Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

X-ray repair cross-complementing protein 6

Gene

Xrcc6

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

Single-stranded DNA-dependent ATP-dependent helicase. Has a role in chromosome translocation. The DNA helicase II complex binds preferentially to fork-like ends of double-stranded DNA in a cell cycle-dependent manner. It works in the 3'-5' direction. Binding to DNA may be mediated by XRCC6. Involved in DNA non-homologous end joining (NHEJ) required for double-strand break repair and V(D)J recombination. The XRCC5/6 dimer acts as regulatory subunit of the DNA-dependent protein kinase complex DNA-PK by increasing the affinity of the catalytic subunit PRKDC to DNA by 100-fold. The XRCC5/6 dimer is probably involved in stabilizing broken DNA ends and bringing them together. The assembly of the DNA-PK complex to DNA ends is required for the NHEJ ligation step. Required for osteocalcin gene expression. Probably also acts as a 5'-deoxyribose-5-phosphate lyase (5'-dRP lyase), by catalyzing the beta-elimination of the 5' deoxyribose-5-phosphate at an abasic site near double-strand breaks. 5'-dRP lyase activity allows to 'clean' the termini of abasic sites, a class of nucleotide damage commonly associated with strand breaks, before such broken ends can be joined. The XRCC5/6 dimer together with APEX1 acts as a negative regulator of transcription. Plays a role in the regulation of DNA virus-mediated innate immune response by assembling into the HDP-RNP complex, a complex that serves as a platform for IRF3 phosphorylation and subsequent innate immune response activation through the cGAS-STING pathway (By similarity).By similarity1 Publication

Miscellaneous

In osteoblasts from XRCC6 knockout mice, osteocalcin gene expression is nearly abolished.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei29Schiff-base intermediate with DNA; for 5'-deoxyribose-5-phosphate lyase activityBy similarity1

<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 functionActivator, DNA-binding, Helicase, Hydrolase, Lyase, Multifunctional enzyme
Biological processDNA damage, DNA recombination, DNA repair, Immunity, Innate immunity, Transcription, Transcription regulation
LigandATP-binding, Nucleotide-binding

<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:
X-ray repair cross-complementing protein 6 (EC:3.6.4.-, EC:4.2.99.-)
Alternative name(s):
5'-deoxyribose-5-phosphate lyase Ku70
Short name:
5'-dRP/AP lyase Ku70
ATP-dependent DNA helicase 2 subunit 1
ATP-dependent DNA helicase II 70 kDa subunit
CTC box-binding factor 75 kDa subunit
Short name:
CTC75
Short name:
CTCBF
DNA repair protein XRCC6
Ku autoantigen protein p70 homolog
Short name:
Ku70
<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:Xrcc6
Synonyms:G22p1, Ku70
<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>OrganismiMus musculus (Mouse)
<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 identifieri10090 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
<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
  • UP000000589 <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: Unplaced

Organism-specific databases

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

More...
MGIi
MGI:95606 Xrcc6

<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 <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemovedBy similarity
<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_00002101802 – 608X-ray repair cross-complementing protein 6Add BLAST607

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 residuei2N-acetylserineBy similarity1
Modified residuei2PhosphoserineBy similarity1
Modified residuei6Phosphoserine; by PRKDCBy similarity1
Modified residuei29N6-acetyllysineBy similarity1
Modified residuei49Phosphoserine; by PRKDCBy similarity1
<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-linki315Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei329N6-acetyllysineBy similarity1
Modified residuei336N6-acetyllysineBy similarity1
Modified residuei459N6-acetyllysineBy similarity1
Modified residuei475PhosphoserineBy similarity1
Modified residuei518PhosphoserineBy similarity1
Modified residuei548PhosphoserineBy similarity1
Cross-linki554Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei558PhosphoserineBy similarity1

<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

Phosphorylation by PRKDC may enhance helicase activity. Phosphorylation of Ser-49 does not affect DNA repair (By similarity).By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
P23475

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P23475

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

More...
PaxDbi
P23475

PeptideAtlas

More...
PeptideAtlasi
P23475

PRoteomics IDEntifications database

More...
PRIDEi
P23475

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P23475

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

More...
PhosphoSitePlusi
P23475

<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 the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified ‘at the protein level’.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stagei

Expression increases during promyelocyte differentiation.1 Publication

<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

Heterodimer composed of XRCC5/Ku80 and XRCC6/Ku70. The dimer associates in a DNA-dependent manner with PRKDC to form the DNA-dependent protein kinase complex DNA-PK, and with the LIG4-XRCC4 complex to form the core of the non-homologous end joining (NHEJ) complex. Additional components of the NHEJ complex include NHEJ1/XLF and PAXX. The dimer also associates with NAA15, and this complex binds to the osteocalcin promoter and activates osteocalcin expression. In addition, XRCC6 interacts with the osteoblast-specific transcription factors MSX2, RUNX2 and DLX5. Interacts with ELF3. Interacts with ATP23. The XRCC5/6 dimer associates in a DNA-dependent manner with APEX1. Binds to CDK9 (By similarity). Identified in a complex with DEAF1 and XRCC5. Interacts with DEAF1 (via the SAND domain); the interaction is direct and may be inhibited by DNA-binding (By similarity). Interacts with CLU (PubMed:12551933). Interacts with NR4A3; the DNA-dependent protein kinase complex DNA-PK phosphorylates and activates NR4A3 and prevents NR4A3 ubiquitinylation and degradation (By similarity). Interacts with CYREN (By similarity). Interacts (via N-terminus) with HSF1 (via N-terminus); this interaction is direct and prevents XRCC5/XRCC6 heterodimeric binding and non-homologous end joining (NHEJ) repair activities induced by ionizing radiation (IR) (By similarity). Part of the HDP-RNP complex composed of at least HEXIM1, PRKDC, XRCC5, XRCC6, paraspeckle proteins (SFPQ, NONO, PSPC1, RBM14, and MATR3) and NEAT1 RNA (By similarity). Interacts with HMBOX1 (By similarity).By similarity1 Publication

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
199785, 10 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...
ComplexPortali
CPX-2047 Ku70:Ku80 complex

CORUM comprehensive resource of mammalian protein complexes

More...
CORUMi
P23475

Protein interaction database and analysis system

More...
IntActi
P23475, 7 interactors

Molecular INTeraction database

More...
MINTi
P23475

STRING: functional protein association networks

More...
STRINGi
10090.ENSMUSP00000068559

<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

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
P23475

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

More...
SMRi
P23475

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

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini259 – 466KuAdd BLAST208
Domaini571 – 605SAPPROSITE-ProRule annotationAdd BLAST35

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>Regioni548 – 607Interaction with DEAF1By similarityAdd BLAST60

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 amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi11 – 27Asp/Glu-rich (acidic)Add BLAST17
Compositional biasi328 – 340Asp/Glu-rich (acidic)Add BLAST13

<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 ku70 family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG2327 Eukaryota
ENOG410XNXU LUCA

The HOVERGEN Database of Homologous Vertebrate Genes

More...
HOVERGENi
HBG006236

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P23475

KEGG Orthology (KO)

More...
KOi
K10884

TreeFam database of animal gene trees

More...
TreeFami
TF315101

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.10.720.30, 1 hit
2.40.290.10, 1 hit
3.40.50.410, 1 hit
4.10.970.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR006165 Ku70
IPR006164 Ku70/Ku80_beta-barrel_dom
IPR027388 Ku70_bridge/pillars_dom_sf
IPR005160 Ku_C
IPR005161 Ku_N
IPR003034 SAP_dom
IPR036361 SAP_dom_sf
IPR016194 SPOC-like_C_dom_sf
IPR036465 vWFA_dom_sf

The PANTHER Classification System

More...
PANTHERi
PTHR12604:SF2 PTHR12604:SF2, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF02735 Ku, 1 hit
PF03730 Ku_C, 1 hit
PF03731 Ku_N, 1 hit
PF02037 SAP, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF003033 Ku70, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00559 Ku78, 1 hit
SM00513 SAP, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF100939 SSF100939, 1 hit
SSF53300 SSF53300, 1 hit
SSF68906 SSF68906, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR00578 ku70, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50800 SAP, 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.

<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 in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry has 1 described isoform and 5 potential isoforms that are computationally mapped.Show allAlign All

P23475-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSEWESYYKT EGEEEEEEEE SPDTGGEYKY SGRDSLIFLV DASRAMFESQ
60 70 80 90 100
GEDELTPFDM SIQCIQSVYT SKIISSDRDL LAVVFYGTEK DKNSVNFKNI
110 120 130 140 150
YVLQDLDNPG AKRVLELDQF KGQQGKKHFR DTVGHGSDYS LSEVLWVCAN
160 170 180 190 200
LFSDVQLKMS HKRIMLFTNE DDPHGRDSAK ASRARTKASD LRDTGIFLDL
210 220 230 240 250
MHLKKPGGFD VSVFYRDIIT TAEDEDLGVH FEESSKLEDL LRKVRAKETK
260 270 280 290 300
KRVLSRLKFK LGEDVVLMVG IYNLVQKANK PFPVRLYRET NEPVKTKTRT
310 320 330 340 350
FNVNTGSLLL PSDTKRSLTY GTRQIVLEKE ETEELKRFDE PGLILMGFKP
360 370 380 390 400
TVMLKKQHYL RPSLFVYPEE SLVSGSSTLF SALLTKCVEK KVIAVCRYTP
410 420 430 440 450
RKNVSPYFVA LVPQEEELDD QNIQVTPGGF QLVFLPYADD KRKVPFTEKV
460 470 480 490 500
TANQEQIDKM KAIVQKLRFT YRSDSFENPV LQQHFRNLEA LALDMMESEQ
510 520 530 540 550
VVDLTLPKVE AIKKRLGSLA DEFKELVYPP GYNPEGKVAK RKQDDEGSTS
560 570 580 590 600
KKPKVELSEE ELKAHFRKGT LGKLTVPTLK DICKAHGLKS GPKKQELLDA

LIRHLEKN
Length:608
Mass (Da):69,484
Last modified:February 5, 2008 - v5
<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:i1C27DBF1DB7A1154
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 5 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A0R4J187A0A0R4J187_MOUSE
X-ray repair cross-complementing pr...
Xrcc6
608Annotation score:

Annotation score:4 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>
A0A2R8VHZ9A0A2R8VHZ9_MOUSE
X-ray repair cross-complementing pr...
Xrcc6
263Annotation 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>
E9Q163E9Q163_MOUSE
X-ray repair cross-complementing pr...
Xrcc6
106Annotation 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>
E9PZD4E9PZD4_MOUSE
X-ray repair cross-complementing pr...
Xrcc6
97Annotation 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>
E9Q4A4E9Q4A4_MOUSE
X-ray repair cross-complementing pr...
Xrcc6
27Annotation 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>

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 conflicti225E → G in BAE27139 (PubMed:16141072).Curated1
Sequence conflicti225E → G in BAE27137 (PubMed:16141072).Curated1
Sequence conflicti225E → G in BAE27135 (PubMed:16141072).Curated1
Sequence conflicti391K → E in BAE25441 (PubMed:11471062).Curated1
Sequence conflicti391K → E in AAL90775 (PubMed:11471062).Curated1
Sequence conflicti391K → E in AAL90774 (PubMed:11471062).Curated1
Sequence conflicti400P → H in AAA39396 (PubMed:1701785).Curated1
Sequence conflicti466 – 467KL → NV in AAC52675 (PubMed:8661113).Curated2
Sequence conflicti466 – 467KL → NV in AAA39396 (PubMed:1701785).Curated2

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
U50378
, U50367, U50368, U50369, U50370, U50371, U50372, U50373, U50374, U50375, U50376, U50377 Genomic DNA Translation: AAC52675.1
U34878 Genomic DNA Translation: AAC53575.1
AB010282 mRNA Translation: BAA28874.1
AF483500 mRNA Translation: AAL90774.1
AF483501 mRNA Translation: AAL90775.1
AK143570 mRNA Translation: BAE25441.1
AK146392 mRNA Translation: BAE27135.1
AK146394 mRNA Translation: BAE27137.1
AK146396 mRNA Translation: BAE27139.1
BC031422 mRNA Translation: AAH31422.1
Z14157 mRNA Translation: CAA78526.1
M38700 mRNA Translation: AAA39396.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS37153.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A43534
S25149

NCBI Reference Sequences

More...
RefSeqi
NP_034377.2, NM_010247.2
XP_006520505.1, XM_006520442.3
XP_006520506.1, XM_006520443.3
XP_011243758.1, XM_011245456.2

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Mm.288809

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
14375

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
mmu:14375

UCSC genome browser

More...
UCSCi
uc007wxy.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
U50378
, U50367, U50368, U50369, U50370, U50371, U50372, U50373, U50374, U50375, U50376, U50377 Genomic DNA Translation: AAC52675.1
U34878 Genomic DNA Translation: AAC53575.1
AB010282 mRNA Translation: BAA28874.1
AF483500 mRNA Translation: AAL90774.1
AF483501 mRNA Translation: AAL90775.1
AK143570 mRNA Translation: BAE25441.1
AK146392 mRNA Translation: BAE27135.1
AK146394 mRNA Translation: BAE27137.1
AK146396 mRNA Translation: BAE27139.1
BC031422 mRNA Translation: AAH31422.1
Z14157 mRNA Translation: CAA78526.1
M38700 mRNA Translation: AAA39396.1
CCDSiCCDS37153.1
PIRiA43534
S25149
RefSeqiNP_034377.2, NM_010247.2
XP_006520505.1, XM_006520442.3
XP_006520506.1, XM_006520443.3
XP_011243758.1, XM_011245456.2
UniGeneiMm.288809

3D structure databases

ProteinModelPortaliP23475
SMRiP23475
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi199785, 10 interactors
ComplexPortaliCPX-2047 Ku70:Ku80 complex
CORUMiP23475
IntActiP23475, 7 interactors
MINTiP23475
STRINGi10090.ENSMUSP00000068559

PTM databases

iPTMnetiP23475
PhosphoSitePlusiP23475

Proteomic databases

EPDiP23475
MaxQBiP23475
PaxDbiP23475
PeptideAtlasiP23475
PRIDEiP23475

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi14375
KEGGimmu:14375
UCSCiuc007wxy.1 mouse

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
2547
MGIiMGI:95606 Xrcc6

Phylogenomic databases

eggNOGiKOG2327 Eukaryota
ENOG410XNXU LUCA
HOVERGENiHBG006236
InParanoidiP23475
KOiK10884
TreeFamiTF315101

Miscellaneous databases

Protein Ontology

More...
PROi
PR:P23475

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Family and domain databases

Gene3Di1.10.720.30, 1 hit
2.40.290.10, 1 hit
3.40.50.410, 1 hit
4.10.970.10, 1 hit
InterProiView protein in InterPro
IPR006165 Ku70
IPR006164 Ku70/Ku80_beta-barrel_dom
IPR027388 Ku70_bridge/pillars_dom_sf
IPR005160 Ku_C
IPR005161 Ku_N
IPR003034 SAP_dom
IPR036361 SAP_dom_sf
IPR016194 SPOC-like_C_dom_sf
IPR036465 vWFA_dom_sf
PANTHERiPTHR12604:SF2 PTHR12604:SF2, 1 hit
PfamiView protein in Pfam
PF02735 Ku, 1 hit
PF03730 Ku_C, 1 hit
PF03731 Ku_N, 1 hit
PF02037 SAP, 1 hit
PIRSFiPIRSF003033 Ku70, 1 hit
SMARTiView protein in SMART
SM00559 Ku78, 1 hit
SM00513 SAP, 1 hit
SUPFAMiSSF100939 SSF100939, 1 hit
SSF53300 SSF53300, 1 hit
SSF68906 SSF68906, 1 hit
TIGRFAMsiTIGR00578 ku70, 1 hit
PROSITEiView protein in PROSITE
PS50800 SAP, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
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 nameiXRCC6_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: P23475
Secondary accession number(s): O88212
, Q3UJL8, Q62027, Q62382, Q62453, Q6GTV8, Q8QZX7
<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: November 1, 1991
Last sequence update: February 5, 2008
Last modified: November 7, 2018
This is version 177 of the entry and version 5 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
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again