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Entry version 138 (12 Aug 2020)
Sequence version 1 (01 Jun 2003)
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Protein

DNA endonuclease RBBP8

Gene

Rbbp8

Organism
Mus musculus (Mouse)
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. 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. During immunoglobulin heavy chain class-switch recombination, promotes microhomology-mediated alternative end joining (A-NHEJ) and plays an essential role in chromosomal translocations.3 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

GO - Biological processi

<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

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-MMU-5685938, HDR through Single Strand Annealing (SSA)
R-MMU-5685939, HDR through MMEJ (alt-NHEJ)
R-MMU-5685942, HDR through Homologous Recombination (HRR)
R-MMU-5693554, Resolution of D-loop Structures through Synthesis-Dependent Strand Annealing (SDSA)
R-MMU-5693568, Resolution of D-loop Structures through Holliday Junction Intermediates
R-MMU-5693579, Homologous DNA Pairing and Strand Exchange
R-MMU-5693607, Processing of DNA double-strand break ends
R-MMU-5693616, Presynaptic phase of homologous DNA pairing and strand exchange
R-MMU-6804756, Regulation of TP53 Activity through Phosphorylation
R-MMU-69473, G2/M DNA damage checkpoint

<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>OrganismiMus musculus (Mouse)
<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 identifieri10090 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
<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
  • UP000000589 <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

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

More...
MGIi
MGI:2442995, Rbbp8

<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

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Chromosome, Nucleus

<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_00004170361 – 893DNA endonuclease RBBP8Add BLAST893

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)By similarity
Cross-linki115Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki193Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
<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 residuei276PhosphoserineBy similarity1
Modified residuei315PhosphothreonineBy similarity1
Modified residuei325PhosphoserineBy similarity1
Modified residuei326PhosphoserineBy similarity1
Modified residuei348PhosphoserineBy similarity1
Cross-linki359Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki377Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei378PhosphoserineBy similarity1
Cross-linki394Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki403Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki409Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei431N6-acetyllysineBy similarity1
Cross-linki437Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei525N6-acetyllysine; alternateBy similarity1
Cross-linki525Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Cross-linki529Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki570Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki576Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei602N6-acetyllysine; alternateBy similarity1
Cross-linki602Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Cross-linki611Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki636Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki638Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei662Phosphoserine; by ATMBy similarity1
Cross-linki674Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei677PhosphoserineBy similarity1
Cross-linki716Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei720PhosphoserineCombined sources1
Modified residuei742Phosphoserine; by ATMBy similarity1
Cross-linki778Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei843PhosphothreonineBy similarity1
Cross-linki865Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity

<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-843 by CDK1 is essential for the recruitment to DNA and the DNA repair function. Phosphorylated at Ser-326 as cells enter G2 phase. This phosphorylation is required for binding BRCA1 and for the G2/M DNA damage transition checkpoint control (By similarity). Phosphorylation at Thr-315 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 (By similarity).By similarity
Acetylated. Deacetylation by SIRT6 upon DNA damage promotes DNA end resection.By similarity
Ubiquitinated. 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. Ubiquitinated by RNF138 at its N-terminus. Ubiquitinated through 'Lys-48' by the E3 CUL3-KLHL15 complex; this modification leads to proteasomal degradation. Ubiquitinated by the E3 FZR1/APC/C complex; this modification leads to proteasomal degradation.By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
Q80YR6

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
Q80YR6

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

More...
PaxDbi
Q80YR6

PRoteomics IDEntifications database

More...
PRIDEi
Q80YR6

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q80YR6

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

More...
PhosphoSitePlusi
Q80YR6

<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

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSMUSG00000041238, Expressed in urothelium and 243 other tissues

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
Q80YR6, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
Q80YR6, MM

<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.

Interacts (via the PXDLS motif) with CTBP1; the interaction is disrupted via binding of the adenovirus E1A to CTBP1.

Component of the BRCA1-RBBP8 complex.

Interacts (the Ser-326 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 MRE11; 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).

Interacts with SIAH1.

Interacts with RNF138.

Interacts with EXD2.

Interacts with CUL3 and KLHL15; this interaction leads to RBBP8 proteasomal degradation. Directly interacts with PIN1; this interaction depends upon RBBP8 phosphorylation, predominantly at Thr-315.

Interacts with FZR1; this interaction leads to APC/C-mediated RBBP8 proteasomal degradation.

Interacts with AUNIP; leading to recruit RBBP8 to sites of DNA damage.

Interacts with SAMHD1.

By similarity

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
230366, 6 interactors

ComplexPortal: manually curated resource of macromolecular complexes

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ComplexPortali
CPX-4722, BRCA1-C complex

Protein interaction database and analysis system

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IntActi
Q80YR6, 1 interactor

STRING: functional protein association networks

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STRINGi
10090.ENSMUSP00000046255

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...
RNActi
Q80YR6, 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

3D structure databases

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

More...
SMRi
Q80YR6

Database of comparative protein structure models

More...
ModBasei
Search...

<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 damageBy similarityAdd BLAST24
Regioni489 – 493PXDLS motif5
Regioni508 – 556Damage-recruitment motifBy similarityAdd BLAST49

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 coili54 – 149Sequence analysisAdd BLAST96

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>Motifi836 – 838KLHL15-bindingBy similarity3

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

<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

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GeneTreei
ENSGT00530000063835

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_019262_0_0_1

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q80YR6

KEGG Orthology (KO)

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KOi
K20773

Identification of Orthologs from Complete Genome Data

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OMAi
PCRIAKT

Database of Orthologous Groups

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OrthoDBi
962036at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q80YR6

TreeFam database of animal gene trees

More...
TreeFami
TF106469

Family and domain databases

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

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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>Sequence (1+)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 has 1 described isoform and 4 potential isoforms that are computationally mapped.Show allAlign All

Q80YR6-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSISGSGCGS PNSADASNDF KELWTKLKEY HDKEVQGLQV KVTKLKKERI
60 70 80 90 100
LDAQRLEEFF TKNQQLRDQQ KVLQETIKIL EDRLRAGLCD RCAVTEEHMH
110 120 130 140 150
KKQQEFENIR QQNLKLITEL MNEKNTLQEE NKKLSEQLQQ KMENGQQDQV
160 170 180 190 200
AELACEENII PDSPVTSFSF SGINRLRKKE NLHVRYVEQT HTKLERSLCT
210 220 230 240 250
NELRKISKDS APAPVNSEEH EILVADTCDQ NHSPLSKICE TSSYPTDKTS
260 270 280 290 300
FNLDTVVAET LGLNGQEESE PQGPMSPLGS ELYHCLKEDH KKHPFMESAR
310 320 330 340 350
SKEDSLRFSD SASKTPPQEF TTRASSPVFG ATSTVKAHLG LNTSFSPSLL
360 370 380 390 400
DIGKKNLLKT APFSNIAVSR SEKVRSKSED NALFTQHSLG SEVKVISQSF
410 420 430 440 450
SSKQILTNKT VSDSVDEQCS ADHMNTTVAD KYLVPLKSLG GKASKRKRTE
460 470 480 490 500
EESEHAVKCP QACFDKENAL PFPMENQFSM NGDHVMDKPL DLSDRFAATQ
510 520 530 540 550
RQEKNHGNET SKNKLKQATI YEALKPIPKG SSSGRKALSG DCMPAKDSWE
560 570 580 590 600
TYCLQPRSLQ SSSKFSPDQK TPLQIKEENP VFKTPPCSQE SLETENLFGD
610 620 630 640 650
VKGTGSLVPT KVKSRAVHGG CELASVLQLN PCRVAKTKAL PSNQDTSFEN
660 670 680 690 700
IQWSVDPGAD LSQYKMDVTV IDTKDSSHSR LGGETVDMDC TLVSETVLLK
710 720 730 740 750
MKKQEQKERS PNGDIKMNDS LEDMFDRTTH EEYESCLADS FSQVPDEEEL
760 770 780 790 800
PDTTKKTNIP ADKQDGVKQK AFVGPYFKDK ERETSIQNFP HIEVVRKKEE
810 820 830 840 850
RRKLLGHTCK ECEIYYADLP AEEREKKLAS CSRHRFRYIP PNTPENFWEV
860 870 880 890
GFPSTQTCLE RGYIKEDLDL SPRPKRRQPY NAVFSPKGKE QRT
Length:893
Mass (Da):100,831
Last modified:June 1, 2003 - v1
<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:i2F363F88D2190F13
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 4 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A3Q4EGK0A0A3Q4EGK0_MOUSE
DNA endonuclease RBBP8
Rbbp8
612Annotation 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>
A0A3Q4EGL1A0A3Q4EGL1_MOUSE
DNA endonuclease RBBP8
Rbbp8
247Annotation 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>
A0A3Q4L2U0A0A3Q4L2U0_MOUSE
DNA endonuclease RBBP8
Rbbp8
118Annotation 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>
A0A3Q4EBX2A0A3Q4EBX2_MOUSE
DNA endonuclease RBBP8
Rbbp8
26Annotation 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>

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
AC090479 Genomic DNA No translation available.
AC115894 Genomic DNA No translation available.
BC050849 mRNA Translation: AAH50849.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS37738.1

NCBI Reference Sequences

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RefSeqi
NP_001074692.1, NM_001081223.2
NP_001239424.1, NM_001252495.1
XP_006525875.1, XM_006525812.3

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENSMUST00000047322; ENSMUSP00000046255; ENSMUSG00000041238
ENSMUST00000115861; ENSMUSP00000111527; ENSMUSG00000041238

Database of genes from NCBI RefSeq genomes

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GeneIDi
225182

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
mmu:225182

UCSC genome browser

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UCSCi
uc008ebl.1, mouse

<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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC090479 Genomic DNA No translation available.
AC115894 Genomic DNA No translation available.
BC050849 mRNA Translation: AAH50849.1
CCDSiCCDS37738.1
RefSeqiNP_001074692.1, NM_001081223.2
NP_001239424.1, NM_001252495.1
XP_006525875.1, XM_006525812.3

3D structure databases

SMRiQ80YR6
ModBaseiSearch...

Protein-protein interaction databases

BioGRIDi230366, 6 interactors
ComplexPortaliCPX-4722, BRCA1-C complex
IntActiQ80YR6, 1 interactor
STRINGi10090.ENSMUSP00000046255

PTM databases

iPTMnetiQ80YR6
PhosphoSitePlusiQ80YR6

Proteomic databases

EPDiQ80YR6
jPOSTiQ80YR6
PaxDbiQ80YR6
PRIDEiQ80YR6

Protocols and materials databases

Antibodypedia a portal for validated antibodies

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Antibodypediai
7316, 426 antibodies

Genome annotation databases

EnsembliENSMUST00000047322; ENSMUSP00000046255; ENSMUSG00000041238
ENSMUST00000115861; ENSMUSP00000111527; ENSMUSG00000041238
GeneIDi225182
KEGGimmu:225182
UCSCiuc008ebl.1, mouse

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
5932
MGIiMGI:2442995, Rbbp8

Phylogenomic databases

eggNOGiENOG502QTV5, Eukaryota
GeneTreeiENSGT00530000063835
HOGENOMiCLU_019262_0_0_1
InParanoidiQ80YR6
KOiK20773
OMAiPCRIAKT
OrthoDBi962036at2759
PhylomeDBiQ80YR6
TreeFamiTF106469

Enzyme and pathway databases

ReactomeiR-MMU-5685938, HDR through Single Strand Annealing (SSA)
R-MMU-5685939, HDR through MMEJ (alt-NHEJ)
R-MMU-5685942, HDR through Homologous Recombination (HRR)
R-MMU-5693554, Resolution of D-loop Structures through Synthesis-Dependent Strand Annealing (SDSA)
R-MMU-5693568, Resolution of D-loop Structures through Holliday Junction Intermediates
R-MMU-5693579, Homologous DNA Pairing and Strand Exchange
R-MMU-5693607, Processing of DNA double-strand break ends
R-MMU-5693616, Presynaptic phase of homologous DNA pairing and strand exchange
R-MMU-6804756, Regulation of TP53 Activity through Phosphorylation
R-MMU-69473, G2/M DNA damage checkpoint

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

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BioGRID-ORCSi
225182, 4 hits in 19 CRISPR screens

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

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ChiTaRSi
Rbbp8, mouse

Protein Ontology

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PROi
PR:Q80YR6
RNActiQ80YR6, protein

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
Search...

Gene expression databases

BgeeiENSMUSG00000041238, Expressed in urothelium and 243 other tissues
ExpressionAtlasiQ80YR6, baseline and differential
GenevisibleiQ80YR6, MM

Family and domain databases

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

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

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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_MOUSE
<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: Q80YR6
<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: May 16, 2012
Last sequence update: June 1, 2003
Last modified: August 12, 2020
This is version 138 of the entry and version 1 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

<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

Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families
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