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Protein

Putative hydrolase RBBP9

Gene

RBBP9

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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)DescriptionActionsGraphical viewLength
Active sitei75Charge relay systemSequence analysis1
Active sitei138Charge relay systemSequence analysis1
Active sitei165Charge relay systemSequence analysis1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Enzyme and pathway databases

BioCyciZFISH:ENSG00000089050-MONOMER.

Protein family/group databases

ESTHERihuman-RBBP9. Duf_1234.

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
Proteomesi
  • UP000005640 Componenti: Chromosome 20

Organism-specific databases

HGNCiHGNC:9892. RBBP9.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: HPA
  • extracellular exosome Source: UniProtKB
  • nucleolus Source: HPA
  • nucleus Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi63L → Q: Loss of retinoblastoma protein binding. 1 Publication1

Organism-specific databases

DisGeNETi10741.
OpenTargetsiENSG00000089050.
PharmGKBiPA34256.

Chemistry databases

ChEMBLiCHEMBL1075121.
GuidetoPHARMACOLOGYi2874.

Polymorphism and mutation databases

BioMutaiRBBP9.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000971801 – 186Putative hydrolase RBBP9Add BLAST186

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei49Phosphothreonine; by CK2Sequence analysis1
Modified residuei135Phosphoserine; by CK2Sequence analysis1

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiO75884.
MaxQBiO75884.
PaxDbiO75884.
PeptideAtlasiO75884.
PRIDEiO75884.

PTM databases

iPTMnetiO75884.
PhosphoSitePlusiO75884.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiENSG00000089050.
CleanExiHS_RBBP9.
GenevisibleiO75884. HS.

Organism-specific databases

HPAiHPA015830.
HPA049005.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
TERF2IPQ9NYB02EBI-11310604,EBI-750109

Protein-protein interaction databases

BioGridi115964. 4 interactors.
IntActiO75884. 2 interactors.
STRINGi9606.ENSP00000336866.

Chemistry databases

BindingDBiO75884.

Structurei

Secondary structure

1186
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi6 – 10Combined sources5
Beta strandi13 – 16Combined sources4
Turni18 – 20Combined sources3
Helixi24 – 31Combined sources8
Beta strandi39 – 41Combined sources3
Turni47 – 49Combined sources3
Helixi52 – 61Combined sources10
Beta strandi69 – 74Combined sources6
Helixi76 – 87Combined sources12
Beta strandi91 – 97Combined sources7
Helixi106 – 110Combined sources5
Helixi120 – 126Combined sources7
Beta strandi128 – 135Combined sources8
Beta strandi139 – 141Combined sources3
Helixi143 – 153Combined sources11
Beta strandi156 – 162Combined sources7
Helixi172 – 182Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2QS9X-ray1.72A/B1-186[»]
ProteinModelPortaliO75884.
SMRiO75884.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO75884.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni56 – 70Retinoblastoma protein bindingSequence analysisAdd BLAST15

Sequence similaritiesi

Belongs to the RBBP9 family.Curated

Phylogenomic databases

eggNOGiENOG410IK06. Eukaryota.
ENOG411109T. LUCA.
GeneTreeiENSGT00390000014861.
HOGENOMiHOG000231689.
HOVERGENiHBG056175.
InParanoidiO75884.
KOiK07002.
OMAiIVPGNGC.
OrthoDBiEOG091G0MJ3.
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. AlignAdd to basket

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

        10         20         30         40         50
MASPSKAVIV PGNGGGDVTT HGWYGWVKKE LEKIPGFQCL AKNMPDPITA
60 70 80 90 100
RESIWLPFME TELHCDEKTI IIGHSSGAIA AMRYAETHRV YAIVLVSAYT
110 120 130 140 150
SDLGDENERA SGYFTRPWQW EKIKANCPYI VQFGSTDDPF LPWKEQQEVA
160 170 180
DRLETKLHKF TDCGHFQNTE FHELITVVKS LLKVPA
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)DescriptionActionsGraphical viewLength
Sequence conflicti2A → V in AAC63498 (PubMed:9697699).Curated1
Sequence conflicti13 – 14NG → KI in AAC63498 (PubMed:9697699).Curated2
Sequence conflicti18V → E in AAC63498 (PubMed:9697699).Curated1
Sequence conflicti93 – 94IV → LI in AAC63498 (PubMed:9697699).Curated2
Sequence conflicti102 – 103DL → EF in AAC63498 (PubMed:9697699).Curated2
Sequence conflicti115T → S in AAC63498 (PubMed:9697699).Curated1
Sequence conflicti129Y → H in AAC63498 (PubMed:9697699).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_004374152 – 186RLETK…LKVPA → SWTPNCTNSLTVVTFRTQSS MN in isoform 2. 1 PublicationAdd BLAST35

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.5. human. [O75884-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2QS9X-ray1.72A/B1-186[»]
ProteinModelPortaliO75884.
SMRiO75884.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115964. 4 interactors.
IntActiO75884. 2 interactors.
STRINGi9606.ENSP00000336866.

Chemistry databases

BindingDBiO75884.
ChEMBLiCHEMBL1075121.
GuidetoPHARMACOLOGYi2874.

Protein family/group databases

ESTHERihuman-RBBP9. Duf_1234.

PTM databases

iPTMnetiO75884.
PhosphoSitePlusiO75884.

Polymorphism and mutation databases

BioMutaiRBBP9.

Proteomic databases

EPDiO75884.
MaxQBiO75884.
PaxDbiO75884.
PeptideAtlasiO75884.
PRIDEiO75884.

Protocols and materials databases

DNASUi10741.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000337227; ENSP00000336866; ENSG00000089050. [O75884-1]
GeneIDi10741.
KEGGihsa:10741.
UCSCiuc002wqy.5. human. [O75884-1]

Organism-specific databases

CTDi10741.
DisGeNETi10741.
GeneCardsiRBBP9.
HGNCiHGNC:9892. RBBP9.
HPAiHPA015830.
HPA049005.
MIMi602908. gene.
neXtProtiNX_O75884.
OpenTargetsiENSG00000089050.
PharmGKBiPA34256.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IK06. Eukaryota.
ENOG411109T. LUCA.
GeneTreeiENSGT00390000014861.
HOGENOMiHOG000231689.
HOVERGENiHBG056175.
InParanoidiO75884.
KOiK07002.
OMAiIVPGNGC.
OrthoDBiEOG091G0MJ3.
PhylomeDBiO75884.
TreeFamiTF106470.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000089050-MONOMER.

Miscellaneous databases

EvolutionaryTraceiO75884.
GeneWikiiRBBP9.
GenomeRNAii10741.
PROiO75884.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000089050.
CleanExiHS_RBBP9.
GenevisibleiO75884. HS.

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...

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: November 30, 2016
This is version 141 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

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 one 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.