ID   RBBP6_MOUSE             Reviewed;        1790 AA.
AC   P97868; P70287; Q3TTR9; Q3TUM7; Q3UMP7; Q4U217; Q7TT06; Q8BNY8; Q8R399;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 5.
DT   02-SEP-2026, entry version 190.
DE   RecName: Full=E3 ubiquitin-protein ligase RBBP6;
DE            EC=2.3.2.27;
DE   AltName: Full=Proliferation potential-related protein;
DE   AltName: Full=Protein P2P-R;
DE   AltName: Full=RING-type E3 ubiquitin transferase RBBP6 {ECO:0000305};
DE   AltName: Full=Retinoblastoma-binding protein 6;
DE   AltName: Full=p53-associated cellular protein of testis;
GN   Name=Rbbp6; Synonyms=P2pr, Pact;
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 [LARGE SCALE MRNA] (ISOFORM 3), NUCLEOTIDE SEQUENCE
RP   [LARGE SCALE MRNA] OF 546-1148 (ISOFORM 2), AND NUCLEOTIDE SEQUENCE [LARGE
RP   SCALE MRNA] OF 1356-1790 (ISOFORMS 1/2).
RC   STRAIN=C57BL/6J;
RC   TISSUE=Corpora quadrigemina, Corpus striatum, Embryo, Head, and Lung;
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   [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 MRNA] (ISOFORM 3).
RC   STRAIN=FVB/N-3; 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   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 154-1790 (ISOFORM 2), INTERACTION WITH RB1,
RP   TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC   STRAIN=BALB/cJ;
RX   PubMed=9037032; DOI=10.1073/pnas.94.4.1212;
RA   Witte M.M., Scott R.E.;
RT   "The proliferation potential protein-related (P2P-R) gene with domains
RT   encoding heterogeneous nuclear ribonucleoprotein association and Rb1
RT   binding shows repressed expression during terminal differentiation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 94:1212-1217(1997).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 204-1790 (ISOFORM 1), INTERACTION WITH TP53
RP   AND RB1, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC   STRAIN=BALB/cJ; TISSUE=Testis;
RX   PubMed=9010216; DOI=10.1038/sj.onc.1200825;
RA   Simons A., Melamed-Bessudo C., Wolkowicz R., Sperling J., Sperling R.,
RA   Eisenbach L., Rotter V.;
RT   "PACT: cloning and characterization of a cellular p53 binding protein that
RT   interacts with Rb.";
RL   Oncogene 14:145-155(1997).
RN   [6]
RP   SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX   PubMed=12064457; DOI=10.1002/jcp.10084;
RA   Gao S., Witte M.M., Scott R.E.;
RT   "P2P-R protein localizes to the nucleolus of interphase cells and the
RT   periphery of chromosomes in mitotic cells which show maximum P2P-R
RT   immunoreactivity.";
RL   J. Cell. Physiol. 191:145-154(2002).
RN   [7]
RP   ERRATUM OF PUBMED:12064457.
RA   Gao S., Witte M.M., Scott R.E.;
RL   J. Cell. Physiol. 192:359-360(2002).
RN   [8]
RP   SUBCELLULAR LOCATION.
RX   PubMed=12384997; DOI=10.1002/jcp.10163;
RA   Gao S., Scott R.E.;
RT   "P2P-R protein overexpression restricts mitotic progression at prometaphase
RT   and promotes mitotic apoptosis.";
RL   J. Cell. Physiol. 193:199-207(2002).
RN   [9]
RP   INTERACTION WITH TP53.
RX   PubMed=14566974; DOI=10.1002/jcp.10381;
RA   Gao S., Scott R.E.;
RT   "Stable overexpression of specific segments of the P2P-R protein in human
RT   MCF-7 cells promotes camptothecin-induced apoptosis.";
RL   J. Cell. Physiol. 197:445-452(2003).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-985; SER-1179; THR-1272 AND
RP   SER-1329, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [11]
RP   DISRUPTION PHENOTYPE, AND FUNCTION.
RX   PubMed=17470788; DOI=10.1073/pnas.0701916104;
RA   Li L., Deng B., Xing G., Teng Y., Tian C., Cheng X., Yin X., Yang J.,
RA   Gao X., Zhu Y., Sun Q., Zhang L., Yang X., He F.;
RT   "PACT is a negative regulator of p53 and essential for cell growth and
RT   embryonic development.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:7951-7956(2007).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1179 AND SER-1329, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-361; THR-985; SER-1179;
RP   SER-1278; SER-1329; SER-1648 AND SER-1651, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Pancreas,
RC   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   [14]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-130, 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   [15]
RP   FUNCTION.
RX   PubMed=24726359; DOI=10.1016/j.celrep.2014.03.030;
RA   Miotto B., Chibi M., Xie P., Koundrioukoff S., Moolman-Smook H., Pugh D.,
RA   Debatisse M., He F., Zhang L., Defossez P.A.;
RT   "The RBBP6/ZBTB38/MCM10 axis regulates DNA replication and common fragile
RT   site stability.";
RL   Cell Rep. 7:575-587(2014).
CC   -!- FUNCTION: E3 ubiquitin-protein ligase which promotes ubiquitination of
CC       YBX1, leading to its degradation by the proteasome (By similarity). May
CC       play a role as a scaffold protein to promote the assembly of the
CC       p53/TP53-MDM2 complex, resulting in increase of MDM2-mediated
CC       ubiquitination and degradation of p53/TP53; may function as negative
CC       regulator of p53/TP53, leading to both apoptosis and cell growth
CC       retardation (PubMed:17470788). Regulates DNA-replication and common
CC       fragile sites (CFS) stability in a ZBTB38- and MCM10-dependent manner.
CC       Controls ZBTB38 protein stability and abundance via ubiquitination and
CC       proteasomal degradation, and ZBTB38 in turn negatively regulates the
CC       expression of MCM10 which plays an important role in DNA-replication
CC       (PubMed:24726359). {ECO:0000250|UniProtKB:Q7Z6E9,
CC       ECO:0000269|PubMed:17470788, ECO:0000269|PubMed:24726359}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC         [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC         cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC         EC=2.3.2.27;
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: Interacts with MDM2 and YBX1 (By similarity). Also interacts
CC       with p53/TP53 and RB1. Interacts with NEK6 (By similarity). Interacts
CC       with ZBTB38 (By similarity). {ECO:0000250|UniProtKB:Q7Z6E9,
CC       ECO:0000269|PubMed:14566974, ECO:0000269|PubMed:9010216,
CC       ECO:0000269|PubMed:9037032}.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus. Chromosome. Cytoplasm,
CC       cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}.
CC       Note=Colocalizes with mitotic chromosomes. Co-localizes with NEK6 in
CC       the centrosome (By similarity). {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=P97868-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P97868-2; Sequence=VSP_018287;
CC       Name=3;
CC         IsoId=P97868-3; Sequence=VSP_018285, VSP_018286;
CC   -!- TISSUE SPECIFICITY: Highly expressed in testis. Expressed at lower
CC       levels in brain, heart, kidney, liver, lung, skeletal muscle, spleen,
CC       thymus and tongue. {ECO:0000269|PubMed:9010216,
CC       ECO:0000269|PubMed:9037032}.
CC   -!- DEVELOPMENTAL STAGE: Expression is reduced during terminal
CC       differentiation. Expression is induced in the G2/M phase of the cell
CC       cycle (at protein level). {ECO:0000269|PubMed:12064457,
CC       ECO:0000269|PubMed:9037032}.
CC   -!- DOMAIN: Contains a N-terminus DWNN domain, a zinc-finger domain and a
CC       C4C4 zinc-binding RING finger domain (By similarity). The ring finger
CC       may indeed be a U-box domain (By similarity).
CC       {ECO:0000250|UniProtKB:Q7Z6E9}.
CC   -!- PTM: Phosphorylated by NEK6. {ECO:0000250}.
CC   -!- DISRUPTION PHENOTYPE: Early embryonic lethality before 7.5 dpc,
CC       accompanied by accumulation of p53 and widespread apoptosis.
CC       {ECO:0000269|PubMed:17470788}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC72432.1; Type=Frameshift; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AK045635; BAC32441.1; -; mRNA.
DR   EMBL; AK079129; BAC37553.1; -; mRNA.
DR   EMBL; AK081261; BAC38179.1; -; mRNA.
DR   EMBL; AK144758; BAE26051.1; -; mRNA.
DR   EMBL; AK160656; BAE35944.1; -; mRNA.
DR   EMBL; AK161231; BAE36255.1; -; mRNA.
DR   EMBL; AC125221; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC025874; AAH25874.1; -; mRNA.
DR   EMBL; U83913; AAC72432.1; ALT_FRAME; mRNA.
DR   EMBL; U28789; AAB49620.1; -; mRNA.
DR   CCDS; CCDS52387.1; -. [P97868-1]
DR   PIR; T42727; T42727.
DR   RefSeq; NP_001390012.1; NM_001403083.1. [P97868-2]
DR   RefSeq; NP_035377.2; NM_011247.3. [P97868-1]
DR   RefSeq; NP_778188.1; NM_175023.4.
DR   AlphaFoldDB; P97868; -.
DR   BMRB; P97868; -.
DR   SMR; P97868; -.
DR   BioGRID; 202817; 8.
DR   FunCoup; P97868; 3512.
DR   IntAct; P97868; 2.
DR   MINT; P97868; -.
DR   STRING; 10090.ENSMUSP00000049528; -.
DR   GlyGen; P97868; 2 sites, 1 N-linked glycan (1 site), 1 O-linked glycan (1 site).
DR   iPTMnet; P97868; -.
DR   PhosphoSitePlus; P97868; -.
DR   jPOST; P97868; -.
DR   PaxDb; 10090-ENSMUSP00000049528; -.
DR   PeptideAtlas; P97868; -.
DR   ProteomicsDB; 255114; -. [P97868-1]
DR   ProteomicsDB; 255115; -. [P97868-2]
DR   ProteomicsDB; 255116; -. [P97868-3]
DR   Pumba; P97868; -.
DR   Antibodypedia; 26070; 354 antibodies from 31 providers.
DR   DNASU; 19647; -.
DR   Ensembl; ENSMUST00000052135.14; ENSMUSP00000049528.8; ENSMUSG00000030779.17. [P97868-1]
DR   Ensembl; ENSMUST00000071590.6; ENSMUSP00000071519.6; ENSMUSG00000030779.17. [P97868-2]
DR   GeneID; 19647; -.
DR   KEGG; mmu:19647; -.
DR   UCSC; uc009jow.2; mouse. [P97868-3]
DR   UCSC; uc009joy.2; mouse. [P97868-1]
DR   AGR; MGI:894835; -.
DR   CTD; 5930; -.
DR   MGI; MGI:894835; Rbbp6.
DR   VEuPathDB; HostDB:ENSMUSG00000030779; -.
DR   eggNOG; KOG0314; Eukaryota.
DR   GeneTree; ENSGT00940000157561; -.
DR   HOGENOM; CLU_239162_0_0_1; -.
DR   InParanoid; P97868; -.
DR   OMA; IRAMMTQ; -.
DR   OrthoDB; 106784at2759; -.
DR   PhylomeDB; P97868; -.
DR   Reactome; R-MMU-9013422; RHOBTB1 GTPase cycle.
DR   Reactome; R-MMU-9770562; mRNA Polyadenylation.
DR   Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   UniPathway; UPA00143; -.
DR   BioGRID-ORCS; 19647; 27 hits in 76 CRISPR screens.
DR   PRO; PR:P97868; -.
DR   Proteomes; UP000000589; Chromosome 7.
DR   RNAct; P97868; protein.
DR   Bgee; ENSMUSG00000030779; Expressed in embryonic post-anal tail and 259 other cell types or tissues.
DR   ExpressionAtlas; P97868; baseline and differential.
DR   GO; GO:0005813; C:centrosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0016607; C:nuclear speck; ISO:GO_Central.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0032991; C:protein-containing complex; ISO:GO_Central.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0019901; F:protein kinase binding; ISO:GO_Central.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; ISS:UniProtKB.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; ISS:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006974; P:DNA damage response; ISS:UniProtKB.
DR   GO; GO:0048568; P:embryonic organ development; IGI:MGI.
DR   GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR   GO; GO:0006397; P:mRNA processing; IEA:InterPro.
DR   GO; GO:0035264; P:multicellular organism growth; IMP:MGI.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006275; P:regulation of DNA replication; ISS:UniProtKB.
DR   GO; GO:0061053; P:somite development; IMP:MGI.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IMP:UniProtKB.
DR   CDD; cd16620; vRING-HC-C4C4_RBBP6; 1.
DR   FunFam; 4.10.60.10:FF:000005; E3 ubiquitin-protein ligase RBBP6; 1.
DR   FunFam; 3.30.40.10:FF:000139; E3 ubiquitin-protein ligase RBBP6 isoform X1; 1.
DR   FunFam; 3.10.20.90:FF:000070; E3 ubiquitin-protein ligase RBBP6 isoform X2; 1.
DR   Gene3D; 3.10.20.90; Phosphatidylinositol 3-kinase Catalytic Subunit, Chain A, domain 1; 1.
DR   Gene3D; 4.10.60.10; Zinc finger, CCHC-type; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR014891; DWNN_domain.
DR   InterPro; IPR033489; RBBP6.
DR   InterPro; IPR063314; RBBP6_link.
DR   InterPro; IPR003613; Ubox_domain.
DR   InterPro; IPR025829; Zn_knuckle_CX2CX3GHX4C.
DR   InterPro; IPR001878; Znf_CCHC.
DR   InterPro; IPR036875; Znf_CCHC_sf.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR15439:SF0; CELL DIVISION CYCLE AND APOPTOSIS REGULATOR PROTEIN 1-RELATED; 1.
DR   PANTHER; PTHR15439; RETINOBLASTOMA-BINDING PROTEIN 6; 1.
DR   Pfam; PF08783; DWNN; 1.
DR   Pfam; PF30896; RBBP6_link; 1.
DR   Pfam; PF04564; U-box; 1.
DR   Pfam; PF13696; zf-CCHC_2; 1.
DR   SMART; SM01180; DWNN; 1.
DR   SMART; SM00184; RING; 1.
DR   SMART; SM00343; ZnF_C2HC; 1.
DR   SUPFAM; SSF57756; Retrovirus zinc finger-like domains; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS51282; DWNN; 1.
DR   PROSITE; PS50158; ZF_CCHC; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Chromosome; Cytoplasm; Cytoskeleton;
KW   DNA damage; DNA replication; Isopeptide bond; Metal-binding; Nucleus;
KW   Phosphoprotein; Reference proteome; Transferase; Ubl conjugation;
KW   Ubl conjugation pathway; Zinc; Zinc-finger.
FT   CHAIN           1..1790
FT                   /note="E3 ubiquitin-protein ligase RBBP6"
FT                   /id="PRO_0000234355"
FT   DOMAIN          4..76
FT                   /note="DWNN"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00612"
FT   ZN_FING         160..177
FT                   /note="CCHC-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT   ZN_FING         260..301
FT                   /note="RING-type; degenerate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT   REGION          329..353
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          374..408
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          533..599
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          622..641
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          648..667
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          675..797
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          850..1292
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          983..1139
FT                   /note="Interaction with RB1"
FT   REGION          1322..1790
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1434..1544
FT                   /note="Interaction with p53"
FT   COMPBIAS        337..349
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        376..390
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        558..599
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        622..635
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        686..720
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        736..771
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        903..923
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        932..941
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        956..972
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        980..991
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1002..1018
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1042..1072
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1096..1161
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1182..1200
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1231..1249
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1260..1277
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1281..1291
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1336..1358
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1363..1392
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1400..1440
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1449..1460
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1469..1507
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1515..1580
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1618..1627
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1634..1646
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1663..1675
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1689..1724
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1727..1750
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1751..1760
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1761..1773
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1774..1790
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         130
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         245
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q7Z6E9"
FT   MOD_RES         246
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q7Z6E9"
FT   MOD_RES         247
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q7Z6E9"
FT   MOD_RES         248
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q7Z6E9"
FT   MOD_RES         361
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         517
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q7Z6E9"
FT   MOD_RES         769
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q7Z6E9"
FT   MOD_RES         771
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q7Z6E9"
FT   MOD_RES         773
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q7Z6E9"
FT   MOD_RES         781
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q7Z6E9"
FT   MOD_RES         816
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q7Z6E9"
FT   MOD_RES         862
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q7Z6E9"
FT   MOD_RES         874
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q7Z6E9"
FT   MOD_RES         958
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q7Z6E9"
FT   MOD_RES         985
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:17242355,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         1179
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355,
FT                   ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT   MOD_RES         1272
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:17242355"
FT   MOD_RES         1278
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         1329
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355,
FT                   ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT   MOD_RES         1342
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q7Z6E9"
FT   MOD_RES         1348
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q7Z6E9"
FT   MOD_RES         1469
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q7Z6E9"
FT   MOD_RES         1646
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q7Z6E9"
FT   MOD_RES         1648
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         1651
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   CROSSLNK        1107
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q7Z6E9"
FT   CROSSLNK        1169
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q7Z6E9"
FT   VAR_SEQ         102..123
FT                   /note="IDDASASISLAQLTKTANLAEA -> VCKNTITLFLHNCFYLYNVSVT (in
FT                   isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15489334,
FT                   ECO:0000303|PubMed:16141072"
FT                   /id="VSP_018285"
FT   VAR_SEQ         124..1756
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15489334,
FT                   ECO:0000303|PubMed:16141072"
FT                   /id="VSP_018286"
FT   VAR_SEQ         653..686
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072,
FT                   ECO:0000303|PubMed:9037032"
FT                   /id="VSP_018287"
FT   CONFLICT        254
FT                   /note="I -> F (in Ref. 5; AAB49620)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        317..318
FT                   /note="RQ -> GR (in Ref. 4; AAC72432)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        341
FT                   /note="P -> H (in Ref. 5; AAB49620)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        418
FT                   /note="S -> F (in Ref. 4; AAC72432)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        421
FT                   /note="V -> S (in Ref. 5; AAB49620)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        580
FT                   /note="P -> L (in Ref. 4; AAC72432)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        595
FT                   /note="P -> T (in Ref. 4; AAC72432)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        615..622
FT                   /note="PWVSSGVQ -> ACFSPGVP (in Ref. 4; AAC72432)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        629
FT                   /note="I -> M (in Ref. 4; AAC72432)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        636
FT                   /note="P -> L (in Ref. 4; AAC72432)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        647
FT                   /note="R -> K (in Ref. 4; AAC72432)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        689
FT                   /note="S -> F (in Ref. 4; AAC72432)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        703
FT                   /note="Y -> D (in Ref. 4; AAC72432)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        789
FT                   /note="Q -> R (in Ref. 4; AAC72432)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        940
FT                   /note="R -> Q (in Ref. 1; BAE36255)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        941
FT                   /note="R -> RNEE (in Ref. 4; AAC72432)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        956..958
FT                   /note="ETS -> GKF (in Ref. 4; AAC72432)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        963
FT                   /note="E -> G (in Ref. 4; AAC72432)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        978
FT                   /note="L -> F (in Ref. 4; AAC72432)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        982
FT                   /note="D -> E (in Ref. 4; AAC72432)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1012
FT                   /note="K -> N (in Ref. 5; AAB49620)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1290
FT                   /note="K -> T (in Ref. 4; AAC72432)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1316
FT                   /note="Q -> H (in Ref. 4; AAC72432)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1564
FT                   /note="N -> I (in Ref. 4; AAC72432)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1581
FT                   /note="E -> D (in Ref. 4; AAC72432)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1591
FT                   /note="P -> L (in Ref. 4; AAC72432)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1596
FT                   /note="P -> L (in Ref. 4; AAC72432)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1604
FT                   /note="A -> V (in Ref. 4; AAC72432)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1790 AA;  199587 MW;  3909C30EB9DD2CE3 CRC64;
     MSCVHYKFSS KLNYDTVTFD GLHISLCDLK KQIMGREKLK AADSDLQITN AQTKEEYTDD
     NALIPKNSSV IVRRIPIGGV KSTSKTYVIS RTEPVMGTTK AIDDASASIS LAQLTKTANL
     AEANASEEDK IKAMMSQSGH EYDPINYMKK TLVGPPPPSY TCFRCGKPGH YIKNCPTNGD
     KNFESGPRIK KSTGIPRSFM MEVKDPNMKG AMLTNTGKYA IPTIDAEAYA IGKKEKPPFL
     PEEPSSSSEE DDPIPDELLC LICKDIMTDA VVIPCCGNSY CDECIRTALL ESDEHTCPTC
     HQNDVSPDAL IANKFLRQAV NNFKNETGYT KRLRKQLPPP PPPVPPPRPL MQRNLQPLMR
     SPISRQQDPL MIPVTSSSAH SAPSISSLTS NPSALAPSVS GNPSSAPAPV PDITATVSIS
     VHSEKSDGPF RDSDNKLLPA AALTSEHSKG ASSIAITALM EEKGYQVPVL GTPSLLGQSL
     LHGQLIPTTG PVRINAARPG GGRPGWEHSN KLGYLVSPPQ QIRRGERSCY RSINRGRHHS
     ERSQRTQGPS LPATPVFVPV PPPPLYPPPP HTLPLPPGVP PPQFSPQFPP GQPPPAGYSV
     PPPGFPPAPA NISTPWVSSG VQTAHSNTIP TTQAPPLSRE EFYREQRRLK EEEKKKSKLD
     EFTNDFAKEL MEYKKIQKER RRSFSRSKSP YSGSSYSRSS YTYSKSRSGS TRSRSYSRSF
     SRSHSRSYSR SPPYPRRGRG KSRNYRSRSR SHGYHRSRSR SPPYRRYHSR SRSPQAFRGQ
     SPTKRNVPQG ETEREYFNRY REVPPPYDIK AYYGRSVDFR DPFEKERYRE WERKYREWYE
     KYYKGYAVGA QPRPSANRED FSPERLLPLN IRNSPFTRGR REDYAAGQSH RNRNLGGNYP
     EKLSTRDSHN AKDNPKSKEK ESENVPGDGK GNKHKKHRKR RKGEESESFL NPELLETSRK
     CRESSGIDET KTDTLFVLPS RDDATPVRDE PMDAESITFK SVSDKDKREK DKPKVKSDKT
     KRKSDGSATA KKDNVLKPSK GPQEKVDGDR EKSPRSEPPL KKAKEEATKI DSVKPSSSSQ
     KDEKVTGTPR KAHSKSAKEH QEAKPAKDEK VKKDCSKDIK SEKPASKDEK AKKPEKNKLL
     DSKGEKRKRK TEEKSVDKDF ESSSMKISKV EGTEIVKPSP KRKMEGDVEK LERTPEKDKI
     ASSTTPAKKI KLNRETGKKI GNAENASTTK EPSEKLESTS SKIKQEKVKG KAKRKVAGSE
     GSSSTLVDYT STSSTGGSPV RKSEEKTDTK RTVIKTMEEY NNDNTAPAED VIIMIQVPQS
     KWDKDDFESE EEDVKTTQPI QSVGKPSSII KNVTTKPSAT AKYTEKESEQ PEKLQKLPKE
     ASHELMQHEL RSSKGSASSE KGRAKDREHS GSEKDNPDKR KSGAQPDKES TVDRLSEQGH
     FKTLSQSSKE TRTSEKHESV RGSSNKDFTP GRDKKVDYDS RDYSSSKRRD ERGELARRKD
     SPPRGKESLS GQKSKLREER DLPKKGAESK KSNSSPPRDK KPHDHKAPYE TKRPCEETKP
     VDKNSGKERE KHAAEARNGK ESSGGKLPCI PNPPDPPMEK ELAAGQVEKS AVKPKPQLSH
     SSRLSSDLTR ETDEAAFEPD YNESDSESNV SVKEEEAVAS ISKDLKEKTT EKAKESLTVA
     TASQPGADRS QSQSSPSVSP SRSHSPSGSQ TRSHSSSASS AGSQDSKKKK KKKEKKKHKK
     HKKHKKHKKH AGADGDVEKS QKHKHKKKKA KKNKDKEKEK DDQKVRSVTV
//