALVLVSAYT
110 120 130 140 150
SDLGDENERA SGYFSRPWQW EKIKANCPHI VQFGSTDDPF LPWKEQQEVA
160 170 180
DRLDAKLYKF TDRGHFQNTE FHELISVVKS MLKGPE
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. Curated
The sequence AK017606 differs from that shown. Reason: Frameshift at position 20. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti131 – 1311V → I in AAC63497 (Ref. 3) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

IntActiO88851. 4 interactions.
MINTiMINT-4131919.

Chemistry

ChEMBLiCHEMBL3259487.

PTM databases

PhosphoSiteiO88851.

2D gel databases

REPRODUCTION-2DPAGEO88851.

Proteomic databases

MaxQBiO88851.
PaxDbiO88851.
PRIDEiO88851.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi10741.
MGIiMGI:1347074. Rbbp9.

Phylogenomic databases

eggNOGiNOG79530.
GeneTreeiENSGT00390000014861.
HOGENOMiHOG000231689.
HOVERGENiHBG056175.
InParanoidiO88851.
KOiK07002.
OMAiHCDERTI.
OrthoDBiEOG7XWPPP.
PhylomeDBiO88851.
TreeFamiTF106470.

Miscellaneous databases

NextBioi304553.
PROiO88851.
SOURCEiSearch...

Gene expression databases

BgeeiO88851.
CleanExiMM_RBBP9.
ExpressionAtlasiO88851. baseline and differential.
GenevestigatoriO88851.

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.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: April 1, 2015
This is version 115 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.