Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q09028

- RBBP4_HUMAN

UniProt

Q09028 - RBBP4_HUMAN

(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)

Protein

Histone-binding protein RBBP4

Gene

RBBP4

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Core histone-binding subunit that may target chromatin assembly factors, chromatin remodeling factors 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 chromatin assembly factor 1 (CAF-1) complex, which is required for chromatin assembly following DNA replication and DNA repair; 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; the PRC2/EED-EZH2 complex, which promotes repression of homeotic genes during development; and the NURF (nucleosome remodeling factor) complex.1 Publication

GO - Molecular functioni

  1. histone binding Source: BHF-UCL
  2. histone deacetylase binding Source: BHF-UCL

GO - Biological processi

  1. ATP catabolic process Source: GOC
  2. ATP-dependent chromatin remodeling Source: UniProt
  3. CENP-A containing nucleosome assembly Source: Reactome
  4. chromatin assembly Source: UniProtKB
  5. chromatin remodeling Source: HGNC
  6. DNA replication Source: UniProtKB-KW
  7. DNA replication-dependent nucleosome assembly Source: UniProt
  8. DNA replication-independent nucleosome assembly Source: UniProt
  9. G2/M transition of mitotic cell cycle Source: Reactome
  10. mitotic cell cycle Source: Reactome
  11. negative regulation of cell proliferation Source: ProtInc
  12. nucleosome assembly Source: Reactome
  13. regulation of cell cycle Source: Reactome
  14. regulation of transcription, DNA-templated Source: UniProtKB-KW
  15. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Repressor

Keywords - Biological processi

Cell cycle, DNA replication, Transcription, Transcription regulation

Enzyme and pathway databases

ReactomeiREACT_1006. Polo-like kinase mediated events.
REACT_111214. G0 and Early G1.
REACT_169436. Oxidative Stress Induced Senescence.
REACT_200808. PRC2 methylates histones and DNA.
REACT_22186. Deposition of new CENPA-containing nucleosomes at the centromere.
REACT_953. RNA Polymerase I Transcription Initiation.
SignaLinkiQ09028.

Names & Taxonomyi

Protein namesi
Recommended name:
Histone-binding protein RBBP4
Alternative name(s):
Chromatin assembly factor 1 subunit C
Short name:
CAF-1 subunit C
Chromatin assembly factor I p48 subunit
Short name:
CAF-I 48 kDa subunit
Short name:
CAF-I p48
Nucleosome-remodeling factor subunit RBAP48
Retinoblastoma-binding protein 4
Short name:
RBBP-4
Retinoblastoma-binding protein p48
Gene namesi
Name:RBBP4
Synonyms:RBAP48
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:9887. RBBP4.

Subcellular locationi

GO - Cellular componenti

  1. CAF-1 complex Source: UniProtKB
  2. ESC/E(Z) complex Source: UniProtKB
  3. nuclear chromatin Source: UniProt
  4. nucleoplasm Source: UniProt
  5. nucleus Source: HGNC
  6. NuRD complex Source: UniProtKB
  7. NURF complex Source: UniProtKB
  8. protein complex Source: UniProt
  9. Sin3 complex Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA34251.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed5 Publications
Chaini2 – 425424Histone-binding protein RBBP4PRO_0000051186Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine5 Publications
Modified residuei4 – 41N6-acetyllysine; alternate1 Publication
Cross-linki4 – 4Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate
Modified residuei110 – 1101Phosphoserine1 Publication
Modified residuei160 – 1601N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ09028.
PaxDbiQ09028.
PRIDEiQ09028.

PTM databases

PhosphoSiteiQ09028.

Expressioni

Gene expression databases

BgeeiQ09028.
CleanExiHS_RBBP4.
ExpressionAtlasiQ09028. baseline and differential.
GenevestigatoriQ09028.

Organism-specific databases

HPAiCAB006264.

Interactioni

Subunit structurei

Interacts with SUV39H1 and HDAC7 (By similarity). 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 chromatin assembly factor 1 (CAF-1) complex, which is composed of RBBP4, CHAF1B and CHAF1A. 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, SUDS3/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. Component of the PRC2/EED-EZH1 complex, which includes EED, EZH1, SUZ12, RBBP4 and AEBP2. 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 SPEN/MINT. Interacts with BRCA1. Interacts with CREBBP, and this interaction may be enhanced by the binding of phosphorylated CREB1 to CREBBP. Component of the DREAM complex (also named LINC complex) at least composed of E2F4, E2F5, LIN9, LIN37, LIN52, LIN54, MYBL1, MYBL2, RBL1, RBL2, RBBP4, TFDP1 and TFDP2. The complex exists in quiescent cells where it represses cell cycle-dependent genes. It dissociates in S phase when LIN9, LIN37, LIN52 and LIN54 form a subcomplex that binds to MYBL2. Interacts with PHF6.By similarity25 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
DHX30Q7L2E33EBI-620823,EBI-1211456
HDAC1Q135476EBI-620823,EBI-301834
NR2E3Q9Y5X42EBI-620823,EBI-7216962
ZFPM1Q8IX074EBI-620823,EBI-3942619

Protein-protein interaction databases

BioGridi111863. 153 interactions.
DIPiDIP-33495N.
IntActiQ09028. 57 interactions.
MINTiMINT-90543.
STRINGi9606.ENSP00000362592.

Structurei

Secondary structure

1
425
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi17 – 3115
Beta strandi32 – 398
Beta strandi48 – 547
Beta strandi62 – 698
Beta strandi73 – 753
Beta strandi78 – 869
Beta strandi115 – 1228
Beta strandi128 – 1336
Beta strandi136 – 1438
Beta strandi145 – 1473
Beta strandi149 – 1535
Helixi154 – 1563
Beta strandi170 – 1745
Beta strandi180 – 1856
Beta strandi187 – 1893
Beta strandi192 – 1976
Beta strandi202 – 2065
Helixi207 – 2093
Beta strandi213 – 2186
Beta strandi220 – 2234
Beta strandi230 – 2356
Beta strandi242 – 2476
Beta strandi250 – 2567
Beta strandi262 – 2643
Beta strandi266 – 2705
Beta strandi276 – 2816
Beta strandi288 – 2936
Beta strandi296 – 3027
Beta strandi310 – 3145
Beta strandi320 – 3256
Beta strandi332 – 3376
Beta strandi342 – 3465
Helixi347 – 3493
Beta strandi366 – 3705
Beta strandi377 – 3826
Beta strandi384 – 3863
Beta strandi389 – 3946
Beta strandi397 – 4048
Helixi406 – 4094

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2XU7X-ray1.90A/B1-425[»]
3GFCX-ray2.30A1-425[»]
4PBYX-ray2.50A/B1-425[»]
4PBZX-ray2.15A1-425[»]
4PC0X-ray2.50A/B1-425[»]
ProteinModelPortaliQ09028.
SMRiQ09028. Positions 7-410.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ09028.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati122 – 15534WD 1Add
BLAST
Repeati175 – 20632WD 2Add
BLAST
Repeati225 – 25632WD 3Add
BLAST
Repeati271 – 30232WD 4Add
BLAST
Repeati315 – 34632WD 5Add
BLAST
Repeati372 – 40332WD 6Add
BLAST

Sequence similaritiesi

Contains 6 WD repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, WD repeat

Phylogenomic databases

eggNOGiCOG2319.
GeneTreeiENSGT00570000079069.
HOVERGENiHBG053236.
InParanoidiQ09028.
KOiK10752.
OMAiCQPDLRL.
OrthoDBiEOG70PBXB.
PhylomeDBiQ09028.
TreeFamiTF106485.

Family and domain databases

Gene3Di2.130.10.10. 1 hit.
InterProiIPR020472. G-protein_beta_WD-40_rep.
IPR022052. Histone-bd_RBBP4_N.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamiPF12265. CAF1C_H4-bd. 1 hit.
PF00400. WD40. 5 hits.
[Graphical view]
PRINTSiPR00320. GPROTEINBRPT.
SMARTiSM00320. WD40. 6 hits.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 1 hit.
PROSITEiPS00678. WD_REPEATS_1. 3 hits.
PS50082. WD_REPEATS_2. 5 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q09028-1) [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
MADKEAAFDD AVEERVINEE YKIWKKNTPF LYDLVMTHAL EWPSLTAQWL
60 70 80 90 100
PDVTRPEGKD FSIHRLVLGT HTSDEQNHLV IASVQLPNDD AQFDASHYDS
110 120 130 140 150
EKGEFGGFGS VSGKIEIEIK INHEGEVNRA RYMPQNPCII ATKTPSSDVL
160 170 180 190 200
VFDYTKHPSK PDPSGECNPD LRLRGHQKEG YGLSWNPNLS GHLLSASDDH
210 220 230 240 250
TICLWDISAV PKEGKVVDAK TIFTGHTAVV EDVSWHLLHE SLFGSVADDQ
260 270 280 290 300
KLMIWDTRSN NTSKPSHSVD AHTAEVNCLS FNPYSEFILA TGSADKTVAL
310 320 330 340 350
WDLRNLKLKL HSFESHKDEI FQVQWSPHNE TILASSGTDR RLNVWDLSKI
360 370 380 390 400
GEEQSPEDAE DGPPELLFIH GGHTAKISDF SWNPNEPWVI CSVSEDNIMQ
410 420
VWQMAENIYN DEDPEGSVDP EGQGS
Length:425
Mass (Da):47,656
Last modified:January 23, 2007 - v3
Checksum:iB71E2D55A444C360
GO
Isoform 2 (identifier: Q09028-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     7-7: Missing.

Note: No experimental confirmation available.

Show »
Length:424
Mass (Da):47,585
Checksum:i52055B5C74BCF3D8
GO
Isoform 3 (identifier: Q09028-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     405-425: AENIYNDEDPEGSVDPEGQGS → ELVLDH

Note: No experimental confirmation available.

Show »
Length:410
Mass (Da):46,158
Checksum:i59B630D6055A70B2
GO
Isoform 4 (identifier: Q09028-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-35: Missing.

Note: No experimental confirmation available.

Show »
Length:390
Mass (Da):43,482
Checksum:iA61A43F6AC30C8CE
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti61 – 611F → G in AAH15123. (PubMed:15489334)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 3535Missing in isoform 4. 1 PublicationVSP_040087Add
BLAST
Alternative sequencei7 – 71Missing in isoform 2. 1 PublicationVSP_040088
Alternative sequencei405 – 42521AENIY…EGQGS → ELVLDH in isoform 3. 1 PublicationVSP_040089Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X74262 mRNA. Translation: CAA52321.1.
X71810 mRNA. Translation: CAA50685.1.
BT007309 mRNA. Translation: AAP35973.1.
AK299251 mRNA. Translation: BAG61282.1.
AK312571 mRNA. Translation: BAG35466.1.
AK222779 mRNA. Translation: BAD96499.1.
AC114489 Genomic DNA. No translation available.
CH471059 Genomic DNA. Translation: EAX07513.1.
CH471059 Genomic DNA. Translation: EAX07514.1.
BC003092 mRNA. Translation: AAH03092.1.
BC015123 mRNA. Translation: AAH15123.1.
BC053904 mRNA. Translation: AAH53904.1.
BC075836 mRNA. Translation: AAH75836.1.
CCDSiCCDS366.1. [Q09028-1]
CCDS44105.1. [Q09028-2]
CCDS44106.1. [Q09028-4]
PIRiS36112.
RefSeqiNP_001128727.1. NM_001135255.1. [Q09028-2]
NP_001128728.1. NM_001135256.1. [Q09028-4]
NP_005601.1. NM_005610.2. [Q09028-1]
UniGeneiHs.16003.

Genome annotation databases

EnsembliENST00000373485; ENSP00000362584; ENSG00000162521. [Q09028-3]
ENST00000373493; ENSP00000362592; ENSG00000162521. [Q09028-1]
ENST00000414241; ENSP00000398242; ENSG00000162521. [Q09028-2]
ENST00000458695; ENSP00000396057; ENSG00000162521. [Q09028-4]
GeneIDi5928.
KEGGihsa:5928.
UCSCiuc001bvr.3. human. [Q09028-1]
uc001bvs.3. human. [Q09028-2]

Polymorphism databases

DMDMi1172846.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X74262 mRNA. Translation: CAA52321.1 .
X71810 mRNA. Translation: CAA50685.1 .
BT007309 mRNA. Translation: AAP35973.1 .
AK299251 mRNA. Translation: BAG61282.1 .
AK312571 mRNA. Translation: BAG35466.1 .
AK222779 mRNA. Translation: BAD96499.1 .
AC114489 Genomic DNA. No translation available.
CH471059 Genomic DNA. Translation: EAX07513.1 .
CH471059 Genomic DNA. Translation: EAX07514.1 .
BC003092 mRNA. Translation: AAH03092.1 .
BC015123 mRNA. Translation: AAH15123.1 .
BC053904 mRNA. Translation: AAH53904.1 .
BC075836 mRNA. Translation: AAH75836.1 .
CCDSi CCDS366.1. [Q09028-1 ]
CCDS44105.1. [Q09028-2 ]
CCDS44106.1. [Q09028-4 ]
PIRi S36112.
RefSeqi NP_001128727.1. NM_001135255.1. [Q09028-2 ]
NP_001128728.1. NM_001135256.1. [Q09028-4 ]
NP_005601.1. NM_005610.2. [Q09028-1 ]
UniGenei Hs.16003.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2XU7 X-ray 1.90 A/B 1-425 [» ]
3GFC X-ray 2.30 A 1-425 [» ]
4PBY X-ray 2.50 A/B 1-425 [» ]
4PBZ X-ray 2.15 A 1-425 [» ]
4PC0 X-ray 2.50 A/B 1-425 [» ]
ProteinModelPortali Q09028.
SMRi Q09028. Positions 7-410.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111863. 153 interactions.
DIPi DIP-33495N.
IntActi Q09028. 57 interactions.
MINTi MINT-90543.
STRINGi 9606.ENSP00000362592.

Chemistry

ChEMBLi CHEMBL3137287.

PTM databases

PhosphoSitei Q09028.

Polymorphism databases

DMDMi 1172846.

Proteomic databases

MaxQBi Q09028.
PaxDbi Q09028.
PRIDEi Q09028.

Protocols and materials databases

DNASUi 5928.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000373485 ; ENSP00000362584 ; ENSG00000162521 . [Q09028-3 ]
ENST00000373493 ; ENSP00000362592 ; ENSG00000162521 . [Q09028-1 ]
ENST00000414241 ; ENSP00000398242 ; ENSG00000162521 . [Q09028-2 ]
ENST00000458695 ; ENSP00000396057 ; ENSG00000162521 . [Q09028-4 ]
GeneIDi 5928.
KEGGi hsa:5928.
UCSCi uc001bvr.3. human. [Q09028-1 ]
uc001bvs.3. human. [Q09028-2 ]

Organism-specific databases

CTDi 5928.
GeneCardsi GC01P033116.
HGNCi HGNC:9887. RBBP4.
HPAi CAB006264.
MIMi 602923. gene.
neXtProti NX_Q09028.
PharmGKBi PA34251.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG2319.
GeneTreei ENSGT00570000079069.
HOVERGENi HBG053236.
InParanoidi Q09028.
KOi K10752.
OMAi CQPDLRL.
OrthoDBi EOG70PBXB.
PhylomeDBi Q09028.
TreeFami TF106485.

Enzyme and pathway databases

Reactomei REACT_1006. Polo-like kinase mediated events.
REACT_111214. G0 and Early G1.
REACT_169436. Oxidative Stress Induced Senescence.
REACT_200808. PRC2 methylates histones and DNA.
REACT_22186. Deposition of new CENPA-containing nucleosomes at the centromere.
REACT_953. RNA Polymerase I Transcription Initiation.
SignaLinki Q09028.

Miscellaneous databases

ChiTaRSi RBBP4. human.
EvolutionaryTracei Q09028.
GeneWikii RBBP4.
GenomeRNAii 5928.
NextBioi 23094.
PROi Q09028.
SOURCEi Search...

Gene expression databases

Bgeei Q09028.
CleanExi HS_RBBP4.
ExpressionAtlasi Q09028. baseline and differential.
Genevestigatori Q09028.

Family and domain databases

Gene3Di 2.130.10.10. 1 hit.
InterProi IPR020472. G-protein_beta_WD-40_rep.
IPR022052. Histone-bd_RBBP4_N.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view ]
Pfami PF12265. CAF1C_H4-bd. 1 hit.
PF00400. WD40. 5 hits.
[Graphical view ]
PRINTSi PR00320. GPROTEINBRPT.
SMARTi SM00320. WD40. 6 hits.
[Graphical view ]
SUPFAMi SSF50978. SSF50978. 1 hit.
PROSITEi PS00678. WD_REPEATS_1. 3 hits.
PS50082. WD_REPEATS_2. 5 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "A retinoblastoma-binding protein related to a negative regulator of Ras in yeast."
    Qian Y.-W., Wang Y.-C.J., Hollingsworth R.E. Jr., Jones D., Ling N., Lee E.Y.-H.P.
    Nature 364:648-652(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 134-158 AND 254-271.
  2. "Molecular cloning and expression of two novel human cDNAs encoding proteins containing WD-40 repeats and sharing similarity to yeast MSI1 a negative regulation of the RAS-cAMP pathway."
    Nielsen M.S., Rasmussen H.H., Celis J.E., Leffers H.
    Submitted (MAY-1993) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
  3. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4).
    Tissue: Brain.
  5. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
    Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Liver.
  6. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "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: Bone marrow, Brain, Eye and Uterus.
  9. Bienvenut W.V.
    Submitted (FEB-2005) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-15 AND 297-304, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: B-cell lymphoma.
  10. "Two-dimensional gel electrophoresis, protein electroblotting and microsequencing: a direct link between proteins and genes."
    Bauw G., Rasmussen H.H., van den Bulcke M., van Damme J., Puype M., Gesser B., Celis J.E., Vandekerckhove J.
    Electrophoresis 11:528-536(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 60-65; 144-160 AND 221-240.
    Tissue: Keratinocyte.
  11. "Microsequences of 145 proteins recorded in the two-dimensional gel protein database of normal human epidermal keratinocytes."
    Rasmussen H.H., van Damme J., Puype M., Gesser B., Celis J.E., Vandekerckhove J.
    Electrophoresis 13:960-969(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 60-65; 144-160 AND 221-240.
    Tissue: Keratinocyte.
  12. "Nucleosome assembly by a complex of CAF-1 and acetylated histones H3/H4."
    Verreault A., Kaufman P.D., Kobayashi R., Stillman B.
    Cell 87:95-104(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL PROTEIN SEQUENCE, IDENTIFICATION IN THE CAF-1 COMPLEX, INTERACTION WITH HISTONE H4.
  13. "Histone deacetylases and SAP18, a novel polypeptide, are components of a human Sin3 complex."
    Zhang Y., Iratni R., Erdjument-Bromage H., Tempst P., Reinberg D.
    Cell 89:357-364(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL PROTEIN SEQUENCE, IDENTIFICATION IN THE SIN3 HDAC COMPLEX.
  14. "Dual retinoblastoma-binding proteins with properties related to a negative regulator of ras in yeast."
    Qian Y.-W., Lee E.Y.-H.P.
    J. Biol. Chem. 270:25507-25513(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RB1.
  15. "A mammalian histone deacetylase related to the yeast transcriptional regulator Rpd3p."
    Taunton J., Hassig C.A., Schreiber S.L.
    Science 272:408-411(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HDAC1.
  16. "The dermatomyositis-specific autoantigen Mi2 is a component of a complex containing histone deacetylase and nucleosome remodeling activities."
    Zhang Y., LeRoy G., Seelig H.-P., Lane W.S., Reinberg D.
    Cell 95:279-289(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE NURD COMPLEX.
  17. "Nucleosomal DNA regulates the core-histone-binding subunit of the human Hat1 acetyltransferase."
    Verreault A., Kaufman P.D., Kobayashi R., Stillman B.
    Curr. Biol. 8:96-108(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HISTONE H4.
  18. "SAP30, a novel protein conserved between human and yeast, is a component of a histone deacetylase complex."
    Zhang Y., Sun Z.-W., Iratni R., Erdjument-Bromage H., Tempst P., Hampsey M., Reinberg D.
    Mol. Cell 1:1021-1031(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE SIN3 HDAC COMPLEX.
  19. "A role for histone deacetylase activity in HDAC1-mediated transcriptional repression."
    Hassig C.A., Tong J.K., Fleischer T.C., Owa T., Grable P.G., Ayer D.E., Schreiber S.L.
    Proc. Natl. Acad. Sci. U.S.A. 95:3519-3524(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HDAC1.
  20. "Analysis of the NuRD subunits reveals a histone deacetylase core complex and a connection with DNA methylation."
    Zhang Y., Ng H.-H., Erdjument-Bromage H., Tempst P., Bird A., Reinberg D.
    Genes Dev. 13:1924-1935(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE NURD COMPLEX.
  21. "BRCA1 interacts with components of the histone deacetylase complex."
    Yarden R.I., Brody L.C.
    Proc. Natl. Acad. Sci. U.S.A. 96:4983-4988(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH BRCA1.
  22. "RbAp48 belongs to the histone deacetylase complex that associates with the retinoblastoma protein."
    Nicolas E., Morales V., Magnaghi-Jaulin L., Harel-Bellan A., Richard-Foy H., Trouche D.
    J. Biol. Chem. 275:9797-9804(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HDAC1 AND RB1.
  23. "Histone binding protein RbAp48 interacts with a complex of CREB binding protein and phosphorylated CREB."
    Zhang Q., Vo N., Goodman R.H.
    Mol. Cell. Biol. 20:4970-4978(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CREBBP.
  24. "Sharp, an inducible cofactor that integrates nuclear receptor repression and activation."
    Shi Y., Downes M., Xie W., Kao H.-Y., Ordentlich P., Tsai C.-C., Hon M., Evans R.M.
    Genes Dev. 15:1140-1151(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SPEN.
  25. "Stable histone deacetylase complexes distinguished by the presence of SANT domain proteins CoREST/kiaa0071 and Mta-L1."
    Humphrey G.W., Wang Y., Russanova V.R., Hirai T., Qin J., Nakatani Y., Howard B.H.
    J. Biol. Chem. 276:6817-6824(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE NURD COMPLEX.
  26. "Differential association of products of alternative transcripts of the candidate tumor suppressor ING1 with the mSin3/HDAC1 transcriptional corepressor complex."
    Skowyra D., Zeremski M., Neznanov N., Li M., Choi Y., Uesugi M., Hauser C.A., Gu W., Gudkov A.V., Qin J.
    J. Biol. Chem. 276:8734-8739(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A SIN3 HDAC COMPLEX.
  27. "Histone methyltransferase activity associated with a human multiprotein complex containing the Enhancer of Zeste protein."
    Kuzmichev A., Nishioka K., Erdjument-Bromage H., Tempst P., Reinberg D.
    Genes Dev. 16:2893-2905(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE PRC2/EED-EZH2 COMPLEX WITH EED; EZH2; RBBP7 AND SUZ12, TRANSIENT INTERACTION WITH HDAC1, METHYLTRANSFERASE ACTIVITY OF THE COMPLEX.
  28. "Role of the Sin3-histone deacetylase complex in growth regulation by the candidate tumor suppressor p33(ING1)."
    Kuzmichev A., Zhang Y., Erdjument-Bromage H., Tempst P., Reinberg D.
    Mol. Cell. Biol. 22:835-848(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN MULTIPLE SIN3 HDAC COMPLEXES.
  29. "Role of histone H3 lysine 27 methylation in Polycomb-group silencing."
    Cao R., Wang L., Wang H., Xia L., Erdjument-Bromage H., Tempst P., Jones R.S., Zhang Y.
    Science 298:1039-1043(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE PRC2/EED-EZH2 COMPLEX WITH AEBP2; EED; EZH2 AND SUZ12, METHYLTRANSFERASE ACTIVITY OF THE COMPLEX.
  30. "Isolation of human NURF: a regulator of Engrailed gene expression."
    Barak O., Lazzaro M.A., Lane W.S., Speicher D.W., Picketts D.J., Shiekhattar R.
    EMBO J. 22:6089-6100(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE NURF COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
  31. "The metastasis-associated proteins 1 and 2 form distinct protein complexes with histone deacetylase activity."
    Yao Y.-L., Yang W.-M.
    J. Biol. Chem. 278:42560-42568(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MTA1.
  32. "MBD3L1 is a transcriptional repressor that interacts with methyl-CpG-binding protein 2 (MBD2) and components of the NuRD complex."
    Jiang C.-L., Jin S.-G., Pfeifer G.P.
    J. Biol. Chem. 279:52456-52464(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MBD3L1.
  33. "MBD3L2 interacts with MBD3 and components of the NuRD complex and can oppose MBD2-MeCP1-mediated methylation silencing."
    Jin S.-G., Jiang C.-L., Rauch T., Li H., Pfeifer G.P.
    J. Biol. Chem. 280:12700-12709(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MBD3L2.
  34. "LINC, a human complex that is related to pRB-containing complexes in invertebrates regulates the expression of G2/M genes."
    Schmit F., Korenjak M., Mannefeld M., Schmitt K., Franke C., von Eyss B., Gagrica S., Haenel F., Brehm A., Gaubatz S.
    Cell Cycle 6:1903-1913(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE DREAM COMPLEX.
  35. "Evolutionarily conserved multisubunit RBL2/p130 and E2F4 protein complex represses human cell cycle-dependent genes in quiescence."
    Litovchick L., Sadasivam S., Florens L., Zhu X., Swanson S.K., Velmurugan S., Chen R., Washburn M.P., Liu X.S., DeCaprio J.A.
    Mol. Cell 26:539-551(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE DREAM COMPLEX.
  36. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  37. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-110, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  38. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2 AND LYS-4, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  39. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  40. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  41. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  42. "Structural and functional insights into the human Borjeson-Forssman-Lehmann syndrome-associated protein PHF6."
    Liu Z., Li F., Ruan K., Zhang J., Mei Y., Wu J., Shi Y.
    J. Biol. Chem. 289:10069-10083(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PHF6.

Entry informationi

Entry nameiRBBP4_HUMAN
AccessioniPrimary (citable) accession number: Q09028
Secondary accession number(s): B2R6G9
, B4DRH0, D3DPQ3, P31149, Q53H02, Q96BV9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: January 23, 2007
Last modified: October 29, 2014
This is version 161 of the entry and version 3 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

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: 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