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Q9NXR7

- BRE_HUMAN

UniProt

Q9NXR7 - BRE_HUMAN

Protein

BRCA1-A complex subunit BRE

Gene

BRE

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 103 (01 Oct 2014)
      Sequence version 2 (05 May 2009)
      Previous versions | rss
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    Functioni

    Component of the BRCA1-A complex, a complex that specifically recognizes 'Lys-63'-linked ubiquitinated histones H2A and H2AX at DNA lesions sites, leading to target the BRCA1-BARD1 heterodimer to sites of DNA damage at double-strand breaks (DSBs). The BRCA1-A complex also possesses deubiquitinase activity that specifically removes 'Lys-63'-linked ubiquitin on histones H2A and H2AX. In the BRCA1-A complex, it acts as an adapter that bridges the interaction between BABAM1/NBA1 and the rest of the complex, thereby being required for the complex integrity and modulating the E3 ubiquitin ligase activity of the BRCA1-BARD1 heterodimer. Probably also plays a role as a component of the BRISC complex, a multiprotein complex that specifically cleaves 'Lys-63'-linked ubiquitin. May play a role in homeostasis or cellular differentiation in cells of neural, epithelial and germline origins. May also act as a death receptor-associated anti-apoptotic protein, which inhibits the mitochondrial apoptotic pathway. May regulate TNF-alpha signaling through its interactions with TNFRSF1A; however these effects may be indirect.4 Publications

    GO - Molecular functioni

    1. peroxisome targeting sequence binding Source: UniProtKB
    2. polyubiquitin binding Source: UniProtKB
    3. protein binding Source: UniProtKB
    4. tumor necrosis factor receptor binding Source: UniProtKB

    GO - Biological processi

    1. apoptotic process Source: UniProtKB-KW
    2. cellular response to DNA damage stimulus Source: UniProtKB
    3. chromatin modification Source: UniProtKB-KW
    4. double-strand break repair Source: UniProtKB
    5. G2 DNA damage checkpoint Source: UniProtKB
    6. positive regulation of DNA repair Source: UniProtKB
    7. response to ionizing radiation Source: UniProtKB
    8. signal transduction Source: ProtInc

    Keywords - Molecular functioni

    Chromatin regulator

    Keywords - Biological processi

    Apoptosis, DNA damage, DNA repair

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    BRCA1-A complex subunit BRE
    Alternative name(s):
    BRCA1/BRCA2-containing complex subunit 45
    Brain and reproductive organ-expressed protein
    Gene namesi
    Name:BREImported
    Synonyms:BRCC45
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:1106. BRE.

    Subcellular locationi

    Cytoplasm. Nucleus
    Note: Localizes at sites of DNA damage at double-strand breaks (DSBs).

    GO - Cellular componenti

    1. BRCA1-A complex Source: UniProtKB
    2. BRISC complex Source: UniProtKB
    3. cytoplasm Source: UniProtKB
    4. nuclear ubiquitin ligase complex Source: UniProtKB
    5. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA25419.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 383383BRCA1-A complex subunit BREPRO_0000224189Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine3 Publications
    Modified residuei2 – 21Phosphoserine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ9NXR7.
    PaxDbiQ9NXR7.
    PRIDEiQ9NXR7.

    PTM databases

    PhosphoSiteiQ9NXR7.

    Expressioni

    Tissue specificityi

    Expressed in all cell lines examined. Highly expressed in placenta.1 Publication

    Inductioni

    Down-regulated by DNA-damaging agents in fibroblasts, by retinoic acid in brain glioma U-251MG and promyelocytic HL-60 cell lines, and by bacterial lipopolysaccharides (LPS) in peripheral blood mononuclear cells (PBMC).2 Publications

    Gene expression databases

    ArrayExpressiQ9NXR7.
    BgeeiQ9NXR7.
    CleanExiHS_BRE.
    GenevestigatoriQ9NXR7.

    Organism-specific databases

    HPAiHPA017926.

    Interactioni

    Subunit structurei

    Component of the BRCA1-A complex, at least composed of the BRCA1, BARD1, UIMC1/RAP80, FAM175A/Abraxas, BRCC3/BRCC36, BRE/BRCC45 and BABAM1/NBA1. In the BRCA1-A complex, interacts directly with FAM175A/Abraxas, BRCC3/BRCC36 and BABAM1/NBA1. Binds polyubiquitin. Component of the BRISC complex, at least composed of the FAM175B/ABRO1, BRCC3/BRCC36, BRE/BRCC45 and BABAM1/NBA1. Component of the BRCA1/BRCA2 containing complex (BRCC), which also contains BRCA1, BRCA2, BARD1, BRCC3/BRCC36 and RAD51. BRCC is a ubiquitin E3 ligase complex that enhances cellular survival following DNA damage. May interact with FAS and TNFRSF1A.7 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    BABAM1Q9NWV83EBI-949389,EBI-745725

    Protein-protein interaction databases

    BioGridi114946. 41 interactions.
    IntActiQ9NXR7. 22 interactions.
    MINTiMINT-2867020.
    STRINGi9606.ENSP00000343412.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9NXR7.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni30 – 147118UEV-like 1Add
    BLAST
    Regioni275 – 36490UEV-like 2Add
    BLAST

    Domaini

    Contains 2 ubiquitin-conjugating enzyme family-like (UEV-like) regions. These regions lack the critical Cys residues required for ubiquitination but retain the ability to bind ubiquitin.1 Publication

    Sequence similaritiesi

    Belongs to the BRE family.Sequence Analysis

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG71563.
    HOVERGENiHBG071492.
    InParanoidiQ9NXR7.
    KOiK12173.
    OMAiHIPAFPS.
    PhylomeDBiQ9NXR7.
    TreeFamiTF328507.

    Family and domain databases

    InterProiIPR010358. Brain/reproduct-express_prot.
    [Graphical view]
    PfamiPF06113. BRE. 1 hit.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Note: Additional isoforms may exist.Curated

    Isoform 21 Publication (identifier: Q9NXR7-2) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MSPEVALNRI SPMLSPFISS VVRNGKVGLD ATNCLRITDL KSGCTSLTPG    50
    PNCDRFKLHI PYAGETLKWD IIFNAQYPEL PPDFIFGEDA EFLPDPSALQ 100
    NLASWNPSNP ECLLLVVKEL VQQYHQFQCS RLRESSRLMF EYQTLLEEPQ 150
    YGENMEIYAG KKNNWTGEFS ARFLLKLPVD FSNIPTYLLK DVNEDPGEDV 200
    ALLSVSFEDT EATQVYPKLY LSPRIEHALG GSSALHIPAF PGGGCLIDYV 250
    PQVCHLLTNK VQYVIQGYHK RREYIAAFLS HFGTGVVEYD AEGFTKLTLL 300
    LMWKDFCFLV HIDLPLFFPR DQPTLTFQSV YHFTNSGQLY SQAQKNYPYS 350
    PRWDGNEMAK RAKAYFKTFV PQFQEAAFAN GKL 383
    Length:383
    Mass (Da):43,552
    Last modified:May 5, 2009 - v2
    Checksum:iD830226E2B8F2C4B
    GO
    Isoform 1Curated (identifier: Q9NXR7-1) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         364-383: AYFKTFVPQFQEAAFANGKL → GCQGSRDACSPWEQVLAFAVAKTGCKLLQPQRNWPSSRGPPWRASEGERTAQ

    Show »
    Length:415
    Mass (Da):46,974
    Checksum:i0501C5447AAFB3BA
    GO
    Isoform 31 Publication (identifier: Q9NXR7-3) [UniParc]FASTAAdd to Basket

    Also known as: Alpha a'

    The sequence of this isoform differs from the canonical sequence as follows:
         363-383: KAYFKTFVPQFQEAAFANGKL → NSRRQHLPMESSRKHQS

    Show »
    Length:379
    Mass (Da):43,224
    Checksum:i2A8816CC439FDFB5
    GO
    Isoform 4 (identifier: Q9NXR7-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         364-383: AYFKTFVPQFQEAAFANGKL → RESNRDGEESSSA

    Show »
    Length:376
    Mass (Da):42,697
    Checksum:i56488D883F2A27AE
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti192 – 1921V → L in BAF83775. (PubMed:14702039)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei363 – 38321KAYFK…ANGKL → NSRRQHLPMESSRKHQS in isoform 3. 1 PublicationVSP_051957Add
    BLAST
    Alternative sequencei364 – 38320AYFKT…ANGKL → GCQGSRDACSPWEQVLAFAV AKTGCKLLQPQRNWPSSRGP PWRASEGERTAQ in isoform 1. 1 PublicationVSP_051956Add
    BLAST
    Alternative sequencei364 – 38320AYFKT…ANGKL → RESNRDGEESSSA in isoform 4. 1 PublicationVSP_037261Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L38616 mRNA. Translation: AAA64231.1.
    AF420605 mRNA. Translation: AAL17818.1.
    AY438031 mRNA. Translation: AAR30499.1.
    AF015767 mRNA. Translation: AAB69387.1.
    AF420602 mRNA. Translation: AAL17814.1.
    AF420603 mRNA. Translation: AAL17816.1.
    AK000097 mRNA. Translation: BAA90943.1.
    AK291086 mRNA. Translation: BAF83775.1.
    AC021171 Genomic DNA. Translation: AAY24156.1.
    AC093690 Genomic DNA. No translation available.
    AC096552 Genomic DNA. Translation: AAX88935.1.
    CH471053 Genomic DNA. Translation: EAX00545.1.
    CH471053 Genomic DNA. Translation: EAX00546.1.
    CH471053 Genomic DNA. Translation: EAX00547.1.
    CH471053 Genomic DNA. Translation: EAX00548.1.
    BC001251 mRNA. Translation: AAH01251.1.
    CCDSiCCDS1763.1. [Q9NXR7-2]
    CCDS1764.1. [Q9NXR7-1]
    CCDS1765.1. [Q9NXR7-4]
    PIRiJC2472.
    RefSeqiNP_001248769.1. NM_001261840.1. [Q9NXR7-3]
    NP_004890.2. NM_004899.4. [Q9NXR7-1]
    NP_954661.1. NM_199191.2. [Q9NXR7-2]
    NP_954662.1. NM_199192.2. [Q9NXR7-4]
    NP_954663.1. NM_199193.2. [Q9NXR7-4]
    NP_954664.1. NM_199194.2. [Q9NXR7-2]
    UniGeneiHs.258314.

    Genome annotation databases

    EnsembliENST00000342045; ENSP00000339371; ENSG00000158019. [Q9NXR7-2]
    ENST00000344773; ENSP00000343412; ENSG00000158019. [Q9NXR7-1]
    ENST00000361704; ENSP00000354699; ENSG00000158019. [Q9NXR7-4]
    ENST00000379624; ENSP00000368945; ENSG00000158019. [Q9NXR7-2]
    ENST00000379632; ENSP00000368953; ENSG00000158019. [Q9NXR7-4]
    GeneIDi9577.
    KEGGihsa:9577.
    UCSCiuc002rlp.2. human. [Q9NXR7-3]
    uc002rlq.3. human. [Q9NXR7-4]
    uc002rlr.3. human. [Q9NXR7-2]
    uc002rls.3. human. [Q9NXR7-1]

    Polymorphism databases

    DMDMi229462810.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L38616 mRNA. Translation: AAA64231.1 .
    AF420605 mRNA. Translation: AAL17818.1 .
    AY438031 mRNA. Translation: AAR30499.1 .
    AF015767 mRNA. Translation: AAB69387.1 .
    AF420602 mRNA. Translation: AAL17814.1 .
    AF420603 mRNA. Translation: AAL17816.1 .
    AK000097 mRNA. Translation: BAA90943.1 .
    AK291086 mRNA. Translation: BAF83775.1 .
    AC021171 Genomic DNA. Translation: AAY24156.1 .
    AC093690 Genomic DNA. No translation available.
    AC096552 Genomic DNA. Translation: AAX88935.1 .
    CH471053 Genomic DNA. Translation: EAX00545.1 .
    CH471053 Genomic DNA. Translation: EAX00546.1 .
    CH471053 Genomic DNA. Translation: EAX00547.1 .
    CH471053 Genomic DNA. Translation: EAX00548.1 .
    BC001251 mRNA. Translation: AAH01251.1 .
    CCDSi CCDS1763.1. [Q9NXR7-2 ]
    CCDS1764.1. [Q9NXR7-1 ]
    CCDS1765.1. [Q9NXR7-4 ]
    PIRi JC2472.
    RefSeqi NP_001248769.1. NM_001261840.1. [Q9NXR7-3 ]
    NP_004890.2. NM_004899.4. [Q9NXR7-1 ]
    NP_954661.1. NM_199191.2. [Q9NXR7-2 ]
    NP_954662.1. NM_199192.2. [Q9NXR7-4 ]
    NP_954663.1. NM_199193.2. [Q9NXR7-4 ]
    NP_954664.1. NM_199194.2. [Q9NXR7-2 ]
    UniGenei Hs.258314.

    3D structure databases

    ProteinModelPortali Q9NXR7.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114946. 41 interactions.
    IntActi Q9NXR7. 22 interactions.
    MINTi MINT-2867020.
    STRINGi 9606.ENSP00000343412.

    PTM databases

    PhosphoSitei Q9NXR7.

    Polymorphism databases

    DMDMi 229462810.

    Proteomic databases

    MaxQBi Q9NXR7.
    PaxDbi Q9NXR7.
    PRIDEi Q9NXR7.

    Protocols and materials databases

    DNASUi 9577.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000342045 ; ENSP00000339371 ; ENSG00000158019 . [Q9NXR7-2 ]
    ENST00000344773 ; ENSP00000343412 ; ENSG00000158019 . [Q9NXR7-1 ]
    ENST00000361704 ; ENSP00000354699 ; ENSG00000158019 . [Q9NXR7-4 ]
    ENST00000379624 ; ENSP00000368945 ; ENSG00000158019 . [Q9NXR7-2 ]
    ENST00000379632 ; ENSP00000368953 ; ENSG00000158019 . [Q9NXR7-4 ]
    GeneIDi 9577.
    KEGGi hsa:9577.
    UCSCi uc002rlp.2. human. [Q9NXR7-3 ]
    uc002rlq.3. human. [Q9NXR7-4 ]
    uc002rlr.3. human. [Q9NXR7-2 ]
    uc002rls.3. human. [Q9NXR7-1 ]

    Organism-specific databases

    CTDi 9577.
    GeneCardsi GC02P028025.
    HGNCi HGNC:1106. BRE.
    HPAi HPA017926.
    MIMi 610497. gene.
    neXtProti NX_Q9NXR7.
    PharmGKBi PA25419.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG71563.
    HOVERGENi HBG071492.
    InParanoidi Q9NXR7.
    KOi K12173.
    OMAi HIPAFPS.
    PhylomeDBi Q9NXR7.
    TreeFami TF328507.

    Miscellaneous databases

    ChiTaRSi BRE. human.
    GeneWikii BRE_(gene).
    GenomeRNAii 9577.
    NextBioi 35917.
    PROi Q9NXR7.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9NXR7.
    Bgeei Q9NXR7.
    CleanExi HS_BRE.
    Genevestigatori Q9NXR7.

    Family and domain databases

    InterProi IPR010358. Brain/reproduct-express_prot.
    [Graphical view ]
    Pfami PF06113. BRE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Identification of a brain- and reproductive-organs-specific gene responsive to DNA damage and retinoic acid."
      Li L., Yoo H., Becker F.F., Ali-Osman F., Chan J.Y.-H.
      Biochem. Biophys. Res. Commun. 206:764-774(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), INDUCTION.
    2. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 4), TISSUE SPECIFICITY, INDUCTION.
      Tissue: Monocyte1 Publication.
    3. "Regulation of BRCC, a holoenzyme complex containing BRCA1 and BRCA2, by a signalosome-like subunit and its role in DNA repair."
      Dong Y., Hakimi M.-A., Chen X., Kumaraswamy E., Cooch N.S., Godwin A.K., Shiekhattar R.
      Mol. Cell 12:1087-1099(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, IDENTIFICATION IN BRCC COMPLEX.
    4. Keeton K.R., Miles W.M.
      Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    5. "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] (ISOFORM 1).
      Tissue: ColonImported and Teratocarcinoma.
    6. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "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] (ISOFORM 2).
      Tissue: CervixImported.
    9. "A death receptor-associated anti-apoptotic protein, BRE, inhibits mitochondrial apoptotic pathway."
      Li Q., Ching A.K.-K., Chan B.C.-L., Chow S.K.-Y., Lim P.-L., Ho T.C.-Y., Ip W.-K., Wong C.-K., Lam C.W.-K., Lee K.K.-H., Chan J.Y.-H., Chui Y.-L.
      J. Biol. Chem. 279:52106-52116(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH FAS AND TNFRSF1A, SUBCELLULAR LOCATION.
    10. "RAP80 targets BRCA1 to specific ubiquitin structures at DNA damage sites."
      Sobhian B., Shao G., Lilli D.R., Culhane A.C., Moreau L.A., Xia B., Livingston D.M., Greenberg R.A.
      Science 316:1198-1202(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE BRCA1-A COMPLEX.
    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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "K63-specific deubiquitination by two JAMM/MPN+ complexes: BRISC-associated Brcc36 and proteasomal Poh1."
      Cooper E.M., Cutcliffe C., Kristiansen T.Z., Pandey A., Pickart C.M., Cohen R.E.
      EMBO J. 28:621-631(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE BRISC COMPLEX.
    13. "MERIT40 controls BRCA1-Rap80 complex integrity and recruitment to DNA double-strand breaks."
      Shao G., Patterson-Fortin J., Messick T.E., Feng D., Shanbhag N., Wang Y., Greenberg R.A.
      Genes Dev. 23:740-754(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE BRCA1-A COMPLEX.
    14. "NBA1, a new player in the Brca1 A complex, is required for DNA damage resistance and checkpoint control."
      Wang B., Hurov K., Hofmann K., Elledge S.J.
      Genes Dev. 23:729-739(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, IDENTIFICATION IN THE BRCA1-A COMPLEX, DOMAIN UEV-LIKE, UBIQUITIN-BINDING, INTERACTION WITH FAM175A.
    15. "MERIT40 facilitates BRCA1 localization and DNA damage repair."
      Feng L., Huang J., Chen J.
      Genes Dev. 23:719-728(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE BRCA1-A COMPLEX, SUBCELLULAR LOCATION, INTERACTION WITH FAM175A; BABAM1 AND BRCC3.
    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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiBRE_HUMAN
    AccessioniPrimary (citable) accession number: Q9NXR7
    Secondary accession number(s): A8K4X1
    , D6W562, D6W563, Q13880, Q4ZFX8, Q53SD0, Q969X9, Q96P06
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 21, 2006
    Last sequence update: May 5, 2009
    Last modified: October 1, 2014
    This is version 103 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 2
      Human chromosome 2: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3