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Q5VTR2

- BRE1A_HUMAN

UniProt

Q5VTR2 - BRE1A_HUMAN

Protein

E3 ubiquitin-protein ligase BRE1A

Gene

RNF20

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 114 (01 Oct 2014)
      Sequence version 2 (20 Dec 2005)
      Previous versions | rss
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    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 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.3 Publications

    Pathwayi

    Regions

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

    GO - Molecular functioni

    1. chromatin binding Source: Ensembl
    2. histone binding Source: UniProtKB
    3. ligase activity Source: UniProtKB-KW
    4. p53 binding Source: UniProtKB
    5. protein binding Source: UniProtKB
    6. transcription coactivator activity Source: UniProtKB
    7. ubiquitin protein ligase binding Source: UniProtKB
    8. ubiquitin-protein transferase activity Source: UniProtKB
    9. zinc ion binding Source: InterPro

    GO - Biological processi

    1. histone H2B ubiquitination Source: UniProtKB
    2. histone monoubiquitination Source: UniProtKB
    3. negative regulation of cell migration Source: UniProtKB
    4. positive regulation of histone methylation Source: Ensembl
    5. positive regulation of transcription, DNA-templated Source: UniProtKB
    6. protein polyubiquitination Source: UniProtKB
    7. regulation of transcription, DNA-templated Source: UniProtKB
    8. ubiquitin-dependent protein catabolic process Source: UniProtKB

    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

    Organism-specific databases

    HGNCiHGNC:10062. RNF20.

    Subcellular locationi

    Nucleus 1 Publication

    GO - Cellular componenti

    1. HULC complex Source: UniProtKB
    2. nucleolus Source: UniProtKB
    3. nucleus Source: UniProtKB
    4. ubiquitin ligase complex Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA34427.

    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 – 1361Phosphoserine1 Publication
    Modified residuei138 – 1381Phosphoserine3 Publications
    Modified residuei348 – 3481N6-acetyllysine1 Publication
    Modified residuei522 – 5221Phosphoserine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ5VTR2.
    PaxDbiQ5VTR2.
    PRIDEiQ5VTR2.

    PTM databases

    PhosphoSiteiQ5VTR2.

    Expressioni

    Gene expression databases

    ArrayExpressiQ5VTR2.
    BgeeiQ5VTR2.
    GenevestigatoriQ5VTR2.

    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.4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    COPS5Q929052EBI-2372238,EBI-594661
    HTTP428583EBI-2372238,EBI-466029
    RNF40O7515010EBI-2372238,EBI-744408
    UBE2E1P519652EBI-2372238,EBI-348546

    Protein-protein interaction databases

    BioGridi121119. 52 interactions.
    DIPiDIP-53411N.
    IntActiQ5VTR2. 16 interactions.
    MINTiMINT-3054538.

    Structurei

    3D structure databases

    ProteinModelPortaliQ5VTR2.
    SMRiQ5VTR2. Positions 917-967.
    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 annotations

    Zinc finger

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

    Keywords - Domaini

    Coiled coil, Zinc-finger

    Phylogenomic databases

    eggNOGiNOG263074.
    HOVERGENiHBG080312.
    KOiK10696.
    OMAiHTMSQEF.
    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]
    ProtoNetiSearch...

    Sequencei

    Sequence statusi: Complete.

    Q5VTR2-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSGIGNKRAA GEPGTSMPPE KKAAVEDSGT TVETIKLGGV SSTEELDIRT    50
    LQTKNRKLAE MLDQRQAIED ELREHIEKLE RRQATDDASL LIVNRYWSQF 100
    DENIRIILKR YDLEQGLGDL LTERKALVVP EPEPDSDSNQ ERKDDRERGE 150
    GQEPAFSFLA TLASSSSEEM ESQLQERVES SRRAVSQIVT VYDKLQEKVE 200
    LLSRKLNSGD NLIVEEAVQE LNSFLAQENM RLQELTDLLQ EKHRTMSQEF 250
    SKLQSKVETA ESRVSVLESM IDDLQWDIDK IRKREQRLNR HLAEVLERVN 300
    SKGYKVYGAG SSLYGGTITI NARKFEEMNA ELEENKELAQ NRLCELEKLR 350
    QDFEEVTTQN EKLKVELRSA VEQVVKETPE YRCMQSQFSV LYNESLQLKA 400
    HLDEARTLLH GTRGTHQHQV ELIERDEVSL HKKLRTEVIQ LEDTLAQVRK 450
    EYEMLRIEFE QTLAANEQAG PINREMRHLI SSLQNHNHQL KGEVLRYKRK 500
    LREAQSDLNK TRLRSGSALL QSQSSTEDPK DEPAELKPDS EDLSSQSSAS 550
    KASQEDANEI KSKRDEEERE RERREKERER EREREKEKER EREKQKLKES 600
    EKERDSAKDK EKGKHDDGRK KEAEIIKQLK IELKKAQESQ KEMKLLLDMY 650
    RSAPKEQRDK VQLMAAEKKS KAELEDLRQR LKDLEDKEKK ENKKMADEDA 700
    LRKIRAVEEQ IEYLQKKLAM AKQEEEALLS EMDVTGQAFE DMQEQNIRLM 750
    QQLREKDDAN FKLMSERIKS NQIHKLLKEE KEELADQVLT LKTQVDAQLQ 800
    VVRKLEEKEH LLQSNIGTGE KELGLRTQAL EMNKRKAMEA AQLADDLKAQ 850
    LELAQKKLHD FQDEIVENSV TKEKDMFNFK RAQEDISRLR RKLETTKKPD 900
    NVPKCDEILM EEIKDYKARL TCPCCNMRKK DAVLTKCFHV FCFECVKTRY 950
    DTRQRKCPKC NAAFGANDFH RIYIG 975
    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. 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.

    Sequence conflict

    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. 1 PublicationCurated
    Sequence conflicti322 – 3221A → V in BAB14081. (PubMed:14702039)Curated
    Sequence conflicti668 – 6681K → E in BAB14081. (PubMed:14702039)Curated
    Sequence conflicti693 – 6931K → T in AAK58539. 1 PublicationCurated
    Sequence conflicti699 – 6991D → E in BAB14081. (PubMed:14702039)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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.
    UniGeneiHs.729085.

    Genome annotation databases

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

    Polymorphism databases

    DMDMi84027766.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS35084.1.
    RefSeqi NP_062538.5. NM_019592.6.
    UniGenei Hs.729085.

    3D structure databases

    ProteinModelPortali Q5VTR2.
    SMRi Q5VTR2. Positions 917-967.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 121119. 52 interactions.
    DIPi DIP-53411N.
    IntActi Q5VTR2. 16 interactions.
    MINTi MINT-3054538.

    PTM databases

    PhosphoSitei Q5VTR2.

    Polymorphism databases

    DMDMi 84027766.

    Proteomic databases

    MaxQBi Q5VTR2.
    PaxDbi Q5VTR2.
    PRIDEi Q5VTR2.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000389120 ; ENSP00000373772 ; ENSG00000155827 .
    GeneIDi 56254.
    KEGGi hsa:56254.
    UCSCi uc004bbn.3. human.

    Organism-specific databases

    CTDi 56254.
    GeneCardsi GC09P104296.
    HGNCi HGNC:10062. RNF20.
    HPAi CAB012478.
    HPA051773.
    MIMi 607699. gene.
    neXtProti NX_Q5VTR2.
    PharmGKBi PA34427.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG263074.
    HOVERGENi HBG080312.
    KOi K10696.
    OMAi HTMSQEF.
    OrthoDBi EOG7DVD99.
    PhylomeDBi Q5VTR2.
    TreeFami TF323183.

    Enzyme and pathway databases

    UniPathwayi UPA00143 .

    Miscellaneous databases

    ChiTaRSi RNF20. human.
    GeneWikii RNF20.
    GenomeRNAii 56254.
    NextBioi 61893.
    PROi Q5VTR2.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q5VTR2.
    Bgeei Q5VTR2.
    Genevestigatori Q5VTR2.

    Family and domain databases

    Gene3Di 3.30.40.10. 1 hit.
    InterProi IPR018957. Znf_C3HC4_RING-type.
    IPR001841. Znf_RING.
    IPR013083. Znf_RING/FYVE/PHD.
    IPR017907. Znf_RING_CS.
    [Graphical view ]
    Pfami PF00097. zf-C3HC4. 1 hit.
    [Graphical view ]
    SMARTi SM00184. RING. 1 hit.
    [Graphical view ]
    PROSITEi PS00518. ZF_RING_1. 1 hit.
    PS50089. ZF_RING_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. "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. 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].

    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: October 1, 2014
    This is version 114 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

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