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Q99708

- COM1_HUMAN

UniProt

Q99708 - COM1_HUMAN

Protein

DNA endonuclease RBBP8

Gene

RBBP8

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 134 (01 Oct 2014)
      Sequence version 2 (17 Oct 2006)
      Previous versions | rss
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    Functioni

    Endonuclease that cooperates with the MRE11-RAD50-NBN (MRN) complex in processing meiotic and mitotic double-strand breaks (DSBs) by ensuring both resection and intrachromosomal association of the broken ends. Functions downstream of the MRN complex and ATM, promotes ATR activation and its recruitment to DSBs in the S/G2 phase facilitating the generation of ssDNA. Component of the BRCA1-RBBP8 complex that regulates CHEK1 activation and controls cell cycle G2/M checkpoints on DNA damage. Promotes microhomology-mediated alternative end joining (A-NHEJ) during class-switch recombination and plays an essential role in chromosomal translocations.10 Publications

    GO - Molecular functioni

    1. damaged DNA binding Source: UniProtKB
    2. protein binding Source: UniProtKB
    3. RNA polymerase II repressing transcription factor binding Source: BHF-UCL
    4. RNA polymerase II transcription corepressor activity Source: BHF-UCL
    5. single-stranded DNA endodeoxyribonuclease activity Source: UniProtKB

    GO - Biological processi

    1. blastocyst hatching Source: Ensembl
    2. cell cycle checkpoint Source: ProtInc
    3. DNA catabolic process, endonucleolytic Source: GOC
    4. DNA double-strand break processing involved in repair via single-strand annealing Source: UniProtKB
    5. DNA repair Source: ProtInc
    6. double-strand break repair via homologous recombination Source: UniProtKB
    7. G1/S transition of mitotic cell cycle Source: Ensembl
    8. G2 DNA damage checkpoint Source: UniProtKB
    9. meiotic nuclear division Source: UniProtKB-KW
    10. mitotic nuclear division Source: UniProtKB-KW
    11. negative regulation of transcription from RNA polymerase II promoter Source: GOC
    12. regulation of transcription from RNA polymerase II promoter Source: ProtInc

    Keywords - Molecular functioni

    Endonuclease, Hydrolase, Nuclease

    Keywords - Biological processi

    Cell cycle, Cell division, DNA damage, DNA repair, Meiosis, Mitosis

    Keywords - Ligandi

    DNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_27271. Meiotic recombination.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    DNA endonuclease RBBP8 (EC:3.1.-.-)
    Alternative name(s):
    CtBP-interacting protein
    Short name:
    CtIP
    Retinoblastoma-binding protein 8
    Short name:
    RBBP-8
    Retinoblastoma-interacting protein and myosin-like
    Short name:
    RIM
    Sporulation in the absence of SPO11 protein 2 homolog
    Short name:
    SAE2
    Gene namesi
    Name:RBBP8
    Synonyms:CTIP
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 18

    Organism-specific databases

    HGNCiHGNC:9891. RBBP8.

    Subcellular locationi

    Nucleus 2 Publications
    Note: Associates with sites of DNA damage in S/G2 phase. Ubiquitinated RBBP8 binds to chromatin following DNA damage.

    GO - Cellular componenti

    1. nucleolus Source: HPA
    2. nucleus Source: HPA
    3. transcriptional repressor complex Source: BHF-UCL

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Seckel syndrome 2 (SCKL2) [MIM:606744]: A rare autosomal recessive disorder characterized by proportionate dwarfism of prenatal onset associated with low birth weight, growth retardation, severe microcephaly with a bird-headed like appearance, and mental retardation.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Jawad syndrome (JWDS) [MIM:251255]: A syndrome characterized by congenital microcephaly, moderately severe mental retardation, and symmetrical digital anomalies. Digital malformations of variable degree include hallux valgus, syndactyly of toes 4 and 5, short fifth fingers, single flexion crease of fifth fingers, polydactyly and synpolydactyly.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Genetic variability in RBBP8 is noted as a factor in BRCA1-associated breast cancer risk. Exhibits sensitivity to tamoxifen in certain breast cancer cell lines.

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi31 – 311H → A: No effect on RPA focus formation on DNA damage. 1 Publication
    Mutagenesisi35 – 351V → A: No effect on RPA focus formation on DNA damage. 1 Publication
    Mutagenesisi41 – 411K → A: No effect on RPA focus formation on DNA damage. 1 Publication
    Mutagenesisi45 – 451L → A: No effect on RPA focus formation on DNA damage. 1 Publication
    Mutagenesisi327 – 3271S → A: Abolishes BRCA1 interaction and ubiquitination. No activation of CHEK1 after DNA damage. 2 Publications
    Mutagenesisi432 – 4321K → R: Greatly reduced acetylation. Alleviates resection defects caused by depletion of SIRT6; when associated with R-526 and R-604. 1 Publication
    Mutagenesisi513 – 5131K → A: Abolishes damage recruitment capability. 1 Publication
    Mutagenesisi515 – 5151K → A: Abolishes damage recruitment capability. 1 Publication
    Mutagenesisi526 – 5261K → R: Greatly reduced acetylation. Alleviates resection defects caused by depletion of SIRT6; when associated with R-432 and R-604. 1 Publication
    Mutagenesisi604 – 6041K → R: Greatly reduced acetylation. Alleviates resection defects caused by depletion of SIRT6; when associated with R-432 and R-526. 1 Publication
    Mutagenesisi664 – 6641S → A: Abrogates dissociation of BRCA1. 1 Publication
    Mutagenesisi745 – 7451S → A: Abrogates dissociation of BRCA1. 1 Publication
    Mutagenesisi847 – 8471T → A: Impairs DNA resection. 1 Publication
    Mutagenesisi847 – 8471T → E: Mimics constitutive phosphorylation. 1 Publication

    Keywords - Diseasei

    Dwarfism, Mental retardation

    Organism-specific databases

    MIMi251255. phenotype.
    606744. phenotype.
    Orphaneti313795. Jawad syndrome.
    808. Seckel syndrome.
    PharmGKBiPA34255.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 897897DNA endonuclease RBBP8PRO_0000097179Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei326 – 3261Phosphoserine1 Publication
    Modified residuei327 – 3271Phosphoserine2 Publications
    Modified residuei349 – 3491Phosphoserine1 Publication
    Modified residuei432 – 4321N6-acetyllysine1 Publication
    Modified residuei526 – 5261N6-acetyllysine1 Publication
    Modified residuei604 – 6041N6-acetyllysine1 Publication
    Modified residuei664 – 6641Phosphoserine; by ATM2 Publications
    Modified residuei679 – 6791Phosphoserine1 Publication
    Modified residuei723 – 7231Phosphoserine2 Publications
    Modified residuei745 – 7451Phosphoserine; by ATM2 Publications
    Modified residuei847 – 8471Phosphothreonine; by CDK12 Publications

    Post-translational modificationi

    Acetylated. Deacetylation by SIRT6 upon DNA damage promotes DNA end resection.1 Publication
    Hyperphosphorylation upon ionizing radiation results in dissociation from BRCA1. Phosphorylation at Thr-847 by CDK1 is essential for the recruitment to DNA and the DNA repair function. Phosphorylated on Ser-327 as cells enter G2 phase. This phosphorylation is required for binding BRCA1 and for the G2/M DNA damage transition checkpoint control.5 Publications
    Ubiquitinated. Ubiquitination at multiple sites by BRCA1 (via its N-terminal RING domain) does not lead to its proteosomal degradation but instead the ubiquitinated RBBP8 binds to chromatin following DNA damage and may play a role in G2/M checkpoint control.2 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ99708.
    PaxDbiQ99708.
    PRIDEiQ99708.

    PTM databases

    PhosphoSiteiQ99708.

    Expressioni

    Inductioni

    Levels increase dramatically as dividing cells traverse the G1/S boubdary. Down-regulated in tamoxifen-resistant breast cancer cells.

    Gene expression databases

    ArrayExpressiQ99708.
    BgeeiQ99708.
    CleanExiHS_RBBP8.
    GenevestigatoriQ99708.

    Organism-specific databases

    HPAiHPA039890.
    HPA052946.

    Interactioni

    Subunit structurei

    Homodimer; dimerizes via the coiled coil domain. Interacts (via the PXDLS motif) with CTBP1; the interaction is disrupted via binding of the adenovirus E1A to CTBP1. Component of the BRCA1-RBBBP8 complex. Interacts (the Ser-327 phosphorylated form) with BRCA1 (via the C-terminal BRCA1 domains): the interaction occurs in the G2 phase, ubiquitinates RBBP8 and involves RBBP8 in BRCA1-dependent G2/M checkpoint control on DNA damage. Interacts with RB1. Interacts with the MRN complex. Interacts directly with MRE11A; the interaction is required for efficient homologous recombination (HR) and regulation of the MRN complex. Interacts directly with RAD50. Interacts directly with NBN. Interacts with SIRT6; the interaction deacetylates RBBP8 upon DNA damage. Interacts with LM04 (via the LIM zinc-binding 1 domain).11 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    BRCA1P383989EBI-745715,EBI-349905
    EXO1Q9UQ843EBI-745715,EBI-944667

    Protein-protein interaction databases

    BioGridi111867. 38 interactions.
    DIPiDIP-24244N.
    IntActiQ99708. 25 interactions.
    MINTiMINT-102295.
    STRINGi9606.ENSP00000323050.

    Structurei

    Secondary structure

    1
    897
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi648 – 6503
    Helixi651 – 6533
    Turni662 – 6665
    Beta strandi677 – 6793

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2L4ZNMR-A641-685[»]
    ProteinModelPortaliQ99708.
    SMRiQ99708. Positions 641-677.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ99708.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni22 – 4524Essential for binding to the MRN complex and for RPA focus formation on DNA damageAdd
    BLAST
    Regioni509 – 55749Damage-recruitment motifAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili28 – 157130Sequence AnalysisAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi490 – 4945PXDLS motif

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi750 – 7534Poly-Glu

    Domaini

    The PXDLS motif binds to a cleft in CtBP proteins.
    The damage-recruitment motif is required for DNA binding and translocation to sites of DNA damage.

    Sequence similaritiesi

    Belongs to the COM1/SAE2/CtIP family.Curated

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiNOG145529.
    HOGENOMiHOG000293331.
    HOVERGENiHBG057046.
    OrthoDBiEOG771274.
    PhylomeDBiQ99708.
    TreeFamiTF106469.

    Family and domain databases

    InterProiIPR019518. CtIP_N.
    IPR013882. DNA-repair_Sae2/CtIP.
    [Graphical view]
    PfamiPF10482. CtIP_N. 1 hit.
    PF08573. SAE2. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q99708-1) [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

    MNISGSSCGS PNSADTSSDF KDLWTKLKEC HDREVQGLQV KVTKLKQERI    50
    LDAQRLEEFF TKNQQLREQQ KVLHETIKVL EDRLRAGLCD RCAVTEEHMR 100
    KKQQEFENIR QQNLKLITEL MNERNTLQEE NKKLSEQLQQ KIENDQQHQA 150
    AELECEEDVI PDSPITAFSF SGVNRLRRKE NPHVRYIEQT HTKLEHSVCA 200
    NEMRKVSKSS THPQHNPNEN EILVADTYDQ SQSPMAKAHG TSSYTPDKSS 250
    FNLATVVAET LGLGVQEESE TQGPMSPLGD ELYHCLEGNH KKQPFEESTR 300
    NTEDSLRFSD STSKTPPQEE LPTRVSSPVF GATSSIKSGL DLNTSLSPSL 350
    LQPGKKKHLK TLPFSNTCIS RLEKTRSKSE DSALFTHHSL GSEVNKIIIQ 400
    SSNKQILINK NISESLGEQN RTEYGKDSNT DKHLEPLKSL GGRTSKRKKT 450
    EEESEHEVSC PQASFDKENA FPFPMDNQFS MNGDCVMDKP LDLSDRFSAI 500
    QRQEKSQGSE TSKNKFRQVT LYEALKTIPK GFSSSRKASD GNCTLPKDSP 550
    GEPCSQECII LQPLNKCSPD NKPSLQIKEE NAVFKIPLRP RESLETENVL 600
    DDIKSAGSHE PIKIQTRSDH GGCELASVLQ LNPCRTGKIK SLQNNQDVSF 650
    ENIQWSIDPG ADLSQYKMDV TVIDTKDGSQ SKLGGETVDM DCTLVSETVL 700
    LKMKKQEQKG EKSSNEERKM NDSLEDMFDR TTHEEYESCL ADSFSQAADE 750
    EEELSTATKK LHTHGDKQDK VKQKAFVEPY FKGDERETSL QNFPHIEVVR 800
    KKEERRKLLG HTCKECEIYY ADMPAEEREK KLASCSRHRF RYIPPNTPEN 850
    FWEVGFPSTQ TCMERGYIKE DLDPCPRPKR RQPYNAIFSP KGKEQKT 897
    Length:897
    Mass (Da):101,942
    Last modified:October 17, 2006 - v2
    Checksum:iE028DE56DE55C0F2
    GO
    Isoform 2 (identifier: Q99708-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         714-714: S → SMLFYI

    Show »
    Length:902
    Mass (Da):102,610
    Checksum:i43DEA11A0349322B
    GO
    Isoform 3 (identifier: Q99708-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         786-867: RETSLQNFPH...STQTCMERGY → SIMQICQQKK...QKARSRRHRR
         868-897: Missing.

    Note: No experimental confirmation available.Curated

    Show »
    Length:867
    Mass (Da):98,434
    Checksum:iA8CFDB72587619E3
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti4 – 41S → L in AAC14371. (PubMed:9721205)Curated
    Sequence conflicti74 – 741H → Q in BX648221. (PubMed:17974005)Curated
    Sequence conflicti92 – 921C → Y in BAF85170. (PubMed:14702039)Curated
    Sequence conflicti123 – 1231E → G in BAF85170. (PubMed:14702039)Curated
    Sequence conflicti341 – 3411D → G in BX648221. (PubMed:17974005)Curated
    Sequence conflicti515 – 5151K → R in BX648221. (PubMed:17974005)Curated
    Sequence conflicti521 – 5211L → P in BAF85170. (PubMed:14702039)Curated
    Sequence conflicti642 – 6421L → P in BX648221. (PubMed:17974005)Curated
    Isoform 3 (identifier: Q99708-3)
    Sequence conflicti862 – 8621S → G in BX648221. (PubMed:17974005)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti357 – 3571K → N.
    Corresponds to variant rs34678569 [ dbSNP | Ensembl ].
    VAR_051308
    Natural varianti387 – 3871H → Y.
    Corresponds to variant rs1804732 [ dbSNP | Ensembl ].
    VAR_028308

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei714 – 7141S → SMLFYI in isoform 2. 1 PublicationVSP_043220
    Alternative sequencei786 – 86782RETSL…MERGY → SIMQICQQKKEKRNWLPAQD TDSATFHPTHQRIFGKLVFL PLRLVWKEVILRKILILVLV QKDVSLTTQYFLQKARSRRH RR in isoform 3. 1 PublicationVSP_045247Add
    BLAST
    Alternative sequencei868 – 89730Missing in isoform 3. 1 PublicationVSP_045248Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF043431 mRNA. Translation: AAC34368.1.
    U72066 mRNA. Translation: AAC14371.1.
    AK292481 mRNA. Translation: BAF85170.1.
    BX648221 mRNA. No translation available.
    AC091147 Genomic DNA. No translation available.
    AC106033 Genomic DNA. No translation available.
    CH471088 Genomic DNA. Translation: EAX01144.1.
    BC030590 mRNA. Translation: AAH30590.1.
    CCDSiCCDS11874.1. [Q99708-3]
    CCDS11875.1. [Q99708-1]
    RefSeqiNP_002885.1. NM_002894.2. [Q99708-1]
    NP_976036.1. NM_203291.1. [Q99708-1]
    NP_976037.1. NM_203292.1. [Q99708-3]
    XP_006722582.1. XM_006722519.1. [Q99708-1]
    XP_006722583.1. XM_006722520.1. [Q99708-1]
    XP_006722584.1. XM_006722521.1. [Q99708-1]
    XP_006722585.1. XM_006722522.1. [Q99708-1]
    UniGeneiHs.546282.

    Genome annotation databases

    EnsembliENST00000327155; ENSP00000323050; ENSG00000101773. [Q99708-1]
    ENST00000399722; ENSP00000382628; ENSG00000101773. [Q99708-1]
    ENST00000399725; ENSP00000382630; ENSG00000101773. [Q99708-3]
    GeneIDi5932.
    KEGGihsa:5932.
    UCSCiuc002ktw.3. human. [Q99708-1]
    uc002ktz.3. human.

    Polymorphism databases

    DMDMi116242745.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF043431 mRNA. Translation: AAC34368.1 .
    U72066 mRNA. Translation: AAC14371.1 .
    AK292481 mRNA. Translation: BAF85170.1 .
    BX648221 mRNA. No translation available.
    AC091147 Genomic DNA. No translation available.
    AC106033 Genomic DNA. No translation available.
    CH471088 Genomic DNA. Translation: EAX01144.1 .
    BC030590 mRNA. Translation: AAH30590.1 .
    CCDSi CCDS11874.1. [Q99708-3 ]
    CCDS11875.1. [Q99708-1 ]
    RefSeqi NP_002885.1. NM_002894.2. [Q99708-1 ]
    NP_976036.1. NM_203291.1. [Q99708-1 ]
    NP_976037.1. NM_203292.1. [Q99708-3 ]
    XP_006722582.1. XM_006722519.1. [Q99708-1 ]
    XP_006722583.1. XM_006722520.1. [Q99708-1 ]
    XP_006722584.1. XM_006722521.1. [Q99708-1 ]
    XP_006722585.1. XM_006722522.1. [Q99708-1 ]
    UniGenei Hs.546282.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2L4Z NMR - A 641-685 [» ]
    ProteinModelPortali Q99708.
    SMRi Q99708. Positions 641-677.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111867. 38 interactions.
    DIPi DIP-24244N.
    IntActi Q99708. 25 interactions.
    MINTi MINT-102295.
    STRINGi 9606.ENSP00000323050.

    PTM databases

    PhosphoSitei Q99708.

    Polymorphism databases

    DMDMi 116242745.

    Proteomic databases

    MaxQBi Q99708.
    PaxDbi Q99708.
    PRIDEi Q99708.

    Protocols and materials databases

    DNASUi 5932.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000327155 ; ENSP00000323050 ; ENSG00000101773 . [Q99708-1 ]
    ENST00000399722 ; ENSP00000382628 ; ENSG00000101773 . [Q99708-1 ]
    ENST00000399725 ; ENSP00000382630 ; ENSG00000101773 . [Q99708-3 ]
    GeneIDi 5932.
    KEGGi hsa:5932.
    UCSCi uc002ktw.3. human. [Q99708-1 ]
    uc002ktz.3. human.

    Organism-specific databases

    CTDi 5932.
    GeneCardsi GC18P020402.
    GeneReviewsi RBBP8.
    HGNCi HGNC:9891. RBBP8.
    HPAi HPA039890.
    HPA052946.
    MIMi 251255. phenotype.
    604124. gene.
    606744. phenotype.
    neXtProti NX_Q99708.
    Orphaneti 313795. Jawad syndrome.
    808. Seckel syndrome.
    PharmGKBi PA34255.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG145529.
    HOGENOMi HOG000293331.
    HOVERGENi HBG057046.
    OrthoDBi EOG771274.
    PhylomeDBi Q99708.
    TreeFami TF106469.

    Enzyme and pathway databases

    Reactomei REACT_27271. Meiotic recombination.

    Miscellaneous databases

    ChiTaRSi RBBP8. human.
    EvolutionaryTracei Q99708.
    GeneWikii RBBP8.
    GenomeRNAii 5932.
    NextBioi 23118.
    PROi Q99708.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q99708.
    Bgeei Q99708.
    CleanExi HS_RBBP8.
    Genevestigatori Q99708.

    Family and domain databases

    InterProi IPR019518. CtIP_N.
    IPR013882. DNA-repair_Sae2/CtIP.
    [Graphical view ]
    Pfami PF10482. CtIP_N. 1 hit.
    PF08573. SAE2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning and characterization of a novel retinoblastoma-binding protein."
      Fusco C., Reymond A., Zervos A.S.
      Genomics 51:351-358(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH RB1.
    2. "Interaction between a cellular protein that binds to the C-terminal region of adenovirus E1A (CtBP) and a novel cellular protein is disrupted by E1A through a conserved PLDLS motif."
      Schaeper U., Subramanian T., Lim L., Boyd J.M., Chinnadurai G.
      J. Biol. Chem. 273:8549-8552(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH CTBP1.
    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] (ISOFORM 1).
      Tissue: Testis.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
      Tissue: Endometrial cancer.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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: Testis.
    8. "Nuclear localization and cell cycle-specific expression of CtIP, a protein that associates with the BRCA1 tumor suppressor."
      Yu X., Baer R.
      J. Biol. Chem. 275:18541-18549(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH BRCA1.
    9. "Functional link of BRCA1 and ataxia telangiectasia gene product in DNA damage response."
      Li S., Ting N.S.Y., Zheng L., Chen P.-L., Ziv Y., Shiloh Y., Lee E.Y.-H.P., Lee W.-H.
      Nature 406:210-215(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, PHOSPHORYLATION AT SER-664 AND SER-745, MUTAGENESIS OF SER-664 AND SER-745.
    10. "The LIM domain protein LMO4 interacts with the cofactor CtIP and the tumor suppressor BRCA1 and inhibits BRCA1 activity."
      Sum E.Y., Peng B., Yu X., Chen J., Byrne J., Lindeman G.J., Visvader J.E.
      J. Biol. Chem. 277:7849-7856(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH LMO4.
    11. Cited for: INTERACTION WITH SIAH1, UBIQUITINATION.
    12. "Dimerization of CtIP, a BRCA1- and CtBP-interacting protein, is mediated by an N-terminal coiled-coil motif."
      Dubin M.J., Stokes P.H., Sum E.Y., Williams R.S., Valova V.A., Robinson P.J., Lindeman G.J., Glover J.N., Visvader J.E., Matthews J.M.
      J. Biol. Chem. 279:26932-26938(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT, IDENTIFICATION BY MASS SPECTROMETRY.
    13. "DNA damage-induced cell cycle checkpoint control requires CtIP, a phosphorylation-dependent binding partner of BRCA1 C-terminal domains."
      Yu X., Chen J.
      Mol. Cell. Biol. 24:9478-9486(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, PHOSPHORYLATION AT SER-327, INTERACTION WITH BRCA1, MUTAGENESIS OF SER-327.
    14. "BRCA1 ubiquitinates its phosphorylation-dependent binding partner CtIP."
      Yu X., Fu S., Lai M., Baer R., Chen J.
      Genes Dev. 20:1721-1726(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH BRCA1, FUNCTION, UBIQUITINATION, MUTAGENESIS OF SER-327.
    15. "CtIP activates its own and cyclin D1 promoters via the E2F/RB pathway during G1/S progression."
      Liu F., Lee W.H.
      Mol. Cell. Biol. 26:3124-3134(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    16. Cited for: FUNCTION, PHOSPHORYLATION, SUBCELLULAR LOCATION, INTERACTION WITH BRCA1; MRE11A AND RAD50.
    17. "Functional complementation studies identify candidate genes and common genetic variants associated with ovarian cancer survival."
      Quaye L., Dafou D., Ramus S.J., Song H., Gentry-Maharaj A., Notaridou M., Hogdall E., Kjaer S.K., Christensen L., Hogdall C., Easton D.F., Jacobs I., Menon U., Pharoah P.D., Gayther S.A.
      Hum. Mol. Genet. 18:1869-1878(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ASSOCIATION WITH OVARIAN CANCER SURVIVAL.
    18. "Human CtIP mediates cell cycle control of DNA end resection and double strand break repair."
      Huertas P., Jackson S.P.
      J. Biol. Chem. 284:9558-9565(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DNA-BINDING, PHOSPHORYLATION AT THR-847, MUTAGENESIS OF THR-847.
    19. "N terminus of CtIP is critical for homologous recombination-mediated double-strand break repair."
      Yuan J., Chen J.
      J. Biol. Chem. 284:31746-31752(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH MRE11A; RAD50 AND NBN, MUTAGENESIS OF HIS-31; VAL-35; LYS-41 AND LEU-45.
    20. Cited for: FUNCTION, MUTAGENESIS OF LYS-513 AND LYS-515.
    21. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    22. "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-723, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    23. "Human SIRT6 promotes DNA end resection through CtIP deacetylation."
      Kaidi A., Weinert B.T., Choudhary C., Jackson S.P.
      Science 329:1348-1353(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, ACETYLATION AT LYS-432; LYS-526 AND LYS-604, INTERACTION WITH SIRT6, IDENTIFICATION BY MASS SPECTROMETRY, MUTAGENESIS OF LYS-432; LYS-526 AND LYS-604.
    24. Cited for: ASSOCIATION WITH BREAST CANCER.
    25. "CtIP mutations cause Seckel and Jawad syndromes."
      Jackson S.P., Borglum A.D.
      PLoS Genet. 7:E1002310-E1002310(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN JWDS, INVOLVEMENT IN SCKL2.

    Entry informationi

    Entry nameiCOM1_HUMAN
    AccessioniPrimary (citable) accession number: Q99708
    Secondary accession number(s): A6NKN2
    , A8K8W6, E7ETY1, O75371, Q8NHQ3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: October 17, 2006
    Last modified: October 1, 2014
    This is version 134 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 18
      Human chromosome 18: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3