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UniProtKB - P12956 (XRCC6_HUMAN)

Protein

X-ray repair cross-complementing protein 6

Gene

XRCC6

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. 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.8 Publications

Miscellaneous

Individuals with systemic lupus erythematosus (SLE) and related disorders produce extremely large amounts of autoantibodies to XRCC5 and XRCC6. Existence of a major autoantigenic epitope or epitopes on the C-terminal 190 amino acids of XRCC6 containing the leucine repeat. The majority of autoantibodies to XRCC6 in most sera from patients with SLE seem to be reactive with this region.

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 sitei31Schiff-base intermediate with DNA; for 5'-deoxyribose-5-phosphate lyase activityCurated1

<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

  • 5'-deoxyribose-5-phosphate lyase activity Source: UniProtKB
  • ATP binding Source: UniProtKB-KW
  • ATP-dependent DNA helicase activity Source: ProtInc
  • cyclin binding Source: UniProtKB
  • damaged DNA binding Source: InterPro
  • DNA binding Source: UniProtKB
  • double-stranded DNA binding Source: ProtInc
  • protein-containing complex binding Source: BHF-UCL
  • protein C-terminus binding Source: UniProtKB
  • RNA binding Source: UniProtKB
  • telomeric DNA binding Source: GO_Central
  • transcription regulatory region DNA binding Source: BHF-UCL
View the complete GO annotation on QuickGO ...

GO - Biological processi

View the complete GO annotation on QuickGO ...

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

Molecular 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

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

More...SIGNORi		P12956

Protein family/group databases

MoonDB Database of extreme multifunctional and moonlighting proteins

More...MoonDBi		P12956 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 6 (EC:3.6.4.-, EC:4.2.99.-)
Alternative name(s):
5'-deoxyribose-5-phosphate lyase Ku70
Short name:
5'-dRP lyase Ku70
70 kDa subunit of Ku antigen
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
Lupus Ku autoantigen protein p70
Short name:
Ku70
Thyroid-lupus autoantigen
Short name:
TLAA
X-ray repair complementing defective repair in Chinese hamster cells 6
<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
<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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_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 22

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...EuPathDBi		HostDB:ENSG00000196419.12

Human Gene Nomenclature Database

More...HGNCi		HGNC:4055 XRCC6

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		152690 gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_P12956

<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>Mutagenesisi31K → A: Diminishes the ability to form a Schiff base. Abolishes adduct formation; when associated with A-160 and A-164. 1 Publication1
Mutagenesisi160K → A: Abolishes adduct formation; when associated with A-31 and A-160. 1 Publication1
Mutagenesisi164K → A: Abolishes adduct formation; when associated with A-31 and A-164. 1 Publication1

Keywords - Diseasei

Systemic lupus erythematosus

Organism-specific databases

DisGeNET

More...DisGeNETi		2547

Open Targets

More...OpenTargetsi		ENSG00000196419

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA28467

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		XRCC6

Domain mapping of disease mutations (DMDM)

More...DMDMi		125729

<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 methionineiRemovedCombined sources
<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_00002101792 – 609X-ray repair cross-complementing protein 6Add BLAST608

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-acetylserineCombined sources1
Modified residuei2PhosphoserineCombined sources1
Modified residuei6Phosphoserine; by PRKDC1 Publication1
Modified residuei27PhosphoserineCombined sources1
Modified residuei31N6-acetyllysineCombined sources1
Modified residuei51Phosphoserine; by PRKDC1 Publication1
<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-linki287Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei306PhosphoserineCombined sources1
Cross-linki317Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei331N6-acetyllysineCombined sources1
Modified residuei338N6-acetyllysineCombined sources1
Modified residuei455PhosphothreonineCombined sources1
Modified residuei461N6-acetyllysineCombined sources1
Modified residuei477PhosphoserineCombined sources1
Modified residuei520PhosphoserineCombined sources1
Modified residuei550PhosphoserineCombined sources1
Cross-linki556Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei560PhosphoserineCombined sources1

<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-51 does not affect DNA repair.3 Publications
ADP-ribosylated by PARP3.1 Publication

Keywords - PTMi

Acetylation, ADP-ribosylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		P12956

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P12956

MaxQB - The MaxQuant DataBase

More...MaxQBi		P12956

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

More...PaxDbi		P12956

PeptideAtlas

More...PeptideAtlasi		P12956

PRoteomics IDEntifications database

More...PRIDEi		P12956

ProteomicsDB human proteome resource

More...ProteomicsDBi		52888

2D gel databases

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

More...SWISS-2DPAGEi		P12956

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P12956

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

More...PhosphoSitePlusi		P12956

SwissPalm database of S-palmitoylation events

More...SwissPalmi		P12956

Miscellaneous databases

CutDB - Proteolytic event database

More...PMAP-CutDBi		P12956

<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 does not increase 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

More...Bgeei		ENSG00000196419 Expressed in 232 organ(s), highest expression level in testis

CleanEx database of gene expression profiles

More...CleanExi		HS_XRCC6

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		P12956 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P12956 HS

Organism-specific databases

Human Protein Atlas

More...HPAi		CAB004254
HPA047549
HPA062226

<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 (PubMed:25574025, PubMed:25941166, PubMed:25670504). 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 isoform 2. 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 (PubMed:10219089, PubMed:11493912, PubMed:12145306, PubMed:12509254, PubMed:12547193, PubMed:15075319, PubMed:20493174, PubMed:22442688, PubMed:8621488, PubMed:9742108). Interacts with CLU (By similarity). 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 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). 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). Interacts with HMBOX1 (PubMed:23685356).By similarity16 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

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		108822, 313 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...ComplexPortali		CPX-1993 Ku70:Ku80 complex

CORUM comprehensive resource of mammalian protein complexes

More...CORUMi		P12956

Database of interacting proteins

More...DIPi		DIP-24188N

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

More...ELMi		P12956

Protein interaction database and analysis system

More...IntActi		P12956, 170 interactors

Molecular INTeraction database

More...MINTi		P12956

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000352257

<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

1609
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1JEQX-ray2.70A1-609[»]
1JEYX-ray2.50A1-609[»]
1JJRNMR-A556-609[»]
3RZXX-ray2.61B537-558[»]
5Y3Relectron microscopy6.60A34-534[»]
6ERFX-ray3.01A/C/E/G1-544[»]
6ERGX-ray2.90A/D1-544[»]
6ERHX-ray2.80A/C1-544[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...ProteinModelPortali		P12956

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

More...SMRi		P12956

Database of comparative protein structure models

More...ModBasei		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P12956

<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>Domaini261 – 468KuAdd BLAST208
Domaini573 – 607SAPPROSITE-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>Regioni550 – 609Interaction with DEAF11 PublicationAdd 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 biasi2 – 61Ser-rich (potentially targets for phosphorylation)Add BLAST60
Compositional biasi11 – 29Asp/Glu-rich (acidic)Add BLAST19
Compositional biasi330 – 342Asp/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

Ensembl GeneTree

More...GeneTreei		ENSGT00940000153239

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000006588

The HOVERGEN Database of Homologous Vertebrate Genes

More...HOVERGENi		HBG006236

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P12956

KEGG Orthology (KO)

More...KOi		K10884

Identification of Orthologs from Complete Genome Data

More...OMAi		DVFTSCN

Database of Orthologous Groups

More...OrthoDBi		402798at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		P12956

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>Sequences (2+)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 describes 2 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 2 described isoforms and 1 potential isoform that is computationally mapped.Show allAlign All

Isoform 1 (identifier: P12956-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MSGWESYYKT EGDEEAEEEQ EENLEASGDY KYSGRDSLIF LVDASKAMFE 
        60         70         80         90        100
SQSEDELTPF DMSIQCIQSV YISKIISSDR DLLAVVFYGT EKDKNSVNFK 
       110        120        130        140        150
NIYVLQELDN PGAKRILELD QFKGQQGQKR FQDMMGHGSD YSLSEVLWVC 
       160        170        180        190        200
ANLFSDVQFK MSHKRIMLFT NEDNPHGNDS AKASRARTKA GDLRDTGIFL 
       210        220        230        240        250
DLMHLKKPGG FDISLFYRDI ISIAEDEDLR VHFEESSKLE DLLRKVRAKE 
       260        270        280        290        300
TRKRALSRLK LKLNKDIVIS VGIYNLVQKA LKPPPIKLYR ETNEPVKTKT 
       310        320        330        340        350
RTFNTSTGGL LLPSDTKRSQ IYGSRQIILE KEETEELKRF DDPGLMLMGF 
       360        370        380        390        400
KPLVLLKKHH YLRPSLFVYP EESLVIGSST LFSALLIKCL EKEVAALCRY 
       410        420        430        440        450
TPRRNIPPYF VALVPQEEEL DDQKIQVTPP GFQLVFLPFA DDKRKMPFTE 
       460        470        480        490        500
KIMATPEQVG KMKAIVEKLR FTYRSDSFEN PVLQQHFRNL EALALDLMEP 
       510        520        530        540        550
EQAVDLTLPK VEAMNKRLGS LVDEFKELVY PPDYNPEGKV TKRKHDNEGS 
       560        570        580        590        600
GSKRPKVEYS EEELKTHISK GTLGKFTVPM LKEACRAYGL KSGLKKQELL 

EALTKHFQD
Length:609
Mass (Da):69,843
Last modified:January 23, 2007 - v2
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iBBD3CD434526DFCB
GO
Isoform 2 (identifier: P12956-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     65-105: Missing.

Note: No experimental confirmation available.
Show »
Length:568
Mass (Da):65,149
Checksum:iB6DBBED4C80118C1
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
B1AHC9B1AHC9_HUMAN
X-ray repair cross-complementing pr...
XRCC6
559Annotation score:

Annotation score:2 out of 5

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

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 conflicti20Q → D AA sequence (PubMed:1537839).Curated1
Sequence conflicti101N → K AA sequence (PubMed:8605992).Curated1
Sequence conflicti103Y → L AA sequence (PubMed:8605992).Curated1
Sequence conflicti116I → S AA sequence (PubMed:8605992).Curated1
Sequence conflicti125Q → S AA sequence (PubMed:8605992).Curated1
Sequence conflicti181A → T in CAG47015 (Ref. 5) Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_05603065 – 105Missing in isoform 2. 1 PublicationAdd BLAST41

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
J04607 mRNA Translation: AAA61177.1
J04611 mRNA Translation: AAA51733.1
M32865 mRNA Translation: AAA36155.1
S38729 mRNA Translation: AAB22381.1
AK055786 mRNA Translation: BAG51575.1
CR542219 mRNA Translation: CAG47015.1
AY870329 Genomic DNA Translation: AAW34364.1
Z83840 Genomic DNA No translation available.
CH471095 Genomic DNA Translation: EAW60448.1
BC008343 mRNA Translation: AAH08343.1
BC010034 mRNA Translation: AAH10034.1
BC012154 mRNA Translation: AAH12154.1
BC018259 mRNA Translation: AAH18259.1
BC072449 mRNA Translation: AAH72449.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS14021.1 [P12956-1]
CCDS74870.1 [P12956-2]

Protein sequence database of the Protein Information Resource

More...PIRi		A30299 A30894

NCBI Reference Sequences

More...RefSeqi		NP_001275905.1, NM_001288976.1 [P12956-1]
NP_001275906.1, NM_001288977.1 [P12956-2]
NP_001460.1, NM_001469.4 [P12956-1]

UniGene gene-oriented nucleotide sequence clusters

More...UniGenei		Hs.292493
Hs.730702

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000359308; ENSP00000352257; ENSG00000196419 [P12956-1]
ENST00000360079; ENSP00000353192; ENSG00000196419 [P12956-1]
ENST00000402580; ENSP00000384941; ENSG00000196419 [P12956-2]
ENST00000405878; ENSP00000384257; ENSG00000196419 [P12956-1]

Database of genes from NCBI RefSeq genomes

More...GeneIDi		2547

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:2547

UCSC genome browser

More...UCSCi		uc003bao.3 human [P12956-1]

Keywords - Coding sequence diversityi

Alternative splicing

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

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

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_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
J04607 mRNA Translation: AAA61177.1
J04611 mRNA Translation: AAA51733.1
M32865 mRNA Translation: AAA36155.1
S38729 mRNA Translation: AAB22381.1
AK055786 mRNA Translation: BAG51575.1
CR542219 mRNA Translation: CAG47015.1
AY870329 Genomic DNA Translation: AAW34364.1
Z83840 Genomic DNA No translation available.
CH471095 Genomic DNA Translation: EAW60448.1
BC008343 mRNA Translation: AAH08343.1
BC010034 mRNA Translation: AAH10034.1
BC012154 mRNA Translation: AAH12154.1
BC018259 mRNA Translation: AAH18259.1
BC072449 mRNA Translation: AAH72449.1
CCDSiCCDS14021.1 [P12956-1]
CCDS74870.1 [P12956-2]
PIRiA30299 A30894
RefSeqiNP_001275905.1, NM_001288976.1 [P12956-1]
NP_001275906.1, NM_001288977.1 [P12956-2]
NP_001460.1, NM_001469.4 [P12956-1]
UniGeneiHs.292493
Hs.730702

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1JEQX-ray2.70A1-609[»]
1JEYX-ray2.50A1-609[»]
1JJRNMR-A556-609[»]
3RZXX-ray2.61B537-558[»]
5Y3Relectron microscopy6.60A34-534[»]
6ERFX-ray3.01A/C/E/G1-544[»]
6ERGX-ray2.90A/D1-544[»]
6ERHX-ray2.80A/C1-544[»]
ProteinModelPortaliP12956
SMRiP12956
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108822, 313 interactors
ComplexPortaliCPX-1993 Ku70:Ku80 complex
CORUMiP12956
DIPiDIP-24188N
ELMiP12956
IntActiP12956, 170 interactors
MINTiP12956
STRINGi9606.ENSP00000352257

Protein family/group databases

MoonDBiP12956 Curated

PTM databases

iPTMnetiP12956
PhosphoSitePlusiP12956
SwissPalmiP12956

Polymorphism and mutation databases

BioMutaiXRCC6
DMDMi125729

2D gel databases

SWISS-2DPAGEiP12956

Proteomic databases

EPDiP12956
jPOSTiP12956
MaxQBiP12956
PaxDbiP12956
PeptideAtlasiP12956
PRIDEiP12956
ProteomicsDBi52888

Protocols and materials databases

The DNASU plasmid repository

More...DNASUi		2547
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000359308; ENSP00000352257; ENSG00000196419 [P12956-1]
ENST00000360079; ENSP00000353192; ENSG00000196419 [P12956-1]
ENST00000402580; ENSP00000384941; ENSG00000196419 [P12956-2]
ENST00000405878; ENSP00000384257; ENSG00000196419 [P12956-1]
GeneIDi2547
KEGGihsa:2547
UCSCiuc003bao.3 human [P12956-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		2547
DisGeNETi2547
EuPathDBiHostDB:ENSG00000196419.12

GeneCards: human genes, protein and diseases

More...GeneCardsi		XRCC6
HGNCiHGNC:4055 XRCC6
HPAiCAB004254
HPA047549
HPA062226
MIMi152690 gene
neXtProtiNX_P12956
OpenTargetsiENSG00000196419
PharmGKBiPA28467

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG2327 Eukaryota
ENOG410XNXU LUCA
GeneTreeiENSGT00940000153239
HOGENOMiHOG000006588
HOVERGENiHBG006236
InParanoidiP12956
KOiK10884
OMAiDVFTSCN
OrthoDBi402798at2759
PhylomeDBiP12956
TreeFamiTF315101

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
SIGNORiP12956

Miscellaneous databases

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

More...ChiTaRSi		XRCC6 human
EvolutionaryTraceiP12956

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		Ku70

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

More...GenomeRNAii		2547
PMAP-CutDBiP12956

Protein Ontology

More...PROi		PR:P12956

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000196419 Expressed in 232 organ(s), highest expression level in testis
CleanExiHS_XRCC6
ExpressionAtlasiP12956 baseline and differential
GenevisibleiP12956 HS

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_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: P12956
Secondary accession number(s): B1AHC8
, Q6FG89, Q9UCQ2, Q9UCQ3
<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: January 16, 2019
This is version 225 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

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

Keywords - Technical termi

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

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Human chromosome 22
    Human chromosome 22: entries, gene names and cross-references to MIM
  3. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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