BRE1A_HUMAN
ID BRE1A_HUMAN Reviewed; 975 AA.
AC Q5VTR2; A7MCT5; Q2TB34; Q69YL5; Q6P527; Q8N3J4; Q96JD3; Q9H9Y7; Q9HA51;
AC Q9NUR4; Q9NWQ3; Q9NX83;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 2.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=E3 ubiquitin-protein ligase BRE1A;
DE Short=BRE1-A;
DE Short=hBRE1;
DE EC=2.3.2.27 {ECO:0000269|PubMed:16307923, ECO:0000269|PubMed:16337599, ECO:0000269|PubMed:19410543};
DE AltName: Full=RING finger protein 20;
DE AltName: Full=RING-type E3 ubiquitin transferase BRE1A {ECO:0000305};
GN Name=RNF20; Synonyms=BRE1A;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RA Wu H., Xie Y., Ying K., Mao Y.M.;
RT "A novel RING finger protein RNF20 gene specially expressed in testis.";
RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ileal mucosa, Mammary gland, Placenta, and Teratocarcinoma;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Thyroid;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 453-975.
RC TISSUE=Amygdala, and Melanoma;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, AND IDENTIFICATION IN A COMPLEX WITH
RP RNF40 AND UBE2E1.
RX PubMed=16307923; DOI=10.1016/j.molcel.2005.09.025;
RA Zhu B., Zheng Y., Pham A.-D., Mandal S.S., Erdjument-Bromage H., Tempst P.,
RA Reinberg D.;
RT "Monoubiquitination of human histone H2B: the factors involved and their
RT roles in HOX gene regulation.";
RL Mol. Cell 20:601-611(2005).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND INTERACTION WITH
RP TP53.
RX PubMed=16337599; DOI=10.1016/j.molcel.2005.11.012;
RA Kim J., Hake S.B., Roeder R.G.;
RT "The human homolog of yeast BRE1 functions as a transcriptional coactivator
RT through direct activator interactions.";
RL Mol. Cell 20:759-770(2005).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-522, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [12]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBUNIT.
RX PubMed=19410543; DOI=10.1016/j.cell.2009.02.027;
RA Kim J., Guermah M., McGinty R.K., Lee J.S., Tang Z., Milne T.A.,
RA Shilatifard A., Muir T.W., Roeder R.G.;
RT "RAD6-mediated transcription-coupled H2B ubiquitylation directly stimulates
RT H3K4 methylation in human cells.";
RL Cell 137:459-471(2009).
RN [13]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PA2G4, AND TISSUE
RP SPECIFICITY.
RX PubMed=19037095; DOI=10.1091/mbc.e08-09-0983;
RA Liu Z., Oh S.M., Okada M., Liu X., Cheng D., Peng J., Brat D.J., Sun S.Y.,
RA Zhou W., Gu W., Ye K.;
RT "Human BRE1 is an E3 ubiquitin ligase for Ebp1 tumor suppressor.";
RL Mol. Biol. Cell 20:757-768(2009).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-136 AND SER-138, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-348, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-138, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [18]
RP INTERACTION WITH WAC.
RX PubMed=21329877; DOI=10.1016/j.molcel.2011.01.024;
RA Zhang F., Yu X.;
RT "WAC, a functional partner of RNF20/40, regulates histone H2B
RT ubiquitination and gene transcription.";
RL Mol. Cell 41:384-397(2011).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-138, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41; SER-136 AND SER-138, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-136 AND SER-138, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: Component of the RNF20/40 E3 ubiquitin-protein ligase complex
CC that mediates monoubiquitination of 'Lys-120' of histone H2B
CC (H2BK120ub1). H2BK120ub1 gives a specific tag for epigenetic
CC transcriptional activation and is also prerequisite for histone H3
CC 'Lys-4' and 'Lys-79' methylation (H3K4me and H3K79me, respectively). It
CC thereby plays a central role inb histone code and gene regulation. The
CC RNF20/40 complex forms a H2B ubiquitin ligase complex in cooperation
CC with the E2 enzyme UBE2A or UBE2B; reports about the cooperation with
CC UBE2E1/UBCH are contradictory. Required for transcriptional activation
CC of Hox genes. Recruited to the MDM2 promoter, probably by being
CC recruited by p53/TP53, and thereby acts as a transcriptional
CC coactivator. Mediates the polyubiquitination of isoform 2 of PA2G4 in
CC cancer cells leading to its proteasome-mediated degradation.
CC {ECO:0000269|PubMed:16307923, ECO:0000269|PubMed:16337599,
CC ECO:0000269|PubMed:19037095, ECO:0000269|PubMed:19410543}.
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; Evidence={ECO:0000269|PubMed:16307923,
CC ECO:0000269|PubMed:16337599, ECO:0000269|PubMed:19410543};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Component of the RNF20/40 complex (also known as BRE1 complex)
CC probably composed of 2 copies of RNF20/BRE1A and 2 copies of
CC RNF40/BRE1B. Interacts with UBE2E1/UBCH6. Interacts with p53/TP53 and
CC WAC. Interacts with PAF1; the interaction mediates the association of
CC the PAF1 and RNF20/40 complexes which is a prerequsite for recruitment
CC of UBE2A/B. Interacts with isoform 1 and isoform 2 of PA2G4.
CC {ECO:0000269|PubMed:16307923, ECO:0000269|PubMed:16337599,
CC ECO:0000269|PubMed:19037095, ECO:0000269|PubMed:19410543,
CC ECO:0000269|PubMed:21329877}.
CC -!- INTERACTION:
CC Q5VTR2; Q9Y2J4: AMOTL2; NbExp=4; IntAct=EBI-2372238, EBI-746752;
CC Q5VTR2; Q9Y2J4-4: AMOTL2; NbExp=3; IntAct=EBI-2372238, EBI-10187270;
CC Q5VTR2; Q8WUW1: BRK1; NbExp=3; IntAct=EBI-2372238, EBI-2837444;
CC Q5VTR2; Q9NX04: C1orf109; NbExp=3; IntAct=EBI-2372238, EBI-8643161;
CC Q5VTR2; Q6P1J9: CDC73; NbExp=3; IntAct=EBI-2372238, EBI-930143;
CC Q5VTR2; O96017: CHEK2; NbExp=3; IntAct=EBI-2372238, EBI-1180783;
CC Q5VTR2; Q92905: COPS5; NbExp=2; IntAct=EBI-2372238, EBI-594661;
CC Q5VTR2; P42858: HTT; NbExp=24; IntAct=EBI-2372238, EBI-466029;
CC Q5VTR2; Q09161: NCBP1; NbExp=3; IntAct=EBI-2372238, EBI-464743;
CC Q5VTR2; Q5VTR2: RNF20; NbExp=3; IntAct=EBI-2372238, EBI-2372238;
CC Q5VTR2; O75150: RNF40; NbExp=10; IntAct=EBI-2372238, EBI-744408;
CC Q5VTR2; Q9Y6A5: TACC3; NbExp=3; IntAct=EBI-2372238, EBI-2554984;
CC Q5VTR2; P51965: UBE2E1; NbExp=2; IntAct=EBI-2372238, EBI-348546;
CC Q5VTR2; Q8N6Y0: USHBP1; NbExp=3; IntAct=EBI-2372238, EBI-739895;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19037095,
CC ECO:0000305|PubMed:16337599}.
CC -!- TISSUE SPECIFICITY: Expressed in the normal brain and also in malignant
CC gliomas (at protein level). {ECO:0000269|PubMed:19037095}.
CC -!- SIMILARITY: Belongs to the BRE1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH63115.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=BAA91326.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAA92057.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB14005.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF265230; AAK58539.1; -; mRNA.
DR EMBL; AK000389; BAA91134.1; ALT_SEQ; mRNA.
DR EMBL; AK000697; BAA91326.1; ALT_INIT; mRNA.
DR EMBL; AK002051; BAA92057.1; ALT_INIT; mRNA.
DR EMBL; AK022300; BAB14005.1; ALT_INIT; mRNA.
DR EMBL; AK022532; BAB14081.1; -; mRNA.
DR EMBL; AK314401; BAG37025.1; -; mRNA.
DR EMBL; AL353621; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL591377; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC063115; AAH63115.1; ALT_SEQ; mRNA.
DR EMBL; BC110584; AAI10585.1; -; mRNA.
DR EMBL; BC110585; AAI10586.1; -; mRNA.
DR EMBL; BC152309; AAI52310.1; -; mRNA.
DR EMBL; AL832910; CAH10630.1; -; mRNA.
DR EMBL; AL834272; CAD38947.1; -; mRNA.
DR CCDS; CCDS35084.1; -.
DR RefSeq; NP_062538.5; NM_019592.6.
DR RefSeq; XP_011517164.1; XM_011518862.1.
DR PDB; 5TRB; X-ray; 1.80 A; A=906-975.
DR PDBsum; 5TRB; -.
DR AlphaFoldDB; Q5VTR2; -.
DR SMR; Q5VTR2; -.
DR BioGRID; 121119; 162.
DR CORUM; Q5VTR2; -.
DR DIP; DIP-53411N; -.
DR IntAct; Q5VTR2; 68.
DR MINT; Q5VTR2; -.
DR STRING; 9606.ENSP00000373772; -.
DR GlyGen; Q5VTR2; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q5VTR2; -.
DR MetOSite; Q5VTR2; -.
DR PhosphoSitePlus; Q5VTR2; -.
DR BioMuta; RNF20; -.
DR DMDM; 84027766; -.
DR EPD; Q5VTR2; -.
DR jPOST; Q5VTR2; -.
DR MassIVE; Q5VTR2; -.
DR MaxQB; Q5VTR2; -.
DR PaxDb; Q5VTR2; -.
DR PeptideAtlas; Q5VTR2; -.
DR PRIDE; Q5VTR2; -.
DR ProteomicsDB; 65346; -.
DR Antibodypedia; 29174; 352 antibodies from 32 providers.
DR DNASU; 56254; -.
DR Ensembl; ENST00000389120.8; ENSP00000373772.3; ENSG00000155827.12.
DR GeneID; 56254; -.
DR KEGG; hsa:56254; -.
DR MANE-Select; ENST00000389120.8; ENSP00000373772.3; NM_019592.7; NP_062538.5.
DR UCSC; uc004bbn.5; human.
DR CTD; 56254; -.
DR DisGeNET; 56254; -.
DR GeneCards; RNF20; -.
DR HGNC; HGNC:10062; RNF20.
DR HPA; ENSG00000155827; Low tissue specificity.
DR MIM; 607699; gene.
DR neXtProt; NX_Q5VTR2; -.
DR OpenTargets; ENSG00000155827; -.
DR PharmGKB; PA34427; -.
DR VEuPathDB; HostDB:ENSG00000155827; -.
DR eggNOG; KOG0978; Eukaryota.
DR GeneTree; ENSGT00390000002866; -.
DR HOGENOM; CLU_002640_0_0_1; -.
DR InParanoid; Q5VTR2; -.
DR OMA; DENTSCT; -.
DR OrthoDB; 782448at2759; -.
DR PhylomeDB; Q5VTR2; -.
DR TreeFam; TF323183; -.
DR BRENDA; 2.3.2.27; 2681.
DR PathwayCommons; Q5VTR2; -.
DR Reactome; R-HSA-8866654; E3 ubiquitin ligases ubiquitinate target proteins.
DR Reactome; R-HSA-9013422; RHOBTB1 GTPase cycle.
DR SignaLink; Q5VTR2; -.
DR SIGNOR; Q5VTR2; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 56254; 610 hits in 1136 CRISPR screens.
DR ChiTaRS; RNF20; human.
DR GeneWiki; RNF20; -.
DR GenomeRNAi; 56254; -.
DR Pharos; Q5VTR2; Tbio.
DR PRO; PR:Q5VTR2; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q5VTR2; protein.
DR Bgee; ENSG00000155827; Expressed in tibialis anterior and 193 other tissues.
DR ExpressionAtlas; Q5VTR2; baseline and differential.
DR Genevisible; Q5VTR2; HS.
DR GO; GO:0033503; C:HULC complex; IDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0000151; C:ubiquitin ligase complex; IDA:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
DR GO; GO:0042393; F:histone binding; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; IDA:UniProtKB.
DR GO; GO:0002039; F:p53 binding; IDA:UniProtKB.
DR GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0071894; P:histone H2B conserved C-terminal lysine ubiquitination; IBA:GO_Central.
DR GO; GO:0033523; P:histone H2B ubiquitination; IDA:UniProtKB.
DR GO; GO:0010390; P:histone monoubiquitination; IDA:UniProtKB.
DR GO; GO:0030336; P:negative regulation of cell migration; IDA:UniProtKB.
DR GO; GO:0031062; P:positive regulation of histone methylation; IEA:Ensembl.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:UniProtKB.
DR GO; GO:0000209; P:protein polyubiquitination; IDA:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:UniProtKB.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IMP:UniProtKB.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR013956; E3_ubiquit_lig_Bre1.
DR InterPro; IPR018957; Znf_C3HC4_RING-type.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR23163; PTHR23163; 1.
DR Pfam; PF00097; zf-C3HC4; 1.
DR SMART; SM00184; RING; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Chromatin regulator; Coiled coil; Metal-binding;
KW Nucleus; Phosphoprotein; Reference proteome; Transferase;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..975
FT /note="E3 ubiquitin-protein ligase BRE1A"
FT /id="PRO_0000055836"
FT ZN_FING 922..961
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 125..155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 507..622
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 43..90
FT /evidence="ECO:0000255"
FT COILED 168..375
FT /evidence="ECO:0000255"
FT COILED 429..898
FT /evidence="ECO:0000255"
FT COMPBIAS 126..152
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 510..527
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 540..555
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 556..622
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 21
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q3U319"
FT MOD_RES 41
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 136
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 138
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 348
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 510
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q3U319"
FT MOD_RES 522
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 562
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3U319"
FT CONFLICT 285
FT /note="E -> Q (in Ref. 2; BAA91134/BAA91326)"
FT /evidence="ECO:0000305"
FT CONFLICT 289
FT /note="N -> D (in Ref. 1; AAK58539)"
FT /evidence="ECO:0000305"
FT CONFLICT 322
FT /note="A -> V (in Ref. 2; BAB14081)"
FT /evidence="ECO:0000305"
FT CONFLICT 668
FT /note="K -> E (in Ref. 2; BAB14081)"
FT /evidence="ECO:0000305"
FT CONFLICT 693
FT /note="K -> T (in Ref. 1; AAK58539)"
FT /evidence="ECO:0000305"
FT CONFLICT 699
FT /note="D -> E (in Ref. 2; BAB14081)"
FT /evidence="ECO:0000305"
FT HELIX 908..920
FT /evidence="ECO:0007829|PDB:5TRB"
FT TURN 923..925
FT /evidence="ECO:0007829|PDB:5TRB"
FT STRAND 926..929
FT /evidence="ECO:0007829|PDB:5TRB"
FT STRAND 932..934
FT /evidence="ECO:0007829|PDB:5TRB"
FT TURN 935..937
FT /evidence="ECO:0007829|PDB:5TRB"
FT HELIX 943..951
FT /evidence="ECO:0007829|PDB:5TRB"
FT TURN 958..960
FT /evidence="ECO:0007829|PDB:5TRB"
FT STRAND 968..971
FT /evidence="ECO:0007829|PDB:5TRB"
SQ SEQUENCE 975 AA; 113662 MW; D75C7BE02880594A CRC64;
MSGIGNKRAA GEPGTSMPPE KKAAVEDSGT TVETIKLGGV SSTEELDIRT LQTKNRKLAE
MLDQRQAIED ELREHIEKLE RRQATDDASL LIVNRYWSQF DENIRIILKR YDLEQGLGDL
LTERKALVVP EPEPDSDSNQ ERKDDRERGE GQEPAFSFLA TLASSSSEEM ESQLQERVES
SRRAVSQIVT VYDKLQEKVE LLSRKLNSGD NLIVEEAVQE LNSFLAQENM RLQELTDLLQ
EKHRTMSQEF SKLQSKVETA ESRVSVLESM IDDLQWDIDK IRKREQRLNR HLAEVLERVN
SKGYKVYGAG SSLYGGTITI NARKFEEMNA ELEENKELAQ NRLCELEKLR QDFEEVTTQN
EKLKVELRSA VEQVVKETPE YRCMQSQFSV LYNESLQLKA HLDEARTLLH GTRGTHQHQV
ELIERDEVSL HKKLRTEVIQ LEDTLAQVRK EYEMLRIEFE QTLAANEQAG PINREMRHLI
SSLQNHNHQL KGEVLRYKRK LREAQSDLNK TRLRSGSALL QSQSSTEDPK DEPAELKPDS
EDLSSQSSAS KASQEDANEI KSKRDEEERE RERREKERER EREREKEKER EREKQKLKES
EKERDSAKDK EKGKHDDGRK KEAEIIKQLK IELKKAQESQ KEMKLLLDMY RSAPKEQRDK
VQLMAAEKKS KAELEDLRQR LKDLEDKEKK ENKKMADEDA LRKIRAVEEQ IEYLQKKLAM
AKQEEEALLS EMDVTGQAFE DMQEQNIRLM QQLREKDDAN FKLMSERIKS NQIHKLLKEE
KEELADQVLT LKTQVDAQLQ VVRKLEEKEH LLQSNIGTGE KELGLRTQAL EMNKRKAMEA
AQLADDLKAQ LELAQKKLHD FQDEIVENSV TKEKDMFNFK RAQEDISRLR RKLETTKKPD
NVPKCDEILM EEIKDYKARL TCPCCNMRKK DAVLTKCFHV FCFECVKTRY DTRQRKCPKC
NAAFGANDFH RIYIG
