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UniProtKB - Q99708 (CTIP_HUMAN)

Entry version 197 (25 May 2022)
Sequence version 2 (17 Oct 2006)
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Protein

DNA endonuclease RBBP8

Gene

RBBP8

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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 (PubMed:17965729, PubMed:19202191, PubMed:19759395, PubMed:20064462, PubMed:26721387).

HR is restricted to S and G2 phases of the cell cycle and preferentially repairs DSBs resulting from replication fork collapse (PubMed:17965729, PubMed:19202191).

Key determinant of DSB repair pathway choice, as it commits cells to HR by preventing classical non-homologous end-joining (NHEJ) (PubMed:19202191).

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 (PubMed:16581787, PubMed:17965729, PubMed:19759395, PubMed:20064462).

Component of the BRCA1-RBBP8 complex that regulates CHEK1 activation and controls cell cycle G2/M checkpoints on DNA damage (PubMed:15485915, PubMed:16818604).

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 similarity8 Publications

Caution

Upon DNA damage, was shown to interact with SIRT6 resulting in its deacetylation. However, this study was later retracted.2 Publications

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionDNA-binding, Endonuclease, Hydrolase, Nuclease
Biological processCell cycle, Cell division, DNA damage, DNA repair, Meiosis, Mitosis

Enzyme and pathway databases

Pathway Commons web resource for biological pathway data

More...PathwayCommonsi		Q99708

Reactome - a knowledgebase of biological pathways and processes

More...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
R-HSA-9701192, Defective HDR through Homologous Recombination (HRR) due to BRCA1 loss-of-function
R-HSA-9704331, Defective HDR through Homologous Recombination Repair (HRR) due to PALB2 loss of BRCA1 binding function
R-HSA-9704646, Defective HDR through Homologous Recombination Repair (HRR) due to PALB2 loss of BRCA2/RAD51/RAD51C binding function

SignaLink: a signaling pathway resource with multi-layered regulatory networks

More...SignaLinki		Q99708

SIGNOR Signaling Network Open Resource

More...SIGNORi		Q99708

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>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
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:RBBP8
Synonyms:CTIP
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 18

Organism-specific databases

Human Gene Nomenclature Database

More...HGNCi		HGNC:9891, RBBP8

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		604124, gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_Q99708

Eukaryotic Pathogen, Vector and Host Database Resources

More...VEuPathDBi		HostDB:ENSG00000101773

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Keywords - Cellular componenti

Chromosome, Nucleus

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the 'Pathology and Biotech' section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Seckel syndrome 2 (SCKL2)2 Publications
The disease is caused by variants 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.
Related information in OMIM
Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_075824100R → W in SCKL2. 1 PublicationCorresponds to variant dbSNP:rs373804633EnsemblClinVar.1
Jawad syndrome (JWDS)1 Publication
The disease is caused by variants 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.
Related information in OMIM
Genetic 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 keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi31H → A: No effect on RPA focus formation on DNA damage. 1 Publication1
Mutagenesisi35V → A: No effect on RPA focus formation on DNA damage. 1 Publication1
Mutagenesisi41K → A: No effect on RPA focus formation on DNA damage. 1 Publication1
Mutagenesisi45L → A: No effect on RPA focus formation on DNA damage. 1 Publication1
Mutagenesisi62K → 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 Publication1
Mutagenesisi78K → 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 Publication1
Mutagenesisi115K → 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 Publication1
Mutagenesisi132K → 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 Publication1
Mutagenesisi133K → 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 Publication1
Mutagenesisi179K → A: No effect on FZR1-binding. 1 Publication1
Mutagenesisi276S → 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 Publications1
Mutagenesisi315T → 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 Publications1
Mutagenesisi327S → A: Abolishes BRCA1 interaction and ubiquitination. No activation of CHEK1 after DNA damage. 2 Publications1
Mutagenesisi404K → 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 Publication1
Mutagenesisi467K → 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 Publications1
Mutagenesisi513K → A: Abolishes damage recruitment capability. 1 Publication1
Mutagenesisi515K → A: Abolishes damage recruitment capability. 1 Publication1
Mutagenesisi572K → 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 Publication1
Mutagenesisi578K → 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 Publication1
Mutagenesisi640K → 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 Publication1
Mutagenesisi664S → A: Abrogates dissociation of BRCA1. 1 Publication1
Mutagenesisi745S → A: Abrogates dissociation of BRCA1. 1 Publication1
Mutagenesisi759K → 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 Publication1
Mutagenesisi760K → 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 Publication1
Mutagenesisi782K → 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 Publication1
Mutagenesisi839R → A: No effect on CUL3/KLHL15-mediated proteasomal degradation. 1 Publication1
Mutagenesisi840F → A: Decreased CUL3/KLHL15-mediated proteasomal degradation. 1 Publication1
Mutagenesisi842Y → A: Decreased interaction with KLHL15, decreased polyubiquitination and CUL3/KLHL15-mediated proteasomal degradation. No effect on DNA-end resection activity. 1 Publication1
Mutagenesisi842Y → F: No effect on KLHL15-binding, nor on CUL3/KLHL15-mediated proteasomal degradation. 1 Publication1
Mutagenesisi847T → A: Impairs DNA resection. 1 Publication1
Mutagenesisi847T → E: Mimics constitutive phosphorylation. 1 Publication1

Keywords - Diseasei

Disease variant, Dwarfism, Mental retardation

Organism-specific databases

DisGeNET

More...DisGeNETi		5932

MalaCards human disease database

More...MalaCardsi		RBBP8
MIMi251255, phenotype
606744, phenotype

Open Targets

More...OpenTargetsi		ENSG00000101773

Orphanet; a database dedicated to information on rare diseases and orphan drugs

More...Orphaneti		313795, Jawad syndrome
808, Seckel syndrome

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA34255

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...Pharosi		Q99708, Tbio

Genetic variation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		RBBP8

Domain mapping of disease mutations (DMDM)

More...DMDMi		116242745

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000971791 – 897DNA endonuclease RBBP8Add BLAST897

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki62Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki115Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki193Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei233PhosphoserineCombined sources1
Modified residuei276Phosphoserine1 Publication1
Modified residuei315Phosphothreonine; by CDK2Combined sources1 Publication1
Modified residuei326Phosphoserine1 Publication1
Modified residuei327PhosphoserineCombined sources1 Publication1
Modified residuei349Phosphoserine1 Publication1
Cross-linki360Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki378Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei379PhosphoserineCombined sources1
Cross-linki396Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki404Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki410Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki438Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki449Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki526Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Cross-linki530Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki572Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki578Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki604Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Cross-linki613Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki638Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki640Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei664Phosphoserine; by ATM1 Publication1
Cross-linki676Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei679Phosphoserine1 Publication1
Cross-linki719Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei723PhosphoserineCombined sources1
Modified residuei745Phosphoserine; by ATM1 Publication1
Cross-linki782Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei847Phosphothreonine; by CDK11 Publication1
Cross-linki869Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

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 proteasomal 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

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		Q99708

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		Q99708

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...MassIVEi		Q99708

MaxQB - The MaxQuant DataBase

More...MaxQBi		Q99708

PaxDb, a database of protein abundance averages across all three domains of life

More...PaxDbi		Q99708

PeptideAtlas

More...PeptideAtlasi		Q99708

PRoteomics IDEntifications database

More...PRIDEi		Q99708

ProteomicsDB: a multi-organism proteome resource

More...ProteomicsDBi		1422
78424 [Q99708-1]
78425 [Q99708-2]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		Q99708

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...PhosphoSitePlusi		Q99708

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Expressed in ER-positive breast cancer lines, but tends to be down-regulated ER-negative cells (at protein level).1 Publication

<p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>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

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000101773, Expressed in testis and 222 other tissues

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		Q99708, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		Q99708, HS

Organism-specific databases

Human Protein Atlas

More...HPAi		ENSG00000101773, Low tissue specificity

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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 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, PubMed:10764811, PubMed:11751867, PubMed:14654780, PubMed:15084581, PubMed:15485915, PubMed:16818604, PubMed:17965729, PubMed:19759395, PubMed:23623683, PubMed:25349192, PubMed:26502057, PubMed:26807646, PubMed:27561354, PubMed:9535825, PubMed:9721205).

Interacts with SAMHD1 (PubMed:28834754).

Interacts with HDGFL2 (PubMed:26721387).

18 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		111867, 106 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...ComplexPortali		CPX-4441, BRCA1-C complex

CORUM comprehensive resource of mammalian protein complexes

More...CORUMi		Q99708

Database of interacting proteins

More...DIPi		DIP-24244N

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

More...ELMi		Q99708

Protein interaction database and analysis system

More...IntActi		Q99708, 44 interactors

Molecular INTeraction database

More...MINTi		Q99708

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000382628

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		Q99708, protein

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1897
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

AlphaFold Protein Structure Database

More...AlphaFoldDBi		Q99708

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		Q99708

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		Q99708

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni22 – 45Essential for binding to the MRN complex and for RPA focus formation on DNA damageAdd BLAST24
Regioni292 – 325DisorderedSequence analysisAdd BLAST34
Regioni419 – 464DisorderedSequence analysisAdd BLAST46
Regioni509 – 557Damage-recruitment motifAdd BLAST49
Regioni704 – 723DisorderedSequence analysisAdd BLAST20
Regioni873 – 897DisorderedSequence analysisAdd BLAST25

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and domains' section denotes the positions of regions of coiled coil within the protein.<p><a href='/help/coiled' target='_top'>More...</a></p>Coiled coili28 – 157Sequence analysisAdd BLAST130

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi490 – 494PXDLS motif5
Motifi840 – 842KLHL15-binding1 Publication3

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular type of amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi305 – 325Polar residuesSequence analysisAdd BLAST21
Compositional biasi420 – 462Basic and acidic residuesSequence analysisAdd BLAST43

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>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.

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the COM1/SAE2/CtIP family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		ENOG502QTV5, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT00530000063835

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_019262_0_0_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		Q99708

Identification of Orthologs from Complete Genome Data

More...OMAi		FKIPLCP

Database for complete collections of gene phylogenies

More...PhylomeDBi		Q99708

TreeFam database of animal gene trees

More...TreeFami		TF106469

Family and domain databases

Intrinsically Disordered proteins with Extensive Annotations and Literature

More...IDEALi		IID00340

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR019518, CtIP_N
IPR013882, Ctp1_C
IPR033594, RBBP8
IPR033316, RBBP8-like

The PANTHER Classification System

More...PANTHERi		PTHR15107, PTHR15107, 1 hit
PTHR15107:SF4, PTHR15107:SF4, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF10482, CtIP_N, 1 hit
PF08573, SAE2, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (3+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry describes 3 <p>This subsection of the 'Sequence' section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 3 described isoforms and 11 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: Q99708-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the <p><strong>What is the canonical sequence?</strong><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali 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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> 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.

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

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 11 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
I6L8A6I6L8A6_HUMAN
DNA endonuclease RBBP8
RBBP8
902Annotation score:

Annotation score:3 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
F6Q6H0F6Q6H0_HUMAN
DNA endonuclease RBBP8
RBBP8
580Annotation score:

Annotation score:3 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
J3QL00J3QL00_HUMAN
DNA endonuclease RBBP8
RBBP8
160Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
J3QL93J3QL93_HUMAN
DNA endonuclease RBBP8
RBBP8
84Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
J3QLW6J3QLW6_HUMAN
DNA endonuclease RBBP8
RBBP8
205Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
J3KSA4J3KSA4_HUMAN
DNA endonuclease RBBP8
RBBP8
64Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
J3QLH2J3QLH2_HUMAN
DNA endonuclease RBBP8
RBBP8
75Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
J3QSH7J3QSH7_HUMAN
DNA endonuclease RBBP8
RBBP8
324Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
J3QRM0J3QRM0_HUMAN
DNA endonuclease RBBP8
RBBP8
29Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
V9GZ40V9GZ40_HUMAN
DNA endonuclease RBBP8
RBBP8
45Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
There is more potential isoformShow all

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti4S → L in AAC14371 (PubMed:9721205).Curated1
Sequence conflicti74H → Q in BX648221 (PubMed:17974005).Curated1
Sequence conflicti92C → Y in BAF85170 (PubMed:14702039).Curated1
Sequence conflicti123E → G in BAF85170 (PubMed:14702039).Curated1
Sequence conflicti341D → G in BX648221 (PubMed:17974005).Curated1
Sequence conflicti515K → R in BX648221 (PubMed:17974005).Curated1
Sequence conflicti521L → P in BAF85170 (PubMed:14702039).Curated1
Sequence conflicti642L → P in BX648221 (PubMed:17974005).Curated1
Isoform 3 (identifier: Q99708-3)
Sequence conflicti862S → G in BX648221 (PubMed:17974005).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_075824100R → W in SCKL2. 1 PublicationCorresponds to variant dbSNP:rs373804633EnsemblClinVar.1
Natural variantiVAR_051308357K → N. Corresponds to variant dbSNP:rs34678569EnsemblClinVar.1
Natural variantiVAR_028308387H → Y. Corresponds to variant dbSNP:rs1804732Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_043220714S → SMLFYI in isoform 2. 1 Publication1
Alternative sequenceiVSP_045247786 – 867RETSL…MERGY → SIMQICQQKKEKRNWLPAQD TDSATFHPTHQRIFGKLVFL PLRLVWKEVILRKILILVLV QKDVSLTTQYFLQKARSRRH RR in isoform 3. 1 PublicationAdd BLAST82
Alternative sequenceiVSP_045248868 – 897Missing in isoform 3. 1 PublicationAdd BLAST30

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...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

The Consensus CDS (CCDS) project

More...CCDSi		CCDS11874.1 [Q99708-3]
CCDS11875.1 [Q99708-1]

NCBI Reference Sequences

More...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]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000327155.10; ENSP00000323050.5; ENSG00000101773.19
ENST00000399722.6; ENSP00000382628.2; ENSG00000101773.19
ENST00000399725.6; ENSP00000382630.2; ENSG00000101773.19 [Q99708-3]

Database of genes from NCBI RefSeq genomes

More...GeneIDi		5932

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:5932

Matched Annotation from NCBI and EMBL-EBI (MANE) - Phase one

More...MANE-Selecti		ENST00000327155.10; ENSP00000323050.5; NM_002894.3; NP_002885.1

UCSC genome browser

More...UCSCi		uc002ktw.4, human [Q99708-1]

Keywords - Coding sequence diversityi

Alternative splicing

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross%5Freferences%5Fsection">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>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_006722519.2 [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]

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2L4ZNMR-A641-685[»]
4D2HX-ray1.90A/B/C/D/E/F/G/H18-52[»]
7BGFX-ray2.80A/B31-152[»]
AlphaFoldDBiQ99708
SMRiQ99708
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi111867, 106 interactors
ComplexPortaliCPX-4441, BRCA1-C complex
CORUMiQ99708
DIPiDIP-24244N
ELMiQ99708
IntActiQ99708, 44 interactors
MINTiQ99708
STRINGi9606.ENSP00000382628

PTM databases

iPTMnetiQ99708
PhosphoSitePlusiQ99708

Genetic variation databases

BioMutaiRBBP8
DMDMi116242745

Proteomic databases

EPDiQ99708
jPOSTiQ99708
MassIVEiQ99708
MaxQBiQ99708
PaxDbiQ99708
PeptideAtlasiQ99708
PRIDEiQ99708
ProteomicsDBi1422
78424 [Q99708-1]
78425 [Q99708-2]

Protocols and materials databases

Antibodypedia a portal for validated antibodies

More...Antibodypediai		7316, 450 antibodies from 42 providers

The DNASU plasmid repository

More...DNASUi		5932

Genome annotation databases

EnsembliENST00000327155.10; ENSP00000323050.5; ENSG00000101773.19
ENST00000399722.6; ENSP00000382628.2; ENSG00000101773.19
ENST00000399725.6; ENSP00000382630.2; ENSG00000101773.19 [Q99708-3]
GeneIDi5932
KEGGihsa:5932
MANE-SelectiENST00000327155.10; ENSP00000323050.5; NM_002894.3; NP_002885.1
UCSCiuc002ktw.4, human [Q99708-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		5932
DisGeNETi5932

GeneCards: human genes, protein and diseases

More...GeneCardsi		RBBP8
HGNCiHGNC:9891, RBBP8
HPAiENSG00000101773, Low tissue specificity
MalaCardsiRBBP8
MIMi251255, phenotype
604124, gene
606744, phenotype
neXtProtiNX_Q99708
OpenTargetsiENSG00000101773
Orphaneti313795, Jawad syndrome
808, Seckel syndrome
PharmGKBiPA34255
VEuPathDBiHostDB:ENSG00000101773

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiENOG502QTV5, Eukaryota
GeneTreeiENSGT00530000063835
HOGENOMiCLU_019262_0_0_1
InParanoidiQ99708
OMAiFKIPLCP
PhylomeDBiQ99708
TreeFamiTF106469

Enzyme and pathway databases

PathwayCommonsiQ99708
ReactomeiR-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
R-HSA-9701192, Defective HDR through Homologous Recombination (HRR) due to BRCA1 loss-of-function
R-HSA-9704331, Defective HDR through Homologous Recombination Repair (HRR) due to PALB2 loss of BRCA1 binding function
R-HSA-9704646, Defective HDR through Homologous Recombination Repair (HRR) due to PALB2 loss of BRCA2/RAD51/RAD51C binding function
SignaLinkiQ99708
SIGNORiQ99708

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...BioGRID-ORCSi		5932, 660 hits in 1090 CRISPR screens

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...ChiTaRSi		RBBP8, human
EvolutionaryTraceiQ99708

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		RBBP8

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...GenomeRNAii		5932
PharosiQ99708, Tbio

Protein Ontology

More...PROi		PR:Q99708
RNActiQ99708, protein

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000101773, Expressed in testis and 222 other tissues
ExpressionAtlasiQ99708, baseline and differential
GenevisibleiQ99708, HS

Family and domain databases

IDEALiIID00340
InterProiView protein in InterPro
IPR019518, CtIP_N
IPR013882, Ctp1_C
IPR033594, RBBP8
IPR033316, RBBP8-like
PANTHERiPTHR15107, PTHR15107, 1 hit
PTHR15107:SF4, PTHR15107:SF4, 1 hit
PfamiView protein in Pfam
PF10482, CtIP_N, 1 hit
PF08573, SAE2, 1 hit

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiCTIP_HUMAN
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q99708
Secondary accession number(s): A6NKN2
, A8K8W6, E7ETY1, O75371, Q8NHQ3
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: October 17, 2006
Last modified: May 25, 2022
This is version 197 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>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.

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Reference proteome

Documents

  1. Human chromosome 18
    Human chromosome 18: entries, gene names and cross-references to MIM
  2. Human entries with genetic variants
    List of human entries with genetic variants
  3. Human variants curated from literature reports
    Index of human variants curated from literature reports
  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
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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