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Q16576

- RBBP7_HUMAN

UniProt

Q16576 - RBBP7_HUMAN

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Protein

Histone-binding protein RBBP7

Gene

RBBP7

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 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.1 Publication

GO - Molecular functioni

  1. RNA binding Source: Ensembl

GO - Biological processi

  1. cell proliferation Source: ProtInc
  2. cellular heat acclimation Source: UniProtKB
  3. CENP-A containing nucleosome assembly Source: Reactome
  4. chromatin organization Source: Reactome
  5. DNA replication Source: UniProtKB-KW
  6. multicellular organismal development Source: ProtInc
  7. negative regulation of cell growth Source: UniProtKB
  8. negative regulation of transcription from RNA polymerase II promoter Source: Ensembl
  9. nucleosome assembly Source: Reactome
  10. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Chaperone, Chromatin regulator, Repressor

Keywords - Biological processi

DNA replication, Transcription, Transcription regulation

Enzyme and pathway databases

ReactomeiREACT_169436. Oxidative Stress Induced Senescence.
REACT_172610. HATs acetylate histones.
REACT_200808. PRC2 methylates histones and DNA.
REACT_22186. Deposition of new CENPA-containing nucleosomes at the centromere.
REACT_228108. RMTs methylate histone arginines.
REACT_228222. HDACs deacetylate histones.
REACT_953. RNA Polymerase I Transcription Initiation.
SignaLinkiQ16576.

Names & Taxonomyi

Protein namesi
Recommended name:
Histone-binding protein RBBP7
Alternative name(s):
Histone acetyltransferase type B subunit 2
Nucleosome-remodeling factor subunit RBAP46
Retinoblastoma-binding protein 7
Short name:
RBBP-7
Retinoblastoma-binding protein p46
Gene namesi
Name:RBBP7
Synonyms:RBAP46
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome X

Organism-specific databases

HGNCiHGNC:9890. RBBP7.

Subcellular locationi

GO - Cellular componenti

  1. ESC/E(Z) complex Source: UniProtKB
  2. nucleoplasm Source: Reactome
  3. nucleus Source: UniProt
  4. NuRD complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA34254.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed5 Publications
Chaini2 – 425424Histone-binding protein RBBP7PRO_0000051195Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine4 Publications
Modified residuei3 – 31Phosphoserine1 Publication
Modified residuei4 – 41N6-acetyllysine; alternate1 Publication
Cross-linki4 – 4Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate
Modified residuei119 – 1191N6-acetyllysineBy similarity
Modified residuei159 – 1591N6-acetyllysineBy similarity
Modified residuei354 – 3541Phosphoserine3 Publications

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ16576.
PaxDbiQ16576.
PeptideAtlasiQ16576.
PRIDEiQ16576.

PTM databases

PhosphoSiteiQ16576.

Miscellaneous databases

PMAP-CutDBQ16576.

Expressioni

Gene expression databases

BgeeiQ16576.
CleanExiHS_RBBP7.
ExpressionAtlasiQ16576. baseline and differential.
GenevestigatoriQ16576.

Organism-specific databases

HPAiCAB037084.

Interactioni

Subunit structurei

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, 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. 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 SUV39H1.16 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
DHX30Q7L2E34EBI-352227,EBI-1211456
HDAC1Q135475EBI-352227,EBI-301834
HIST2H4BP628054EBI-352227,EBI-302023
NR2E3Q9Y5X42EBI-352227,EBI-7216962
TBL3Q127882EBI-352227,EBI-715766

Protein-protein interaction databases

BioGridi111866. 140 interactions.
DIPiDIP-436N.
IntActiQ16576. 40 interactions.
MINTiMINT-90512.
STRINGi9606.ENSP00000369427.

Structurei

Secondary structure

1
425
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi10 – 3021Combined sources
Beta strandi31 – 388Combined sources
Beta strandi46 – 538Combined sources
Beta strandi59 – 679Combined sources
Beta strandi72 – 743Combined sources
Beta strandi76 – 8611Combined sources
Beta strandi113 – 12412Combined sources
Beta strandi127 – 1315Combined sources
Beta strandi138 – 1425Combined sources
Beta strandi144 – 1463Combined sources
Beta strandi148 – 1525Combined sources
Helixi153 – 1553Combined sources
Beta strandi169 – 1735Combined sources
Beta strandi182 – 1843Combined sources
Beta strandi186 – 1883Combined sources
Beta strandi191 – 1955Combined sources
Beta strandi201 – 2055Combined sources
Beta strandi214 – 2174Combined sources
Beta strandi219 – 2224Combined sources
Beta strandi229 – 2346Combined sources
Beta strandi241 – 2466Combined sources
Beta strandi249 – 25911Combined sources
Beta strandi261 – 2633Combined sources
Beta strandi265 – 2695Combined sources
Beta strandi275 – 2806Combined sources
Beta strandi287 – 2926Combined sources
Beta strandi295 – 3017Combined sources
Beta strandi305 – 3073Combined sources
Beta strandi310 – 3134Combined sources
Beta strandi319 – 3246Combined sources
Beta strandi331 – 3366Combined sources
Beta strandi341 – 3455Combined sources
Helixi346 – 3483Combined sources
Helixi355 – 3584Combined sources
Beta strandi365 – 3695Combined sources
Beta strandi376 – 3816Combined sources
Beta strandi383 – 3853Combined sources
Beta strandi388 – 3936Combined sources
Beta strandi396 – 4038Combined sources
Helixi405 – 4084Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3CFSX-ray2.40B1-411[»]
3CFVX-ray2.60A/B1-411[»]
ProteinModelPortaliQ16576.
SMRiQ16576. Positions 1-410.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ16576.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati47 – 12276WD 1Add
BLAST
Repeati128 – 17346WD 2Add
BLAST
Repeati181 – 21737WD 3Add
BLAST
Repeati228 – 26942WD 4Add
BLAST
Repeati275 – 31238WD 5Add
BLAST
Repeati318 – 36952WD 6Add
BLAST
Repeati376 – 40328WD 7Add
BLAST

Sequence similaritiesi

Contains 7 WD repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, WD repeat

Phylogenomic databases

eggNOGiCOG2319.
GeneTreeiENSGT00570000079069.
HOGENOMiHOG000160330.
HOVERGENiHBG053236.
InParanoidiQ16576.
KOiK11659.
OMAiHEDAVNC.
PhylomeDBiQ16576.
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 (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q16576-1) [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
MASKEMFEDT VEERVINEEY KIWKKNTPFL YDLVMTHALQ WPSLTVQWLP
60 70 80 90 100
EVTKPEGKDY ALHWLVLGTH TSDEQNHLVV ARVHIPNDDA QFDASHCDSD
110 120 130 140 150
KGEFGGFGSV TGKIECEIKI NHEGEVNRAR YMPQNPHIIA TKTPSSDVLV
160 170 180 190 200
FDYTKHPAKP DPSGECNPDL RLRGHQKEGY GLSWNSNLSG HLLSASDDHT
210 220 230 240 250
VCLWDINAGP KEGKIVDAKA IFTGHSAVVE DVAWHLLHES LFGSVADDQK
260 270 280 290 300
LMIWDTRSNT TSKPSHLVDA HTAEVNCLSF NPYSEFILAT GSADKTVALW
310 320 330 340 350
DLRNLKLKLH TFESHKDEIF QVHWSPHNET ILASSGTDRR LNVWDLSKIG
360 370 380 390 400
EEQSAEDAED GPPELLFIHG GHTAKISDFS WNPNEPWVIC SVSEDNIMQI
410 420
WQMAENIYND EESDVTTSEL EGQGS
Length:425
Mass (Da):47,820
Last modified:November 1, 1997 - v1
Checksum:i1A4B4CD1A8E96815
GO
Isoform 2 (identifier: Q16576-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-6: MASKEM → MAAEAGVVGAGASPDGDWRDQACGLLLHVHLSSRLGRAAPVRTGRHLRTV

Note: No experimental confirmation available. Initiator Met-1 is removed. Contains a N-acetylalanine at position 2. Contains a phosphoserine at position 13.

Show »
Length:469
Mass (Da):52,314
Checksum:iD668D0B6D5715261
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 66MASKEM → MAAEAGVVGAGASPDGDWRD QACGLLLHVHLSSRLGRAAP VRTGRHLRTV in isoform 2. 1 PublicationVSP_043016

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U35143 mRNA. Translation: AAC50231.1.
X72841 mRNA. Translation: CAA51360.1.
AK091911 mRNA. Translation: BAG52439.1.
AL929302 Genomic DNA. Translation: CAI41283.1.
CCDSiCCDS14179.1. [Q16576-1]
CCDS56598.1. [Q16576-2]
PIRiI39181.
RefSeqiNP_001185648.1. NM_001198719.1. [Q16576-2]
NP_002884.1. NM_002893.3. [Q16576-1]
UniGeneiHs.495755.

Genome annotation databases

EnsembliENST00000380084; ENSP00000369424; ENSG00000102054. [Q16576-2]
ENST00000380087; ENSP00000369427; ENSG00000102054. [Q16576-1]
GeneIDi5931.
KEGGihsa:5931.
UCSCiuc004cxs.2. human. [Q16576-2]
uc004cxt.3. human. [Q16576-1]

Polymorphism databases

DMDMi2494891.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U35143 mRNA. Translation: AAC50231.1 .
X72841 mRNA. Translation: CAA51360.1 .
AK091911 mRNA. Translation: BAG52439.1 .
AL929302 Genomic DNA. Translation: CAI41283.1 .
CCDSi CCDS14179.1. [Q16576-1 ]
CCDS56598.1. [Q16576-2 ]
PIRi I39181.
RefSeqi NP_001185648.1. NM_001198719.1. [Q16576-2 ]
NP_002884.1. NM_002893.3. [Q16576-1 ]
UniGenei Hs.495755.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3CFS X-ray 2.40 B 1-411 [» ]
3CFV X-ray 2.60 A/B 1-411 [» ]
ProteinModelPortali Q16576.
SMRi Q16576. Positions 1-410.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111866. 140 interactions.
DIPi DIP-436N.
IntActi Q16576. 40 interactions.
MINTi MINT-90512.
STRINGi 9606.ENSP00000369427.

PTM databases

PhosphoSitei Q16576.

Polymorphism databases

DMDMi 2494891.

Proteomic databases

MaxQBi Q16576.
PaxDbi Q16576.
PeptideAtlasi Q16576.
PRIDEi Q16576.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000380084 ; ENSP00000369424 ; ENSG00000102054 . [Q16576-2 ]
ENST00000380087 ; ENSP00000369427 ; ENSG00000102054 . [Q16576-1 ]
GeneIDi 5931.
KEGGi hsa:5931.
UCSCi uc004cxs.2. human. [Q16576-2 ]
uc004cxt.3. human. [Q16576-1 ]

Organism-specific databases

CTDi 5931.
GeneCardsi GC0XM016772.
HGNCi HGNC:9890. RBBP7.
HPAi CAB037084.
MIMi 300825. gene.
neXtProti NX_Q16576.
PharmGKBi PA34254.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG2319.
GeneTreei ENSGT00570000079069.
HOGENOMi HOG000160330.
HOVERGENi HBG053236.
InParanoidi Q16576.
KOi K11659.
OMAi HEDAVNC.
PhylomeDBi Q16576.
TreeFami TF106485.

Enzyme and pathway databases

Reactomei REACT_169436. Oxidative Stress Induced Senescence.
REACT_172610. HATs acetylate histones.
REACT_200808. PRC2 methylates histones and DNA.
REACT_22186. Deposition of new CENPA-containing nucleosomes at the centromere.
REACT_228108. RMTs methylate histone arginines.
REACT_228222. HDACs deacetylate histones.
REACT_953. RNA Polymerase I Transcription Initiation.
SignaLinki Q16576.

Miscellaneous databases

ChiTaRSi RBBP7. human.
EvolutionaryTracei Q16576.
GeneWikii RBBP7.
GenomeRNAii 5931.
NextBioi 23110.
PMAP-CutDB Q16576.
PROi Q16576.
SOURCEi Search...

Gene expression databases

Bgeei Q16576.
CleanExi HS_RBBP7.
ExpressionAtlasi Q16576. baseline and differential.
Genevestigatori Q16576.

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. "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: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH RB1.
  2. Nielsen M.S., Rasmussen H.H., Dejgaard K., Celis J.E., Leffers H.
    Submitted (MAY-1993) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  3. "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] (ISOFORM 2).
    Tissue: Kidney.
  4. "The DNA sequence of the human X chromosome."
    Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
    , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
    Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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.
  6. "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.
  7. "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 HAT1 AND HISTONE H4.
  8. "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.
  9. "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.
  10. "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 AND RB1.
  11. "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.
  12. "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.
  13. "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 THE SIN3 HDAC COMPLEX.
  14. "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; RBBP4 AND SUZ12, METHYLTRANSFERASE ACTIVITY OF THE COMPLEX.
  15. "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 THE SIN3 HDAC COMPLEX.
  16. "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.
  17. "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: IDENTIFICATION IN THE MTA1 HDAC COMPLEX.
  18. "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.
  19. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-354, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  20. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-354, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  21. "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], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  22. "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].
  23. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2 (ISOFORM 2), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-354, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13 (ISOFORM 2), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  24. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  25. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  26. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  27. Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 2-411 IN COMPLEX WITH HISTONE H4, DOMAINS WD REPEATS.

Entry informationi

Entry nameiRBBP7_HUMAN
AccessioniPrimary (citable) accession number: Q16576
Secondary accession number(s): Q5JP00
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: November 26, 2014
This is version 148 of the entry and version 1 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 X
    Human chromosome X: 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