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E3 ubiquitin-protein ligase BRE1A (BRE1-A) (hBRE1) (EC 2.3.2.27) (RING finger protein 20) (RING-type E3 ubiquitin transferase BRE1A)

 BRE1A_HUMAN             Reviewed;         975 AA.
Q5VTR2; A7MCT5; Q2TB34; Q69YL5; Q6P527; Q8N3J4; Q96JD3; Q9H9Y7;
Q9HA51; Q9NUR4; Q9NWQ3; Q9NX83;
20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
20-DEC-2005, sequence version 2.
25-OCT-2017, entry version 147.
RecName: Full=E3 ubiquitin-protein ligase BRE1A;
Short=BRE1-A;
Short=hBRE1;
EC=2.3.2.27 {ECO:0000269|PubMed:16307923, ECO:0000269|PubMed:16337599, ECO:0000269|PubMed:19410543};
AltName: Full=RING finger protein 20;
AltName: Full=RING-type E3 ubiquitin transferase BRE1A {ECO:0000305};
Name=RNF20; Synonyms=BRE1A;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Brain;
Wu H., Xie Y., Ying K., Mao Y.M.;
"A novel RING finger protein RNF20 gene specially expressed in
testis.";
Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Ileal mucosa, Mammary gland, Placenta, and Teratocarcinoma;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164053; DOI=10.1038/nature02465;
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
Rogers J., Dunham I.;
"DNA sequence and analysis of human chromosome 9.";
Nature 429:369-374(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Thyroid;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 453-975.
TISSUE=Amygdala, and Melanoma;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[6]
FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, AND IDENTIFICATION IN A COMPLEX
WITH RNF40 AND UBE2E1.
PubMed=16307923; DOI=10.1016/j.molcel.2005.09.025;
Zhu B., Zheng Y., Pham A.-D., Mandal S.S., Erdjument-Bromage H.,
Tempst P., Reinberg D.;
"Monoubiquitination of human histone H2B: the factors involved and
their roles in HOX gene regulation.";
Mol. Cell 20:601-611(2005).
[7]
FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND INTERACTION
WITH TP53.
PubMed=16337599; DOI=10.1016/j.molcel.2005.11.012;
Kim J., Hake S.B., Roeder R.G.;
"The human homolog of yeast BRE1 functions as a transcriptional
coactivator through direct activator interactions.";
Mol. Cell 20:759-770(2005).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic kidney;
PubMed=17525332; DOI=10.1126/science.1140321;
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
"ATM and ATR substrate analysis reveals extensive protein networks
responsive to DNA damage.";
Science 316:1160-1166(2007).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-522, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[12]
FUNCTION, CATALYTIC ACTIVITY, AND SUBUNIT.
PubMed=19410543; DOI=10.1016/j.cell.2009.02.027;
Kim J., Guermah M., McGinty R.K., Lee J.S., Tang Z., Milne T.A.,
Shilatifard A., Muir T.W., Roeder R.G.;
"RAD6-mediated transcription-coupled H2B ubiquitylation directly
stimulates H3K4 methylation in human cells.";
Cell 137:459-471(2009).
[13]
FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PA2G4, AND TISSUE
SPECIFICITY.
PubMed=19037095; DOI=10.1091/mbc.E08-09-0983;
Liu Z., Oh S.M., Okada M., Liu X., Cheng D., Peng J., Brat D.J.,
Sun S.Y., Zhou W., Gu W., Ye K.;
"Human BRE1 is an E3 ubiquitin ligase for Ebp1 tumor suppressor.";
Mol. Biol. Cell 20:757-768(2009).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-136 AND SER-138, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[15]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-348, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-138, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[18]
INTERACTION WITH WAC.
PubMed=21329877; DOI=10.1016/j.molcel.2011.01.024;
Zhang F., Yu X.;
"WAC, a functional partner of RNF20/40, regulates histone H2B
ubiquitination and gene transcription.";
Mol. Cell 41:384-397(2011).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-138, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41; SER-136 AND SER-138,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-136 AND SER-138, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
-!- FUNCTION: Component of the RNF20/40 E3 ubiquitin-protein ligase
complex that mediates monoubiquitination of 'Lys-120' of histone
H2B (H2BK120ub1). H2BK120ub1 gives a specific tag for epigenetic
transcriptional activation and is also prerequisite for histone H3
'Lys-4' and 'Lys-79' methylation (H3K4me and H3K79me,
respectively). It thereby plays a central role inb histone code
and gene regulation. The RNF20/40 complex forms a H2B ubiquitin
ligase complex in cooperation with the E2 enzyme UBE2A or UBE2B;
reports about the cooperation with UBE2E1/UBCH are contradictory.
Required for transcriptional activation of Hox genes. Recruited to
the MDM2 promoter, probably by being recruited by p53/TP53, and
thereby acts as a transcriptional coactivator. Mediates the
polyubiquitination of isoform 2 of PA2G4 in cancer cells leading
to its proteasome-mediated degradation.
{ECO:0000269|PubMed:16307923, ECO:0000269|PubMed:16337599,
ECO:0000269|PubMed:19037095, ECO:0000269|PubMed:19410543}.
-!- CATALYTIC ACTIVITY: S-ubiquitinyl-[E2 ubiquitin-conjugating
enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-
conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor
protein]-L-lysine. {ECO:0000269|PubMed:16307923,
ECO:0000269|PubMed:16337599, ECO:0000269|PubMed:19410543}.
-!- PATHWAY: Protein modification; protein ubiquitination.
-!- SUBUNIT: Component of the RNF20/40 complex (also known as BRE1
complex) probably composed of 2 copies of RNF20/BRE1A and 2 copies
of RNF40/BRE1B. Interacts with UBE2E1/UBCH6. Interacts with
p53/TP53 and WAC. Interacts with PAF1; the interaction mediates
the association of the PAF1 and RNF20/40 complexes which is a
prerequsite for recruitment of UBE2A/B. Interacts with isoform 1
and isoform 2 of PA2G4. {ECO:0000269|PubMed:16307923,
ECO:0000269|PubMed:16337599, ECO:0000269|PubMed:19037095,
ECO:0000269|PubMed:19410543, ECO:0000269|PubMed:21329877}.
-!- INTERACTION:
Q9Y2J4:AMOTL2; NbExp=4; IntAct=EBI-2372238, EBI-746752;
Q9Y2J4-4:AMOTL2; NbExp=3; IntAct=EBI-2372238, EBI-10187270;
O96017:CHEK2; NbExp=3; IntAct=EBI-2372238, EBI-1180783;
Q92905:COPS5; NbExp=2; IntAct=EBI-2372238, EBI-594661;
P42858:HTT; NbExp=3; IntAct=EBI-2372238, EBI-466029;
O75150:RNF40; NbExp=10; IntAct=EBI-2372238, EBI-744408;
P51965:UBE2E1; NbExp=2; IntAct=EBI-2372238, EBI-348546;
Q8N6Y0:USHBP1; NbExp=3; IntAct=EBI-2372238, EBI-739895;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19037095,
ECO:0000305|PubMed:16337599}.
-!- TISSUE SPECIFICITY: Expressed in the normal brain and also in
malignant gliomas (at protein level).
{ECO:0000269|PubMed:19037095}.
-!- SIMILARITY: Belongs to the BRE1 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAH63115.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
Sequence=BAA91326.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=BAA92057.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=BAB14005.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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EMBL; AF265230; AAK58539.1; -; mRNA.
EMBL; AK000389; BAA91134.1; ALT_SEQ; mRNA.
EMBL; AK000697; BAA91326.1; ALT_INIT; mRNA.
EMBL; AK002051; BAA92057.1; ALT_INIT; mRNA.
EMBL; AK022300; BAB14005.1; ALT_INIT; mRNA.
EMBL; AK022532; BAB14081.1; -; mRNA.
EMBL; AK314401; BAG37025.1; -; mRNA.
EMBL; AL591377; CAH69963.1; -; Genomic_DNA.
EMBL; AL353621; CAH69963.1; JOINED; Genomic_DNA.
EMBL; AL353621; CAI14618.1; -; Genomic_DNA.
EMBL; AL591377; CAI14618.1; JOINED; Genomic_DNA.
EMBL; BC063115; AAH63115.1; ALT_SEQ; mRNA.
EMBL; BC110584; AAI10585.1; -; mRNA.
EMBL; BC110585; AAI10586.1; -; mRNA.
EMBL; BC152309; AAI52310.1; -; mRNA.
EMBL; AL832910; CAH10630.1; -; mRNA.
EMBL; AL834272; CAD38947.1; -; mRNA.
CCDS; CCDS35084.1; -.
RefSeq; NP_062538.5; NM_019592.6.
RefSeq; XP_011517164.1; XM_011518862.1.
UniGene; Hs.729085; -.
PDB; 5TRB; X-ray; 1.80 A; A=906-975.
PDBsum; 5TRB; -.
ProteinModelPortal; Q5VTR2; -.
SMR; Q5VTR2; -.
BioGrid; 121119; 91.
CORUM; Q5VTR2; -.
DIP; DIP-53411N; -.
IntAct; Q5VTR2; 42.
MINT; MINT-3054538; -.
STRING; 9606.ENSP00000373772; -.
iPTMnet; Q5VTR2; -.
PhosphoSitePlus; Q5VTR2; -.
DMDM; 84027766; -.
EPD; Q5VTR2; -.
MaxQB; Q5VTR2; -.
PaxDb; Q5VTR2; -.
PeptideAtlas; Q5VTR2; -.
PRIDE; Q5VTR2; -.
Ensembl; ENST00000389120; ENSP00000373772; ENSG00000155827.
GeneID; 56254; -.
KEGG; hsa:56254; -.
UCSC; uc004bbn.5; human.
CTD; 56254; -.
DisGeNET; 56254; -.
EuPathDB; HostDB:ENSG00000155827.11; -.
GeneCards; RNF20; -.
HGNC; HGNC:10062; RNF20.
HPA; CAB012478; -.
HPA; HPA051773; -.
MIM; 607699; gene.
neXtProt; NX_Q5VTR2; -.
OpenTargets; ENSG00000155827; -.
PharmGKB; PA34427; -.
eggNOG; KOG0978; Eukaryota.
eggNOG; ENOG410Y5C6; LUCA.
GeneTree; ENSGT00390000002866; -.
HOVERGEN; HBG080312; -.
InParanoid; Q5VTR2; -.
KO; K10696; -.
OMA; NRYWNQF; -.
OrthoDB; EOG091G01SA; -.
PhylomeDB; Q5VTR2; -.
TreeFam; TF323183; -.
Reactome; R-HSA-8866654; E3 ubiquitin ligases ubiquitinate target proteins.
SIGNOR; Q5VTR2; -.
UniPathway; UPA00143; -.
ChiTaRS; RNF20; human.
GeneWiki; RNF20; -.
GenomeRNAi; 56254; -.
PRO; PR:Q5VTR2; -.
Proteomes; UP000005640; Chromosome 9.
Bgee; ENSG00000155827; -.
ExpressionAtlas; Q5VTR2; baseline and differential.
Genevisible; Q5VTR2; HS.
GO; GO:0033503; C:HULC complex; IDA:UniProtKB.
GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0000151; C:ubiquitin ligase complex; IDA:UniProtKB.
GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
GO; GO:0042393; F:histone binding; IDA:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0003730; F:mRNA 3'-UTR binding; IDA:UniProtKB.
GO; GO:0002039; F:p53 binding; IDA:UniProtKB.
GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB.
GO; GO:0033523; P:histone H2B ubiquitination; IDA:UniProtKB.
GO; GO:0010390; P:histone monoubiquitination; IDA:UniProtKB.
GO; GO:0030336; P:negative regulation of cell migration; IDA:UniProtKB.
GO; GO:1900364; P:negative regulation of mRNA polyadenylation; IMP:UniProtKB.
GO; GO:2001168; P:positive regulation of histone H2B ubiquitination; IMP:UniProtKB.
GO; GO:0031062; P:positive regulation of histone methylation; IEA:Ensembl.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:UniProtKB.
GO; GO:0000209; P:protein polyubiquitination; IDA:UniProtKB.
GO; GO:0016567; P:protein ubiquitination; TAS:Reactome.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:UniProtKB.
GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IMP:UniProtKB.
Gene3D; 3.30.40.10; -; 1.
Gene3D; 3.90.1150.10; -; 1.
InterPro; IPR015422; PyrdxlP-dep_Trfase_sub2.
InterPro; IPR001841; Znf_RING.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
InterPro; IPR017907; Znf_RING_CS.
SMART; SM00184; RING; 1.
PROSITE; PS00518; ZF_RING_1; 1.
PROSITE; PS50089; ZF_RING_2; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Chromatin regulator; Coiled coil;
Complete proteome; Metal-binding; Nucleus; Phosphoprotein;
Reference proteome; Transferase; Ubl conjugation pathway; Zinc;
Zinc-finger.
CHAIN 1 975 E3 ubiquitin-protein ligase BRE1A.
/FTId=PRO_0000055836.
ZN_FING 922 961 RING-type. {ECO:0000255|PROSITE-
ProRule:PRU00175}.
COILED 43 90 {ECO:0000255}.
COILED 168 375 {ECO:0000255}.
COILED 429 898 {ECO:0000255}.
MOD_RES 21 21 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q3U319}.
MOD_RES 41 41 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 136 136 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 138 138 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 348 348 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 510 510 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q3U319}.
MOD_RES 522 522 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 562 562 Phosphoserine.
{ECO:0000250|UniProtKB:Q3U319}.
CONFLICT 149 149 G -> GKW (in Ref. 3; CAH69963/CAI14618).
{ECO:0000305}.
CONFLICT 285 285 E -> Q (in Ref. 2; BAA91134/BAA91326).
{ECO:0000305}.
CONFLICT 289 289 N -> D (in Ref. 1; AAK58539).
{ECO:0000305}.
CONFLICT 322 322 A -> V (in Ref. 2; BAB14081).
{ECO:0000305}.
CONFLICT 668 668 K -> E (in Ref. 2; BAB14081).
{ECO:0000305}.
CONFLICT 693 693 K -> T (in Ref. 1; AAK58539).
{ECO:0000305}.
CONFLICT 699 699 D -> E (in Ref. 2; BAB14081).
{ECO:0000305}.
HELIX 908 920 {ECO:0000244|PDB:5TRB}.
TURN 923 925 {ECO:0000244|PDB:5TRB}.
STRAND 926 929 {ECO:0000244|PDB:5TRB}.
STRAND 932 934 {ECO:0000244|PDB:5TRB}.
TURN 935 937 {ECO:0000244|PDB:5TRB}.
HELIX 943 951 {ECO:0000244|PDB:5TRB}.
TURN 958 960 {ECO:0000244|PDB:5TRB}.
STRAND 968 971 {ECO:0000244|PDB:5TRB}.
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


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