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Entry version 178 (16 Oct 2019)
Sequence version 4 (05 Feb 2008)
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Protein

X-ray repair cross-complementing protein 5

Gene

Xrcc5

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. In association with NAA15, the XRCC5/6 dimer binds to the osteocalcin promoter and activates osteocalcin expression. 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. 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

<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
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-MMU-5693571 Nonhomologous End-Joining (NHEJ)
R-MMU-6798695 Neutrophil degranulation

<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):
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
Ku autoantigen protein p86 homolog
Ku80
Nuclear factor IV
<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>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: Chromosome 1

Organism-specific databases

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

More...
MGIi
MGI:104517 Xrcc5

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

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

Keywords - Cellular componenti

Chromosome, Nucleus

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000843411 – 732X-ray repair cross-complementing protein 5Add BLAST732

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki195Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei258PhosphoserineBy similarity1
Modified residuei265N6-acetyllysineBy similarity1
Modified residuei318PhosphoserineBy similarity1
Modified residuei332N6-acetyllysineBy similarity1
Cross-linki532Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki534Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei535PhosphothreonineBy similarity1
Cross-linki567Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki569Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei578Phosphoserine; by PRKDCBy similarity1
Modified residuei580Phosphoserine; by PRKDCBy similarity1
Modified residuei581Phosphoserine; by PRKDCBy similarity1
Modified residuei666N6-acetyllysineBy similarity1
Cross-linki670Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki689Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei716Phosphothreonine; by PRKDCBy 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

ADP-ribosylated by PARP3.By similarity
Phosphorylated on serine residues. Phosphorylation by PRKDC may enhance helicase activity.By similarity
Sumoylated.By similarity
Ubiquitinated by RNF8 via 'Lys-48'-linked ubiquitination following DNA damage, leading to its degradation and removal from DNA damage sites. Ubiquitinated by RNF138, leading to remove the Ku complex from DNA breaks.By similarity

Keywords - PTMi

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

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
P27641

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
P27641

MaxQB - The MaxQuant DataBase

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MaxQBi
P27641

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

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PaxDbi
P27641

PeptideAtlas

More...
PeptideAtlasi
P27641

PRoteomics IDEntifications database

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PRIDEi
P27641

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P27641

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

More...
PhosphoSitePlusi
P27641

<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

Up-regulation during myogenesis is inhibited by cAMP, 3-aminobenzamide and sodium butyrate. Expression in myoblasts is unaffected by X-rays and UV light.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSMUSG00000026187 Expressed in 262 organ(s), highest expression level in cochlea

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P27641 MM

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_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 displays DNA binding activity towards the osteocalcin FGF response element (OCFRE). In addition, XRCC5 binds to the osteoblast-specific transcription factors MSX2 and RUNX2.

Interacts with ELF3. May interact with APLF. The XRCC5/XRCC6 dimer associates in a DNA-dependent manner with APEX1.

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.

Interacts with RNF138.

Interacts with CYREN.

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).

Interacts with DHX9; this interaction occurs in a RNA-dependent manner. 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 ERCC6 (By similarity).

By similarity

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
204608, 11 interactors

ComplexPortal: manually curated resource of macromolecular complexes

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ComplexPortali
CPX-2047 Ku70:Ku80 complex

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
P27641

Protein interaction database and analysis system

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IntActi
P27641, 6 interactors

Molecular INTeraction database

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MINTi
P27641

STRING: functional protein association networks

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STRINGi
10090.ENSMUSP00000027379

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

3D structure databases

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

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SMRi
P27641

Database of comparative protein structure models

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ModBasei
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

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 – 520Pro-richAdd BLAST43

<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.By similarity

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the ku80 family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG2326 Eukaryota
ENOG410YKH9 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000153239

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P27641

KEGG Orthology (KO)

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KOi
K10885

Identification of Orthologs from Complete Genome Data

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OMAi
FIHALYE

Database of Orthologous Groups

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OrthoDBi
598957at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
P27641

TreeFam database of animal gene trees

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TreeFami
TF101205

Family and domain databases

Conserved Domains Database

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CDDi
cd00873 KU80, 1 hit

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
IPR036465 vWFA_dom_sf

Pfam protein domain database

More...
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

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>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<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.

P27641-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAWSGNKAAV VLCVDVGVAM GNSFPGEESP IEQAKKVMTM FVQRQVFSES
60 70 80 90 100
KDEIALVLYG TDGTDNALAG KDQYQNITVC RHLMLPDFDL LEDIGNKIQP
110 120 130 140 150
SSQQADFLDA LIVCMDLIQR ETIGKKFGKK HIEVFTDLSS PFSQDQLDVI
160 170 180 190 200
ICNLKKSGIS LQFFLPFPID KNGEPGERGD LDSGLDHLKP SFPQKGLTEQ
210 220 230 240 250
QKEGIRMVTR VMLSLEGEDG LDEIYSFSES LRQLCVFKKI ERRSMPWPCQ
260 270 280 290 300
LTIGPNLSIK IVAYKSIVQE KFKKSWVVVD ARTLKKEDIQ KETVYCLNDD
310 320 330 340 350
DETEVSKEDT IQGYRYGSDI IPFSKVDEEQ MKYKSEGKCF SVLGFCKSSQ
360 370 380 390 400
VHRRFFMGHQ VLKVFAAKDD EAAAVALSSL VHALDELNMV AIVRYAYDKR
410 420 430 440 450
SNPQVGVAFP YIKDAYECLV YVQLPFMEDL RQYMFSSLKN NKKCTPTEAQ
460 470 480 490 500
LSAIDDLIDS MSLVKKNEEE DIVEDLFPTS KIPNPEFQRL YQCLLHRALH
510 520 530 540 550
LQERLPPIQQ HILNMLDPPT EMKAKCESPL SKVKTLFPLT EVIKKKNQVT
560 570 580 590 600
AQDVFQDNHE EGPAAKKYKT EKEEDHISIS SLAEGNITKV GSVNPVENFR
610 620 630 640 650
FLVRQKIASF EEASLQLISH IEQFLDTNET LYFMKSMDCI KAFREEAIQF
660 670 680 690 700
SEEQRFNSFL EALREKVEIK QLNHFWEIVV QDGVTLITKD EGPGSSITAE
710 720 730
EATKFLAPKD KAKEDTTGPE EAGDVDDLLD MI
Length:732
Mass (Da):83,057
Last modified:February 5, 2008 - v4
<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:i391F0FAF7EB04288
GO

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 conflicti5G → V in CAA46999 (PubMed:1641347).Curated1
Sequence conflicti24F → I in CAA46999 (PubMed:1641347).Curated1
Sequence conflicti57V → A in CAA46999 (PubMed:1641347).Curated1
Sequence conflicti66 – 69NALA → MPLS in CAA46999 (PubMed:1641347).Curated4
Sequence conflicti120R → H in AAD49720 (Ref. 2) Curated1
Sequence conflicti139S → G in BAE38207 (PubMed:16141072).Curated1
Sequence conflicti139S → R in CAA46999 (PubMed:1641347).Curated1
Sequence conflicti144Q → K in CAA46999 (PubMed:1641347).Curated1
Sequence conflicti157S → C in CAA46999 (PubMed:1641347).Curated1
Sequence conflicti226S → F in AAD49720 (Ref. 2) Curated1
Sequence conflicti409 – 410FP → SL in CAA46999 (PubMed:1641347).Curated2
Sequence conflicti414D → G in BAC38276 (PubMed:16141072).Curated1
Sequence conflicti415A → T in AAD49720 (Ref. 2) Curated1
Sequence conflicti418C → R in CAA46999 (PubMed:1641347).Curated1
Sequence conflicti442K → M in AAD49720 (Ref. 2) Curated1
Sequence conflicti479T → A in CAA46999 (PubMed:1641347).Curated1
Sequence conflicti515 – 516ML → IW in CAA46999 (PubMed:1641347).Curated2
Sequence conflicti524A → Q in CAA46999 (PubMed:1641347).Curated1
Sequence conflicti530 – 531LS → PL in CAA46999 (PubMed:1641347).Curated2
Sequence conflicti558N → H in AAD49720 (Ref. 2) Curated1
Sequence conflicti692G → A in CAA46999 (PubMed:1641347).Curated1
Sequence conflicti703T → K in CAA46999 (PubMed:1641347).Curated1
Sequence conflicti708P → H in BAE39415 (PubMed:16141072).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
X66323 mRNA Translation: CAA46999.1
AF166486 mRNA Translation: AAD49720.1
AK081633 mRNA Translation: BAC38276.1
AK165470 mRNA Translation: BAE38207.1
AK167312 mRNA Translation: BAE39415.1
AK168913 mRNA Translation: BAE40726.1
AK169838 mRNA Translation: BAE41402.1
BC029218 mRNA Translation: AAH29218.1
BC051660 mRNA Translation: AAH51660.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS35608.1

Protein sequence database of the Protein Information Resource

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PIRi
S26303

NCBI Reference Sequences

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RefSeqi
NP_033559.2, NM_009533.2

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENSMUST00000027379; ENSMUSP00000027379; ENSMUSG00000026187

Database of genes from NCBI RefSeq genomes

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GeneIDi
22596

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
mmu:22596

UCSC genome browser

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UCSCi
uc007bkl.2 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
X66323 mRNA Translation: CAA46999.1
AF166486 mRNA Translation: AAD49720.1
AK081633 mRNA Translation: BAC38276.1
AK165470 mRNA Translation: BAE38207.1
AK167312 mRNA Translation: BAE39415.1
AK168913 mRNA Translation: BAE40726.1
AK169838 mRNA Translation: BAE41402.1
BC029218 mRNA Translation: AAH29218.1
BC051660 mRNA Translation: AAH51660.1
CCDSiCCDS35608.1
PIRiS26303
RefSeqiNP_033559.2, NM_009533.2

3D structure databases

SMRiP27641
ModBaseiSearch...

Protein-protein interaction databases

BioGridi204608, 11 interactors
ComplexPortaliCPX-2047 Ku70:Ku80 complex
CORUMiP27641
IntActiP27641, 6 interactors
MINTiP27641
STRINGi10090.ENSMUSP00000027379

PTM databases

iPTMnetiP27641
PhosphoSitePlusiP27641

Proteomic databases

EPDiP27641
jPOSTiP27641
MaxQBiP27641
PaxDbiP27641
PeptideAtlasiP27641
PRIDEiP27641

Genome annotation databases

EnsembliENSMUST00000027379; ENSMUSP00000027379; ENSMUSG00000026187
GeneIDi22596
KEGGimmu:22596
UCSCiuc007bkl.2 mouse

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
7520
MGIiMGI:104517 Xrcc5

Phylogenomic databases

eggNOGiKOG2326 Eukaryota
ENOG410YKH9 LUCA
GeneTreeiENSGT00940000153239
InParanoidiP27641
KOiK10885
OMAiFIHALYE
OrthoDBi598957at2759
PhylomeDBiP27641
TreeFamiTF101205

Enzyme and pathway databases

ReactomeiR-MMU-5693571 Nonhomologous End-Joining (NHEJ)
R-MMU-6798695 Neutrophil degranulation

Miscellaneous databases

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

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ChiTaRSi
Xrcc5 mouse

Protein Ontology

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PROi
PR:P27641

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
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Gene expression databases

BgeeiENSMUSG00000026187 Expressed in 262 organ(s), highest expression level in cochlea
GenevisibleiP27641 MM

Family and domain databases

CDDicd00873 KU80, 1 hit
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
IPR036465 vWFA_dom_sf
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
SUPFAMiSSF100939 SSF100939, 1 hit
SSF101420 SSF101420, 1 hit
SSF53300 SSF53300, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiXRCC5_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: P27641
Secondary accession number(s): Q3TE46
, Q3TJT0, Q3TN82, Q80UT1, Q8C4N6, Q8K1K7, Q9R169
<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: August 1, 1992
Last sequence update: February 5, 2008
Last modified: October 16, 2019
This is version 178 of the entry and version 4 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
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