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Protein Page:
RBBP7 (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
RBBP7 Core histone-binding subunit that may target chromatin remodeling factors, histone acetyltransferases and histone deacetylases to their histone substrates in a manner that is regulated by nucleosomal DNA. Component of several complexes which regulate chromatin metabolism. These include the type B histone acetyltransferase (HAT) complex, which is required for chromatin assembly following DNA replication; the core histone deacetylase (HDAC) complex, which promotes histone deacetylation and consequent transcriptional repression; the nucleosome remodeling and histone deacetylase complex (the NuRD complex), which promotes transcriptional repression by histone deacetylation and nucleosome remodeling; and the PRC2/EED-EZH2 complex, which promotes repression of homeotic genes during development; and the NURF (nucleosome remodeling factor) complex. Binds directly to helix 1 of the histone fold of histone H4, a region that is not accessible when H4 is in chromatin. Subunit of the type B histone acetyltransferase (HAT) complex, composed of RBBP7 and HAT1. Subunit of the core histone deacetylase (HDAC) complex, which is composed of HDAC1, HDAC2, RBBP4 and RBBP7. The core HDAC complex associates with SIN3A, ARID4B/SAP180, SAP18, SAP30, SAP130, SDS3/SAP45 and possibly ARID4A/RBP1 and ING1 to form the SIN3 HDAC complex. The core HDAC complex may also associate with MTA2, MBD3, CHD3 and CHD4 to form the nucleosome remodeling and histone deacetylase complex (the NuRD complex). The NuRD complex may also interact with MBD3L1 and MBD3L2. Interacts with MTA1. Subunit of the PRC2/EED-EZH2 complex, which is composed of at least EED, EZH2, RBBP4, RBBP7 and SUZ12. The PRC2/EED-EZH2 complex may also associate with HDAC1. Part of the nucleosome remodeling factor (NURF) complex which consists of SMARCA1; BPTF; RBBP4 and RBBP7. Interacts with the viral protein- binding domain of the retinoblastoma protein (RB1). Interacts with CREBBP, and this interaction may be enhanced by the binding of phosphorylated CREB1 to CREBBP. Interacts with BRCA1, HDAC7 and SUV39H1. Belongs to the WD repeat RBAP46/RBAP48/MSI1 family. 2 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB.
Protein type: Tumor suppressor
Cellular Component: nucleoplasm; ESC/E(Z) complex; NuRD complex; nucleus
Molecular Function: protein binding
Biological Process: cell proliferation; nucleosome assembly; establishment and/or maintenance of chromatin architecture; DNA replication-independent nucleosome assembly at centromere; transcription, DNA-dependent; multicellular organismal development; negative regulation of transcription from RNA polymerase II promoter; negative regulation of cell growth; DNA replication
Reference #:  Q16576 (UniProtKB)
Alt. Names/Synonyms: G1/S transition control protein-binding protein RbAp46; Histone acetyltransferase type B subunit 2; Histone-binding protein RBBP7; MGC138867; MGC138868; Nucleosome-remodeling factor subunit RBAP46; RBAP46; RBBP-7; RBBP7; retinoblastoma binding protein 7; Retinoblastoma-binding protein 7; Retinoblastoma-binding protein p46; retinoblastoma-binding protein RbAp46
Gene Symbols: RBBP7
Molecular weight: 47,820 Da
Basal Isoelectric point: 4.89  Predict pI for various phosphorylation states
CST Pathways:  Crosstalk between PTMs  |  Histone Methylation  |  Protein Acetylation
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

RBBP7

Protein Structure Not Found.


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Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

► Hide Isoforms
 
0 2 S3-p _____MAskEMFEDt
0 1 K4-ub ____MAskEMFEDtV
0 2 K4-ac ____MAskEMFEDtV
0 2 - gap
0 2 T10-p skEMFEDtVEERVIN
0 1 K21-ac RVINEEYkIWKkNTP
0 5 K25-ub EEYkIWKkNTPFLYD
0 1 T45 ALQWPSLTVQWLPEV
0 1 T53 VQWLPEVTKPEGKDy
0 1 Y60-p TKPEGKDyALHWLVL
0 5 S95-p DDAQFDAsHCdsDkG
0 1 D98-ca QFDAsHCdsDkGEFG
0 2 S99-p FDAsHCdsDkGEFGG
0 23 K101-ub AsHCdsDkGEFGGFG
0 2 S109-p GEFGGFGsVTGKIEC
0 7 K119-ac GKIECEIkINHEGEV
0 2 K142-ub NPHIIATkTPssDVL
0 3 S145-p IIATkTPssDVLVFD
0 2 S146-p IATkTPssDVLVFDY
0 1 K155-ub VLVFDYTkHPAkPDP
0 1 K159-m1 DYTkHPAkPDPSGEC
0 1 R171 GECNPDLRLRGHQKE
0 1 T200 LSASDDHTVCLWDIN
0 1 K316-ub LHTFESHkDEIFQVH
0 4 S347-p RLNVWDLskIGEEQs
0 4 K348-ub LNVWDLskIGEEQsA
0 13 S354-p skIGEEQsAEDAEDG
0 1 S413-p NIYNDEEsDVtTSEL
0 1 T416-p NDEEsDVtTSELEGQ
  RBBP7 iso2  
- gap
- gap
- gap
S13-p GVVGAGAsPDGDWRD
T54 LRTVFEDTVEERVIN
K65 RVINEEYKIWKKNTP
K69 EEYKIWKKNTPFLYD
T89 ALQWPSLTVQWLPEV
T97 VQWLPEVTKPEGKDY
Y104 TKPEGKDYALHWLVL
S139 DDAQFDASHCDSDKG
D142 QFDASHCDSDKGEFG
S143 FDASHCDSDKGEFGG
K145 ASHCDSDKGEFGGFG
S153 GEFGGFGSVTGKIEC
K163 GKIECEIKINHEGEV
K186 NPHIIATKTPSSDVL
S189 IIATKTPSSDVLVFD
S190 IATKTPSSDVLVFDY
K199 VLVFDYTKHPAKPDP
K203 DYTKHPAKPDPSGEC
R215 GECNPDLRLRGHQKE
T244 LSASDDHTVCLWDIN
K360 LHTFESHKDEIFQVH
S391 RLNVWDLSKIGEEQS
K392 LNVWDLSKIGEEQSA
S398 SKIGEEQSAEDAEDG
S457 NIYNDEESDVTTSEL
T460 NDEESDVTTSELEGQ
  mouse

 
S3 _____MASkEMFEDT
K4 ____MASKEMFEDTV
K4-ac ____MASkEMFEDTV
- gap
T10 SkEMFEDTVEERVIN
K21 RVINEEYKIWKkNTP
K25-ub EEYKIWKkNTPFLYD
T45-p ALQWPSLtVQWLPEV
T53-p VQWLPEVtKPEGKDY
Y60 tKPEGKDYALHWLVL
S95-p DDAQFDAsHCDsDkG
D98 QFDAsHCDsDkGEFG
S99-p FDAsHCDsDkGEFGG
K101-ub AsHCDsDkGEFGGFG
S109 GEFGGFGSVTGKIEC
K119 GKIECEIKINHEGEV
K142 NPHIIATKTPSsDVL
S145 IIATKTPSsDVLVFD
S146-p IATKTPSsDVLVFDY
K155 VLVFDYTKHPAKPDP
K159 DYTKHPAKPDPSGEC
R171-m1 GECNPDLrLRGHQKE
T200-gl LSASDDHtVCLWDIN
K316 LHTFESHKDEIFQVH
S347 RLNVWDLSKIGEEQs
K348 LNVWDLSKIGEEQsA
S354-p SKIGEEQsAEDAEDG
S413 NIYNDEESDVTASEL
T416 NDEESDVTASELEGQ
  rat

 
S3 _____MASkEMFEDT
K4 ____MASKEMFEDTV
K4-ac ____MASkEMFEDTV
- gap
T10 SkEMFEDTVEERVIN
K21-ac RVINEEYkIWKKNTP
K25 EEYkIWKKNTPFLYD
T45 ALQWPSLTVQWLPEV
T53 VQWLPEVTKPEGKDY
Y60 TKPEGKDYALHWLVL
S95 DDAQFDASHCDSDKG
D98 QFDASHCDSDKGEFG
S99 FDASHCDSDKGEFGG
K101 ASHCDSDKGEFGGFG
S109 GEFGGFGSVTGKIEC
K119-ac GKIECEIkINHEGEV
K142 NPHIIATKTPSSDVL
S145 IIATKTPSSDVLVFD
S146 IATKTPSSDVLVFDY
K155 VLVFDYTKHPAKPDP
K159 DYTKHPAKPDPSGEC
R171 GECNPDLRLRGHQKE
T200 LSASDDHTVCLWDIN
K316 LHTFESHKDEIFQVH
S347 RLNVWDLSKIGEEQs
K348 LNVWDLSKIGEEQsA
S354-p SKIGEEQsAEDAEDG
S413 NIYNDEESDVTTSEL
T416 NDEESDVTTSELEGQ
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