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Q9NWV8

- BABA1_HUMAN

UniProt

Q9NWV8 - BABA1_HUMAN

Protein

BRISC and BRCA1-A complex member 1

Gene

BABAM1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 98 (01 Oct 2014)
      Sequence version 1 (01 Oct 2000)
      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 is required for the complex integrity and its localization at DSBs. Probably also plays a role as a component of the BRISC complex, a multiprotein complex that specifically cleaves 'Lys-63'-linked ubiquitin. In these 2 complexes, it is probably required to maintain the stability of BRE/BRCC45 and help the 'Lys-63'-linked deubiquitinase activity mediated by BRCC3/BRCC36 component.3 Publications

    GO - Molecular functioni

    1. protein binding Source: UniProtKB

    GO - Biological processi

    1. chromatin modification Source: UniProtKB-KW
    2. double-strand break repair Source: UniProtKB
    3. G2 DNA damage checkpoint Source: UniProtKB
    4. positive regulation of DNA repair Source: UniProtKB
    5. protein K63-linked deubiquitination Source: UniProtKB
    6. response to ionizing radiation Source: UniProtKB

    Keywords - Molecular functioni

    Chromatin regulator

    Keywords - Biological processi

    DNA damage, DNA repair

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    BRISC and BRCA1-A complex member 1
    Alternative name(s):
    Mediator of RAP80 interactions and targeting subunit of 40 kDa
    New component of the BRCA1-A complex
    Gene namesi
    Name:BABAM1
    Synonyms:C19orf62, MERIT40, NBA1
    ORF Names:HSPC142
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:25008. BABAM1.

    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. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA162378767.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 329329BRISC and BRCA1-A complex member 1PRO_0000288458Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine3 Publications
    Modified residuei29 – 291Phosphoserine1 Publication
    Modified residuei49 – 491Phosphoserine3 Publications
    Modified residuei62 – 621Phosphoserine1 Publication
    Modified residuei65 – 651Phosphothreonine1 Publication
    Modified residuei66 – 661Phosphoserine2 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ9NWV8.
    PaxDbiQ9NWV8.
    PRIDEiQ9NWV8.

    PTM databases

    PhosphoSiteiQ9NWV8.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9NWV8.
    BgeeiQ9NWV8.
    CleanExiHS_C19orf62.
    GenevestigatoriQ9NWV8.

    Organism-specific databases

    HPAiHPA054386.

    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 and BRE/BRCC45. Component of the BRISC complex, at least composed of the FAM175B/ABRO1, BRCC3/BRCC36, BRE/BRCC45 and BABAM1/NBA1.4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    BREQ9NXR73EBI-745725,EBI-949389
    TNKS2Q9H2K24EBI-745725,EBI-4398527

    Protein-protein interaction databases

    BioGridi118855. 53 interactions.
    IntActiQ9NWV8. 73 interactions.
    MINTiMINT-4712566.
    STRINGi9606.ENSP00000352408.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9NWV8.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni95 – 298204VWFA-likeAdd
    BLAST

    Domaini

    The VWFA-like region is similar to the VWFA domain. Its presence reveals similarities between the structure of the 19S proteasome and the BRCA1-A complexes.1 Publication

    Sequence similaritiesi

    Belongs to the BABAM1 family.Curated

    Phylogenomic databases

    eggNOGiNOG76997.
    OMAiSCSTFNI.
    OrthoDBiEOG7VB2FR.
    PhylomeDBiQ9NWV8.
    TreeFamiTF329070.

    Family and domain databases

    InterProiIPR026126. BABAM1.
    IPR002035. VWF_A.
    [Graphical view]
    PANTHERiPTHR15660. PTHR15660. 1 hit.
    SUPFAMiSSF53300. SSF53300. 1 hit.

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9NWV8-1) [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

    MEVAEPSSPT EEEEEEEEHS AEPRPRTRSN PEGAEDRAVG AQASVGSRSE    50
    GEGEAASADD GSLNTSGAGP KSWQVPPPAP EVQIRTPRVN CPEKVIICLD 100
    LSEEMSLPKL ESFNGSKTNA LNVSQKMIEM FVRTKHKIDK SHEFALVVVN 150
    DDTAWLSGLT SDPRELCSCL YDLETASCST FNLEGLFSLI QQKTELPVTE 200
    NVQTIPPPYV VRTILVYSRP PCQPQFSLTE PMKKMFQCPY FFFDVVYIHN 250
    GTEEKEEEMS WKDMFAFMGS LDTKGTSYKY EVALAGPALE LHNCMAKLLA 300
    HPLQRPCQSH ASYSLLEEED EAIEVEATV 329
    Length:329
    Mass (Da):36,560
    Last modified:October 1, 2000 - v1
    Checksum:i7A84D8EE6D03C1DB
    GO
    Isoform 2 (identifier: Q9NWV8-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-115: MEVAEPSSPT...SLPKLESFNG → MMGASTLQEP...HHGSTVQRKC
         263-329: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:184
    Mass (Da):21,028
    Checksum:iFC1769F1757DAC76
    GO
    Isoform 3 (identifier: Q9NWV8-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         116-190: Missing.
         234-329: KMFQCPYFFF...DEAIEVEATV → VGEAWEREGCLQP

    Note: No experimental confirmation available.

    Show »
    Length:171
    Mass (Da):18,621
    Checksum:i1848B7FE13066DF1
    GO

    Sequence cautioni

    The sequence AAF29106.1 differs from that shown. Reason: Frameshift at position 263.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti76 – 761P → S in CAG38557. 1 PublicationCurated
    Sequence conflicti288 – 2881A → V in CAG38557. 1 PublicationCurated
    Sequence conflicti302 – 3021P → S in CAG38557. 1 PublicationCurated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 115115MEVAE…ESFNG → MMGASTLQEPALSPGRCPRQ PLRSKFGHHGSTVQRKC in isoform 2. 1 PublicationVSP_037246Add
    BLAST
    Alternative sequencei116 – 19075Missing in isoform 3. 1 PublicationVSP_037247Add
    BLAST
    Alternative sequencei234 – 32996KMFQC…VEATV → VGEAWEREGCLQP in isoform 3. 1 PublicationVSP_037248Add
    BLAST
    Alternative sequencei263 – 32967Missing in isoform 2. 1 PublicationVSP_037249Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF161491 mRNA. Translation: AAF29106.1. Frameshift.
    AL136692 mRNA. Translation: CAB66627.1.
    AK000578 mRNA. Translation: BAA91268.1.
    AK299493 mRNA. Translation: BAG61451.1.
    AK301193 mRNA. Translation: BAG62773.1.
    CR533526 mRNA. Translation: CAG38557.1.
    AC104522 Genomic DNA. No translation available.
    BC000788 mRNA. Translation: AAH00788.1.
    BC006244 mRNA. Translation: AAH06244.1.
    BC091491 mRNA. Translation: AAH91491.1.
    CCDSiCCDS46012.1. [Q9NWV8-1]
    RefSeqiNP_001028721.1. NM_001033549.2. [Q9NWV8-1]
    NP_001275685.1. NM_001288756.1. [Q9NWV8-1]
    NP_001275686.1. NM_001288757.1.
    NP_054892.2. NM_014173.3. [Q9NWV8-1]
    UniGeneiHs.190722.

    Genome annotation databases

    EnsembliENST00000359435; ENSP00000352408; ENSG00000105393. [Q9NWV8-1]
    ENST00000598188; ENSP00000471605; ENSG00000105393. [Q9NWV8-1]
    ENST00000601043; ENSP00000470920; ENSG00000105393. [Q9NWV8-1]
    GeneIDi29086.
    KEGGihsa:29086.
    UCSCiuc002nfu.3. human. [Q9NWV8-1]
    uc010xpl.1. human. [Q9NWV8-3]

    Polymorphism databases

    DMDMi74734678.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF161491 mRNA. Translation: AAF29106.1 . Frameshift.
    AL136692 mRNA. Translation: CAB66627.1 .
    AK000578 mRNA. Translation: BAA91268.1 .
    AK299493 mRNA. Translation: BAG61451.1 .
    AK301193 mRNA. Translation: BAG62773.1 .
    CR533526 mRNA. Translation: CAG38557.1 .
    AC104522 Genomic DNA. No translation available.
    BC000788 mRNA. Translation: AAH00788.1 .
    BC006244 mRNA. Translation: AAH06244.1 .
    BC091491 mRNA. Translation: AAH91491.1 .
    CCDSi CCDS46012.1. [Q9NWV8-1 ]
    RefSeqi NP_001028721.1. NM_001033549.2. [Q9NWV8-1 ]
    NP_001275685.1. NM_001288756.1. [Q9NWV8-1 ]
    NP_001275686.1. NM_001288757.1.
    NP_054892.2. NM_014173.3. [Q9NWV8-1 ]
    UniGenei Hs.190722.

    3D structure databases

    ProteinModelPortali Q9NWV8.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 118855. 53 interactions.
    IntActi Q9NWV8. 73 interactions.
    MINTi MINT-4712566.
    STRINGi 9606.ENSP00000352408.

    PTM databases

    PhosphoSitei Q9NWV8.

    Polymorphism databases

    DMDMi 74734678.

    Proteomic databases

    MaxQBi Q9NWV8.
    PaxDbi Q9NWV8.
    PRIDEi Q9NWV8.

    Protocols and materials databases

    DNASUi 29086.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000359435 ; ENSP00000352408 ; ENSG00000105393 . [Q9NWV8-1 ]
    ENST00000598188 ; ENSP00000471605 ; ENSG00000105393 . [Q9NWV8-1 ]
    ENST00000601043 ; ENSP00000470920 ; ENSG00000105393 . [Q9NWV8-1 ]
    GeneIDi 29086.
    KEGGi hsa:29086.
    UCSCi uc002nfu.3. human. [Q9NWV8-1 ]
    uc010xpl.1. human. [Q9NWV8-3 ]

    Organism-specific databases

    CTDi 29086.
    GeneCardsi GC19P017456.
    H-InvDB HIX0014885.
    HGNCi HGNC:25008. BABAM1.
    HPAi HPA054386.
    MIMi 612766. gene.
    neXtProti NX_Q9NWV8.
    PharmGKBi PA162378767.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG76997.
    OMAi SCSTFNI.
    OrthoDBi EOG7VB2FR.
    PhylomeDBi Q9NWV8.
    TreeFami TF329070.

    Miscellaneous databases

    ChiTaRSi BABAM1. human.
    GeneWikii C19orf62.
    GenomeRNAii 29086.
    NextBioi 52072.
    PROi Q9NWV8.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9NWV8.
    Bgeei Q9NWV8.
    CleanExi HS_C19orf62.
    Genevestigatori Q9NWV8.

    Family and domain databases

    InterProi IPR026126. BABAM1.
    IPR002035. VWF_A.
    [Graphical view ]
    PANTHERi PTHR15660. PTHR15660. 1 hit.
    SUPFAMi SSF53300. SSF53300. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells."
      Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., Tao J., Huang Q.-H., Zhou J., Hu G.-X.
      , Gu J., Chen S.-J., Chen Z.
      Genome Res. 10:1546-1560(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Umbilical cord blood.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Brain.
    3. "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] (ISOFORMS 1; 2 AND 3).
      Tissue: Brain and Spleen.
    4. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    5. "The DNA sequence and biology of human chromosome 19."
      Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
      , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
      Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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 1).
      Tissue: Ovary, Pituitary and Placenta.
    7. "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.
    8. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-62, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49 AND SER-66, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. "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].
    11. "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.
    12. "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: FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE BRCA1-A COMPLEX, SUBCELLULAR LOCATION.
    13. "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, SUBCELLULAR LOCATION, DOMAIN VWFA-LIKE, INTERACTION WITH FAM175A.
    14. "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 BRE.
    15. "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-29; SER-49; THR-65 AND SER-66, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiBABA1_HUMAN
    AccessioniPrimary (citable) accession number: Q9NWV8
    Secondary accession number(s): A8MQT0
    , B4DRY9, B4DVR1, Q6FIA0, Q9P018
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 29, 2007
    Last sequence update: October 1, 2000
    Last modified: October 1, 2014
    This is version 98 of the entry and version 1 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 19
      Human chromosome 19: 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