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Q99708 - COM1_HUMAN

UniProt

Q99708 - COM1_HUMAN

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Protein

DNA endonuclease RBBP8

Gene

RBBP8

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

GO - Biological processi

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

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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
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. nucleoplasm Source: HPA
  3. nucleus Source: ProtInc
  4. transcriptional repressor complex Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

Seckel syndrome 21 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA 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.

See also OMIM:606744
Jawad syndrome1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA 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.

See also OMIM:251255

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 – 3271Phosphoserine1 Publication
Modified residuei349 – 3491Phosphoserine1 Publication
Modified residuei432 – 4321N6-acetyllysine1 Publication
Modified residuei526 – 5261N6-acetyllysine1 Publication
Modified residuei604 – 6041N6-acetyllysine1 Publication
Modified residuei664 – 6641Phosphoserine; by ATM1 Publication
Modified residuei679 – 6791Phosphoserine1 Publication
Modified residuei723 – 7231Phosphoserine1 Publication
Modified residuei745 – 7451Phosphoserine; by ATM1 Publication
Modified residuei847 – 8471Phosphothreonine; by CDK11 Publication

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

BgeeiQ99708.
CleanExiHS_RBBP8.
ExpressionAtlasiQ99708. baseline and differential.
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. 39 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 – 6503Combined sources
Helixi651 – 6533Combined sources
Turni662 – 6665Combined sources
Beta strandi677 – 6793Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00530000063835.
HOGENOMiHOG000293331.
HOVERGENiHBG057046.
InParanoidiQ99708.
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

        10         20         30         40         50
MNISGSSCGS PNSADTSSDF KDLWTKLKEC HDREVQGLQV KVTKLKQERI 
        60         70         80         90        100
LDAQRLEEFF TKNQQLREQQ KVLHETIKVL EDRLRAGLCD RCAVTEEHMR 
       110        120        130        140        150
KKQQEFENIR QQNLKLITEL MNERNTLQEE NKKLSEQLQQ KIENDQQHQA 
       160        170        180        190        200
AELECEEDVI PDSPITAFSF SGVNRLRRKE NPHVRYIEQT HTKLEHSVCA 
       210        220        230        240        250
NEMRKVSKSS THPQHNPNEN EILVADTYDQ SQSPMAKAHG TSSYTPDKSS 
       260        270        280        290        300
FNLATVVAET LGLGVQEESE TQGPMSPLGD ELYHCLEGNH KKQPFEESTR 
       310        320        330        340        350
NTEDSLRFSD STSKTPPQEE LPTRVSSPVF GATSSIKSGL DLNTSLSPSL 
       360        370        380        390        400
LQPGKKKHLK TLPFSNTCIS RLEKTRSKSE DSALFTHHSL GSEVNKIIIQ 
       410        420        430        440        450
SSNKQILINK NISESLGEQN RTEYGKDSNT DKHLEPLKSL GGRTSKRKKT 
       460        470        480        490        500
EEESEHEVSC PQASFDKENA FPFPMDNQFS MNGDCVMDKP LDLSDRFSAI 
       510        520        530        540        550
QRQEKSQGSE TSKNKFRQVT LYEALKTIPK GFSSSRKASD GNCTLPKDSP 
       560        570        580        590        600
GEPCSQECII LQPLNKCSPD NKPSLQIKEE NAVFKIPLRP RESLETENVL 
       610        620        630        640        650
DDIKSAGSHE PIKIQTRSDH GGCELASVLQ LNPCRTGKIK SLQNNQDVSF 
       660        670        680        690        700
ENIQWSIDPG ADLSQYKMDV TVIDTKDGSQ SKLGGETVDM DCTLVSETVL 
       710        720        730        740        750
LKMKKQEQKG EKSSNEERKM NDSLEDMFDR TTHEEYESCL ADSFSQAADE 
       760        770        780        790        800
EEELSTATKK LHTHGDKQDK VKQKAFVEPY FKGDERETSL QNFPHIEVVR 
       810        820        830        840        850
KKEERRKLLG HTCKECEIYY ADMPAEEREK KLASCSRHRF RYIPPNTPEN 
       860        870        880        890 
FWEVGFPSTQ TCMERGYIKE DLDPCPRPKR RQPYNAIFSP KGKEQKT
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

BioGridi111867. 39 interactions.
DIPiDIP-24244N.
IntActiQ99708. 25 interactions.
MINTiMINT-102295.
STRINGi9606.ENSP00000323050.

PTM databases

PhosphoSiteiQ99708.

Polymorphism databases

DMDMi116242745.

Proteomic databases

MaxQBiQ99708.
PaxDbiQ99708.
PRIDEiQ99708.

Protocols and materials databases

DNASUi5932.
Structural Biology KnowledgebaseSearch...

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.

Organism-specific databases

CTDi5932.
GeneCardsiGC18P020378.
GeneReviewsiRBBP8.
HGNCiHGNC:9891. RBBP8.
HPAiHPA039890.
HPA052946.
MIMi251255. phenotype.
604124. gene.
606744. phenotype.
neXtProtiNX_Q99708.
Orphaneti313795. Jawad syndrome.
808. Seckel syndrome.
PharmGKBiPA34255.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG145529.
GeneTreeiENSGT00530000063835.
HOGENOMiHOG000293331.
HOVERGENiHBG057046.
InParanoidiQ99708.
OrthoDBiEOG771274.
PhylomeDBiQ99708.
TreeFamiTF106469.

Enzyme and pathway databases

ReactomeiREACT_27271. Meiotic recombination.

Miscellaneous databases

ChiTaRSiRBBP8. human.
EvolutionaryTraceiQ99708.
GeneWikiiRBBP8.
GenomeRNAii5932.
NextBioi23118.
PROiQ99708.
SOURCEiSearch...

Gene expression databases

BgeeiQ99708.
CleanExiHS_RBBP8.
ExpressionAtlasiQ99708. baseline and differential.
GenevestigatoriQ99708.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
+Additional computationally mapped references.

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: February 4, 2015
This is version 138 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.