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Protein

E3 ubiquitin-protein ligase BRE1A

Gene

RNF20

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.4 Publications

Pathway:iprotein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri922 – 96140RING-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  • chromatin binding Source: Ensembl
  • histone binding Source: UniProtKB
  • ligase activity Source: UniProtKB-KW
  • mRNA 3'-UTR binding Source: UniProtKB
  • p53 binding Source: UniProtKB
  • transcription coactivator activity Source: UniProtKB
  • ubiquitin protein ligase binding Source: UniProtKB
  • ubiquitin-protein transferase activity Source: UniProtKB
  • zinc ion binding Source: InterPro

GO - Biological processi

  • histone H2B ubiquitination Source: UniProtKB
  • histone monoubiquitination Source: UniProtKB
  • negative regulation of cell migration Source: UniProtKB
  • negative regulation of mRNA polyadenylation Source: UniProtKB
  • positive regulation of histone H2B ubiquitination Source: UniProtKB
  • positive regulation of histone methylation Source: Ensembl
  • positive regulation of transcription, DNA-templated Source: UniProtKB
  • protein polyubiquitination Source: UniProtKB
  • regulation of transcription, DNA-templated Source: UniProtKB
  • ubiquitin-dependent protein catabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Ligase

Keywords - Biological processi

Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
E3 ubiquitin-protein ligase BRE1A (EC:6.3.2.-)
Short name:
BRE1-A
Short name:
hBRE1
Alternative name(s):
RING finger protein 20
Gene namesi
Name:RNF20
Synonyms:BRE1A
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 9

Organism-specific databases

HGNCiHGNC:10062. RNF20.

Subcellular locationi

GO - Cellular componenti

  • HULC complex Source: UniProtKB
  • nucleolus Source: UniProtKB
  • nucleoplasm Source: HPA
  • nucleus Source: UniProtKB
  • ubiquitin ligase complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA34427.

Polymorphism and mutation databases

DMDMi84027766.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 975975E3 ubiquitin-protein ligase BRE1APRO_0000055836Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei136 – 1361Phosphoserine2 Publications
Modified residuei138 – 1381Phosphoserine4 Publications
Modified residuei348 – 3481N6-acetyllysine1 Publication
Modified residuei522 – 5221Phosphoserine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ5VTR2.
PaxDbiQ5VTR2.
PRIDEiQ5VTR2.

PTM databases

PhosphoSiteiQ5VTR2.

Expressioni

Tissue specificityi

Expressed in the normal brain and also in malignant gliomas (at protein level).1 Publication

Gene expression databases

BgeeiQ5VTR2.
ExpressionAtlasiQ5VTR2. baseline and differential.
GenevisibleiQ5VTR2. HS.

Organism-specific databases

HPAiCAB012478.
HPA051773.

Interactioni

Subunit structurei

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 PA2G4.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
AMOTL2Q9Y2J4-43EBI-2372238,EBI-10187270
CHEK2O960173EBI-2372238,EBI-1180783
COPS5Q929052EBI-2372238,EBI-594661
HTTP428583EBI-2372238,EBI-466029
RNF40O7515010EBI-2372238,EBI-744408
UBE2E1P519652EBI-2372238,EBI-348546
USHBP1Q8N6Y03EBI-2372238,EBI-739895

Protein-protein interaction databases

BioGridi121119. 47 interactions.
DIPiDIP-53411N.
IntActiQ5VTR2. 24 interactions.
MINTiMINT-3054538.
STRINGi9606.ENSP00000373772.

Structurei

3D structure databases

ProteinModelPortaliQ5VTR2.
SMRiQ5VTR2. Positions 913-971.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili43 – 9048Sequence AnalysisAdd
BLAST
Coiled coili168 – 375208Sequence AnalysisAdd
BLAST
Coiled coili429 – 898470Sequence AnalysisAdd
BLAST

Sequence similaritiesi

Belongs to the BRE1 family.Curated
Contains 1 RING-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri922 – 96140RING-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Coiled coil, Zinc-finger

Phylogenomic databases

eggNOGiNOG263074.
GeneTreeiENSGT00390000002866.
HOVERGENiHBG080312.
InParanoidiQ5VTR2.
KOiK10696.
OMAiNCDEILM.
OrthoDBiEOG7DVD99.
PhylomeDBiQ5VTR2.
TreeFamiTF323183.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR018957. Znf_C3HC4_RING-type.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PfamiPF00097. zf-C3HC4. 1 hit.
[Graphical view]
SMARTiSM00184. RING. 1 hit.
[Graphical view]
PROSITEiPS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q5VTR2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSGIGNKRAA GEPGTSMPPE KKAAVEDSGT TVETIKLGGV SSTEELDIRT
60 70 80 90 100
LQTKNRKLAE MLDQRQAIED ELREHIEKLE RRQATDDASL LIVNRYWSQF
110 120 130 140 150
DENIRIILKR YDLEQGLGDL LTERKALVVP EPEPDSDSNQ ERKDDRERGE
160 170 180 190 200
GQEPAFSFLA TLASSSSEEM ESQLQERVES SRRAVSQIVT VYDKLQEKVE
210 220 230 240 250
LLSRKLNSGD NLIVEEAVQE LNSFLAQENM RLQELTDLLQ EKHRTMSQEF
260 270 280 290 300
SKLQSKVETA ESRVSVLESM IDDLQWDIDK IRKREQRLNR HLAEVLERVN
310 320 330 340 350
SKGYKVYGAG SSLYGGTITI NARKFEEMNA ELEENKELAQ NRLCELEKLR
360 370 380 390 400
QDFEEVTTQN EKLKVELRSA VEQVVKETPE YRCMQSQFSV LYNESLQLKA
410 420 430 440 450
HLDEARTLLH GTRGTHQHQV ELIERDEVSL HKKLRTEVIQ LEDTLAQVRK
460 470 480 490 500
EYEMLRIEFE QTLAANEQAG PINREMRHLI SSLQNHNHQL KGEVLRYKRK
510 520 530 540 550
LREAQSDLNK TRLRSGSALL QSQSSTEDPK DEPAELKPDS EDLSSQSSAS
560 570 580 590 600
KASQEDANEI KSKRDEEERE RERREKERER EREREKEKER EREKQKLKES
610 620 630 640 650
EKERDSAKDK EKGKHDDGRK KEAEIIKQLK IELKKAQESQ KEMKLLLDMY
660 670 680 690 700
RSAPKEQRDK VQLMAAEKKS KAELEDLRQR LKDLEDKEKK ENKKMADEDA
710 720 730 740 750
LRKIRAVEEQ IEYLQKKLAM AKQEEEALLS EMDVTGQAFE DMQEQNIRLM
760 770 780 790 800
QQLREKDDAN FKLMSERIKS NQIHKLLKEE KEELADQVLT LKTQVDAQLQ
810 820 830 840 850
VVRKLEEKEH LLQSNIGTGE KELGLRTQAL EMNKRKAMEA AQLADDLKAQ
860 870 880 890 900
LELAQKKLHD FQDEIVENSV TKEKDMFNFK RAQEDISRLR RKLETTKKPD
910 920 930 940 950
NVPKCDEILM EEIKDYKARL TCPCCNMRKK DAVLTKCFHV FCFECVKTRY
960 970
DTRQRKCPKC NAAFGANDFH RIYIG
Length:975
Mass (Da):113,662
Last modified:December 20, 2005 - v2
Checksum:iD75C7BE02880594A
GO

Sequence cautioni

The sequence AAH63115.1 differs from that shown.Contaminating sequence. Potential poly-A sequence.Curated
The sequence BAA91326.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAA92057.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAB14005.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti149 – 1491G → GKW in CAH69963 (PubMed:15164053).Curated
Sequence conflicti149 – 1491G → GKW in CAI14618 (PubMed:15164053).Curated
Sequence conflicti285 – 2851E → Q in BAA91134 (PubMed:14702039).Curated
Sequence conflicti285 – 2851E → Q in BAA91326 (PubMed:14702039).Curated
Sequence conflicti289 – 2891N → D in AAK58539 (Ref. 1) Curated
Sequence conflicti322 – 3221A → V in BAB14081 (PubMed:14702039).Curated
Sequence conflicti668 – 6681K → E in BAB14081 (PubMed:14702039).Curated
Sequence conflicti693 – 6931K → T in AAK58539 (Ref. 1) Curated
Sequence conflicti699 – 6991D → E in BAB14081 (PubMed:14702039).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF265230 mRNA. Translation: AAK58539.1.
AK000389 mRNA. Translation: BAA91134.1. Sequence problems.
AK000697 mRNA. Translation: BAA91326.1. Different initiation.
AK002051 mRNA. Translation: BAA92057.1. Different initiation.
AK022300 mRNA. Translation: BAB14005.1. Different initiation.
AK022532 mRNA. Translation: BAB14081.1.
AK314401 mRNA. Translation: BAG37025.1.
AL591377, AL353621 Genomic DNA. Translation: CAH69963.1.
AL353621, AL591377 Genomic DNA. Translation: CAI14618.1.
BC063115 mRNA. Translation: AAH63115.1. Sequence problems.
BC110584 mRNA. Translation: AAI10585.1.
BC110585 mRNA. Translation: AAI10586.1.
BC152309 mRNA. Translation: AAI52310.1.
AL832910 mRNA. Translation: CAH10630.1.
AL834272 mRNA. Translation: CAD38947.1.
CCDSiCCDS35084.1.
RefSeqiNP_062538.5. NM_019592.6.
XP_011517164.1. XM_011518862.1.
UniGeneiHs.729085.

Genome annotation databases

EnsembliENST00000389120; ENSP00000373772; ENSG00000155827.
GeneIDi56254.
KEGGihsa:56254.
UCSCiuc004bbn.3. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF265230 mRNA. Translation: AAK58539.1.
AK000389 mRNA. Translation: BAA91134.1. Sequence problems.
AK000697 mRNA. Translation: BAA91326.1. Different initiation.
AK002051 mRNA. Translation: BAA92057.1. Different initiation.
AK022300 mRNA. Translation: BAB14005.1. Different initiation.
AK022532 mRNA. Translation: BAB14081.1.
AK314401 mRNA. Translation: BAG37025.1.
AL591377, AL353621 Genomic DNA. Translation: CAH69963.1.
AL353621, AL591377 Genomic DNA. Translation: CAI14618.1.
BC063115 mRNA. Translation: AAH63115.1. Sequence problems.
BC110584 mRNA. Translation: AAI10585.1.
BC110585 mRNA. Translation: AAI10586.1.
BC152309 mRNA. Translation: AAI52310.1.
AL832910 mRNA. Translation: CAH10630.1.
AL834272 mRNA. Translation: CAD38947.1.
CCDSiCCDS35084.1.
RefSeqiNP_062538.5. NM_019592.6.
XP_011517164.1. XM_011518862.1.
UniGeneiHs.729085.

3D structure databases

ProteinModelPortaliQ5VTR2.
SMRiQ5VTR2. Positions 913-971.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi121119. 47 interactions.
DIPiDIP-53411N.
IntActiQ5VTR2. 24 interactions.
MINTiMINT-3054538.
STRINGi9606.ENSP00000373772.

PTM databases

PhosphoSiteiQ5VTR2.

Polymorphism and mutation databases

DMDMi84027766.

Proteomic databases

MaxQBiQ5VTR2.
PaxDbiQ5VTR2.
PRIDEiQ5VTR2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000389120; ENSP00000373772; ENSG00000155827.
GeneIDi56254.
KEGGihsa:56254.
UCSCiuc004bbn.3. human.

Organism-specific databases

CTDi56254.
GeneCardsiGC09P104296.
HGNCiHGNC:10062. RNF20.
HPAiCAB012478.
HPA051773.
MIMi607699. gene.
neXtProtiNX_Q5VTR2.
PharmGKBiPA34427.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG263074.
GeneTreeiENSGT00390000002866.
HOVERGENiHBG080312.
InParanoidiQ5VTR2.
KOiK10696.
OMAiNCDEILM.
OrthoDBiEOG7DVD99.
PhylomeDBiQ5VTR2.
TreeFamiTF323183.

Enzyme and pathway databases

UniPathwayiUPA00143.

Miscellaneous databases

ChiTaRSiRNF20. human.
GeneWikiiRNF20.
GenomeRNAii56254.
NextBioi61893.
PROiQ5VTR2.
SOURCEiSearch...

Gene expression databases

BgeeiQ5VTR2.
ExpressionAtlasiQ5VTR2. baseline and differential.
GenevisibleiQ5VTR2. HS.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR018957. Znf_C3HC4_RING-type.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PfamiPF00097. zf-C3HC4. 1 hit.
[Graphical view]
SMARTiSM00184. RING. 1 hit.
[Graphical view]
PROSITEiPS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A novel RING finger protein RNF20 gene specially expressed in testis."
    Wu H., Xie Y., Ying K., Mao Y.M.
    Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain.
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    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.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Ileal mucosa, Mammary gland, Placenta and Teratocarcinoma.
  3. "DNA sequence and analysis of human chromosome 9."
    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.
    Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Thyroid.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 453-975.
    Tissue: Amygdala and Melanoma.
  6. "Monoubiquitination of human histone H2B: the factors involved and their roles in HOX gene regulation."
    Zhu B., Zheng Y., Pham A.-D., Mandal S.S., Erdjument-Bromage H., Tempst P., Reinberg D.
    Mol. Cell 20:601-611(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT, IDENTIFICATION IN A COMPLEX WITH RNF40 AND UBE2E1.
  7. "The human homolog of yeast BRE1 functions as a transcriptional coactivator through direct activator interactions."
    Kim J., Hake S.B., Roeder R.G.
    Mol. Cell 20:759-770(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH TP53.
  8. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-522, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "RAD6-mediated transcription-coupled H2B ubiquitylation directly stimulates H3K4 methylation in human cells."
    Kim J., Guermah M., McGinty R.K., Lee J.S., Tang Z., Milne T.A., Shilatifard A., Muir T.W., Roeder R.G.
    Cell 137:459-471(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT.
  13. "Human BRE1 is an E3 ubiquitin ligase for Ebp1 tumor suppressor."
    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.
    Mol. Biol. Cell 20:757-768(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PA2G4, TISSUE SPECIFICITY.
  14. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-136 AND SER-138, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  15. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-348, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    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.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-138, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "WAC, a functional partner of RNF20/40, regulates histone H2B ubiquitination and gene transcription."
    Zhang F., Yu X.
    Mol. Cell 41:384-397(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH WAC.
  19. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-138, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  20. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-136 AND SER-138, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiBRE1A_HUMAN
AccessioniPrimary (citable) accession number: Q5VTR2
Secondary accession number(s): A7MCT5
, Q2TB34, Q69YL5, Q6P527, Q8N3J4, Q96JD3, Q9H9Y7, Q9HA51, Q9NUR4, Q9NWQ3, Q9NX83
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: December 20, 2005
Last modified: July 22, 2015
This is version 123 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 9
    Human chromosome 9: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.