Q16576 (RBBP7_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	RBBP7
Synonyms:	RBAP46

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	425 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 process	DNA replication Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing
Domain	Repeat WD repeat
Molecular function	Chaperone Chromatin regulator Repressor
PTM	Acetylation Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	CENP-A containing nucleosome assembly at centromere Traceable author statement. Source: Reactome DNA 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 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: Compara transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	ESC/E(Z) complex Inferred from direct assay PubMed 20075857PubMed 23104054PubMed 23273982. Source: UniProtKB NuRD complex Inferred from direct assay PubMed 19644445. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
HDAC1	Q13547	3	EBI-352227,EBI-301834
HIST2H4B	P62805	4	EBI-352227,EBI-302023

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.21 Ref.22

Chain

2 – 425

424

Histone-binding protein RBBP7

PRO_0000051195

Regions

Repeat

47 – 122

76

WD 1

Repeat

128 – 173

46

WD 2

Repeat

181 – 217

37

WD 3

Repeat

228 – 269

42

WD 4

Repeat

275 – 312

38

WD 5

Repeat

318 – 369

52

WD 6

Repeat

376 – 403

28

WD 7

Amino acid modifications

Modified residue

2

1

N-acetylalanine Ref.21 Ref.22 Ref.24

Modified residue

3

1

Phosphoserine Ref.24

Modified residue

4

1

N6-acetyllysine; alternate Ref.21

Modified residue

99

1

Phosphoserine By similarity

Modified residue

354

1

Phosphoserine Ref.19 Ref.20 Ref.22

Cross-link

4

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate

Natural variations

Alternative sequence

1 – 6

6

MASKEM → MAAEAGVVGAGASPDGDWRD QACGLLLHVHLSSRLGRAAP VRTGRHLRTV in isoform 2.

VSP_043016

Secondary structure

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425

Helix Strand Turn

Details...

Helix

10 – 30

21

Beta strand

31 – 38

8

Beta strand

46 – 53

8

Beta strand

59 – 67

9

Beta strand

72 – 74

3

Beta strand

76 – 86

11

Beta strand

113 – 124

12

Beta strand

127 – 131

5

Beta strand

138 – 142

5

Beta strand

144 – 146

3

Beta strand

148 – 152

5

Helix

153 – 155

3

Beta strand

169 – 173

5

Beta strand

182 – 184

3

Beta strand

186 – 188

3

Beta strand

191 – 195

5

Beta strand

201 – 205

5

Beta strand

214 – 217

4

Beta strand

219 – 222

4

Beta strand

229 – 234

6

Beta strand

241 – 246

6

Beta strand

249 – 259

11

Beta strand

261 – 263

3

Beta strand

265 – 269

5

Beta strand

275 – 280

6

Beta strand

287 – 292

6

Beta strand

295 – 301

7

Beta strand

305 – 307

3

Beta strand

310 – 313

4

Beta strand

319 – 324

6

Beta strand

331 – 336

6

Beta strand

341 – 345

5

Helix

346 – 348

3

Helix

355 – 358

4

Beta strand

365 – 369

5

Beta strand

376 – 381

6

Beta strand

383 – 385

3

Beta strand

388 – 393

6

Beta strand

396 – 403

8

Helix

405 – 408

4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 1, 1997. Version 1. Checksum: 1A4B4CD1A8E96815	FASTA	425	47,820
	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
	Isoform 2 [UniParc]. Checksum: D668D0B6D5715261	FASTA	469	52,314
	10 20 30 40 50 60 MAAEAGVVGA GASPDGDWRD QACGLLLHVH LSSRLGRAAP VRTGRHLRTV FEDTVEERVI 70 80 90 100 110 120 NEEYKIWKKN TPFLYDLVMT HALQWPSLTV QWLPEVTKPE GKDYALHWLV LGTHTSDEQN 130 140 150 160 170 180 HLVVARVHIP NDDAQFDASH CDSDKGEFGG FGSVTGKIEC EIKINHEGEV NRARYMPQNP 190 200 210 220 230 240 HIIATKTPSS DVLVFDYTKH PAKPDPSGEC NPDLRLRGHQ KEGYGLSWNS NLSGHLLSAS 250 260 270 280 290 300 DDHTVCLWDI NAGPKEGKIV DAKAIFTGHS AVVEDVAWHL LHESLFGSVA DDQKLMIWDT 310 320 330 340 350 360 RSNTTSKPSH LVDAHTAEVN CLSFNPYSEF ILATGSADKT VALWDLRNLK LKLHTFESHK 370 380 390 400 410 420 DEIFQVHWSP HNETILASSG TDRRLNVWDL SKIGEEQSAE DAEDGPPELL FIHGGHTAKI 430 440 450 460 SDFSWNPNEP WVICSVSEDN IMQIWQMAEN IYNDEESDVT TSELEGQGS

References

	« Hide 'large scale' referencesShow '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. , 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, 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[21]	"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, MASS SPECTROMETRY, CLEAVAGE OF INITIATOR METHIONINE.
[22]	"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), MASS SPECTROMETRY, CLEAVAGE OF INITIATOR METHIONINE. Tissue: Cervix carcinoma.
[23]	"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].
[24]	"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, MASS SPECTROMETRY.
[25]	"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.

IPI

IPI00395865.
IPI00646512.

PIR

I39181.

RefSeq

NP_001185648.1. NM_001198719.1.
NP_002884.1. NM_002893.3.

UniGene

Hs.495755.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3CFS	X-ray	2.40	B	1-411	[»]
3CFV	X-ray	2.60	A/B	1-411	[»]

ProteinModelPortal

Q16576.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-436N.

IntAct

Q16576. 24 interactions.

MINT

MINT-90512.

STRING

9606.ENSP00000369427.

PTM databases

PhosphoSite

Q16576.

Polymorphism databases

DMDM

2494891.

Proteomic databases

PaxDb

Q16576.

PeptideAtlas

Q16576.

PRIDE

Q16576.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000380084; ENSP00000369424; ENSG00000102054.
ENST00000380087; ENSP00000369427; ENSG00000102054.

GeneID

5931.

KEGG

hsa:5931.

UCSC

uc004cxt.3. human.

Organism-specific databases

CTD

5931.

GeneCards

GC0XM016772.

HGNC

HGNC:9890. RBBP7.

HPA

CAB037084.

MIM

300825. gene.

neXtProt

NX_Q16576.

PharmGKB

PA34254.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG2319.

HOGENOM

HOG000160330.

HOVERGEN

HBG053236.

KO

K11659.

OMA

DGFLLHV.

OrthoDB

EOG4DBTDH.

PhylomeDB

Q16576.

Enzyme and pathway databases

Pathway_Interaction_DB

hedgehog_glipathway. Hedgehog signaling events mediated by Gli proteins.
smad2_3nuclearpathway. Regulation of nuclear SMAD2/3 signaling.
telomerasepathway. Regulation of Telomerase.
hdac_classi_pathway. Signaling events mediated by HDAC Class I.

Reactome

REACT_115566. Cell Cycle.

Gene expression databases

ArrayExpress

Q16576.

Bgee

Q16576.

CleanEx

HS_RBBP7.

Genevestigator

Q16576.

GermOnline

ENSG00000102054. Homo sapiens.

Family and domain databases

Gene3D

2.130.10.10. 1 hit.

InterPro

IPR020472. G-protein_beta_WD-40_rep.
IPR022052. Histone-bd_RBBP4.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view]

Pfam

PF12265. CAF1C_H4-bd. 1 hit.
PF00400. WD40. 5 hits.
[Graphical view]

PRINTS

PR00320. GPROTEINBRPT.

SMART

SM00320. WD40. 6 hits.
[Graphical view]

SUPFAM

SSF50978. WD40_like. 1 hit.

PROSITE

PS00678. WD_REPEATS_1. 3 hits.
PS50082. WD_REPEATS_2. 5 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

RBBP7. human.

EvolutionaryTrace

Q16576.

GenomeRNAi

5931.

NextBio

23110.

PMAP-CutDB

Q16576.

SOURCE

Search...

Entry information

Entry name

RBBP7_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 130 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.