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Entry version 196 (29 Sep 2021)
Sequence version 2 (01 Mar 2004)
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Protein

DNA repair protein XRCC4

Gene

XRCC4

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

DNA non-homologous end joining (NHEJ) core factor, required for double-strand break repair and V(D)J recombination (PubMed:10757784, PubMed:10854421, PubMed:17124166, PubMed:16412978, PubMed:8548796, PubMed:25742519, PubMed:12517771, PubMed:17290226, PubMed:22228831, PubMed:25597996, PubMed:25934149, PubMed:26100018, PubMed:26774286).

Acts as a scaffold protein that regulates recruitment of other proteins to DNA double-strand breaks (DSBs) (PubMed:15385968, PubMed:20852255, PubMed:26774286, PubMed:27437582).

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 (PubMed:26100018, PubMed:27437582, PubMed:28500754, PubMed:21775435, PubMed:22287571, PubMed:21768349).

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 (PubMed:27437582).

The mobility of the bridges ensures that the ends remain accessible for further processing by other repair factors (PubMed:27437582).

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 (PubMed:9242410, PubMed:10757784, PubMed:10854421, PubMed:12517771, PubMed:17290226, PubMed:19837014).

XRCC4 stabilizes LIG4, regulates its subcellular localization and enhances LIG4's joining activity (PubMed:9242410, PubMed:10757784, PubMed:10854421, PubMed:12517771, PubMed:17290226, PubMed:21982441, PubMed:22228831).

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 (PubMed:10757784, PubMed:10854421).

Promotes displacement of PNKP from processed strand break termini (PubMed:20852255, PubMed:28453785).

24 Publications

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

Caution

Sumoylation at Lys-210 was initially reported to regulate nuclear localization and recombination efficiency of XRCC4 (PubMed:16478998). This result is however not confirmed by another study (PubMed:25934149).2 Publications

<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

Pathway Commons web resource for biological pathway data

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PathwayCommonsi
Q13426

Reactome - a knowledgebase of biological pathways and processes

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Reactomei
R-HSA-164843, 2-LTR circle formation
R-HSA-3108214, SUMOylation of DNA damage response and repair proteins
R-HSA-5693571, Nonhomologous End-Joining (NHEJ)

SIGNOR Signaling Network Open Resource

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SIGNORi
Q13426

<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:
DNA repair protein XRCC4Curated
Short name:
hXRCC41 Publication
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_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:XRCC41 PublicationImported
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 5

Organism-specific databases

Human Gene Nomenclature Database

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HGNCi
HGNC:12831, XRCC4

Online Mendelian Inheritance in Man (OMIM)

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MIMi
194363, gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_Q13426

Eukaryotic Pathogen, Vector and Host Database Resources

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VEuPathDBi
HostDB:ENSG00000152422

<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 provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Short stature, microcephaly, and endocrine dysfunction (SSMED)7 Publications
The disease is caused by variants affecting the gene represented in this entry.
Disease descriptionA disease characterized by short stature and microcephaly apparent at birth, progressive postnatal growth failure, and endocrine dysfunction. In affected adults endocrine features include hypergonadotropic hypogonadism, multinodular goiter, and diabetes mellitus. Variable features observed in some patients are progressive ataxia, and lymphopenia or borderline leukopenia.
Related information in OMIM
Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_07582243W → R in SSMED; impairs the protein function in DNA double-strand break repair. 3 PublicationsCorresponds to variant dbSNP:rs587779351EnsemblClinVar.1
Natural variantiVAR_08496582D → E in SSMED; impaired ability to repair DNA double-strand breaks. 1 Publication1
Natural variantiVAR_084966161 – 336Missing in SSMED. 1 PublicationAdd BLAST176
Natural variantiVAR_075823161R → Q in SSMED; no expression of the protein is observed; complete loss of function in DNA double-strand break repair. 1 PublicationCorresponds to variant dbSNP:rs797045017EnsemblClinVar.1
Natural variantiVAR_084967210 – 336Missing in SSMED. 1 PublicationAdd BLAST127
Natural variantiVAR_084968225 – 336Missing in SSMED. 3 PublicationsAdd BLAST112
Natural variantiVAR_084969275 – 336Missing in SSMED. 2 PublicationsAdd BLAST62

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>Mutagenesisi4K → E: Abolished interaction with NHEJ1/XLF; when associated with E-99. 1 Publication1
Mutagenesisi26K → E: Abolished interaction with NHEJ1/XLF; when associated with E-99. 1 Publication1
Mutagenesisi55E → R: Abolished interaction with NHEJ1/XLF. 1 Publication1
Mutagenesisi58D → R: Abolished interaction with NHEJ1/XLF. 1 Publication1
Mutagenesisi61M → R: Abolished interaction with NHEJ1/XLF. 1 Publication1
Mutagenesisi62E → R: Does not affect interaction with NHEJ1/XLF. 1 Publication1
Mutagenesisi65K → E: Strongly decreased interaction with NHEJ1/XLF. Abolished interaction with NHEJ1/XLF; when associated with E-99. Abolished ability to bridge DNA; when associated with E-99. Abolished interaction with NHEJ1/XLF; when associated with E-102. 3 Publications1
Mutagenesisi69E → R: Does not affect interaction with NHEJ1/XLF. 1 Publication1
Mutagenesisi71R → E: Abolished interaction with NHEJ1/XLF; when associated with E-99. 1 Publication1
Mutagenesisi72K → E: Abolished interaction with NHEJ1/XLF; when associated with E-99. Abolished ability to bridge DNA; when associated with E-90 and E-99. 2 Publications1
Mutagenesisi90K → E: Abolished ability to bridge DNA; when associated with E-72 and E-99. 1 Publication1
Mutagenesisi99K → E: Abolished interaction with NHEJ1/XLF; when associated with E-4 or E-26 or E-65 or E-71 or E-72. Abolished ability to bridge DNA; when associated with E-65. Abolished ability to bridge DNA; when associated with E-72 and E-90. 2 Publications1
Mutagenesisi102K → E: Abolished interaction with NHEJ1/XLF; when associated with E-65. 1 Publication1
Mutagenesisi106F → E: Abolished interaction with NHEJ1/XLF. 1 Publication1
Mutagenesisi140K → R: No change in sumoylation. 1 Publication1
Mutagenesisi170E → A: Abolished DNA-binding. 1 Publication1
Mutagenesisi192R → A: Abolished DNA-binding. 1 Publication1
Mutagenesisi193S → A in XRCC4-Ala mutant; abolished phosphorylation by PRKDC; does not affect ability to bridge DNA when associated with NHEJ1/XLF phosphorylation-defective mutant; when associated with A-260, A-304, A-315, A-320, A-323, A-327 and A-328. 1 Publication1
Mutagenesisi193S → D in XRCC4-Asp mutant; phospho-mimetic mutant; abolished ability to bridge DNA when associated with NHEJ1/XLF phospho-mimetic mutant; when associated with D-260, D-304, D-315, D-320, D-323, D-327 and D-328. 1 Publication1
Mutagenesisi210K → R: Abolishes sumoylation. 5-fold decrease in recombination efficiency. Does not affect nuclear localization of XRCC4 and LIG4. 2 Publications1
Mutagenesisi233T → A: Abolished phosphorylation by CK2, leading to strongly reduced interaction with PNKP. 1 Publication1
Mutagenesisi235E → F: Impaired ability mediate double-strand break repair. 1 Publication1
Mutagenesisi260S → A: Reduced phosphorylation by PRKDC. In XRCC4-Ala mutant; abolished phosphorylation by PRKDC; does not affect ability to bridge DNA when associated with NHEJ1/XLF phosphorylation-defective mutant; when associated with A-193, A-304, A-315, A-320, A-323, A-327 and A-328. 3 Publications1
Mutagenesisi260S → D in XRCC4-Asp mutant; phospho-mimetic mutant; abolished ability to bridge DNA when associated with NHEJ1/XLF phospho-mimetic mutant; when associated with D-193, D-304, D-315, D-320, D-323, D-327 and D-328. 1 Publication1
Mutagenesisi262 – 265DVTD → AVTA in 2DA; abolished cleavage by caspase and ability to regulate phospholipid scramblase activity. 1 Publication4
Mutagenesisi264T → A: Does not affect phosphorylation by CK2. 1 Publication1
Mutagenesisi266I → G: Abolished cleavage by caspase and ability to regulate phospholipid scramblase activity. 1 Publication1
Mutagenesisi270R → A: Impaired ability to localize in the nucleus. 1 Publication1
Mutagenesisi271K → A: Impaired ability to localize in the nucleus, without affecting ability to activate phospholipid scramblase activity of XKR4. 1 Publication1
Mutagenesisi271K → R: Abolished nuclear localization of XRCC4 and LIG4. Impaired ability to repair DNA double-strand breaks (DSBs). Reduced ubiquitination by the SCF(FBXW7) complex caused by impaired localization to the nucleus. 2 Publications1
Mutagenesisi272R → A: Impaired ability to localize in the nucleus, without affecting ability to activate phospholipid scramblase activity of XKR4. 1 Publication1
Mutagenesisi273R → A: Impaired ability to localize in the nucleus, without affecting ability to activate phospholipid scramblase activity of XKR4. 1 Publication1
Mutagenesisi275R → A: Does not affect ability to localize into the nucleus. 1 Publication1
Mutagenesisi282T → A: Does not affect phosphorylation by CK2. 1 Publication1
Mutagenesisi285K → R: Does not affect ubiquitination by the SCF(FBXW7) complex. 1 Publication1
Mutagenesisi296K → R: Abolished ubiquitination by the SCF(FBXW7) complex. 1 Publication1
Mutagenesisi304S → A in XRCC4-Ala mutant; abolished phosphorylation by PRKDC; does not affect ability to bridge DNA when associated with NHEJ1/XLF phosphorylation-defective mutant; when associated with A-193, A-260, A-315, A-320, A-323, A-327 and A-328. 1 Publication1
Mutagenesisi304S → D in XRCC4-Asp mutant; phospho-mimetic mutant; abolished ability to bridge DNA when associated with NHEJ1/XLF phospho-mimetic mutant; when associated with D-193, D-260, D-315, D-320, D-323, D-327 and D-328. 1 Publication1
Mutagenesisi308T → A: Does not affect phosphorylation by CK2. 1 Publication1
Mutagenesisi308T → R: Does not affect ubiquitination by the SCF(FBXW7) complex. 1 Publication1
Mutagenesisi315S → A in XRCC4-Ala mutant; abolished phosphorylation by PRKDC; does not affect ability to bridge DNA when associated with NHEJ1/XLF phosphorylation-defective mutant; when associated with A-193, A-260, A-304, A-320, A-323, A-327 and A-328. 1 Publication1
Mutagenesisi315S → D in XRCC4-Asp mutant; phospho-mimetic mutant; abolished ability to bridge DNA when associated with NHEJ1/XLF phospho-mimetic mutant; when associated with D-193, D-260, D-304, D-320, D-323, D-327 and D-328. 1 Publication1
Mutagenesisi320S → A: Slightly reduced phosphorylation by PRKDC. In XRCC4-Ala mutant; abolished phosphorylation by PRKDC; does not affect ability to bridge DNA when associated with NHEJ1/XLF phosphorylation-defective mutant; when associated with A-193, A-260, A-304, A-315, A-323, A-327 and A-328. 2 Publications1
Mutagenesisi320S → D in XRCC4-Asp mutant; phospho-mimetic mutant; abolished ability to bridge DNA when associated with NHEJ1/XLF phospho-mimetic mutant; when associated with D-193, D-260, D-304, D-315, D-323, D-327 and D-328. 1 Publication1
Mutagenesisi322E → L: Does not affect ability mediate double-strand break repair. 1 Publication1
Mutagenesisi323T → A in XRCC4-Ala mutant; abolished phosphorylation by PRKDC; does not affect ability to bridge DNA when associated with NHEJ1/XLF phosphorylation-defective mutant; when associated with A-193, A-260, A-304, A-315, A-320, A-327 and A-328. Does not affect phosphorylation by CK2. 2 Publications1
Mutagenesisi323T → D: Does not affect ability mediate double-strand break repair. In XRCC4-Asp mutant; phospho-mimetic mutant; abolished ability to bridge DNA when associated with NHEJ1/XLF phospho-mimetic mutant; when associated with D-193, D-260, D-304, D-315, D-320, D-327 and D-328. 2 Publications1
Mutagenesisi324L → W: Does not affect ability mediate double-strand break repair. 1 Publication1
Mutagenesisi326N → L: Abolished ability mediate double-strand break repair; impaired nuclear localization. 1 Publication1
Mutagenesisi327 – 328SS → AA: Reduced ubiquitination by the SCF(FBXW7) complex. 1 Publication2
Mutagenesisi327S → A in XRCC4-Ala mutant; abolished phosphorylation by PRKDC; does not affect ability to bridge DNA when associated with NHEJ1/XLF phosphorylation-defective mutant; when associated with A-193, A-260, A-304, A-315, A-320, A-323 and A-328. 1 Publication1
Mutagenesisi327S → D: Does not affect ability mediate double-strand break repair. In XRCC4-Asp mutant; phospho-mimetic mutant; abolished ability to bridge DNA when associated with NHEJ1/XLF phospho-mimetic mutant; when associated with D-193, D-260, D-304, D-315, D-320, D-323 and D-328. 2 Publications1
Mutagenesisi328S → A in XRCC4-Ala mutant; abolished phosphorylation by PRKDC; does not affect ability to bridge DNA when associated with NHEJ1/XLF phosphorylation-defective mutant; when associated with A-193, A-260, A-304, A-315, A-320, A-323 and A-327. 1 Publication1
Mutagenesisi328S → D: Does not affect ability mediate double-strand break repair. In XRCC4-Asp mutant; phospho-mimetic mutant; abolished ability to bridge DNA when associated with NHEJ1/XLF phospho-mimetic mutant; when associated with D-193, D-260, D-304, D-315, D-320, D-323 and D-327. 2 Publications1
Mutagenesisi329P → W: Does not affect ability mediate double-strand break repair. 1 Publication1
Mutagenesisi330E → L: Does not affect ability mediate double-strand break repair. 1 Publication1
Mutagenesisi331D → L: Does not affect ability mediate double-strand break repair. 1 Publication1
Mutagenesisi332L → W: Does not affect ability mediate double-strand break repair. 1 Publication1
Mutagenesisi333F → Y: Does not affect ability mediate double-strand break repair. 1 Publication1
Mutagenesisi334D → L: Does not affect ability mediate double-strand break repair. 1 Publication1

Keywords - Diseasei

Disease variant, Dwarfism

Organism-specific databases

DisGeNET

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DisGeNETi
7518

MalaCards human disease database

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MalaCardsi
XRCC4
MIMi616541, phenotype

Open Targets

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OpenTargetsi
ENSG00000152422

Orphanet; a database dedicated to information on rare diseases and orphan drugs

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Orphaneti
99812, LIG4 syndrome
436182, Microcephalic primordial dwarfism-insulin resistance syndrome

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA37423

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

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Pharosi
Q13426, Tbio

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL4296097

Drug and drug target database

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DrugBanki
DB03963, S-(Dimethylarsenic)Cysteine

Genetic variation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
XRCC4

Domain mapping of disease mutations (DMDM)

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DMDMi
44888352

<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_00000660471 – 336DNA repair protein XRCC4Add BLAST336
ChainiPRO_0000453296266 – 336Protein XRCC4, C-terminus1 PublicationAdd BLAST71

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 PRKDC3 Publications1
<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-linki210Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)1 Publication
Modified residuei229PhosphotyrosineCombined sources1
Modified residuei232Phosphoserine1 Publication1
Modified residuei233Phosphothreonine; by CK2Combined sources3 Publications1
Modified residuei237PhosphoserineCombined sources1
Modified residuei256PhosphoserineCombined sources1
Modified residuei260Phosphoserine; by PRKDCCombined sources5 Publications1
Cross-linki296Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei303Phosphoserine; by PRKDC2 Publications1
Modified residuei304Phosphoserine; by PRKDCCombined sources1 Publication1
Modified residuei315Phosphoserine; by PRKDC3 Publications1
Modified residuei320Phosphoserine; by PRKDCCombined sources5 Publications1
Modified residuei323Phosphothreonine; by PRKDC3 Publications1
Modified residuei327Phosphoserine; by PRKDCCombined sources4 Publications1
Modified residuei328Phosphoserine; by PRKDCCombined sources4 Publications1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Phosphorylated by PRKDC at the C-terminus in response to DNA damage; Ser-260 and Ser-320 constitute the main phosphorylation sites (PubMed:9430729, PubMed:15177042, PubMed:14599745, PubMed:12547193, PubMed:26666690, PubMed:28500754, PubMed:30247612). Phosphorylations 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 (PubMed:22228831, PubMed:28500754). Phosphorylation by PRKDC does not prevent interaction with NHEJ1/XLF but disrupts ability to bridge DNA and promotes detachment from DNA (PubMed:22228831, PubMed:28500754). Phosphorylation at Ser-327 and Ser-328 by PRKDC promotes recognition by the SCF(FBXW7) complex and subsequent ubiquitination via 'Lys-63'-linked ubiquitin (PubMed:26774286). Phosphorylation at Thr-233 by CK2 promotes interaction with PNKP; regulating PNKP activity and localization to DNA damage sites (PubMed:15385968, PubMed:20852255, PubMed:28453785). Phosphorylation by CK2 promotes interaction with APTX (PubMed:15380105).13 Publications
Ubiquitinated at Lys-296 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-327 and Ser-328 by PRKDC, and 'Lys-63'-linked ubiquitination facilitates DNA non-homologous end joining (NHEJ) by enhancing association with XRCC5/Ku80 and XRCC6/Ku70 (PubMed:26774286). Monoubiquitinated (PubMed:16412978).2 Publications
Undergoes proteolytic processing by caspase-3 (CASP3) (Probable) (PubMed:33725486). 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 (PubMed:33725486).1 Publication1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei265 – 266Cleavage; by caspase-31 Publication2

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
Q13426

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
Q13426

MassIVE - Mass Spectrometry Interactive Virtual Environment

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MassIVEi
Q13426

MaxQB - The MaxQuant DataBase

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MaxQBi
Q13426

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

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PaxDbi
Q13426

PeptideAtlas

More...
PeptideAtlasi
Q13426

PRoteomics IDEntifications database

More...
PRIDEi
Q13426

ProteomicsDB: a multi-organism proteome resource

More...
ProteomicsDBi
59412 [Q13426-1]
59413 [Q13426-2]
59414 [Q13426-3]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q13426

MetOSite database of methionine sulfoxide sites

More...
MetOSitei
Q13426

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

More...
PhosphoSitePlusi
Q13426

<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 a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Widely expressed.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSG00000152422, Expressed in myocardium and 201 other tissues

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
Q13426, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
Q13426, HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
ENSG00000152422, Low tissue specificity

<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

Homodimer and homotetramer in solution (PubMed:25574025, PubMed:25670504, PubMed:25941166, PubMed:31548606, PubMed:11080143).

Interacts with NHEJ1/XLF; the interaction is direct and is mediated via a head-to-head interaction between N-terminal head regions (PubMed:16439205, PubMed:18158905, PubMed:20558749, PubMed:22228831, PubMed:26100018, PubMed:27437582, PubMed:21936820, PubMed:21775435, PubMed:22287571, PubMed:21768349).

Interacts with LIG4; the LIG4-XRCC4 subcomplex has a 1:2 stoichiometry and XRCC4 is required for LIG4 stability (PubMed:9259561, PubMed:12517771, PubMed:17290226, PubMed:21982441, PubMed:24984242, PubMed:25934149, PubMed:11702069, PubMed:19332554, PubMed:9242410).

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 (PubMed:10757784, PubMed:10854421, PubMed:17124166, PubMed:12547193, PubMed:26774286, PubMed:33854234). Additional component of the NHEJ complex includes PAXX (PubMed:16439205). 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 (PubMed:33854234).

Interacts with PRKDC; the interaction is direct (PubMed:12509254).

Interacts with XRCC6/Ku70; the interaction is direct (PubMed:17124166).

Interacts with APTX and APLF (PubMed:15380105, PubMed:17396150, PubMed:17353262, PubMed:18077224).

Forms a heterotetramer with IFFO1; the interaction involves LIG4-free XRCC4 and leads to the relocalization of IFFO1 to the sites of DNA damage (PubMed:31548606).

Interacts with PNKP; mainly interacts with PNKP when phosphorylated at Thr-233, but is also able to interact at much lower level with PNKP when not unphosphorylated (PubMed:15385968, PubMed:20852255, PubMed:28453785).

Interacts with POLL (DNA polymerase lambda) (PubMed:30250067).

39 Publications

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

1 Publication

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section">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="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
113352, 59 interactors

CORUM comprehensive resource of mammalian protein complexes

More...
CORUMi
Q13426

Database of interacting proteins

More...
DIPi
DIP-37957N

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

More...
ELMi
Q13426

Protein interaction database and analysis system

More...
IntActi
Q13426, 33 interactors

Molecular INTeraction database

More...
MINTi
Q13426

STRING: functional protein association networks

More...
STRINGi
9606.ENSP00000421491

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...
RNActi
Q13426, 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

Secondary structure

1336
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

More...
SMRi
Q13426

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
Q13426

<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 – 213Interaction with IFFO11 PublicationAdd BLAST213
Regioni180 – 213Interaction with LIG41 PublicationAdd BLAST34
Regioni212 – 249DisorderedSequence analysisAdd BLAST38
Regioni264 – 336DisorderedSequence analysisAdd BLAST73

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 coili184 – 212Sequence analysisAdd BLAST29

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>Motifi270 – 275Nuclear localization signal2 Publications6

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 biasi295 – 318Basic and acidic residuesSequence analysisAdd BLAST24

<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

Ensembl GeneTree

More...
GeneTreei
ENSGT00390000017079

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_072334_0_0_1

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q13426

Identification of Orthologs from Complete Genome Data

More...
OMAi
MQKDISF

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q13426

TreeFam database of animal gene trees

More...
TreeFami
TF101204

Family and domain databases

Database of protein disorder

More...
DisProti
DP00152

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_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>Sequences (3)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 3 <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
Isoform 1 (identifier: Q13426-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><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
MERKISRIHL VSEPSITHFL QVSWEKTLES GFVITLTDGH SAWTGTVSES
60 70 80 90 100
EISQEADDMA MEKGKYVGEL RKALLSGAGP ADVYTFNFSK ESCYFFFEKN
110 120 130 140 150
LKDVSFRLGS FNLEKVENPA EVIRELICYC LDTIAENQAK NEHLQKENER
160 170 180 190 200
LLRDWNDVQG RFEKCVSAKE ALETDLYKRF ILVLNEKKTK IRSLHNKLLN
210 220 230 240 250
AAQEREKDIK QEGETAICSE MTADRDPVYD ESTDEESENQ TDLSGLASAA
260 270 280 290 300
VSKDDSIISS LDVTDIAPSR KRRQRMQRNL GTEPKMAPQE NQLQEKENSR
310 320 330
PDSSLPETSK KEHISAENMS LETLRNSSPE DLFDEI
Length:336
Mass (Da):38,287
Last modified:March 1, 2004 - 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:iBE5FB99153479A4E
GO
Isoform 2 (identifier: Q13426-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     298-300: NSR → K

Show »
Length:334
Mass (Da):38,058
Checksum:iE32CC403854DCE9B
GO
Isoform 3 (identifier: Q13426-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     298-336: NSRPDSSLPETSKKEHISAENMSLETLRNSSPEDLFDEI → KGRKKETSEKEAV

Show »
Length:310
Mass (Da):35,372
Checksum:i30B8DCC13C64A548
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_02231012S → C1 PublicationCorresponds to variant dbSNP:rs28383138EnsemblClinVar.1
Natural variantiVAR_07582243W → R in SSMED; impairs the protein function in DNA double-strand break repair. 3 PublicationsCorresponds to variant dbSNP:rs587779351EnsemblClinVar.1
Natural variantiVAR_02231156A → T1 PublicationCorresponds to variant dbSNP:rs28383151Ensembl.1
Natural variantiVAR_08496582D → E in SSMED; impaired ability to repair DNA double-strand breaks. 1 Publication1
Natural variantiVAR_022312134I → T1 PublicationCorresponds to variant dbSNP:rs28360135Ensembl.1
Natural variantiVAR_022313142E → Q1 PublicationCorresponds to variant dbSNP:rs28360136EnsemblClinVar.1
Natural variantiVAR_084966161 – 336Missing in SSMED. 1 PublicationAdd BLAST176
Natural variantiVAR_075823161R → Q in SSMED; no expression of the protein is observed; complete loss of function in DNA double-strand break repair. 1 PublicationCorresponds to variant dbSNP:rs797045017EnsemblClinVar.1
Natural variantiVAR_084967210 – 336Missing in SSMED. 1 PublicationAdd BLAST127
Natural variantiVAR_084968225 – 336Missing in SSMED. 3 PublicationsAdd BLAST112
Natural variantiVAR_017810240Q → P. Corresponds to variant dbSNP:rs2974446Ensembl.1
Natural variantiVAR_017811247A → S1 PublicationCorresponds to variant dbSNP:rs3734091Ensembl.1
Natural variantiVAR_084969275 – 336Missing in SSMED. 2 PublicationsAdd BLAST62

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_009474298 – 336NSRPD…LFDEI → KGRKKETSEKEAV in isoform 3. 2 PublicationsAdd BLAST39
Alternative sequenceiVSP_009473298 – 300NSR → K in isoform 2. 1 Publication3

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
U40622 mRNA Translation: AAC50339.1
AF055285 AF055284 Genomic DNA Translation: AAD47297.1
AF055285 AF055284 Genomic DNA Translation: AAD47298.1
AB017445 mRNA Translation: BAB20668.1
BT007216 mRNA Translation: AAP35880.1
AK290739 mRNA Translation: BAF83428.1
AY940097 Genomic DNA Translation: AAX14046.1
CH471084 Genomic DNA Translation: EAW95898.1
BC005259 mRNA Translation: AAH05259.1
BC016314 mRNA Translation: AAH16314.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS4058.1 [Q13426-2]
CCDS4059.1 [Q13426-1]

NCBI Reference Sequences

More...
RefSeqi
NP_001304941.1, NM_001318012.1 [Q13426-1]
NP_001304942.1, NM_001318013.1 [Q13426-3]
NP_003392.1, NM_003401.4 [Q13426-2]
NP_071801.1, NM_022406.3 [Q13426-1]
NP_072044.1, NM_022550.3 [Q13426-2]
XP_011541928.1, XM_011543626.1 [Q13426-1]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000282268; ENSP00000282268; ENSG00000152422 [Q13426-2]
ENST00000338635; ENSP00000342011; ENSG00000152422 [Q13426-1]
ENST00000396027; ENSP00000379344; ENSG00000152422 [Q13426-2]
ENST00000511817; ENSP00000421491; ENSG00000152422 [Q13426-1]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
7518

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:7518

UCSC genome browser

More...
UCSCi
uc003kib.4, human [Q13426-1]

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U40622 mRNA Translation: AAC50339.1
AF055285 AF055284 Genomic DNA Translation: AAD47297.1
AF055285 AF055284 Genomic DNA Translation: AAD47298.1
AB017445 mRNA Translation: BAB20668.1
BT007216 mRNA Translation: AAP35880.1
AK290739 mRNA Translation: BAF83428.1
AY940097 Genomic DNA Translation: AAX14046.1
CH471084 Genomic DNA Translation: EAW95898.1
BC005259 mRNA Translation: AAH05259.1
BC016314 mRNA Translation: AAH16314.1
CCDSiCCDS4058.1 [Q13426-2]
CCDS4059.1 [Q13426-1]
RefSeqiNP_001304941.1, NM_001318012.1 [Q13426-1]
NP_001304942.1, NM_001318013.1 [Q13426-3]
NP_003392.1, NM_003401.4 [Q13426-2]
NP_071801.1, NM_022406.3 [Q13426-1]
NP_072044.1, NM_022550.3 [Q13426-2]
XP_011541928.1, XM_011543626.1 [Q13426-1]

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
1FU1X-ray2.70A/B1-203[»]
1IK9X-ray2.30A/B1-213[»]
3II6X-ray2.40A/B/C/D1-203[»]
3MUDX-ray2.20A/B2-133[»]
3Q4FX-ray5.50C/D/G/H1-157[»]
3RWRX-ray3.94A/B/F/G/J/K/N/P/R/U/V/Y1-157[»]
3SR2X-ray3.97A/B/E/F1-140[»]
3W03X-ray8.49C/D1-164[»]
4XA4X-ray2.33A/B2-147[»]
5CHXX-ray2.30A/B2-143[»]
5CJ0X-ray2.30A/B2-142[»]
5CJ4X-ray3.10A/B/C/D2-144[»]
5E50X-ray1.38C/D229-236[»]
5WJ7X-ray2.50A/B2-132[»]
5WLZX-ray3.50A/B/C/D2-132[»]
6ABOX-ray2.65A1-213[»]
7LSYelectron microscopy8.40F/G/O/P1-336[»]
7LT3electron microscopy4.60F/G/O/P1-336[»]
7M3PX-ray2.00A/B2-132[»]
SMRiQ13426
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi113352, 59 interactors
CORUMiQ13426
DIPiDIP-37957N
ELMiQ13426
IntActiQ13426, 33 interactors
MINTiQ13426
STRINGi9606.ENSP00000421491

Chemistry databases

ChEMBLiCHEMBL4296097
DrugBankiDB03963, S-(Dimethylarsenic)Cysteine

PTM databases

iPTMnetiQ13426
MetOSiteiQ13426
PhosphoSitePlusiQ13426

Genetic variation databases

BioMutaiXRCC4
DMDMi44888352

Proteomic databases

EPDiQ13426
jPOSTiQ13426
MassIVEiQ13426
MaxQBiQ13426
PaxDbiQ13426
PeptideAtlasiQ13426
PRIDEiQ13426
ProteomicsDBi59412 [Q13426-1]
59413 [Q13426-2]
59414 [Q13426-3]

Protocols and materials databases

Antibodypedia a portal for validated antibodies

More...
Antibodypediai
1873, 455 antibodies

The DNASU plasmid repository

More...
DNASUi
7518

Genome annotation databases

EnsembliENST00000282268; ENSP00000282268; ENSG00000152422 [Q13426-2]
ENST00000338635; ENSP00000342011; ENSG00000152422 [Q13426-1]
ENST00000396027; ENSP00000379344; ENSG00000152422 [Q13426-2]
ENST00000511817; ENSP00000421491; ENSG00000152422 [Q13426-1]
GeneIDi7518
KEGGihsa:7518
UCSCiuc003kib.4, human [Q13426-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
7518
DisGeNETi7518

GeneCards: human genes, protein and diseases

More...
GeneCardsi
XRCC4
HGNCiHGNC:12831, XRCC4
HPAiENSG00000152422, Low tissue specificity
MalaCardsiXRCC4
MIMi194363, gene
616541, phenotype
neXtProtiNX_Q13426
OpenTargetsiENSG00000152422
Orphaneti99812, LIG4 syndrome
436182, Microcephalic primordial dwarfism-insulin resistance syndrome
PharmGKBiPA37423
VEuPathDBiHostDB:ENSG00000152422

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiENOG502QWJA, Eukaryota
GeneTreeiENSGT00390000017079
HOGENOMiCLU_072334_0_0_1
InParanoidiQ13426
OMAiMQKDISF
PhylomeDBiQ13426
TreeFamiTF101204

Enzyme and pathway databases

PathwayCommonsiQ13426
ReactomeiR-HSA-164843, 2-LTR circle formation
R-HSA-3108214, SUMOylation of DNA damage response and repair proteins
R-HSA-5693571, Nonhomologous End-Joining (NHEJ)
SIGNORiQ13426

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...
BioGRID-ORCSi
7518, 80 hits in 1020 CRISPR screens

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

More...
ChiTaRSi
XRCC4, human
EvolutionaryTraceiQ13426

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
XRCC4

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

More...
GenomeRNAii
7518
PharosiQ13426, Tbio

Protein Ontology

More...
PROi
PR:Q13426
RNActiQ13426, protein

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000152422, Expressed in myocardium and 201 other tissues
ExpressionAtlasiQ13426, baseline and differential
GenevisibleiQ13426, HS

Family and domain databases

DisProtiDP00152
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

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MobiDBi
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<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_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: Q13426
Secondary accession number(s): A8K3X4, Q9BS72, Q9UP94
<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: March 1, 2004
Last sequence update: March 1, 2004
Last modified: September 29, 2021
This is version 196 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, Reference proteome

Documents

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