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Q5VTR2 (BRE1A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 109. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
E3 ubiquitin-protein ligase BRE1A

Short name=BRE1-A
Short name=hBRE1
EC=6.3.2.-
Alternative name(s):
RING finger protein 20
Gene names
Name:RNF20
Synonyms:BRE1A
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length975 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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 in 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. Ref.6 Ref.7 Ref.12

Pathway

Protein modification; protein ubiquitination.

Subunit structure

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. Ref.6 Ref.7 Ref.12 Ref.17

Subcellular location

Nucleus Probable Ref.7.

Sequence similarities

Belongs to the BRE1 family.

Contains 1 RING-type zinc finger.

Sequence caution

The sequence AAH63115.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.

The sequence BAA91326.1 differs from that shown. Reason: Erroneous initiation.

The sequence BAA92057.1 differs from that shown. Reason: Erroneous initiation.

The sequence BAB14005.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processUbl conjugation pathway
   Cellular componentNucleus
   DomainCoiled coil
Zinc-finger
   LigandMetal-binding
Zinc
   Molecular functionChromatin regulator
Ligase
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processhistone H2B ubiquitination

Inferred from direct assay Ref.6Ref.7. Source: UniProtKB

histone monoubiquitination

Inferred from direct assay Ref.6Ref.7. Source: UniProtKB

negative regulation of cell migration

Inferred from direct assay PubMed 18832071. Source: UniProtKB

positive regulation of histone methylation

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription, DNA-templated

Inferred from mutant phenotype PubMed 16713563. Source: UniProtKB

protein polyubiquitination

Inferred from direct assay PubMed 19037095. Source: UniProtKB

regulation of transcription, DNA-templated

Inferred from mutant phenotype PubMed 18832071. Source: UniProtKB

ubiquitin-dependent protein catabolic process

Inferred from mutant phenotype PubMed 19037095. Source: UniProtKB

   Cellular_componentHULC complex

Inferred from direct assay Ref.12. Source: UniProtKB

nucleolus

Inferred from direct assay PubMed 19037095. Source: UniProtKB

nucleus

Inferred from direct assay Ref.6. Source: UniProtKB

ubiquitin ligase complex

Inferred from direct assay Ref.6. Source: UniProtKB

   Molecular_functionchromatin binding

Inferred from electronic annotation. Source: Ensembl

histone binding

Inferred from direct assay Ref.7. Source: UniProtKB

p53 binding

Inferred from direct assay Ref.7. Source: UniProtKB

transcription coactivator activity

Inferred from direct assay Ref.7. Source: UniProtKB

ubiquitin protein ligase binding

Inferred from physical interaction Ref.6. Source: UniProtKB

ubiquitin-protein ligase activity

Inferred from direct assay PubMed 19037095. Source: UniProtKB

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 975975E3 ubiquitin-protein ligase BRE1A
PRO_0000055836

Regions

Zinc finger922 – 96140RING-type
Coiled coil43 – 9048 Potential
Coiled coil168 – 375208 Potential
Coiled coil429 – 898470 Potential

Amino acid modifications

Modified residue1361Phosphoserine Ref.13
Modified residue1381Phosphoserine Ref.13 Ref.15 Ref.18
Modified residue3481N6-acetyllysine Ref.14
Modified residue5221Phosphoserine Ref.10

Experimental info

Sequence conflict1491G → GKW in CAH69963. Ref.3
Sequence conflict1491G → GKW in CAI14618. Ref.3
Sequence conflict2851E → Q in BAA91134. Ref.2
Sequence conflict2851E → Q in BAA91326. Ref.2
Sequence conflict2891N → D in AAK58539. Ref.1
Sequence conflict3221A → V in BAB14081. Ref.2
Sequence conflict6681K → E in BAB14081. Ref.2
Sequence conflict6931K → T in AAK58539. Ref.1
Sequence conflict6991D → E in BAB14081. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q5VTR2 [UniParc].

Last modified December 20, 2005. Version 2.
Checksum: D75C7BE02880594A

FASTA975113,662
        10         20         30         40         50         60 
MSGIGNKRAA GEPGTSMPPE KKAAVEDSGT TVETIKLGGV SSTEELDIRT LQTKNRKLAE 

        70         80         90        100        110        120 
MLDQRQAIED ELREHIEKLE RRQATDDASL LIVNRYWSQF DENIRIILKR YDLEQGLGDL 

       130        140        150        160        170        180 
LTERKALVVP EPEPDSDSNQ ERKDDRERGE GQEPAFSFLA TLASSSSEEM ESQLQERVES 

       190        200        210        220        230        240 
SRRAVSQIVT VYDKLQEKVE LLSRKLNSGD NLIVEEAVQE LNSFLAQENM RLQELTDLLQ 

       250        260        270        280        290        300 
EKHRTMSQEF SKLQSKVETA ESRVSVLESM IDDLQWDIDK IRKREQRLNR HLAEVLERVN 

       310        320        330        340        350        360 
SKGYKVYGAG SSLYGGTITI NARKFEEMNA ELEENKELAQ NRLCELEKLR QDFEEVTTQN 

       370        380        390        400        410        420 
EKLKVELRSA VEQVVKETPE YRCMQSQFSV LYNESLQLKA HLDEARTLLH GTRGTHQHQV 

       430        440        450        460        470        480 
ELIERDEVSL HKKLRTEVIQ LEDTLAQVRK EYEMLRIEFE QTLAANEQAG PINREMRHLI 

       490        500        510        520        530        540 
SSLQNHNHQL KGEVLRYKRK LREAQSDLNK TRLRSGSALL QSQSSTEDPK DEPAELKPDS 

       550        560        570        580        590        600 
EDLSSQSSAS KASQEDANEI KSKRDEEERE RERREKERER EREREKEKER EREKQKLKES 

       610        620        630        640        650        660 
EKERDSAKDK EKGKHDDGRK KEAEIIKQLK IELKKAQESQ KEMKLLLDMY RSAPKEQRDK 

       670        680        690        700        710        720 
VQLMAAEKKS KAELEDLRQR LKDLEDKEKK ENKKMADEDA LRKIRAVEEQ IEYLQKKLAM 

       730        740        750        760        770        780 
AKQEEEALLS EMDVTGQAFE DMQEQNIRLM QQLREKDDAN FKLMSERIKS NQIHKLLKEE 

       790        800        810        820        830        840 
KEELADQVLT LKTQVDAQLQ VVRKLEEKEH LLQSNIGTGE KELGLRTQAL EMNKRKAMEA 

       850        860        870        880        890        900 
AQLADDLKAQ LELAQKKLHD FQDEIVENSV TKEKDMFNFK RAQEDISRLR RKLETTKKPD 

       910        920        930        940        950        960 
NVPKCDEILM EEIKDYKARL TCPCCNMRKK DAVLTKCFHV FCFECVKTRY DTRQRKCPKC 

       970 
NAAFGANDFH RIYIG 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]"The full-ORF clone resource of the German cDNA consortium."
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.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
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]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
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.
Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
[10]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"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.
[14]"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].
[15]"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.
[16]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]"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.
[18]"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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_062538.5. NM_019592.6.
UniGeneHs.729085.

3D structure databases

ProteinModelPortalQ5VTR2.
SMRQ5VTR2. Positions 933-974.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid121119. 47 interactions.
DIPDIP-53411N.
IntActQ5VTR2. 15 interactions.
MINTMINT-3054538.

PTM databases

PhosphoSiteQ5VTR2.

Polymorphism databases

DMDM84027766.

Proteomic databases

PaxDbQ5VTR2.
PRIDEQ5VTR2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000389120; ENSP00000373772; ENSG00000155827.
GeneID56254.
KEGGhsa:56254.
UCSCuc004bbn.3. human.

Organism-specific databases

CTD56254.
GeneCardsGC09P104296.
HGNCHGNC:10062. RNF20.
HPACAB012478.
HPA051773.
MIM607699. gene.
neXtProtNX_Q5VTR2.
PharmGKBPA34427.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG263074.
HOVERGENHBG080312.
KOK10696.
OMAEHMENDE.
OrthoDBEOG7DVD99.
PhylomeDBQ5VTR2.
TreeFamTF323183.

Enzyme and pathway databases

UniPathwayUPA00143.

Gene expression databases

ArrayExpressQ5VTR2.
BgeeQ5VTR2.
GenevestigatorQ5VTR2.

Family and domain databases

Gene3D3.30.40.10. 1 hit.
InterProIPR018957. Znf_C3HC4_RING-type.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PfamPF00097. zf-C3HC4. 1 hit.
[Graphical view]
SMARTSM00184. RING. 1 hit.
[Graphical view]
PROSITEPS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSRNF20. human.
GeneWikiRNF20.
GenomeRNAi56254.
NextBio61893.
PROQ5VTR2.
SOURCESearch...

Entry information

Entry nameBRE1A_HUMAN
AccessionPrimary (citable) accession number: Q5VTR2
Secondary accession number(s): A7MCT5 expand/collapse secondary AC list , Q2TB34, Q69YL5, Q6P527, Q8N3J4, Q96JD3, Q9H9Y7, Q9HA51, Q9NUR4, Q9NWQ3, Q9NX83
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: December 20, 2005
Last modified: April 16, 2014
This is version 109 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 9

Human chromosome 9: entries, gene names and cross-references to MIM