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Q99708

- COM1_HUMAN

UniProt

Q99708 - COM1_HUMAN

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Protein
DNA endonuclease RBBP8
Gene
RBBP8, CTIP
Organism
Homo sapiens (Human)
Status
Reviewed - 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. RNA polymerase II repressing transcription factor binding Source: BHF-UCL
  2. RNA polymerase II transcription corepressor activity Source: BHF-UCL
  3. damaged DNA binding Source: UniProtKB
  4. protein binding Source: UniProtKB
  5. single-stranded DNA endodeoxyribonuclease activity Source: UniProtKB

GO - Biological processi

  1. DNA catabolic process, endonucleolytic Source: GOC
  2. DNA double-strand break processing involved in repair via single-strand annealing Source: UniProtKB
  3. DNA repair Source: ProtInc
  4. G1/S transition of mitotic cell cycle Source: Ensembl
  5. G2 DNA damage checkpoint Source: UniProtKB
  6. blastocyst hatching Source: Ensembl
  7. cell cycle checkpoint Source: ProtInc
  8. double-strand break repair via homologous recombination 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
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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 18

Organism-specific databases

HGNCiHGNC:9891. RBBP8.

Subcellular locationi

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

GO - Cellular componenti

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

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.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication
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.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication
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 RBBP8
PRO_0000097179Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei326 – 3261Phosphoserine
Modified residuei327 – 3271Phosphoserine1 Publication
Modified residuei349 – 3491Phosphoserine
Modified residuei432 – 4321N6-acetyllysine1 Publication
Modified residuei526 – 5261N6-acetyllysine1 Publication
Modified residuei604 – 6041N6-acetyllysine1 Publication
Modified residuei664 – 6641Phosphoserine; by ATM1 Publication
Modified residuei679 – 6791Phosphoserine
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.4 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. 24 interactions.
MINTiMINT-102295.
STRINGi9606.ENSP00000323050.

Structurei

Secondary structure

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.

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 damage
Add
BLAST
Regioni509 – 55749Damage-recruitment motif
Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili28 – 157130 Reviewed prediction
Add
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.

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.

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

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.
VSP_043220
Alternative sequencei786 – 86782RETSL…MERGY → SIMQICQQKKEKRNWLPAQD TDSATFHPTHQRIFGKLVFL PLRLVWKEVILRKILILVLV QKDVSLTTQYFLQKARSRRH RR in isoform 3.
VSP_045247Add
BLAST
Alternative sequencei868 – 89730Missing in isoform 3.
VSP_045248Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti4 – 41S → L in AAC14371. 1 Publication
Sequence conflicti74 – 741H → Q in BX648221. 1 Publication
Sequence conflicti92 – 921C → Y in BAF85170. 1 Publication
Sequence conflicti123 – 1231E → G in BAF85170. 1 Publication
Sequence conflicti341 – 3411D → G in BX648221. 1 Publication
Sequence conflicti515 – 5151K → R in BX648221. 1 Publication
Sequence conflicti521 – 5211L → P in BAF85170. 1 Publication
Sequence conflicti642 – 6421L → P in BX648221. 1 Publication
Isoform 3 (identifier: Q99708-3)
Sequence conflicti862 – 8621S → G in BX648221. 1 Publication

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. 24 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

« 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.

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: September 3, 2014
This is version 133 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

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