Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 145 (25 May 2022)
Sequence version 1 (01 Dec 2001)
Previous versions | rss
Add a publicationFeedback
Protein

DNA repair protein XRCC4

Gene

Xrcc4

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

DNA non-homologous end joining (NHEJ) core factor, required for double-strand break repair and V(D)J recombination (PubMed:9875844).

Acts as a scaffold protein that regulates recruitment of other proteins to DNA double-strand breaks (DSBs). Associates with NHEJ1/XLF to form alternating helical filaments that bridge DNA and act like a bandage, holding together the broken DNA until it is repaired. The XRCC4-NHEJ1/XLF subcomplex binds to the DNA fragments of a DSB in a highly diffusive manner and robustly bridges two independent DNA molecules, holding the broken DNA fragments in close proximity to one other. The mobility of the bridges ensures that the ends remain accessible for further processing by other repair factors. Plays a key role in the NHEJ ligation step of the broken DNA during DSB repair via direct interaction with DNA ligase IV (LIG4): the LIG4-XRCC4 subcomplex reseals the DNA breaks after the gap filling is completed. XRCC4 stabilizes LIG4, regulates its subcellular localization and enhances LIG4's joining activity. Binding of the LIG4-XRCC4 subcomplex to DNA ends is dependent on the assembly of the DNA-dependent protein kinase complex DNA-PK to these DNA ends. Promotes displacement of PNKP from processed strand break termini (By similarity).

By similarity1 Publication

Acts as an activator of the phospholipid scramblase activity of XKR4 (PubMed:33725486).

This form, which is generated upon caspase-3 (CASP3) cleavage, translocates into the cytoplasm and interacts with XKR4, thereby promoting phosphatidylserine scramblase activity of XKR4 and leading to phosphatidylserine exposure on apoptotic cell surface (PubMed:33725486).

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

GO - Biological processi

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

Molecular functionDNA-binding
Biological processDNA damage, DNA recombination, DNA repair

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-MMU-3108214, SUMOylation of DNA damage response and repair proteins
R-MMU-5693571, Nonhomologous End-Joining (NHEJ)

<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%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
DNA repair protein XRCC4Curated
Alternative name(s):
X-ray repair cross-complementing protein 41 Publication
Cleaved into the following chain:
Protein XRCC4, C-terminus1 Publication
Short name:
XRCC4/C1 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:Xrcc41 PublicationImported
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Unplaced

Organism-specific databases

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

More...
MGIi
MGI:1333799, Xrcc4

<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

Keywords - Cellular componenti

Chromosome, Cytoplasm, 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

<p>This subsection of the 'Pathology and Biotech' section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Mice show growth defects, premature senescence, IR sensitivity, and inability to support V(D)J recombination (PubMed:9875844). XRCC4 deficiency causes late embryonic lethality accompanied by defective lymphogenesis and defective neurogenesis manifested by extensive apoptotic death of newly generated postmitotic neuronal cells (PubMed:9875844).1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'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>Mutagenesisi53S → A in 9A mutant; abolished phosphorylation by PRKDC; does not affect ability to repair double-strand breaks (DSBs), possibly because of redundancy with NHEJ1/XLF phosphorylation sites; when associated with A-193, A-254, A-295, A-307, A-312, A-315, A-319 and A-320. 1 Publication1
Mutagenesisi193S → A in 9A mutant; abolished phosphorylation by PRKDC; does not affect ability to repair double-strand breaks (DSBs), possibly because of redundancy with NHEJ1/XLF phosphorylation sites; when associated with A-53, A-254, A-295, A-307, A-312, A-315, A-319 and A-320. 1 Publication1
Mutagenesisi254S → A in 9A mutant; abolished phosphorylation by PRKDC; does not affect ability to repair double-strand breaks (DSBs), possibly because of redundancy with NHEJ1/XLF phosphorylation sites; when associated with A-53, A-193, A-295, A-307, A-312, A-315, A-319 and A-320. 1 Publication1
Mutagenesisi295S → A in 9A mutant; abolished phosphorylation by PRKDC; does not affect ability to repair double-strand breaks (DSBs), possibly because of redundancy with NHEJ1/XLF phosphorylation sites; when associated with A-53, A-193, A-254, A-307, A-312, A-315, A-319 and A-320. 1 Publication1
Mutagenesisi307S → A in 9A mutant; abolished phosphorylation by PRKDC; does not affect ability to repair double-strand breaks (DSBs), possibly because of redundancy with NHEJ1/XLF phosphorylation sites; when associated with A-53, A-193, A-254, A-295, A-312, A-315, A-319 and A-320. 1 Publication1
Mutagenesisi312S → A in 9A mutant; abolished phosphorylation by PRKDC; does not affect ability to repair double-strand breaks (DSBs), possibly because of redundancy with NHEJ1/XLF phosphorylation sites; when associated with A-53, A-193, A-254, A-295, A-307, A-315, A-319 and A-320. 1 Publication1
Mutagenesisi315T → A in 9A mutant; abolished phosphorylation by PRKDC; does not affect ability to repair double-strand breaks (DSBs), possibly because of redundancy with NHEJ1/XLF phosphorylation sites; when associated with A-53, A-193, A-254, A-295, A-307, A-312, A-319 and A-320. 1 Publication1
Mutagenesisi319S → A in 9A mutant; abolished phosphorylation by PRKDC; does not affect ability to repair double-strand breaks (DSBs), possibly because of redundancy with NHEJ1/XLF phosphorylation sites; when associated with A-53, A-193, A-254, A-295, A-307, A-312, A-315 and A-320. 1 Publication1
Mutagenesisi320S → A in 9A mutant; abolished phosphorylation by PRKDC; does not affect ability to repair double-strand breaks (DSBs), possibly because of redundancy with NHEJ1/XLF phosphorylation sites; when associated with A-53, A-193, A-254, A-295, A-307, A-312, A-315 and A-319. 1 Publication1

<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 or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000660481 – 326DNA repair protein XRCC4Add BLAST326
ChainiPRO_0000453297266 – 326Protein XRCC4, C-terminusBy similarityAdd BLAST61

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 residuei53Phosphoserine; by PRKDC1 Publication1
Modified residuei193Phosphoserine; by PRKDC1 Publication1
Modified residuei227PhosphotyrosineBy similarity1
Modified residuei230PhosphoserineBy similarity1
Modified residuei231PhosphothreonineBy similarity1
Modified residuei235PhosphoserineBy similarity1
Modified residuei244PhosphothreonineCombined sources1
Modified residuei250PhosphoserineBy similarity1
Modified residuei254Phosphoserine; by PRKDC1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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-linki290Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei295Phosphoserine; by PRKDC1 Publication1
Modified residuei296PhosphoserineBy similarity1
Modified residuei307Phosphoserine; by PRKDC1 Publication1
Modified residuei312Phosphoserine; by PRKDC1 Publication1
Modified residuei315Phosphothreonine; by PRKDCCombined sources1 Publication1
Modified residuei319Phosphoserine; by PRKDCCombined sources1 Publication1
Modified residuei320Phosphoserine; by PRKDCCombined sources1 Publication1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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 by PRKDC at the C-terminus in response to DNA damage; Ser-254 and Ser-312 constitute the main phosphorylation sites (PubMed:14599745). Phosphorylation by PRKDC at the C-terminus of XRCC4 and NHEJ1/XLF are highly redundant and regulate ability of the XRCC4-NHEJ1/XLF subcomplex to bridge DNA (By similarity). Phosphorylation by PRKDC does not prevent interaction with NHEJ1/XLF but disrupts ability to bridge DNA and promotes detachment from DNA (By similarity). Phosphorylation at Ser-319 and Ser-320 by PRKDC promotes recognition by the SCF(FBXW7) complex and subsequent ubiquitination via 'Lys-63'-linked ubiquitin (By similarity). Phosphorylation at Thr-231 by CK2 promotes interaction with PNKP; regulating PNKP activity and localization to DNA damage sites (By similarity). Phosphorylation by CK2 promotes interaction with APTX (By similarity).By similarity1 Publication
Ubiquitinated at Lys-290 by the SCF(FBXW7) complex via 'Lys-63'-linked ubiquitination, thereby promoting double-strand break repair: the SCF(FBXW7) complex specifically recognizes XRCC4 when phosphorylated at Ser-319 and Ser-320 by PRKDC, and 'Lys-63'-linked ubiquitination facilitates DNA non-homologous end joining (NHEJ) by enhancing association with XRCC5/Ku80 and XRCC6/Ku70. Monoubiquitinated.By similarity
Undergoes proteolytic processing by caspase-3 (CASP3). This generates the protein XRCC4, C-terminus (XRCC4/C), which translocates to the cytoplasm and activates phospholipid scramblase activity of XKR4, thereby promoting phosphatidylserine exposure on apoptotic cell surface.By similarity

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
Q924T3

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
Q924T3

MaxQB - The MaxQuant DataBase

More...
MaxQBi
Q924T3

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

More...
PaxDbi
Q924T3

PeptideAtlas

More...
PeptideAtlasi
Q924T3

PRoteomics IDEntifications database

More...
PRIDEi
Q924T3

ProteomicsDB: a multi-organism proteome resource

More...
ProteomicsDBi
297570 [Q924T3-1]
297571 [Q924T3-2]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q924T3

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

More...
PhosphoSitePlusi
Q924T3

<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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer and homotetramer in solution.

Interacts with NHEJ1/XLF; the interaction is direct and is mediated via a head-to-head interaction between N-terminal head regions.

Interacts with LIG4; the LIG4-XRCC4 subcomplex has a 1:2 stoichiometry and XRCC4 is required for LIG4 stability.

Component of the core long-range non-homologous end joining (NHEJ) complex (also named DNA-PK complex) composed of PRKDC, LIG4, XRCC4, XRCC6/Ku70, XRCC5/Ku86 and NHEJ1/XLF. Additional component of the NHEJ complex includes PAXX. Following autophosphorylation, PRKDC dissociates from DNA, leading to formation of the short-range NHEJ complex, composed of LIG4, XRCC4, XRCC6/Ku70, XRCC5/Ku86 and NHEJ1/XLF.

Interacts with PRKDC; the interaction is direct.

Interacts with XRCC6/Ku70; the interaction is direct.

Interacts with APTX and APLF.

Forms a heterotetramer with IFFO1; the interaction involves LIG4-free XRCC4 and leads to the relocalization of IFFO1 to the sites of DNA damage.

Interacts with PNKP; mainly interacts with PNKP when phosphorylated at Thr-231, but is also able to interact at much lower level with PNKP when not unphosphorylated.

Interacts with POLL (DNA polymerase lambda).

By similarity

Interacts with XKR4; interacts with the processed form of XKR4, which is cleaved by caspase.

By similarity

GO - Molecular functioni

Protein-protein interaction databases

CORUM comprehensive resource of mammalian protein complexes

More...
CORUMi
Q924T3

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

More...
ELMi
Q924T3

STRING: functional protein association networks

More...
STRINGi
10090.ENSMUSP00000022115

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...
RNActi
Q924T3, protein

<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

AlphaFold Protein Structure Database

More...
AlphaFoldDBi
Q924T3

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

More...
SMRi
Q924T3

Database of comparative protein structure models

More...
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

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>Regioni1 – 212Interaction with IFFO1By similarityAdd BLAST212
Regioni180 – 211Interaction with LIG4By similarityAdd BLAST32
Regioni203 – 326DisorderedSequence analysisAdd BLAST124

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and domains' section denotes the positions of regions of coiled coil within the protein.<p><a href='/help/coiled' target='_top'>More...</a></p>Coiled coili131 – 165Sequence analysisAdd BLAST35
Coiled coili185 – 209Sequence analysisAdd BLAST25

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>Motifi264 – 269Nuclear localization signalBy similarity6

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 type of amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi205 – 230Basic and acidic residuesSequence analysisAdd BLAST26
Compositional biasi293 – 319Polar residuesSequence analysisAdd BLAST27

<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 XRCC4-XLF family. XRCC4 subfamily.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG502QWJA, Eukaryota

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q924T3

Database of Orthologous Groups

More...
OrthoDBi
940052at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q924T3

TreeFam database of animal gene trees

More...
TreeFami
TF101204

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.20.5.370, 1 hit
2.170.210.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR010585, DNA_repair_prot_XRCC4
IPR014751, XRCC4-like_C
IPR038051, XRCC4-like_N_sf
IPR009089, XRCC4_N_sf

The PANTHER Classification System

More...
PANTHERi
PTHR28559, PTHR28559, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF06632, XRCC4, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF50809, SSF50809, 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%5Flength">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>Sequences (2+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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 4 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: Q924T3-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the <p><strong>What is the canonical sequence?</strong><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali 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
MERKVSRIYL ASEPNVPYFL QVSWERAIGS GFVITLTDGH SAWTATVSEL
60 70 80 90 100
EISQEADDMA MEKGKYIDEL RKALVPGSGA AGTYKFLFSK ESQHFSLEKE
110 120 130 140 150
LKDVSFRLGS FNLDKVSNSA EVIRELICYC LDTITEKQAK NEHLQKENER
160 170 180 190 200
LLRDWNDVQG RFEKCVSAKE ALEADLYQRF ILVLNEKKTK IRSLHKLLNE
210 220 230 240 250
VQQLEESTKP ERENPCSDKT PEEHGLYDGS TDEESGAPVQ AAETLHKDDS
260 270 280 290 300
IFSSPDVTDI APSRKRRHRM QKNLGTEPKM APQELPLQEK ERLASSLPQT
310 320
LKEESTSAEN MSLETLRNSS PEDLFD
Length:326
Mass (Da):37,061
Last modified:December 1, 2001 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i58BD3422F7D2CBDB
GO
Isoform 2 (identifier: Q924T3-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     293-326: LASSLPQTLKEESTSAENMSLETLRNSSPEDLFD → KKKYPSIMSTKVQRSLGEGGHG

Show »
Length:314
Mass (Da):35,708
Checksum:i58C2D697E88C17C3
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 4 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A0R4J024A0A0R4J024_MOUSE
DNA repair protein XRCC4
Xrcc4
326Annotation score:

Annotation score:3 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>
A0A0R4J1Y0A0A0R4J1Y0_MOUSE
DNA repair protein XRCC4
Xrcc4
314Annotation 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>
E0CY05E0CY05_MOUSE
DNA repair protein XRCC4
Xrcc4
83Annotation 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>
E0CZC8E0CZC8_MOUSE
DNA repair protein XRCC4
Xrcc4
94Annotation 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 conflicti27A → T in BAB26604 (PubMed:15489334).Curated1
Sequence conflicti27A → T in BAC35447 (PubMed:15489334).Curated1
Sequence conflicti54Q → P in BAC40256 (PubMed:15489334).Curated1
Sequence conflicti93Q → R in BAB26604 (PubMed:15489334).Curated1
Sequence conflicti93Q → R in BAC35447 (PubMed:15489334).Curated1
Sequence conflicti125E → D in BAB26604 (PubMed:15489334).Curated1
Sequence conflicti125E → D in BAC35447 (PubMed:15489334).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.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_009475293 – 326LASSL…EDLFD → KKKYPSIMSTKVQRSLGEGG HG in isoform 2. 1 PublicationAdd BLAST34

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
AB055154 mRNA Translation: BAB62316.1
AK009951 mRNA Translation: BAB26604.1
AK053612 mRNA Translation: BAC35447.1
AK088281 mRNA Translation: BAC40256.1
BC025538 mRNA Translation: AAH25538.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS26673.1 [Q924T3-1]

NCBI Reference Sequences

More...
RefSeqi
NP_082288.1, NM_028012.4
XP_006517104.1, XM_006517041.3
XP_006517105.1, XM_006517042.2
XP_006517106.1, XM_006517043.3

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
108138

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
mmu:108138

UCSC genome browser

More...
UCSCi
uc007rjn.2, mouse [Q924T3-1]

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB055154 mRNA Translation: BAB62316.1
AK009951 mRNA Translation: BAB26604.1
AK053612 mRNA Translation: BAC35447.1
AK088281 mRNA Translation: BAC40256.1
BC025538 mRNA Translation: AAH25538.1
CCDSiCCDS26673.1 [Q924T3-1]
RefSeqiNP_082288.1, NM_028012.4
XP_006517104.1, XM_006517041.3
XP_006517105.1, XM_006517042.2
XP_006517106.1, XM_006517043.3

3D structure databases

AlphaFoldDBiQ924T3
SMRiQ924T3
ModBaseiSearch...

Protein-protein interaction databases

CORUMiQ924T3
ELMiQ924T3
STRINGi10090.ENSMUSP00000022115

PTM databases

iPTMnetiQ924T3
PhosphoSitePlusiQ924T3

Proteomic databases

EPDiQ924T3
jPOSTiQ924T3
MaxQBiQ924T3
PaxDbiQ924T3
PeptideAtlasiQ924T3
PRIDEiQ924T3
ProteomicsDBi297570 [Q924T3-1]
297571 [Q924T3-2]

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
108138

Genome annotation databases

GeneIDi108138
KEGGimmu:108138
UCSCiuc007rjn.2, mouse [Q924T3-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
7518
MGIiMGI:1333799, Xrcc4

Phylogenomic databases

eggNOGiENOG502QWJA, Eukaryota
InParanoidiQ924T3
OrthoDBi940052at2759
PhylomeDBiQ924T3
TreeFamiTF101204

Enzyme and pathway databases

ReactomeiR-MMU-3108214, SUMOylation of DNA damage response and repair proteins
R-MMU-5693571, Nonhomologous End-Joining (NHEJ)

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...
BioGRID-ORCSi
108138, 7 hits in 113 CRISPR screens

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

More...
ChiTaRSi
Xrcc4, mouse

Protein Ontology

More...
PROi
PR:Q924T3
RNActiQ924T3, protein

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Family and domain databases

Gene3Di1.20.5.370, 1 hit
2.170.210.10, 1 hit
InterProiView protein in InterPro
IPR010585, DNA_repair_prot_XRCC4
IPR014751, XRCC4-like_C
IPR038051, XRCC4-like_N_sf
IPR009089, XRCC4_N_sf
PANTHERiPTHR28559, PTHR28559, 1 hit
PfamiView protein in Pfam
PF06632, XRCC4, 1 hit
SUPFAMiSSF50809, SSF50809, 1 hit

MobiDB: a database of protein disorder and mobility annotations

More...
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 nameiXRCC4_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: Q924T3
Secondary accession number(s): Q8BKC9, Q8BU02, Q9D6U6
<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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 1, 2004
Last sequence update: December 1, 2001
Last modified: May 25, 2022
This is version 145 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

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

Keywords - Technical termi

Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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

Do not show this banner again