ID RBBP7_MOUSE Reviewed; 425 AA.
AC Q60973; A2AFJ0; Q3UX20;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 27-MAR-2024, entry version 212.
DE RecName: Full=Histone-binding protein RBBP7;
DE AltName: Full=Histone acetyltransferase type B subunit 2;
DE AltName: Full=Nucleosome-remodeling factor subunit RBAP46;
DE AltName: Full=Retinoblastoma-binding protein 7;
DE Short=RBBP-7;
DE AltName: Full=Retinoblastoma-binding protein p46;
GN Name=Rbbp7; Synonyms=Rbap46;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 7-32 AND 133-155, AND
RP TISSUE SPECIFICITY.
RC TISSUE=Embryo;
RX PubMed=7503932; DOI=10.1074/jbc.270.43.25507;
RA Qian Y.-W., Lee E.Y.-H.P.;
RT "Dual retinoblastoma-binding proteins with properties related to a negative
RT regulator of ras in yeast.";
RL J. Biol. Chem. 270:25507-25513(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD;
RC TISSUE=Egg, Heart, Kidney, Liver, Placenta, Sympathetic ganglion, and
RC Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP INTERACTION WITH SUV39H1.
RX PubMed=11788710; DOI=10.1093/nar/30.2.475;
RA Vaute O., Nicolas E., Vandel L., Trouche D.;
RT "Functional and physical interaction between the histone methyl transferase
RT Suv39H1 and histone deacetylases.";
RL Nucleic Acids Res. 30:475-481(2002).
RN [6]
RP INTERACTION WITH HDAC7.
RX PubMed=10984530; DOI=10.1073/pnas.97.19.10330;
RA Downes M., Ordentlich P., Kao H.-Y., Alvarez J.G.A., Evans R.M.;
RT "Identification of a nuclear domain with deacetylase activity.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:10330-10335(2000).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Liver, Lung, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [8]
RP IDENTIFICATION IN THE PRC2 COMPLEX.
RX PubMed=20144788; DOI=10.1016/j.stem.2009.12.014;
RA Walker E., Chang W.Y., Hunkapiller J., Cagney G., Garcha K., Torchia J.,
RA Krogan N.J., Reiter J.F., Stanford W.L.;
RT "Polycomb-like 2 associates with PRC2 and regulates transcriptional
RT networks during mouse embryonic stem cell self-renewal and
RT differentiation.";
RL Cell Stem Cell 6:153-166(2010).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2; LYS-4; LYS-119 AND LYS-159,
RP CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [10]
RP IDENTIFICATION IN THE NURD COMPLEX, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=27806305; DOI=10.1016/j.celrep.2016.10.022;
RA Nitarska J., Smith J.G., Sherlock W.T., Hillege M.M., Nott A.,
RA Barshop W.D., Vashisht A.A., Wohlschlegel J.A., Mitter R., Riccio A.;
RT "A Functional Switch of NuRD Chromatin Remodeling Complex Subunits
RT Regulates Mouse Cortical Development.";
RL Cell Rep. 17:1683-1698(2016).
RN [11]
RP INTERACTION WITH PWWP2B.
RX PubMed=34180153; DOI=10.1002/advs.202102060;
RA Yan L., Jin W., Zhao Q., Cui X., Shi T., Xu Y., Li F., Jin W., Zhang Z.,
RA Zhang Z., Tang Q.Q., Pan D.;
RT "PWWP2B Fine-Tunes Adipose Thermogenesis by Stabilizing HDACs in a NuRD
RT Subcomplex.";
RL Adv. Sci. 8:e2102060-e2102060(2021).
CC -!- FUNCTION: Core histone-binding subunit that may target chromatin
CC remodeling factors, histone acetyltransferases and histone deacetylases
CC to their histone substrates in a manner that is regulated by
CC nucleosomal DNA. Component of several complexes which regulate
CC chromatin metabolism. These include the type B histone
CC acetyltransferase (HAT) complex, which is required for chromatin
CC assembly following DNA replication; the core histone deacetylase (HDAC)
CC complex, which promotes histone deacetylation and consequent
CC transcriptional repression; the nucleosome remodeling and histone
CC deacetylase complex (the NuRD complex), which promotes transcriptional
CC repression by histone deacetylation and nucleosome remodeling; and the
CC PRC2/EED-EZH2 complex, which promotes repression of homeotic genes
CC during development; and the NURF (nucleosome remodeling factor) complex
CC (By similarity). {ECO:0000250|UniProtKB:Q16576}.
CC -!- SUBUNIT: Binds directly to helix 1 of the histone fold of histone H4, a
CC region that is not accessible when H4 is in chromatin (By similarity).
CC Subunit of the type B histone acetyltransferase (HAT) complex, composed
CC of RBBP7 and HAT1 (By similarity). Subunit of the core histone
CC deacetylase (HDAC) complex, which is composed of HDAC1, HDAC2, RBBP4
CC and RBBP7. The core HDAC complex associates with SIN3A, ARID4B/SAP180,
CC SAP18, SAP30, SAP130, SUDS3/SAP45 and possibly ARID4A/RBP1 and ING1 to
CC form the SIN3 HDAC complex (By similarity). Component of the nucleosome
CC remodeling and deacetylase (NuRD) repressor complex, composed of core
CC proteins MTA1, MTA2, MTA3, RBBP4, RBBP7, HDAC1, HDAC2, MBD2, MBD3, and
CC peripherally associated proteins CDK2AP1, CDK2AP2, GATAD2A, GATAD2B,
CC CHD3, CHD4 and CHD5 (PubMed:27806305). The exact stoichiometry of the
CC NuRD complex is unknown, and some subunits such as MBD2 and MBD3,
CC GATAD2A and GATAD2B, and CHD3, CHD4 and CHD5 define mutually exclusive
CC NuRD complexes (PubMed:27806305). The NuRD complex may interact with
CC MBD3L1. The NuRD complex may interact with MBD3L2 (By similarity).
CC Subunit of the PRC2/EED-EZH2 complex, which is composed of at least
CC EED, EZH2, RBBP4, RBBP7 and SUZ12 (PubMed:20144788). The PRC2/EED-EZH2
CC complex may also associate with HDAC1. Component of the NURF-1 ISWI
CC chromatin remodeling complex (also called the nucleosome-remodeling
CC factor (NURF) complex) at least composed of SMARCA1, BPTF, RBBP4 and
CC RBBP7. Within the complex interacts with SMARCA1. Component of the
CC BPFT-SMARCA1 complex at least composed of SMARCA1, BPFT, RBBP4 and
CC RBBP7; the complex is catalytically inactive and does not remodel
CC chromatin. Within the complex interacts with SMARCA1. Interacts with
CC BRCA1. Interacts with CDK2AP1. Interacts with CENPA. Interacts with
CC CHD3. Interacts with CHD4. Interacts with CREBBP, and this interaction
CC may be enhanced by the binding of phosphorylated CREB1 to CREBBP (By
CC similarity). Interacts with HDAC7 (PubMed:10984530). Interacts with
CC MTA1 (By similarity). Interacts with PWWP2B (PubMed:34180153).
CC Interacts with RB1 (via viral protein-binding domain) (By similarity).
CC Interacts with SUV39H1 (PubMed:11788710).
CC {ECO:0000250|UniProtKB:Q16576, ECO:0000269|PubMed:10984530,
CC ECO:0000269|PubMed:11788710, ECO:0000269|PubMed:20144788,
CC ECO:0000269|PubMed:27806305, ECO:0000269|PubMed:34180153}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- TISSUE SPECIFICITY: Higher levels in brain, thymus, lung, spleen,
CC kidney, testis, and ovary/uterus; lower levels in heart, liver, and
CC muscle. {ECO:0000269|PubMed:7503932}.
CC -!- SIMILARITY: Belongs to the WD repeat RBAP46/RBAP48/MSI1 family.
CC {ECO:0000305}.
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DR EMBL; U35142; AAC52276.1; -; mRNA.
DR EMBL; AK076016; BAC36122.1; -; mRNA.
DR EMBL; AK135779; BAE22658.1; -; mRNA.
DR EMBL; AK135956; BAE22743.1; -; mRNA.
DR EMBL; AK136110; BAE22826.1; -; mRNA.
DR EMBL; AK145531; BAE26487.1; -; mRNA.
DR EMBL; AK145651; BAE26567.1; -; mRNA.
DR EMBL; AK146014; BAE26833.1; -; mRNA.
DR EMBL; AK146904; BAE27517.1; -; mRNA.
DR EMBL; AK146967; BAE27573.1; -; mRNA.
DR EMBL; AK147062; BAE27646.1; -; mRNA.
DR EMBL; AK148852; BAE28678.1; -; mRNA.
DR EMBL; AK153913; BAE32251.1; -; mRNA.
DR EMBL; AK160023; BAE35566.1; -; mRNA.
DR EMBL; AL672123; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC003785; AAH03785.1; -; mRNA.
DR CCDS; CCDS30509.1; -.
DR PIR; I49367; I49367.
DR RefSeq; NP_033057.3; NM_009031.3.
DR AlphaFoldDB; Q60973; -.
DR SMR; Q60973; -.
DR BioGRID; 232827; 46.
DR ComplexPortal; CPX-3441; SIN3A histone deacetylase complex, ES cell-specific variant.
DR ComplexPortal; CPX-3443; SIN3A histone deacetylase complex.
DR ComplexPortal; CPX-3444; SIN3B histone deacetylase complex.
DR ComplexPortal; CPX-694; NuRF chromatin remodeling complex.
DR ComplexPortal; CPX-953; MBD2/NuRD nucleosome remodeling and deacetylase complex.
DR ComplexPortal; CPX-954; MBD3/NuRD nucleosome remodeling and deacetylase complex.
DR CORUM; Q60973; -.
DR DIP; DIP-32856N; -.
DR IntAct; Q60973; 12.
DR MINT; Q60973; -.
DR STRING; 10090.ENSMUSP00000033720; -.
DR GlyGen; Q60973; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; Q60973; -.
DR PhosphoSitePlus; Q60973; -.
DR SwissPalm; Q60973; -.
DR REPRODUCTION-2DPAGE; Q60973; -.
DR EPD; Q60973; -.
DR jPOST; Q60973; -.
DR MaxQB; Q60973; -.
DR PaxDb; 10090-ENSMUSP00000033720; -.
DR PeptideAtlas; Q60973; -.
DR ProteomicsDB; 255117; -.
DR Pumba; Q60973; -.
DR Antibodypedia; 24054; 437 antibodies from 31 providers.
DR DNASU; 245688; -.
DR Ensembl; ENSMUST00000033720.12; ENSMUSP00000033720.6; ENSMUSG00000031353.14.
DR GeneID; 245688; -.
DR KEGG; mmu:245688; -.
DR UCSC; uc009uug.2; mouse.
DR AGR; MGI:1194910; -.
DR MGI; MGI:1194910; Rbbp7.
DR VEuPathDB; HostDB:ENSMUSG00000031353; -.
DR eggNOG; KOG0264; Eukaryota.
DR GeneTree; ENSGT00940000154748; -.
DR InParanoid; Q60973; -.
DR OMA; YALTCGN; -.
DR OrthoDB; 5472072at2759; -.
DR PhylomeDB; Q60973; -.
DR TreeFam; TF106485; -.
DR Reactome; R-MMU-212300; PRC2 methylates histones and DNA.
DR Reactome; R-MMU-2559580; Oxidative Stress Induced Senescence.
DR Reactome; R-MMU-3214815; HDACs deacetylate histones.
DR Reactome; R-MMU-3214841; PKMTs methylate histone lysines.
DR Reactome; R-MMU-3214847; HATs acetylate histones.
DR Reactome; R-MMU-3214858; RMTs methylate histone arginines.
DR Reactome; R-MMU-606279; Deposition of new CENPA-containing nucleosomes at the centromere.
DR Reactome; R-MMU-6804758; Regulation of TP53 Activity through Acetylation.
DR Reactome; R-MMU-73762; RNA Polymerase I Transcription Initiation.
DR Reactome; R-MMU-8943724; Regulation of PTEN gene transcription.
DR Reactome; R-MMU-8951664; Neddylation.
DR Reactome; R-MMU-8953750; Transcriptional Regulation by E2F6.
DR BioGRID-ORCS; 245688; 2 hits in 84 CRISPR screens.
DR ChiTaRS; Rbbp7; mouse.
DR PRO; PR:Q60973; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q60973; Protein.
DR Bgee; ENSMUSG00000031353; Expressed in primitive streak and 270 other cell types or tissues.
DR ExpressionAtlas; Q60973; baseline and differential.
DR Genevisible; Q60973; MM.
DR GO; GO:1904949; C:ATPase complex; ISO:MGI.
DR GO; GO:0000781; C:chromosome, telomeric region; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0035098; C:ESC/E(Z) complex; IDA:MGI.
DR GO; GO:0000118; C:histone deacetylase complex; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0016581; C:NuRD complex; IDA:MGI.
DR GO; GO:0016589; C:NURF complex; ISO:MGI.
DR GO; GO:0042393; F:histone binding; ISO:MGI.
DR GO; GO:0003723; F:RNA binding; IPI:MGI.
DR GO; GO:0007420; P:brain development; NAS:ComplexPortal.
DR GO; GO:0070370; P:cellular heat acclimation; ISS:UniProtKB.
DR GO; GO:0006338; P:chromatin remodeling; ISO:MGI.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR GO; GO:0030308; P:negative regulation of cell growth; ISS:UniProtKB.
DR GO; GO:0030336; P:negative regulation of cell migration; NAS:ComplexPortal.
DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; IDA:MGI.
DR GO; GO:1902455; P:negative regulation of stem cell population maintenance; NAS:ComplexPortal.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; NAS:ComplexPortal.
DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; NAS:ComplexPortal.
DR GO; GO:1902459; P:positive regulation of stem cell population maintenance; NAS:ComplexPortal.
DR GO; GO:0042659; P:regulation of cell fate specification; NAS:ComplexPortal.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; ISO:MGI.
DR GO; GO:2000736; P:regulation of stem cell differentiation; NAS:ComplexPortal.
DR GO; GO:0048545; P:response to steroid hormone; IEA:Ensembl.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR022052; Histone-bd_RBBP4_N.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR InterPro; IPR001680; WD40_rpt.
DR PANTHER; PTHR22850:SF82; HISTONE-BINDING PROTEIN RBBP7; 1.
DR PANTHER; PTHR22850; WD40 REPEAT FAMILY; 1.
DR Pfam; PF12265; CAF1C_H4-bd; 1.
DR Pfam; PF00400; WD40; 5.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 6.
DR SUPFAM; SSF50978; WD40 repeat-like; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 3.
DR PROSITE; PS50082; WD_REPEATS_2; 5.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Acetylation; Chaperone; Chromatin regulator; Direct protein sequencing;
KW DNA replication; Isopeptide bond; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Ubl conjugation; WD repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:23806337"
FT CHAIN 2..425
FT /note="Histone-binding protein RBBP7"
FT /id="PRO_0000051196"
FT REPEAT 47..122
FT /note="WD 1"
FT REPEAT 128..173
FT /note="WD 2"
FT REPEAT 181..217
FT /note="WD 3"
FT REPEAT 228..269
FT /note="WD 4"
FT REPEAT 275..312
FT /note="WD 5"
FT REPEAT 318..369
FT /note="WD 6"
FT REPEAT 376..403
FT /note="WD 7"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 3
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16576"
FT MOD_RES 4
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 10
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q16576"
FT MOD_RES 95
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16576"
FT MOD_RES 119
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 159
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 354
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16576"
FT CROSSLNK 4
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q16576"
FT CROSSLNK 4
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q16576"
FT CROSSLNK 101
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q16576"
FT CROSSLNK 155
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q16576"
FT CROSSLNK 159
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q16576"
SQ SEQUENCE 425 AA; 47790 MW; 0A4A4CD1A8E96815 CRC64;
MASKEMFEDT VEERVINEEY KIWKKNTPFL YDLVMTHALQ WPSLTVQWLP EVTKPEGKDY
ALHWLVLGTH TSDEQNHLVV ARVHIPNDDA QFDASHCDSD KGEFGGFGSV TGKIECEIKI
NHEGEVNRAR YMPQNPHIIA TKTPSSDVLV FDYTKHPAKP DPSGECNPDL RLRGHQKEGY
GLSWNSNLSG HLLSASDDHT VCLWDINAGP KEGKIVDAKA IFTGHSAVVE DVAWHLLHES
LFGSVADDQK LMIWDTRSNT TSKPSHLVDA HTAEVNCLSF NPYSEFILAT GSADKTVALW
DLRNLKLKLH TFESHKDEIF QVHWSPHNET ILASSGTDRR LNVWDLSKIG EEQSAEDAED
GPPELLFIHG GHTAKISDFS WNPNEPWVIC SVSEDNIMQI WQMAENIYND EESDVTASEL
EGQGS
//
