UniProtKB - Q99708 (CTIP_HUMAN)
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Protein
DNA endonuclease RBBP8
Gene
RBBP8
Organism
Homo sapiens (Human)
Status
Functioni
Endonuclease that cooperates with the MRE11-RAD50-NBN (MRN) complex in DNA-end resection, the first step of double-strand break (DSB) repair through the homologous recombination (HR) pathway. HR is restricted to S and G2 phases of the cell cycle and preferentially repairs DSBs resulting from replication fork collapse. Key determinant of DSB repair pathway choice, as it commits cells to HR by preventing classical non-homologous end-joining (NHEJ). 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 (PubMed:10764811, PubMed:10910365, PubMed:15485915, PubMed:16581787, PubMed:16818604, PubMed:17965729, PubMed:19202191, PubMed:19759395, PubMed:20064462, PubMed:20829486). During immunoglobulin heavy chain class-switch recombination, promotes microhomology-mediated alternative end joining (A-NHEJ) and plays an essential role in chromosomal translocations (By similarity).By similarity10 Publications
GO - Molecular functioni
- damaged DNA binding Source: UniProtKB
- identical protein binding Source: IntAct
- RNA polymerase II repressing transcription factor binding Source: BHF-UCL
- RNA polymerase II transcription corepressor activity Source: BHF-UCL
- single-stranded DNA endodeoxyribonuclease activity Source: UniProtKB
GO - Biological processi
- blastocyst hatching Source: Ensembl
- cell division Source: UniProtKB-KW
- DNA double-strand break processing Source: Reactome
- DNA double-strand break processing involved in repair via single-strand annealing Source: UniProtKB
- DNA repair Source: ProtInc
- DNA replication Source: Reactome
- DNA synthesis involved in DNA repair Source: Reactome
- double-strand break repair via homologous recombination Source: UniProtKB
- G1/S transition of mitotic cell cycle Source: Ensembl
- G2 DNA damage checkpoint Source: UniProtKB
- meiotic cell cycle Source: UniProtKB-KW
- negative regulation of G0 to G1 transition Source: Reactome
- nucleotide-excision repair Source: CACAO
- regulation of signal transduction by p53 class mediator Source: Reactome
- regulation of transcription by RNA polymerase II Source: ProtInc
- response to estradiol Source: Ensembl
- strand displacement Source: Reactome
Keywordsi
Molecular function | DNA-binding, Endonuclease, Hydrolase, Nuclease |
Biological process | Cell cycle, Cell division, DNA damage, DNA repair, Meiosis, Mitosis |
Enzyme and pathway databases
Reactomei | R-HSA-5685938. HDR through Single Strand Annealing (SSA). R-HSA-5685939. HDR through MMEJ (alt-NHEJ). R-HSA-5685942. HDR through Homologous Recombination (HRR). R-HSA-5693554. Resolution of D-loop Structures through Synthesis-Dependent Strand Annealing (SDSA). R-HSA-5693568. Resolution of D-loop Structures through Holliday Junction Intermediates. R-HSA-5693579. Homologous DNA Pairing and Strand Exchange. R-HSA-5693607. Processing of DNA double-strand break ends. R-HSA-5693616. Presynaptic phase of homologous DNA pairing and strand exchange. R-HSA-6804756. Regulation of TP53 Activity through Phosphorylation. R-HSA-69473. G2/M DNA damage checkpoint. R-HSA-8953750. Transcriptional Regulation by E2F6. R-HSA-912446. Meiotic recombination. |
SIGNORi | Q99708. |
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 |
Organismi | Homo sapiens (Human) |
Taxonomic identifieri | 9606 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Proteomesi |
|
Organism-specific databases
EuPathDBi | HostDB:ENSG00000101773.16. |
HGNCi | HGNC:9891. RBBP8. |
MIMi | 604124. gene. |
neXtProti | NX_Q99708. |
Pathology & Biotechi
Involvement in diseasei
Seckel syndrome 2 (SCKL2)2 Publications
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:606744Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural variantiVAR_075824 | 100 | R → W in SCKL2. 1 PublicationCorresponds to variant dbSNP:rs373804633Ensembl. | 1 |
Jawad syndrome (JWDS)1 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:251255Genetic variability in RBBP8 is noted as a factor in BRCA1-associated breast cancer risk (PubMed:21799032). Associated with sensitivity to tamoxifen in certain breast cancer cell lines (PubMed:18171986).2 Publications
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 31 | H → A: No effect on RPA focus formation on DNA damage. 1 Publication | 1 | |
Mutagenesisi | 35 | V → A: No effect on RPA focus formation on DNA damage. 1 Publication | 1 | |
Mutagenesisi | 41 | K → A: No effect on RPA focus formation on DNA damage. 1 Publication | 1 | |
Mutagenesisi | 45 | L → A: No effect on RPA focus formation on DNA damage. 1 Publication | 1 | |
Mutagenesisi | 62 | K → R in K12R; defects in ability to promoting DNA resection and homologous recombination; when associated with R-78; R-115; R-132; R-133; R-404; R-572; R-578; R-640; R-759; R-760 and R-782. In K5R; defects in ability to promoting DNA resection and homologous recombination; when associated with R-78; R-115; R-132 and R-133. 1 Publication | 1 | |
Mutagenesisi | 78 | K → R in K12R; defects in ability to promoting DNA resection and homologous recombination; when associated with R-62; R-115; R-132; R-133; R-404; R-572; R-578; R-640; R-759; R-760 and R-782. In K5R; defects in ability to promoting DNA resection and homologous recombination; when associated with R-62; R-115; R-132 and R-133. 1 Publication | 1 | |
Mutagenesisi | 115 | K → R in K12R; defects in ability to promoting DNA resection and homologous recombination; when associated with R-62; R-78; R-132; R-133; R-404; R-572; R-578; R-640; R-759; R-760 and R-782. In K5R; defects in ability to promoting DNA resection and homologous recombination; when associated with R-62; R-78; R-132 and R-133. 1 Publication | 1 | |
Mutagenesisi | 132 | K → R in K12R; defects in ability to promoting DNA resection and homologous recombination; when associated with R-62; R-78; R-115; R-133; R-404; R-572; R-578; R-640; R-759; R-760 and R-782. In K5R; defects in ability to promoting DNA resection and homologous recombination; when associated with R-62; R-78; R-115 and R-133. 1 Publication | 1 | |
Mutagenesisi | 133 | K → R in K12R; defects in ability to promoting DNA resection and homologous recombination; when associated with R-62; R-78; R-115; R-133; R-404; R-572; R-578; R-640; R-759; R-760 and R-782. In K5R; defects in ability to promoting DNA resection and homologous recombination; when associated with R-62; R-78; R-115 and R-132. 1 Publication | 1 | |
Mutagenesisi | 179 | K → A: No effect on FZR1-binding. 1 Publication | 1 | |
Mutagenesisi | 276 | S → A: No effect on PIN1-binding. Impaired PIN1-binding, partially decreased CUL3/KLHL15-mediated proteasomal degradation, no effect on BRCA1-, MRE11-, nor on KLHL15-binding; when associated with A-315. 2 Publications | 1 | |
Mutagenesisi | 315 | T → A: Decreased PIN1-binding. Impaired PIN1-binding, partially decreased CUL3/KLHL15-mediated proteasomal degradation, no effect on BRCA1-, MRE11-, nor on KLHL15-binding; when associated with A-276. 2 Publications | 1 | |
Mutagenesisi | 327 | S → A: Abolishes BRCA1 interaction and ubiquitination. No activation of CHEK1 after DNA damage. 2 Publications | 1 | |
Mutagenesisi | 404 | K → R in K12R; defects in ability to promoting DNA resection and homologous recombination; when associated with R-62; R-78; R-115; R-132; R-133; R-572; R-578; R-640; R-759; R-760 and R-782. 1 Publication | 1 | |
Mutagenesisi | 432 | K → R: Greatly reduced acetylation. Alleviates resection defects caused by depletion of SIRT6; when associated with R-526 and R-604. 1 Publication | 1 | |
Mutagenesisi | 467 | K → A: Impaired FZR1-binding and APC/C-mediated polyubiquitination. Increased stability. No effect on MRE11-binding, nor on CUL3/KLHL15-mediated proteasomal degradation. No effect on DNA-en resection activity. 2 Publications | 1 | |
Mutagenesisi | 513 | K → A: Abolishes damage recruitment capability. 1 Publication | 1 | |
Mutagenesisi | 515 | K → A: Abolishes damage recruitment capability. 1 Publication | 1 | |
Mutagenesisi | 526 | K → R: Greatly reduced acetylation. Alleviates resection defects caused by depletion of SIRT6; when associated with R-432 and R-604. 1 Publication | 1 | |
Mutagenesisi | 572 | K → R in K12R; defects in ability to promoting DNA resection and homologous recombination; when associated with R-62; R-78; R-115; R-132; R-133; R-404; R-578; R-640; R-759; R-760 and R-782. 1 Publication | 1 | |
Mutagenesisi | 578 | K → R in K12R; defects in ability to promoting DNA resection and homologous recombination; when associated with R-62; R-78; R-115; R-132; R-133; R-404; R-572; R-640; R-759; R-760 and R-782. 1 Publication | 1 | |
Mutagenesisi | 604 | K → R: Greatly reduced acetylation. Alleviates resection defects caused by depletion of SIRT6; when associated with R-432 and R-526. 1 Publication | 1 | |
Mutagenesisi | 640 | K → R in K12R; defects in ability to promoting DNA resection and homologous recombination; when associated with R-62; R-78; R-115; R-132; R-133; R-404; R-572; R-578; R-759; R-760 and R-782. 1 Publication | 1 | |
Mutagenesisi | 664 | S → A: Abrogates dissociation of BRCA1. 1 Publication | 1 | |
Mutagenesisi | 745 | S → A: Abrogates dissociation of BRCA1. 1 Publication | 1 | |
Mutagenesisi | 759 | K → R in K12R; defects in ability to promoting DNA resection and homologous recombination; when associated with R-62; R-78; R-115; R-132; R-133; R-404; R-572; R-578; R-640; R-760 and R-782. 1 Publication | 1 | |
Mutagenesisi | 760 | K → R in K12R; defects in ability to promoting DNA resection and homologous recombination; when associated with R-62; R-78; R-115; R-132; R-133; R-404; R-572; R-578; R-640; R-759 and R-782. 1 Publication | 1 | |
Mutagenesisi | 782 | K → R in K12R; defects in ability to promoting DNA resection and homologous recombination; when associated with R-62; R-78; R-115; R-132; R-133; R-404; R-572; R-578; R-640; R-759 and R-760. 1 Publication | 1 | |
Mutagenesisi | 839 | R → A: No effect on CUL3/KLHL15-mediated proteasomal degradation. 1 Publication | 1 | |
Mutagenesisi | 840 | F → A: Decreased CUL3/KLHL15-mediated proteasomal degradation. 1 Publication | 1 | |
Mutagenesisi | 842 | Y → A: Decreased interaction with KLHL15, decreased polyubiquitination and CUL3/KLHL15-mediated proteasomal degradation. No effect on DNA-end resection activity. 1 Publication | 1 | |
Mutagenesisi | 842 | Y → F: No effect on KLHL15-binding, nor on CUL3/KLHL15-mediated proteasomal degradation. 1 Publication | 1 | |
Mutagenesisi | 847 | T → A: Impairs DNA resection. 1 Publication | 1 | |
Mutagenesisi | 847 | T → E: Mimics constitutive phosphorylation. 1 Publication | 1 |
Keywords - Diseasei
Disease mutation, Dwarfism, Mental retardationOrganism-specific databases
DisGeNETi | 5932. |
GeneReviewsi | RBBP8. |
MalaCardsi | RBBP8. |
MIMi | 251255. phenotype. 606744. phenotype. |
OpenTargetsi | ENSG00000101773. |
Orphaneti | 313795. Jawad syndrome. 808. Seckel syndrome. |
PharmGKBi | PA34255. |
Polymorphism and mutation databases
BioMutai | RBBP8. |
DMDMi | 116242745. |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000097179 | 1 – 897 | DNA endonuclease RBBP8Add BLAST | 897 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Cross-linki | 62 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources | ||
Cross-linki | 115 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources | ||
Cross-linki | 193 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources | ||
Modified residuei | 233 | PhosphoserineCombined sources | 1 | |
Modified residuei | 276 | Phosphoserine1 Publication | 1 | |
Modified residuei | 315 | Phosphothreonine; by CDK2Combined sources1 Publication | 1 | |
Modified residuei | 326 | Phosphoserine1 Publication | 1 | |
Modified residuei | 327 | PhosphoserineCombined sources1 Publication | 1 | |
Modified residuei | 349 | Phosphoserine1 Publication | 1 | |
Cross-linki | 360 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources | ||
Cross-linki | 378 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources | ||
Modified residuei | 379 | PhosphoserineCombined sources | 1 | |
Cross-linki | 396 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources | ||
Cross-linki | 404 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources | ||
Cross-linki | 410 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources | ||
Modified residuei | 432 | N6-acetyllysine1 Publication | 1 | |
Cross-linki | 438 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources | ||
Cross-linki | 449 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources | ||
Modified residuei | 526 | N6-acetyllysine; alternate1 Publication | 1 | |
Cross-linki | 526 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources | ||
Cross-linki | 530 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources | ||
Cross-linki | 572 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources | ||
Cross-linki | 578 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources | ||
Modified residuei | 604 | N6-acetyllysine; alternate1 Publication | 1 | |
Cross-linki | 604 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources | ||
Cross-linki | 613 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources | ||
Cross-linki | 638 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources | ||
Cross-linki | 640 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources | ||
Modified residuei | 664 | Phosphoserine; by ATM1 Publication | 1 | |
Cross-linki | 676 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources | ||
Modified residuei | 679 | Phosphoserine1 Publication | 1 | |
Cross-linki | 719 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources | ||
Modified residuei | 723 | PhosphoserineCombined sources | 1 | |
Modified residuei | 745 | Phosphoserine; by ATM1 Publication | 1 | |
Cross-linki | 782 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources | ||
Modified residuei | 847 | Phosphothreonine; by CDK11 Publication | 1 | |
Cross-linki | 869 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources |
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. Phosphorylation at Thr-315, probably catalyzed by CDK2, is required for PIN1-binding, while phosphorylation at Ser-276 serves as a PIN1 isomerization site. Phosphorylation at Thr-315 is cell-cycle dependent. It steadily increases during S phase, peaks at late S/G2 phase, and drops at G1 (PubMed:23623683).5 Publications
Ubiquitinated (PubMed:14654780, PubMed:16818604, PubMed:27561354). 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 (PubMed:16818604). Ubiquitinated by RNF138 at its N-terminus (PubMed:26502057). Ubiquitinated through 'Lys-48' by the E3 CUL3-KLHL15 complex; this modification leads to proteasomal degradation (PubMed:27561354). Ubiquitinated by the E3 FZR1/APC/C complex; this modification leads to proteasomal degradation (PubMed:25349192).5 Publications
Keywords - PTMi
Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugationProteomic databases
MaxQBi | Q99708. |
PaxDbi | Q99708. |
PeptideAtlasi | Q99708. |
PRIDEi | Q99708. |
PTM databases
iPTMneti | Q99708. |
PhosphoSitePlusi | Q99708. |
Expressioni
Tissue specificityi
Expressed in ER-positive breast cancer lines, but tends to be down-regulated ER-negative cells (at protein level).1 Publication
Inductioni
Expression is cell-cycle regulated. Levels increase as dividing cells traverse the G1/S boundary (PubMed:18171986). The protein is degraded by the proteasome pathway during mitotic exit. Also degraded in response to DNA damage in G2 cells; this degradation is mediated by the E3 FZR1/APC/C complex (PubMed:25349192).2 Publications
Gene expression databases
Bgeei | ENSG00000101773. |
CleanExi | HS_RBBP8. |
ExpressionAtlasi | Q99708. baseline and differential. |
Genevisiblei | Q99708. HS. |
Organism-specific databases
HPAi | HPA039890. HPA052946. |
Interactioni
Subunit structurei
Homodimer; dimerizes via the coiled coil domain (PubMed:15084581). Interacts (via the PXDLS motif) with CTBP1; the interaction is disrupted via binding of the adenovirus E1A to CTBP1 (PubMed:9535825). Component of the BRCA1-RBBP8 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 (PubMed:10764811, PubMed:15485915, PubMed:16818604, PubMed:17965729, PubMed:23623683). Interacts with RB1 (PubMed:9721205). Interacts with the MRN complex. Interacts directly with MRE11; the interaction is required for efficient homologous recombination (HR) and regulation of the MRN complex (PubMed:19759395, PubMed:23623683). Interacts directly with RAD50 (PubMed:19759395). Interacts directly with NBN (PubMed:19759395). Interacts with SIRT6; the interaction deacetylates RBBP8 upon DNA damage (PubMed:20829486). Interacts with LM04 (via the LIM zinc-binding 1 domain) (PubMed:11751867). Interacts with SIAH1 (PubMed:14654780). Interacts with RNF138 (PubMed:26502057). Interacts with EXD2 (PubMed:26807646). Interacts with CUL3 and KLHL15; this interaction leads to RBBP8 proteasomal degradation (PubMed:27561354). Directly interacts with PIN1; this interaction depends upon RBBP8 phosphorylation, predominantly at Thr-315 (PubMed:23623683). Interacts with FZR1; this interaction leads to APC/C-mediated RBBP8 proteasomal degradation (PubMed:25349192). Interacts with AUNIP; leading to recruit RBBP8 to sites of DNA damage (PubMed:29042561).17 Publications
Binary interactionsi
GO - Molecular functioni
- identical protein binding Source: IntAct
- RNA polymerase II repressing transcription factor binding Source: BHF-UCL
Protein-protein interaction databases
BioGridi | 111867. 63 interactors. |
CORUMi | Q99708. |
DIPi | DIP-24244N. |
ELMi | Q99708. |
IntActi | Q99708. 43 interactors. |
MINTi | Q99708. |
STRINGi | 9606.ENSP00000323050. |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more detailsFeature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Helixi | 18 – 50 | Combined sources | 33 | |
Beta strandi | 648 – 650 | Combined sources | 3 | |
Helixi | 651 – 653 | Combined sources | 3 | |
Turni | 662 – 666 | Combined sources | 5 | |
Beta strandi | 677 – 679 | Combined sources | 3 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
2L4Z | NMR | - | A | 641-685 | [»] | |
4D2H | X-ray | 1.90 | A/B/C/D/E/F/G/H | 18-52 | [»] | |
ProteinModelPortali | Q99708. | |||||
SMRi | Q99708. | |||||
ModBasei | Search... | |||||
MobiDBi | Search... |
Miscellaneous databases
EvolutionaryTracei | Q99708. |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 22 – 45 | Essential for binding to the MRN complex and for RPA focus formation on DNA damageAdd BLAST | 24 | |
Regioni | 509 – 557 | Damage-recruitment motifAdd BLAST | 49 |
Coiled coil
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Coiled coili | 28 – 157 | Sequence analysisAdd BLAST | 130 |
Motif
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Motifi | 490 – 494 | PXDLS motif | 5 | |
Motifi | 840 – 842 | KLHL15-binding1 Publication | 3 |
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 coilPhylogenomic databases
eggNOGi | ENOG410IJ39. Eukaryota. ENOG410ZSBE. LUCA. |
GeneTreei | ENSGT00530000063835. |
HOGENOMi | HOG000293331. |
HOVERGENi | HBG057046. |
InParanoidi | Q99708. |
KOi | K20773. |
PhylomeDBi | Q99708. |
TreeFami | TF106469. |
Family and domain databases
InterProi | View protein in InterPro IPR019518. CtIP_N. IPR013882. Ctp1_C. IPR033594. RBBP8. IPR033316. RBBP8-like. |
PANTHERi | PTHR15107. PTHR15107. 1 hit. PTHR15107:SF4. PTHR15107:SF4. 1 hit. |
Pfami | View protein in Pfam PF10482. CtIP_N. 1 hit. PF08573. SAE2. 1 hit. |
s (3)i Sequence
Sequence statusi: Complete.
This entry describes 3 produced by isoformsialternative splicing. AlignAdd to basket
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.
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
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length | |
---|---|---|---|---|---|
Sequence conflicti | 4 | S → L in AAC14371 (PubMed:9721205).Curated | 1 | ||
Sequence conflicti | 74 | H → Q in BX648221 (PubMed:17974005).Curated | 1 | ||
Sequence conflicti | 92 | C → Y in BAF85170 (PubMed:14702039).Curated | 1 | ||
Sequence conflicti | 123 | E → G in BAF85170 (PubMed:14702039).Curated | 1 | ||
Sequence conflicti | 341 | D → G in BX648221 (PubMed:17974005).Curated | 1 | ||
Sequence conflicti | 515 | K → R in BX648221 (PubMed:17974005).Curated | 1 | ||
Sequence conflicti | 521 | L → P in BAF85170 (PubMed:14702039).Curated | 1 | ||
Sequence conflicti | 642 | L → P in BX648221 (PubMed:17974005).Curated | 1 | ||
Isoform 3 (identifier: Q99708-3) | |||||
Sequence conflicti | 862 | S → G in BX648221 (PubMed:17974005).Curated | 1 |
Natural variant
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural variantiVAR_075824 | 100 | R → W in SCKL2. 1 PublicationCorresponds to variant dbSNP:rs373804633Ensembl. | 1 | |
Natural variantiVAR_051308 | 357 | K → N. Corresponds to variant dbSNP:rs34678569Ensembl. | 1 | |
Natural variantiVAR_028308 | 387 | H → Y. Corresponds to variant dbSNP:rs1804732Ensembl. | 1 |
Alternative sequence
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Alternative sequenceiVSP_043220 | 714 | S → SMLFYI in isoform 2. 1 Publication | 1 | |
Alternative sequenceiVSP_045247 | 786 – 867 | RETSL…MERGY → SIMQICQQKKEKRNWLPAQD TDSATFHPTHQRIFGKLVFL PLRLVWKEVILRKILILVLV QKDVSLTTQYFLQKARSRRH RR in isoform 3. 1 PublicationAdd BLAST | 82 | |
Alternative sequenceiVSP_045248 | 868 – 897 | Missing in isoform 3. 1 PublicationAdd BLAST | 30 |
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. |
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_006722519.2. [Q99708-1] XP_006722583.1. XM_006722520.2. [Q99708-1] XP_006722584.1. XM_006722521.2. [Q99708-1] XP_011524434.1. XM_011526132.2. [Q99708-1] |
UniGenei | Hs.546282. |
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.4. human. [Q99708-1] |
Keywords - Coding sequence diversityi
Alternative splicing, PolymorphismSimilar proteinsi
Entry informationi
Entry namei | CTIP_HUMAN | |
Accessioni | Q99708Primary (citable) accession number: Q99708 Secondary accession number(s): A6NKN2 Q8NHQ3 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | December 1, 2000 |
Last sequence update: | October 17, 2006 | |
Last modified: | March 28, 2018 | |
This is version 171 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program | |
Disclaimer | Any 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. |