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 27-MAR-2024, entry version 180.
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, Spleen,
RC 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). Interacts also
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};
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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_035377.2; NM_011247.2. [P97868-1]
DR RefSeq; NP_778188.1; NM_175023.3.
DR RefSeq; XP_006507533.1; XM_006507470.3.
DR AlphaFoldDB; P97868; -.
DR BMRB; P97868; -.
DR SMR; P97868; -.
DR BioGRID; 202817; 8.
DR IntAct; P97868; 2.
DR MINT; P97868; -.
DR STRING; 10090.ENSMUSP00000049528; -.
DR GlyGen; P97868; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P97868; -.
DR PhosphoSitePlus; P97868; -.
DR EPD; P97868; -.
DR jPOST; P97868; -.
DR MaxQB; 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; 388 antibodies from 30 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 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; NPPWVAP; -.
DR OrthoDB; 150979at2759; -.
DR PhylomeDB; P97868; -.
DR TreeFam; TF350543; -.
DR Reactome; R-MMU-9013422; RHOBTB1 GTPase cycle.
DR Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 19647; 27 hits in 76 CRISPR screens.
DR ChiTaRS; Rbbp6; mouse.
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 Genevisible; P97868; MM.
DR GO; GO:0005813; C:centrosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0016607; C:nuclear speck; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
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:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR GO; GO:0048568; P:embryonic organ development; IGI:MGI.
DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR GO; GO:0035264; P:multicellular organism growth; IMP:MGI.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
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 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; 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:SF29; 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; 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 335..352
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 554..599
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 687..730
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 736..767
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 773..787
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 905..930
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 983..1030
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1037..1071
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1084..1165
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1175..1204
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1220..1234
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1235..1256
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1258..1280
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1336..1361
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1362..1436
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1449..1579
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1647..1674
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1675..1723
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1726..1750
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
//
