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Protein

DNA endonuclease RBBP8

Gene

Rbbp8

Organism
Rattus norvegicus (Rat)
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 transcript 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 (By similarity). 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 similarity

<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-RNO-5685938 HDR through Single Strand Annealing (SSA)
R-RNO-5685939 HDR through MMEJ (alt-NHEJ)
R-RNO-5685942 HDR through Homologous Recombination (HRR)
R-RNO-5693554 Resolution of D-loop Structures through Synthesis-Dependent Strand Annealing (SDSA)
R-RNO-5693568 Resolution of D-loop Structures through Holliday Junction Intermediates
R-RNO-5693579 Homologous DNA Pairing and Strand Exchange
R-RNO-5693607 Processing of DNA double-strand break ends
R-RNO-5693616 Presynaptic phase of homologous DNA pairing and strand exchange
R-RNO-6804756 Regulation of TP53 Activity through Phosphorylation
R-RNO-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_and_taxonomy_section">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_and_taxonomy_section">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_and_taxonomy_section">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>OrganismiRattus norvegicus (Rat)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 identifieri10116 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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
  • UP000002494 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">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

Rat genome database

More...
RGDi
1308872 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; 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.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00004170371 – 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_processing_section">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-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 residuei233PhosphoserineBy similarity1
Modified residuei276PhosphoserineBy similarity1
Modified residuei325PhosphoserineBy similarity1
Modified residuei326PhosphoserineBy similarity1
Modified residuei348PhosphoserineBy similarity1
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-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 residuei720PhosphoserineBy similarity1
Modified residuei742Phosphoserine; by ATMBy similarity1
Cross-linki778Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei843Phosphothreonine; by CDK1By 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_processing_section">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

Acetylated. Deacetylation by SIRT6 upon DNA damage promotes DNA end resection.By similarity
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 on 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 Ser-276 may serve as a PIN1 isomerization site (By similarity).By similarity
Ubiquitinated. Ubiquitination at multiple sites by BRCA1 (via its N-terminal RING domain) does not lead to its proteosomal degradation but instead the ubiquitinated RBBP8 binds to chromatin following DNA damage and may play a role in G2/M checkpoint control. Ubiquitinated by RNF138 at its N-terminus. Ubiquitinated through 'Lys-48' by the E3 CUL3-KLHL15 complex; this modification leads to proteasomal degradation (By similarity). Ubiquitinated by the E3 FZR1/APC/C complex; this modification leads to proteasomal degradation (By similarity).By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

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

More...
PaxDbi
B1WC58

PRoteomics IDEntifications database

More...
PRIDEi
B1WC58

<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
ENSRNOG00000012899 Expressed in 9 organ(s), highest expression level in lung

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
B1WC58 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
B1WC58 RN

<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_section">'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_section">'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. 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

STRING: functional protein association networks

More...
STRINGi
10116.ENSRNOP00000017291

<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
B1WC58

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
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 – 147Sequence analysisAdd BLAST94

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
ENOG410IJ39 Eukaryota
ENOG410ZSBE LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00530000063835

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000293331

The HOVERGEN Database of Homologous Vertebrate Genes

More...
HOVERGENi
HBG057046

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
B1WC58

KEGG Orthology (KO)

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KOi
K20773

Identification of Orthologs from Complete Genome Data

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OMAi
NPCRIAK

Database of Orthologous Groups

More...
OrthoDBi
EOG091G0QP3

Database for complete collections of gene phylogenies

More...
PhylomeDBi
B1WC58

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

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_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<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_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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 1 potential isoform that is computationally mapped.Show allAlign All

B1WC58-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSISGSSCGS PNSTDISSDF KELWTKLKEY HDKEVQGLQI KVTKLKKERI
60 70 80 90 100
LDAQRLEEFF TKNQQLRDQQ KVLQETIKIL EDRLRAGLCD RCAVTEEHMH
110 120 130 140 150
KKQQEFENIR QQNLRLITEL MNEKSALQEE NKKLSEQLQQ KMESGQQDQV
160 170 180 190 200
AELECEENII PDSPITSFSF SGINRLRRKE NLHVRYVEQT HTKLEHSACT
210 220 230 240 250
SELRKFSKGS TPAPVNSEEH EILVADTCDQ SHSPLSKICG TSSYPADKLS
260 270 280 290 300
SNLDAVVAET LGLDGQEESE PQGPVSPLGN ELYHCLKEDH KKQPFMESAI
310 320 330 340 350
RNEDNVRFSD SASKAPPREL TTRGSSPVFG PTSTVKTHLG LKTSFSPSLL
360 370 380 390 400
DSGKKNLLST APFSSISVSR SEKVRSKSED NALFTQQSAG SEVKVISQSF
410 420 430 440 450
PSKQILTSKN VSDSVDEQGG ADHMKDAVSD KHLVPLKSLG GKASKRKRTE
460 470 480 490 500
EEGEHAVHCP QTCFDKENAL PFPMENQFPV NGDHVMDKPL DLSDRFAANQ
510 520 530 540 550
RQEKNHGDET CKHKLKQVTI YEALKPVPKG SSSGRKALSG ACTLAQDSAE
560 570 580 590 600
TYCLQQRTLQ CSSKFSPDHN TQLQIKEENP VFKTPPRSQE SLETENLFGD
610 620 630 640 650
VKGIGSLVPI KVKGRSAHGG CELASVLQLN PCRVAKTKSL PSNHDMSFEN
660 670 680 690 700
IQWSVDPGAD LSQYKMDVTV IDTKDSSHSR LGGETVDMDC TLVSETMLLK
710 720 730 740 750
MKKQEQREKS PNGDIKMNDS LEDMFDRTTH EEYESCLADN FSQVPDEEEL
760 770 780 790 800
SDTTKKPNIH GDKQDGIKQK AFVEPYFKDK ERETSIQNFP HIEVVRKKEE
810 820 830 840 850
RRKLLGHTCK ECEIYYADLP AEEREKKLAS CSRHRFRYIP TNTPENFWEV
860 870 880 890
GFPSTQTCLE RGYIKEDLDP CPRPKRRQPY NAVFSPKGKE QRT
Length:893
Mass (Da):100,705
Last modified:May 20, 2008 - 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:i57A4189635AA5F9B
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 is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A0G2JVQ4A0A0G2JVQ4_RAT
DNA endonuclease RBBP8
Rbbp8
775Annotation 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

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
BC162012 mRNA Translation: AAI62012.1

NCBI Reference Sequences

More...
RefSeqi
NP_001127889.1, NM_001134417.1
XP_008770161.2, XM_008771939.2

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Rn.128724

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSRNOT00000017291; ENSRNOP00000017291; ENSRNOG00000012899

Database of genes from NCBI RefSeq genomes

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GeneIDi
291787

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
rno:291787

UCSC genome browser

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UCSCi
RGD:1308872 rat

<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
BC162012 mRNA Translation: AAI62012.1
RefSeqiNP_001127889.1, NM_001134417.1
XP_008770161.2, XM_008771939.2
UniGeneiRn.128724

3D structure databases

SMRiB1WC58
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000017291

Proteomic databases

PaxDbiB1WC58
PRIDEiB1WC58

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000017291; ENSRNOP00000017291; ENSRNOG00000012899
GeneIDi291787
KEGGirno:291787
UCSCiRGD:1308872 rat

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
5932
RGDi1308872 Rbbp8

Phylogenomic databases

eggNOGiENOG410IJ39 Eukaryota
ENOG410ZSBE LUCA
GeneTreeiENSGT00530000063835
HOGENOMiHOG000293331
HOVERGENiHBG057046
InParanoidiB1WC58
KOiK20773
OMAiNPCRIAK
OrthoDBiEOG091G0QP3
PhylomeDBiB1WC58
TreeFamiTF106469

Enzyme and pathway databases

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

Miscellaneous databases

Protein Ontology

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PROi
PR:B1WC58

Gene expression databases

BgeeiENSRNOG00000012899 Expressed in 9 organ(s), highest expression level in lung
ExpressionAtlasiB1WC58 baseline and differential
GenevisibleiB1WC58 RN

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
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<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_RAT
<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: B1WC58
<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_and_isoforms">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: May 20, 2008
Last modified: December 5, 2018
This is version 85 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

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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