RBBP4_MOUSE
ID RBBP4_MOUSE Reviewed; 425 AA.
AC Q60972; A2A875;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 5.
DT 03-AUG-2022, entry version 199.
DE RecName: Full=Histone-binding protein RBBP4;
DE AltName: Full=Chromatin assembly factor 1 subunit C;
DE Short=CAF-1 subunit C;
DE AltName: Full=Chromatin assembly factor I p48 subunit;
DE Short=CAF-I 48 kDa subunit;
DE Short=CAF-I p48;
DE AltName: Full=Nucleosome-remodeling factor subunit RBAP48;
DE AltName: Full=Retinoblastoma-binding protein 4;
DE Short=RBBP-4;
DE AltName: Full=Retinoblastoma-binding protein p48;
GN Name=Rbbp4; Synonyms=Rbap48;
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], AND TISSUE SPECIFICITY.
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 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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 IDENTIFICATION IN A SIN3 HDAC COMPLEX, AND INTERACTION WITH SAP30.
RX PubMed=9702189; DOI=10.1016/s1097-2765(00)80111-2;
RA Laherty C.D., Billin A.N., Lavinsky R.M., Yochum G.S., Bush A.C.,
RA Sun J.-M., Mullen T.-M., Davie J.R., Rose D.W., Glass C.K., Rosenfeld M.G.,
RA Ayer D.E., Eisenman R.N.;
RT "SAP30, a component of the mSin3 corepressor complex involved in N-CoR-
RT mediated repression by specific transcription factors.";
RL Mol. Cell 2:33-42(1998).
RN [6]
RP INTERACTION WITH CREBBP.
RX PubMed=10866654; DOI=10.1128/mcb.20.14.4970-4978.2000;
RA Zhang Q., Vo N., Goodman R.H.;
RT "Histone binding protein RbAp48 interacts with a complex of CREB binding
RT protein and phosphorylated CREB.";
RL Mol. Cell. Biol. 20:4970-4978(2000).
RN [7]
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 [8]
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 [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [10]
RP IDENTIFICATION IN THE PRC2/EZH1 COMPLEX.
RX PubMed=19026780; DOI=10.1016/j.molcel.2008.10.016;
RA Shen X., Liu Y., Hsu Y.-J., Fujiwara Y., Kim J., Mao X., Yuan G.-C.,
RA Orkin S.H.;
RT "EZH1 mediates methylation on histone H3 lysine 27 and complements EZH2 in
RT maintaining stem cell identity and executing pluripotency.";
RL Mol. Cell 32:491-502(2008).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Spleen, and
RC 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 [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-160, AND IDENTIFICATION BY MASS
RP 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 [13]
RP IDENTIFICATION IN A COMPLEX WITH SIN3A; SINHCAF; HDAC1; SAP30; OGT AND
RP TET1.
RX PubMed=28554894; DOI=10.15252/embj.201696307;
RA Streubel G., Fitzpatrick D.J., Oliviero G., Scelfo A., Moran B., Das S.,
RA Munawar N., Watson A., Wynne K., Negri G.L., Dillon E.T., Jammula S.,
RA Hokamp K., O'Connor D.P., Pasini D., Cagney G., Bracken A.P.;
RT "Fam60a defines a variant Sin3a-Hdac complex in embryonic stem cells
RT required for self-renewal.";
RL EMBO J. 36:2216-2232(2017).
RN [14]
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 assembly factors, chromatin remodeling factors 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 chromatin assembly factor 1
CC (CAF-1) complex, which is required for chromatin assembly following DNA
CC replication and DNA repair; 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; the PRC2
CC complex, which promotes repression of homeotic genes during
CC development; and the NURF (nucleosome remodeling factor) complex.
CC {ECO:0000250|UniProtKB:Q09028}.
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. Subunit of the
CC chromatin assembly factor 1 (CAF-1) complex, which is composed of
CC RBBP4, CHAF1B and CHAF1A (By similarity). Subunit of the core histone
CC deacetylase (HDAC) complex, which is composed of HDAC1, HDAC2, RBBP4
CC and RBBP7 (By similarity). The core HDAC complex associates with SIN3A,
CC ARID4B/SAP180, SAP18, SAP30, SAP130, SUDS3/SAP45 and possibly
CC ARID4A/RBP1 and ING1 to form the SIN3 HDAC complex (Probable). The core
CC HDAC complex may also associate with MTA2, MBD3, CHD3 and CHD4 to form
CC the nucleosome remodeling and histone deacetylase complex (the NuRD
CC complex) (By similarity). The NuRD complex may also interact with
CC MBD3L1 and MBD3L2 (By similarity). Interacts with MTA1 (By similarity).
CC Component of the PRC2 complex, which consists of the core subunits EED,
CC EZH1 or EZH2, SUZ12, and RBBP4, and various combinations of accessory
CC subunits including AEBP2, JARID2, PHF19, MTF2 and EPOP
CC (PubMed:19026780). Forms a monomeric PRC2.2 (class 2) complex
CC consisting of at least SUZ12, RBBP4, AEBP2 and JARID2 (By similarity).
CC Forms a dimeric PRC2.1 (class 1, PRC-PCL) complex consisting of at
CC least SUZ12, RBBP4, and PHF19; PHF19 stabilizes the dimeric structure
CC which enhances PRC2 interaction with chromatin (By similarity).
CC Component of the NURF-1 ISWI chromatin remodeling complex (also called
CC the nucleosome-remodeling factor (NURF) complex) at least composed of
CC SMARCA1; BPTF; RBBP4 and RBBP7 (PubMed:10866654). Within the complex
CC interacts with SMARCA1 (By similarity). Interacts with the ISWI
CC chromatin remodeling complex component SMARCA5; the interaction is
CC direct (By similarity). Interacts with SUV39H1 and HDAC7
CC (PubMed:10984530, PubMed:11788710). Interacts with the viral protein-
CC binding domain of the retinoblastoma protein (RB1) (By similarity).
CC Interacts with SPEN/MINT (By similarity). Interacts with BRCA1 (By
CC similarity). Interacts with CREBBP, and this interaction may be
CC enhanced by the binding of phosphorylated CREB1 to CREBBP (By
CC similarity). Component of the DREAM complex (also named LINC complex)
CC at least composed of E2F4, E2F5, LIN9, LIN37, LIN52, LIN54, MYBL1,
CC MYBL2, RBL1, RBL2, RBBP4, TFDP1 and TFDP2 (By similarity). The complex
CC exists in quiescent cells where it represses cell cycle-dependent genes
CC (By similarity). It dissociates in S phase when LIN9, LIN37, LIN52 and
CC LIN54 form a subcomplex that binds to MYBL2 (By similarity). Interacts
CC with PHF6 (By similarity). Found in a complex composed of at least
CC SINHCAF, SIN3A, HDAC1, SAP30, RBBP4, OGT and TET1 (PubMed:28554894).
CC Interacts with ERCC6 (By similarity). Interacts with ZNF827; the
CC interaction is direct and recruits RBBP4 to telomeres (By similarity).
CC Interacts with ARMC12 (via ARM domains) (By similarity). Interacts with
CC PWWP2B (PubMed:34180153). {ECO:0000250|UniProtKB:Q09028,
CC ECO:0000269|PubMed:10866654, ECO:0000269|PubMed:10984530,
CC ECO:0000269|PubMed:11788710, ECO:0000269|PubMed:19026780,
CC ECO:0000269|PubMed:28554894, ECO:0000269|PubMed:34180153,
CC ECO:0000305|PubMed:9702189}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q09028}.
CC Chromosome, telomere {ECO:0000250|UniProtKB:Q09028}. Note=Localizes to
CC chromatin as part of the PRC2 complex. {ECO:0000250|UniProtKB:Q09028}.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC52275.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U35141; AAC52275.1; ALT_FRAME; mRNA.
DR EMBL; AL607123; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CU234133; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466552; EDL30202.1; -; Genomic_DNA.
DR EMBL; BC138568; AAI38569.1; -; mRNA.
DR EMBL; BC138570; AAI38571.1; -; mRNA.
DR CCDS; CCDS18688.1; -.
DR PIR; I49366; I49366.
DR RefSeq; NP_033056.2; NM_009030.3.
DR AlphaFoldDB; Q60972; -.
DR SMR; Q60972; -.
DR BioGRID; 202816; 44.
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-570; Chromatin assembly factor 1 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; Q60972; -.
DR DIP; DIP-32855N; -.
DR IntAct; Q60972; 19.
DR MINT; Q60972; -.
DR STRING; 10090.ENSMUSP00000099658; -.
DR iPTMnet; Q60972; -.
DR PhosphoSitePlus; Q60972; -.
DR SwissPalm; Q60972; -.
DR REPRODUCTION-2DPAGE; Q60972; -.
DR EPD; Q60972; -.
DR jPOST; Q60972; -.
DR MaxQB; Q60972; -.
DR PaxDb; Q60972; -.
DR PeptideAtlas; Q60972; -.
DR PRIDE; Q60972; -.
DR ProteomicsDB; 253176; -.
DR Antibodypedia; 3343; 494 antibodies from 38 providers.
DR DNASU; 19646; -.
DR Ensembl; ENSMUST00000102598; ENSMUSP00000099658; ENSMUSG00000057236.
DR GeneID; 19646; -.
DR KEGG; mmu:19646; -.
DR UCSC; uc008uwt.1; mouse.
DR CTD; 5928; -.
DR MGI; MGI:1194912; Rbbp4.
DR VEuPathDB; HostDB:ENSMUSG00000057236; -.
DR eggNOG; KOG0264; Eukaryota.
DR GeneTree; ENSGT00940000153375; -.
DR HOGENOM; CLU_020445_3_1_1; -.
DR InParanoid; Q60972; -.
DR OMA; PHEEGCL; -.
DR OrthoDB; 831322at2759; -.
DR PhylomeDB; Q60972; -.
DR TreeFam; TF106485; -.
DR Reactome; R-MMU-1538133; G0 and Early G1.
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-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-8953750; Transcriptional Regulation by E2F6.
DR BioGRID-ORCS; 19646; 36 hits in 81 CRISPR screens.
DR ChiTaRS; Rbbp4; mouse.
DR PRO; PR:Q60972; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q60972; protein.
DR Bgee; ENSMUSG00000057236; Expressed in ureteric bud tip and 260 other tissues.
DR ExpressionAtlas; Q60972; baseline and differential.
DR Genevisible; Q60972; MM.
DR GO; GO:1904949; C:ATPase complex; ISO:MGI.
DR GO; GO:0033186; C:CAF-1 complex; ISS:UniProtKB.
DR GO; GO:0000785; C:chromatin; 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:UniProtKB.
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:UniProtKB.
DR GO; GO:0016581; C:NuRD complex; IDA:MGI.
DR GO; GO:0016589; C:NURF complex; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0016580; C:Sin3 complex; IC:ComplexPortal.
DR GO; GO:0008094; F:ATP-dependent activity, acting on DNA; ISO:MGI.
DR GO; GO:0042393; F:histone binding; ISO:MGI.
DR GO; GO:0042826; F:histone deacetylase binding; ISO:MGI.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0007420; P:brain development; IC:ComplexPortal.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0031497; P:chromatin assembly; ISS:UniProtKB.
DR GO; GO:0006338; P:chromatin remodeling; ISS:HGNC-UCL.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR GO; GO:0006335; P:DNA replication-dependent chromatin assembly; ISO:MGI.
DR GO; GO:0006336; P:DNA replication-independent chromatin assembly; ISO:MGI.
DR GO; GO:0016575; P:histone deacetylation; ISO:MGI.
DR GO; GO:0030336; P:negative regulation of cell migration; IC:ComplexPortal.
DR GO; GO:1902455; P:negative regulation of stem cell population maintenance; IC:ComplexPortal.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IC:ComplexPortal.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IC:ComplexPortal.
DR GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; IC:ComplexPortal.
DR GO; GO:1902459; P:positive regulation of stem cell population maintenance; IC:ComplexPortal.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IC:ComplexPortal.
DR GO; GO:0042659; P:regulation of cell fate specification; IC:ComplexPortal.
DR GO; GO:2000736; P:regulation of stem cell differentiation; IC:ComplexPortal.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISO:MGI.
DR Gene3D; 2.130.10.10; -; 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; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR Pfam; PF12265; CAF1C_H4-bd; 1.
DR Pfam; PF00400; WD40; 5.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 6.
DR SUPFAM; SSF50978; SSF50978; 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; Cell cycle; Chromatin regulator; Chromosome; DNA replication;
KW Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Repressor; Telomere; Transcription; Transcription regulation;
KW Ubl conjugation; WD repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:16452087"
FT CHAIN 2..425
FT /note="Histone-binding protein RBBP4"
FT /id="PRO_0000051187"
FT REPEAT 122..155
FT /note="WD 1"
FT REPEAT 175..206
FT /note="WD 2"
FT REPEAT 225..256
FT /note="WD 3"
FT REPEAT 271..302
FT /note="WD 4"
FT REPEAT 315..346
FT /note="WD 5"
FT REPEAT 372..403
FT /note="WD 6"
FT REGION 2..132
FT /note="Interaction with ARMC12"
FT /evidence="ECO:0000250|UniProtKB:Q09028"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:16452087"
FT MOD_RES 4
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q09028"
FT MOD_RES 110
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q09028"
FT MOD_RES 160
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 355
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q09028"
FT CROSSLNK 4
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q09028"
FT CROSSLNK 4
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q09028"
FT CROSSLNK 160
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q09028"
FT CONFLICT 213
FT /note="E -> K (in Ref. 1; AAC52275)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 425 AA; 47656 MW; B71E2D55A444C360 CRC64;
MADKEAAFDD AVEERVINEE YKIWKKNTPF LYDLVMTHAL EWPSLTAQWL PDVTRPEGKD
FSIHRLVLGT HTSDEQNHLV IASVQLPNDD AQFDASHYDS EKGEFGGFGS VSGKIEIEIK
INHEGEVNRA RYMPQNPCII ATKTPSSDVL VFDYTKHPSK PDPSGECNPD LRLRGHQKEG
YGLSWNPNLS GHLLSASDDH TICLWDISAV PKEGKVVDAK TIFTGHTAVV EDVSWHLLHE
SLFGSVADDQ KLMIWDTRSN NTSKPSHSVD AHTAEVNCLS FNPYSEFILA TGSADKTVAL
WDLRNLKLKL HSFESHKDEI FQVQWSPHNE TILASSGTDR RLNVWDLSKI GEEQSPEDAE
DGPPELLFIH GGHTAKISDF SWNPNEPWVI CSVSEDNIMQ VWQMAENIYN DEDPEGSVDP
EGQGS
