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Q16576 (RBBP7_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 144. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:RBBP7
Synonyms:RBAP46
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length425 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.11

Subunit structure

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. Ref.1 Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18

Subcellular location

Nucleus.

Sequence similarities

Belongs to the WD repeat RBAP46/RBAP48/MSI1 family.

Contains 7 WD repeats.

Ontologies

Keywords
   Biological processDNA replication
Transcription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
   DomainRepeat
WD repeat
   Molecular functionChaperone
Chromatin regulator
Repressor
   PTMAcetylation
Isopeptide bond
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processDNA replication

Inferred from electronic annotation. Source: UniProtKB-KW

cell proliferation

Traceable author statement Ref.1. Source: ProtInc

cellular heat acclimation

Inferred from direct assay Ref.1. Source: UniProtKB

centromere-specific nucleosome assembly

Traceable author statement. Source: Reactome

chromatin organization

Traceable author statement. Source: Reactome

multicellular organismal development

Traceable author statement Ref.1. Source: ProtInc

negative regulation of cell growth

Inferred from direct assay PubMed 9765217. Source: UniProtKB

negative regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

nucleosome assembly

Traceable author statement. Source: Reactome

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentESC/E(Z) complex

Inferred from direct assay PubMed 20075857PubMed 23104054PubMed 23273982. Source: UniProtKB

NuRD complex

Inferred from direct assay PubMed 19644445. Source: UniProtKB

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay PubMed 22720776. Source: UniProt

   Molecular_functionprotein binding

Inferred from physical interaction Ref.1. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q16576-1)

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.
Isoform 2 (identifier: Q16576-2)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.21 Ref.23
Chain2 – 425424Histone-binding protein RBBP7
PRO_0000051195

Regions

Repeat47 – 12276WD 1
Repeat128 – 17346WD 2
Repeat181 – 21737WD 3
Repeat228 – 26942WD 4
Repeat275 – 31238WD 5
Repeat318 – 36952WD 6
Repeat376 – 40328WD 7

Amino acid modifications

Modified residue21N-acetylalanine Ref.21 Ref.22 Ref.23 Ref.25 Ref.26
Modified residue31Phosphoserine Ref.25
Modified residue41N6-acetyllysine; alternate Ref.22
Modified residue1191N6-acetyllysine By similarity
Modified residue1591N6-acetyllysine By similarity
Modified residue3541Phosphoserine Ref.19 Ref.20 Ref.23
Cross-link4Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate

Natural variations

Alternative sequence1 – 66MASKEM → MAAEAGVVGAGASPDGDWRD QACGLLLHVHLSSRLGRAAP VRTGRHLRTV in isoform 2.
VSP_043016

Secondary structure

.............................................................................. 425
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 1, 1997. Version 1.
Checksum: 1A4B4CD1A8E96815

FASTA42547,820
        10         20         30         40         50         60 
MASKEMFEDT VEERVINEEY KIWKKNTPFL YDLVMTHALQ WPSLTVQWLP EVTKPEGKDY 

        70         80         90        100        110        120 
ALHWLVLGTH TSDEQNHLVV ARVHIPNDDA QFDASHCDSD KGEFGGFGSV TGKIECEIKI 

       130        140        150        160        170        180 
NHEGEVNRAR YMPQNPHIIA TKTPSSDVLV FDYTKHPAKP DPSGECNPDL RLRGHQKEGY 

       190        200        210        220        230        240 
GLSWNSNLSG HLLSASDDHT VCLWDINAGP KEGKIVDAKA IFTGHSAVVE DVAWHLLHES 

       250        260        270        280        290        300 
LFGSVADDQK LMIWDTRSNT TSKPSHLVDA HTAEVNCLSF NPYSEFILAT GSADKTVALW 

       310        320        330        340        350        360 
DLRNLKLKLH TFESHKDEIF QVHWSPHNET ILASSGTDRR LNVWDLSKIG EEQSAEDAED 

       370        380        390        400        410        420 
GPPELLFIHG GHTAKISDFS WNPNEPWVIC SVSEDNIMQI WQMAENIYND EESDVTTSEL 


EGQGS 

« Hide

Isoform 2 [UniParc].

Checksum: D668D0B6D5715261
Show »

FASTA46952,314

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[27]"Structural basis for the recognition of histone H4 by the histone-chaperone RbAp46."
Murzina N.V., Pei X.Y., Zhang W., Sparkes M., Vicente-Garcia J., Pratap J.V., McLaughlin S.H., Ben-Shahar T.R., Verreault A., Luisi B.F., Laue E.D.
Structure 16:1077-1085(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 2-411 IN COMPLEX WITH HISTONE H4, DOMAINS WD REPEATS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U35143 mRNA. Translation: AAC50231.1.
X72841 mRNA. Translation: CAA51360.1.
AK091911 mRNA. Translation: BAG52439.1.
AL929302 Genomic DNA. Translation: CAI41283.1.
CCDSCCDS14179.1. [Q16576-1]
CCDS56598.1. [Q16576-2]
PIRI39181.
RefSeqNP_001185648.1. NM_001198719.1. [Q16576-2]
NP_002884.1. NM_002893.3. [Q16576-1]
UniGeneHs.495755.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3CFSX-ray2.40B1-411[»]
3CFVX-ray2.60A/B1-411[»]
ProteinModelPortalQ16576.
SMRQ16576. Positions 1-410.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111866. 108 interactions.
DIPDIP-436N.
IntActQ16576. 38 interactions.
MINTMINT-90512.
STRING9606.ENSP00000369427.

PTM databases

PhosphoSiteQ16576.

Polymorphism databases

DMDM2494891.

Proteomic databases

MaxQBQ16576.
PaxDbQ16576.
PeptideAtlasQ16576.
PRIDEQ16576.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000380084; ENSP00000369424; ENSG00000102054. [Q16576-2]
ENST00000380087; ENSP00000369427; ENSG00000102054. [Q16576-1]
GeneID5931.
KEGGhsa:5931.
UCSCuc004cxs.2. human. [Q16576-2]
uc004cxt.3. human. [Q16576-1]

Organism-specific databases

CTD5931.
GeneCardsGC0XM016772.
HGNCHGNC:9890. RBBP7.
HPACAB037084.
MIM300825. gene.
neXtProtNX_Q16576.
PharmGKBPA34254.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2319.
HOGENOMHOG000160330.
HOVERGENHBG053236.
KOK11659.
OMAHEDAVNC.
PhylomeDBQ16576.
TreeFamTF106485.

Enzyme and pathway databases

ReactomeREACT_115566. Cell Cycle.
REACT_120956. Cellular responses to stress.
REACT_172623. Chromatin organization.
REACT_71. Gene Expression.
SignaLinkQ16576.

Gene expression databases

ArrayExpressQ16576.
BgeeQ16576.
CleanExHS_RBBP7.
GenevestigatorQ16576.

Family and domain databases

Gene3D2.130.10.10. 1 hit.
InterProIPR020472. 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]
PfamPF12265. CAF1C_H4-bd. 1 hit.
PF00400. WD40. 5 hits.
[Graphical view]
PRINTSPR00320. GPROTEINBRPT.
SMARTSM00320. WD40. 6 hits.
[Graphical view]
SUPFAMSSF50978. SSF50978. 1 hit.
PROSITEPS00678. WD_REPEATS_1. 3 hits.
PS50082. WD_REPEATS_2. 5 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSRBBP7. human.
EvolutionaryTraceQ16576.
GeneWikiRBBP7.
GenomeRNAi5931.
NextBio23110.
PMAP-CutDBQ16576.
PROQ16576.
SOURCESearch...

Entry information

Entry nameRBBP7_HUMAN
AccessionPrimary (citable) accession number: Q16576
Secondary accession number(s): Q5JP00
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: July 9, 2014
This is version 144 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome X

Human chromosome X: entries, gene names and cross-references to MIM