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Protein

X-ray repair cross-complementing protein 5

Gene

XRCC5

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

Annotation score:5 out of 5

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

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

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 (PubMed:12145306, PubMed:20383123, PubMed:7957065, PubMed:8621488). The assembly of the DNA-PK complex to DNA ends is required for the NHEJ ligation step. In association with NAA15, the XRCC5/6 dimer binds to the osteocalcin promoter and activates osteocalcin expression (PubMed:20383123). The XRCC5/6 dimer 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. XRCC5 probably acts as the catalytic subunit of 5'-dRP activity, and 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 (PubMed:8621488). 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.5 Publications

Miscellaneous

Individuals with systemic lupus erythematosus (SLE) and related disorders produce extremely large amounts of autoantibodies to XRCC6 and XRCC5.1 Publication

<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

  • ATP binding Source: UniProtKB-KW
  • ATP-dependent DNA helicase activity Source: ProtInc
  • damaged DNA binding Source: InterPro
  • DNA binding Source: UniProtKB
  • double-stranded DNA binding Source: ProtInc
  • enzyme activator activity Source: BHF-UCL
  • protein-containing complex binding Source: BHF-UCL
  • protein C-terminus binding Source: UniProtKB
  • RNA binding Source: UniProtKB
  • telomeric DNA binding Source: BHF-UCL
  • transcription regulatory region DNA binding Source: BHF-UCL
  • ubiquitin protein ligase binding Source: UniProtKB

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
Biological processDNA damage, DNA recombination, DNA repair, Immunity, Innate immunity, Transcription, Transcription regulation
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-164843 2-LTR circle formation
R-HSA-1834949 Cytosolic sensors of pathogen-associated DNA
R-HSA-3270619 IRF3-mediated induction of type I IFN
R-HSA-5693571 Nonhomologous End-Joining (NHEJ)
R-HSA-6798695 Neutrophil degranulation

SIGNOR Signaling Network Open Resource

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SIGNORi
P13010

Protein family/group databases

MoonDB Database of extreme multifunctional and moonlighting proteins

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MoonDBi
P13010 Curated

<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 5 (EC:3.6.4.-)
Alternative name(s):
86 kDa subunit of Ku antigen
ATP-dependent DNA helicase 2 subunit 2
ATP-dependent DNA helicase II 80 kDa subunit
CTC box-binding factor 85 kDa subunit
Short name:
CTC85
Short name:
CTCBF
DNA repair protein XRCC5
Ku80
Ku86
Lupus Ku autoantigen protein p86
Nuclear factor IV
Thyroid-lupus autoantigen
Short name:
TLAA
X-ray repair complementing defective repair in Chinese hamster cells 5 (double-strand-break rejoining)
<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:XRCC5
Synonyms:G22P2
<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>OrganismiHomo sapiens (Human)
<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 identifieri9606 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<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
  • UP000005640 <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 2

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000079246.15

Human Gene Nomenclature Database

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HGNCi
HGNC:12833 XRCC5

Online Mendelian Inheritance in Man (OMIM)

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MIMi
194364 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_P13010

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

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi720 – 721EE → AA: Abolishes interaction with PRKDC and its recruitment to sites of DNA damage. 1 Publication2
Mutagenesisi726 – 727DD → AA: Abolishes interaction with PRKDC and its recruitment to sites of DNA damage. 1 Publication2

Keywords - Diseasei

Systemic lupus erythematosus

Organism-specific databases

DisGeNET

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DisGeNETi
7520

Open Targets

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OpenTargetsi
ENSG00000079246

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA37425

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
XRCC5

Domain mapping of disease mutations (DMDM)

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DMDMi
125731

<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 methionineiRemoved2 Publications
<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_00000843402 – 732X-ray repair cross-complementing protein 5Add BLAST731

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 residuei144N6-acetyllysineCombined sources1
<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-linki195Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei255PhosphoserineCombined sources1
Modified residuei258PhosphoserineCombined sources1
Modified residuei265N6-acetyllysineCombined sources1
Modified residuei318PhosphoserineCombined sources1
Modified residuei332N6-acetyllysineCombined sources1
Cross-linki532Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki534Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei535PhosphothreonineCombined sources1
Cross-linki566Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki568Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei577Phosphoserine; by PRKDCCombined sources1 Publication1
Modified residuei579Phosphoserine; by PRKDC1 Publication1
Modified residuei580Phosphoserine; by PRKDC1 Publication1
Modified residuei660N6-acetyllysineCombined sources1
Modified residuei665N6-acetyllysineCombined sources1
Cross-linki669Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki688Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei715Phosphothreonine; by PRKDC1 Publication1

<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

Phosphorylated on serine residues. Phosphorylation by PRKDC may enhance helicase activity.1 Publication
Sumoylated.1 Publication
Ubiquitinated by RNF8 via 'Lys-48'-linked ubiquitination following DNA damage, leading to its degradation and removal from DNA damage sites (PubMed:22266820). Ubiquitinated by RNF138, leading to remove the Ku complex from DNA breaks (PubMed:26502055).2 Publications

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
P13010

MaxQB - The MaxQuant DataBase

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MaxQBi
P13010

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

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PaxDbi
P13010

PeptideAtlas

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PeptideAtlasi
P13010

PRoteomics IDEntifications database

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PRIDEi
P13010

ProteomicsDB human proteome resource

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ProteomicsDBi
52890

2D gel databases

Two-dimensional polyacrylamide gel electrophoresis database from the Geneva University Hospital

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SWISS-2DPAGEi
P13010

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P13010

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

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PhosphoSitePlusi
P13010

SwissPalm database of S-palmitoylation events

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SwissPalmi
P13010

Miscellaneous databases

CutDB - Proteolytic event database

More...
PMAP-CutDBi
P13010

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

In osteoblasts, by FGF2.

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000079246 Expressed in 232 organ(s), highest expression level in kidney

CleanEx database of gene expression profiles

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CleanExi
HS_XRCC5

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P13010 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P13010 HS

Organism-specific databases

Human Protein Atlas

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HPAi
CAB004468
HPA025813
HPA064685

<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 (PubMed:25941166, PubMed:25670504, PubMed:11493912, PubMed:22442688). Additional components of the NHEJ complex include NHEJ1/XLF and PAXX (PubMed:25574025, PubMed:25941166, PubMed:25670504). The dimer also associates with NAA15, and this complex displays DNA binding activity towards the osteocalcin FGF response element (OCFRE) (PubMed:12145306). In addition, XRCC5 binds to the osteoblast-specific transcription factors MSX2 and RUNX2 (PubMed:12145306). Interacts with ELF3 (PubMed:15075319). May interact with APLF (PubMed:17353262, PubMed:17396150). The XRCC5/XRCC6 dimer associates in a DNA-dependent manner with APEX1 (PubMed:8621488). Identified in a complex with DEAF1 and XRCC6. Interacts with NR4A3; the DNA-dependent protein kinase complex DNA-PK phosphorylates and activates NR4A3 and prevents NR4A3 ubiquitinylation and degradation (PubMed:25852083). Interacts with RNF138 (PubMed:26502055). Interacts with CYREN isoform 1 (CYREN-1) and isoform 4 (CYREN-2) (PubMed:24610814, PubMed:28959974). 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) (PubMed:26359349). Interacts with DHX9; this interaction occurs in a RNA-dependent manner (PubMed:14704337). 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 (PubMed:28712728).17 Publications
(Microbial infection) Interacts with human T-cell leukemia virus 1/HTLV-1 protein HBZ.1 Publication

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
113353, 247 interactors

ComplexPortal: manually curated resource of macromolecular complexes

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ComplexPortali
CPX-1993 Ku70:Ku80 complex

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
P13010

Database of interacting proteins

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DIPi
DIP-31379N

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

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ELMi
P13010

Protein interaction database and analysis system

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IntActi
P13010, 115 interactors

Molecular INTeraction database

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MINTi
P13010

STRING: functional protein association networks

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STRINGi
9606.ENSP00000375977

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

Secondary structure

1732
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P13010

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

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SMRi
P13010

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
P13010

<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>Domaini251 – 460KuAdd BLAST210

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>Regioni138 – 165Leucine-zipperAdd BLAST28

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>Motifi720 – 728EEXXXDL motif9

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 biasi478 – 519Pro-richAdd BLAST42

<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 EEXXXDDL motif is required for the interaction with catalytic subunit PRKDC and its recruitment to sites of DNA damage.1 Publication

<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 ku80 family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG2326 Eukaryota
ENOG410YKH9 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000153239

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG006237

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P13010

KEGG Orthology (KO)

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KOi
K10885

Identification of Orthologs from Complete Genome Data

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OMAi
YRFPPLD

Database of Orthologous Groups

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OrthoDBi
EOG091G11VD

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P13010

TreeFam database of animal gene trees

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TreeFami
TF101205

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
1.25.40.240, 1 hit
2.40.290.10, 1 hit
3.40.50.410, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR006164 Ku70/Ku80_beta-barrel_dom
IPR024193 Ku80
IPR005160 Ku_C
IPR036494 Ku_C_sf
IPR005161 Ku_N
IPR014893 Ku_PK_bind
IPR016194 SPOC-like_C_dom_sf
IPR002035 VWF_A
IPR036465 vWFA_dom_sf

The PANTHER Classification System

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PANTHERi
PTHR12604:SF4 PTHR12604:SF4, 1 hit

Pfam protein domain database

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Pfami
View protein in Pfam
PF02735 Ku, 1 hit
PF03730 Ku_C, 1 hit
PF03731 Ku_N, 1 hit
PF08785 Ku_PK_bind, 1 hit

PIRSF; a whole-protein classification database

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PIRSFi
PIRSF016570 Ku80, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00559 Ku78, 1 hit
SM00327 VWA, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF100939 SSF100939, 1 hit
SSF101420 SSF101420, 1 hit
SSF53300 SSF53300, 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 2 potential isoforms that are computationally mapped.Show allAlign All

P13010-1 [UniParc]FASTAAdd to basket
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MVRSGNKAAV VLCMDVGFTM SNSIPGIESP FEQAKKVITM FVQRQVFAEN
60 70 80 90 100
KDEIALVLFG TDGTDNPLSG GDQYQNITVH RHLMLPDFDL LEDIESKIQP
110 120 130 140 150
GSQQADFLDA LIVSMDVIQH ETIGKKFEKR HIEIFTDLSS RFSKSQLDII
160 170 180 190 200
IHSLKKCDIS LQFFLPFSLG KEDGSGDRGD GPFRLGGHGP SFPLKGITEQ
210 220 230 240 250
QKEGLEIVKM VMISLEGEDG LDEIYSFSES LRKLCVFKKI ERHSIHWPCR
260 270 280 290 300
LTIGSNLSIR IAAYKSILQE RVKKTWTVVD AKTLKKEDIQ KETVYCLNDD
310 320 330 340 350
DETEVLKEDI IQGFRYGSDI VPFSKVDEEQ MKYKSEGKCF SVLGFCKSSQ
360 370 380 390 400
VQRRFFMGNQ VLKVFAARDD EAAAVALSSL IHALDDLDMV AIVRYAYDKR
410 420 430 440 450
ANPQVGVAFP HIKHNYECLV YVQLPFMEDL RQYMFSSLKN SKKYAPTEAQ
460 470 480 490 500
LNAVDALIDS MSLAKKDEKT DTLEDLFPTT KIPNPRFQRL FQCLLHRALH
510 520 530 540 550
PREPLPPIQQ HIWNMLNPPA EVTTKSQIPL SKIKTLFPLI EAKKKDQVTA
560 570 580 590 600
QEIFQDNHED GPTAKKLKTE QGGAHFSVSS LAEGSVTSVG SVNPAENFRV
610 620 630 640 650
LVKQKKASFE EASNQLINHI EQFLDTNETP YFMKSIDCIR AFREEAIKFS
660 670 680 690 700
EEQRFNNFLK ALQEKVEIKQ LNHFWEIVVQ DGITLITKEE ASGSSVTAEE
710 720 730
AKKFLAPKDK PSGDTAAVFE EGGDVDDLLD MI
Length:732
Mass (Da):82,705
Last modified:January 23, 2007 - v3
<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:i2363CA84834E74A3
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 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
C9JZ81C9JZ81_HUMAN
X-ray repair cross-complementing pr...
XRCC5
131Annotation 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>
H7C0H9H7C0H9_HUMAN
X-ray repair cross-complementing pr...
XRCC5
19Annotation 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 conflicti14 – 16MDV → YSY AA sequence (PubMed:8605992).Curated3
Sequence conflicti117V → A in BAF83429 (PubMed:14702039).Curated1
Sequence conflicti134I → V in BAD96323 (Ref. 4) Curated1
Sequence conflicti178R → S in BAD96323 (Ref. 4) Curated1
Sequence conflicti315R → L in CAA40736 (PubMed:2212941).Curated1
Sequence conflicti461M → R AA sequence (PubMed:8605992).Curated1
Sequence conflicti479T → G AA sequence (PubMed:8605992).Curated1
Sequence conflicti540I → T in BAF83429 (PubMed:14702039).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_014724463L → F. Corresponds to variant dbSNP:rs1805380Ensembl.1
Natural variantiVAR_053784508I → V. Corresponds to variant dbSNP:rs2287558Ensembl.1

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

More...
DDBJi
Links Updated
J04977 mRNA Translation: AAA59475.1
M30938 mRNA Translation: AAA36154.1
AK290740 mRNA Translation: BAF83429.1
AK222603 mRNA Translation: BAD96323.1
DQ787434 Genomic DNA Translation: ABG46942.1
CH471063 Genomic DNA Translation: EAW70562.1
BC019027 mRNA Translation: AAH19027.1
BC095442 mRNA Translation: AAH95442.1
X57500 mRNA Translation: CAA40736.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS2402.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A35051 A32626
D42397
S62889

NCBI Reference Sequences

More...
RefSeqi
NP_066964.1, NM_021141.3

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Hs.388739

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000392132; ENSP00000375977; ENSG00000079246
ENST00000392133; ENSP00000375978; ENSG00000079246

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
7520

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:7520

UCSC genome browser

More...
UCSCi
uc002vfy.4 human

Keywords - Coding sequence diversityi

Polymorphism

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

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

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

NIEHS SNPs
Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J04977 mRNA Translation: AAA59475.1
M30938 mRNA Translation: AAA36154.1
AK290740 mRNA Translation: BAF83429.1
AK222603 mRNA Translation: BAD96323.1
DQ787434 Genomic DNA Translation: ABG46942.1
CH471063 Genomic DNA Translation: EAW70562.1
BC019027 mRNA Translation: AAH19027.1
BC095442 mRNA Translation: AAH95442.1
X57500 mRNA Translation: CAA40736.1
CCDSiCCDS2402.1
PIRiA35051 A32626
D42397
S62889
RefSeqiNP_066964.1, NM_021141.3
UniGeneiHs.388739

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1JEQX-ray2.70B1-565[»]
1JEYX-ray2.50B1-565[»]
1Q2ZNMR-A590-709[»]
1RW2NMR-A566-710[»]
3RZ9X-ray2.29B559-571[»]
5Y3Relectron microscopy6.60B6-541[»]
6ERFX-ray3.01B/D/F/H2-555[»]
6ERGX-ray2.90B/E2-555[»]
6ERHX-ray2.80B/D2-555[»]
ProteinModelPortaliP13010
SMRiP13010
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi113353, 247 interactors
ComplexPortaliCPX-1993 Ku70:Ku80 complex
CORUMiP13010
DIPiDIP-31379N
ELMiP13010
IntActiP13010, 115 interactors
MINTiP13010
STRINGi9606.ENSP00000375977

Protein family/group databases

MoonDBiP13010 Curated

PTM databases

iPTMnetiP13010
PhosphoSitePlusiP13010
SwissPalmiP13010

Polymorphism and mutation databases

BioMutaiXRCC5
DMDMi125731

2D gel databases

SWISS-2DPAGEiP13010

Proteomic databases

EPDiP13010
MaxQBiP13010
PaxDbiP13010
PeptideAtlasiP13010
PRIDEiP13010
ProteomicsDBi52890

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
7520
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000392132; ENSP00000375977; ENSG00000079246
ENST00000392133; ENSP00000375978; ENSG00000079246
GeneIDi7520
KEGGihsa:7520
UCSCiuc002vfy.4 human

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
7520
DisGeNETi7520
EuPathDBiHostDB:ENSG00000079246.15

GeneCards: human genes, protein and diseases

More...
GeneCardsi
XRCC5
HGNCiHGNC:12833 XRCC5
HPAiCAB004468
HPA025813
HPA064685
MIMi194364 gene
neXtProtiNX_P13010
OpenTargetsiENSG00000079246
PharmGKBiPA37425

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG2326 Eukaryota
ENOG410YKH9 LUCA
GeneTreeiENSGT00940000153239
HOVERGENiHBG006237
InParanoidiP13010
KOiK10885
OMAiYRFPPLD
OrthoDBiEOG091G11VD
PhylomeDBiP13010
TreeFamiTF101205

Enzyme and pathway databases

ReactomeiR-HSA-164843 2-LTR circle formation
R-HSA-1834949 Cytosolic sensors of pathogen-associated DNA
R-HSA-3270619 IRF3-mediated induction of type I IFN
R-HSA-5693571 Nonhomologous End-Joining (NHEJ)
R-HSA-6798695 Neutrophil degranulation
SIGNORiP13010

Miscellaneous databases

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

More...
ChiTaRSi
XRCC5 human
EvolutionaryTraceiP13010

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
Ku80

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

More...
GenomeRNAii
7520
PMAP-CutDBiP13010

Protein Ontology

More...
PROi
PR:P13010

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000079246 Expressed in 232 organ(s), highest expression level in kidney
CleanExiHS_XRCC5
ExpressionAtlasiP13010 baseline and differential
GenevisibleiP13010 HS

Family and domain databases

Gene3Di1.25.40.240, 1 hit
2.40.290.10, 1 hit
3.40.50.410, 1 hit
InterProiView protein in InterPro
IPR006164 Ku70/Ku80_beta-barrel_dom
IPR024193 Ku80
IPR005160 Ku_C
IPR036494 Ku_C_sf
IPR005161 Ku_N
IPR014893 Ku_PK_bind
IPR016194 SPOC-like_C_dom_sf
IPR002035 VWF_A
IPR036465 vWFA_dom_sf
PANTHERiPTHR12604:SF4 PTHR12604:SF4, 1 hit
PfamiView protein in Pfam
PF02735 Ku, 1 hit
PF03730 Ku_C, 1 hit
PF03731 Ku_N, 1 hit
PF08785 Ku_PK_bind, 1 hit
PIRSFiPIRSF016570 Ku80, 1 hit
SMARTiView protein in SMART
SM00559 Ku78, 1 hit
SM00327 VWA, 1 hit
SUPFAMiSSF100939 SSF100939, 1 hit
SSF101420 SSF101420, 1 hit
SSF53300 SSF53300, 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 nameiXRCC5_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P13010
Secondary accession number(s): A8K3X5
, Q0Z7V0, Q4VBQ5, Q53HH7, Q7M4N0, Q9UCQ0, Q9UCQ1
<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: January 1, 1990
Last sequence update: January 23, 2007
Last modified: December 5, 2018
This is version 216 of the entry and version 3 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

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

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  6. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
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