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Entry version 228 (02 Jun 2021)
Sequence version 3 (02 Sep 2008)
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Protein

DNA excision repair protein ERCC-5

Gene

ERCC5

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

Annotation score:5 out of 5

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

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

Single-stranded structure-specific DNA endonuclease involved in DNA excision repair (PubMed:8206890, PubMed:8090225, PubMed:8078765, PubMed:7651464, PubMed:32821917, PubMed:32522879).

Makes the 3'incision in DNA nucleotide excision repair (NER) (PubMed:8090225, PubMed:8078765, PubMed:32821917, PubMed:32522879).

Binds and bends DNA repair bubble substrate and breaks base stacking at the single-strand/double-strand DNA junction of the DNA bubble (PubMed:32522879).

Plays a role in base excision repair (BER) by promoting the binding of DNA glycosylase NTHL1 to its substrate and increasing NTHL1 catalytic activity that removes oxidized pyrimidines from DNA (PubMed:9927729).

Involved in transcription-coupled nucleotide excision repair (TCR) which allows RNA polymerase II-blocking lesions to be rapidly removed from the transcribed strand of active genes (PubMed:16246722).

Functions during the initial step of TCR in cooperation with ERCC6/CSB to recognized stalled RNA polymerase II (PubMed:16246722).

Also, stimulates ERCC6/CSB binding to the DNA repair bubble and ERCC6/CSB ATPase activity (PubMed:16246722).

Required for DNA replication fork maintenance and preservation of genomic stability (PubMed:26833090, PubMed:32522879).

Involved in homologous recombination repair (HRR) induced by DNA replication stress by recruiting RAD51, BRCA2, and PALB2 to the damaged DNA site (PubMed:26833090).

During HRR, binds to the replication fork with high specificity and stabilizes it (PubMed:32522879).

Also, acts upstream of HRR, to promote the release of BRCA1 from DNA (PubMed:26833090).

9 Publications

Caution

A paper describing an additional role for this protein in a base excision repair pathway that is not coupled to transcription has been retracted, because some of the experimental data were incorrect.1 Publication1 Publication

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Mg2+1 PublicationNote: Binds 2 magnesium ions per subunit. They probably participate in the reaction catalyzed by the enzyme. May bind an additional third magnesium ion after substrate binding.By similarity

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>pH dependencei

Optimum pH is 6.5-7.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi30Magnesium 1By similarity1
Metal bindingi77Magnesium 1By similarity1
Metal bindingi789Magnesium 1By similarity1
Metal bindingi791Magnesium 1By similarity1
Metal bindingi810Magnesium 2By similarity1
Metal bindingi812Magnesium 2By similarity1
Metal bindingi861Magnesium 2By similarity1

<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, Endonuclease, Hydrolase, Nuclease
Biological processDNA damage, DNA repair
LigandMagnesium, Metal-binding

Enzyme and pathway databases

Pathway Commons web resource for biological pathway data

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PathwayCommonsi
P28715

Reactome - a knowledgebase of biological pathways and processes

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Reactomei
R-HSA-5696395, Formation of Incision Complex in GG-NER
R-HSA-5696400, Dual Incision in GG-NER
R-HSA-6782135, Dual incision in TC-NER

SIGNOR Signaling Network Open Resource

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SIGNORi
P28715

<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 excision repair protein ERCC-5Curated (EC:3.1.-.-6 Publications)
Alternative name(s):
DNA repair protein complementing XP-G cells
Xeroderma pigmentosum group G-complementing protein
<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:ERCC5
Synonyms:ERCM2, XPG, XPGC
<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>OrganismiHomo sapiens (Human)
<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 identifieri9606 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<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
  • UP000005640 <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: Chromosome 13

Organism-specific databases

Human Gene Nomenclature Database

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HGNCi
HGNC:3437, ERCC5

Online Mendelian Inheritance in Man (OMIM)

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MIMi
133530, gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_P28715

Eukaryotic Pathogen, Vector and Host Database Resources

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VEuPathDBi
HostDB:ENSG00000134899.17

<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, 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

Xeroderma pigmentosum complementation group G (XP-G)6 Publications
The disease is caused by variants affecting the gene represented in this entry.
Disease descriptionAn autosomal recessive pigmentary skin disorder characterized by solar hypersensitivity of the skin, high predisposition for developing cancers on areas exposed to sunlight and, in some cases, neurological abnormalities. The skin develops marked freckling and other pigmentation abnormalities. Some XP-G patients present features of Cockayne syndrome, cachectic dwarfism, pigmentary retinopathy, ataxia, decreased nerve conduction velocities. The phenotype combining xeroderma pigmentosum and Cockayne syndrome traits is referred to as XP-CS complex.
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_07577328A → D in XP-G; patient cells show a strong DNA repair defect in response to UV light but not in response to oxidative stress; decreased nucleotide-excision repair activity. 1 PublicationCorresponds to variant dbSNP:rs267607281Ensembl.1
Natural variantiVAR_01528072P → H in XP-G; combined with features of Cockayne syndrome. 1 PublicationCorresponds to variant dbSNP:rs121434574EnsemblClinVar.1
Natural variantiVAR_007733792A → V in XP-G; mild form. 1 PublicationCorresponds to variant dbSNP:rs121434571EnsemblClinVar.1
Natural variantiVAR_017097858L → P in XP-G; reduced stability and greatly impaired endonuclease activity. 1 PublicationCorresponds to variant dbSNP:rs121434575EnsemblClinVar.1
Natural variantiVAR_017096874A → T in XP-G; mild form; residual activity. 1 PublicationCorresponds to variant dbSNP:rs121434576EnsemblClinVar.1
Natural variantiVAR_075774968W → C in XP-G; patient cells show a strong DNA repair defect in response to UV light but not in response to oxidative stress; decreased nucleotide-excision repair activity. 1 PublicationCorresponds to variant dbSNP:rs267607280EnsemblClinVar.1
Cerebro-oculo-facio-skeletal syndrome 3 (COFS3)1 Publication
The disease is caused by variants affecting the gene represented in this entry.
Disease descriptionA disorder of prenatal onset characterized by microcephaly, congenital cataracts, facial dysmorphism, neurogenic arthrogryposis, growth failure and severe psychomotor retardation. COFS is considered to be part of the nucleotide-excision repair disorders spectrum that include also xeroderma pigmentosum, trichothiodystrophy and Cockayne syndrome.
Related information in OMIM

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>Mutagenesisi67 – 68FF → AA: Slight reduction in endonuclease activity. Increased affinity for bubble DNA. 1 Publication2
Mutagenesisi955 – 956LD → AA: Reduced protein stability, two-fold decrease in 15-nt bubble DNA incision activity and smaller decrease in Y DNA incision activity; when associated with A-978 and A-981. 1 Publication2
Mutagenesisi978F → A: Reduced protein stability, two-fold decrease in 15-nt bubble DNA incision activity and smaller decrease in Y DNA incision activity; when associated with 955-A-A-956 and A-981. 1 Publication1
Mutagenesisi981L → A: Reduced protein stability, two-fold decrease in 15-nt bubble DNA incision activity and smaller decrease in Y DNA incision activity; when associated with 955-A-A-956 and A-978. 1 Publication1

Keywords - Diseasei

Cockayne syndrome, Deafness, Disease variant, Dwarfism, Xeroderma pigmentosum

Organism-specific databases

DisGeNET

More...
DisGeNETi
2073

GeneReviews a resource of expert-authored, peer-reviewed disease descriptions.

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GeneReviewsi
ERCC5

MalaCards human disease database

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MalaCardsi
ERCC5
MIMi278780, phenotype
616570, phenotype

Open Targets

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OpenTargetsi
ENSG00000134899

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

More...
Orphaneti
1466, COFS syndrome
910, Xeroderma pigmentosum
220295, Xeroderma pigmentosum-Cockayne syndrome complex

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA27851

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

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Pharosi
P28715, Tchem

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL4736

Genetic variation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
ERCC5

Domain mapping of disease mutations (DMDM)

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DMDMi
205371791

<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_00001540311 – 1186DNA excision repair protein ERCC-5Add BLAST1186

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 residuei8N6-acetyllysineCombined sources1
Modified residuei384PhosphoserineBy similarity1
Modified residuei705PhosphoserineBy similarity1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
P28715

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
P28715

MassIVE - Mass Spectrometry Interactive Virtual Environment

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MassIVEi
P28715

MaxQB - The MaxQuant DataBase

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MaxQBi
P28715

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

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PaxDbi
P28715

PeptideAtlas

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PeptideAtlasi
P28715

PRoteomics IDEntifications database

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PRIDEi
P28715

ProteomicsDB: a multi-organism proteome resource

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ProteomicsDBi
54495 [P28715-1]
54496 [P28715-2]
81837

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P28715

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

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PhosphoSitePlusi
P28715

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

Induced by replication stress caused by DNA double-strand breaks (DBS).1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000134899, Expressed in tendon of biceps brachii and 237 other tissues

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P28715, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P28715, HS

Organism-specific databases

Human Protein Atlas

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HPAi
ENSG00000134899, 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%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

Monomer (PubMed:32522879). Homodimer (PubMed:32522879).

Component of the homologous recombination repair (HR) complex composed of ERCC5/XPG, BRCA2, PALB2, DSS1 and RAD51 (PubMed:26833090). Within the complex, interacts with BRCA2 and PALB2 (PubMed:26833090).

Interacts with RNA polymerase II (PubMed:16246722).

Interacts (via C-terminus) with ERCC6/CSB; the interaction stimulates ERCC6/CSB binding to the DNA repair bubble and ERCC6/CSB ATPase activity (PubMed:16246722). May form a complex composed of RNA polymerase II, ERCC6/CSB and ERCC5/XPG which associates with the DNA repair bubble during transcription-coupled nucleotide excision repair (PubMed:16246722).

Interacts with BRCA1; the interaction promotes the release of BRCA1 from DNA (PubMed:26833090).

Interacts with PCNA (PubMed:9305916).

Interacts with NTHL1; the interaction stimulates NTHL1 activity and NTHL1 binding to its DNA substrate (PubMed:9927729).

5 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">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

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

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BioGRIDi
108385, 30 interactors

Database of interacting proteins

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DIPi
DIP-750N

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

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ELMi
P28715

Protein interaction database and analysis system

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IntActi
P28715, 13 interactors

STRING: functional protein association networks

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STRINGi
9606.ENSP00000347978

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
P28715

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

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RNActi
P28715, 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

11186
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

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SMRi
P28715

Database of comparative protein structure models

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ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

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PDBe-KBi
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 – 78N-domain1 PublicationAdd BLAST78
Regioni31 – 67DNA-binding; may bind to the undamaged single-strand DNA of the DNA repair bubbleCombined sources1 PublicationImportedAdd BLAST37
Regioni79 – 785Spacer region1 PublicationAdd BLAST707
Regioni306 – 342DisorderedSequence analysisAdd BLAST37
Regioni354 – 385DisorderedSequence analysisAdd BLAST32
Regioni404 – 473DisorderedSequence analysisAdd BLAST70
Regioni510 – 533DisorderedSequence analysisAdd BLAST24
Regioni667 – 724DisorderedSequence analysisAdd BLAST58
Regioni786 – 881I-domain1 PublicationAdd BLAST96
Regioni820 – 836DNA-binding; may bind to the undamaged single-strand DNA of the DNA repair bubbleCombined sources1 PublicationImportedAdd BLAST17
Regioni848 – 880DNA-binding; H2TH (helix-2turn-helix) motif which binds double-stranded DNACombined sources1 PublicationImportedAdd BLAST33
Regioni912 – 918DNA-binding; may bind double-stranded DNACombined sources1 PublicationImported7
Regioni981 – 1009Interaction with PCNA1 PublicationAdd BLAST29
Regioni1011 – 1186Interaction with ERCC6/CSB1 PublicationAdd BLAST176
Regioni1056 – 1081DisorderedSequence analysisAdd BLAST26
Regioni1095 – 1186DisorderedSequence analysisAdd BLAST92

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>Motifi1057 – 1074Nuclear localization signal 11 PublicationAdd BLAST18
Motifi1169 – 1186Nuclear localization signal 21 PublicationAdd BLAST18

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 biasi443 – 458Polar residuesSequence analysisAdd BLAST16
Compositional biasi676 – 724Basic and acidic residuesSequence analysisAdd BLAST49
Compositional biasi1095 – 1150Polar residuesSequence analysisAdd BLAST56
Compositional biasi1168 – 1186Basic residuesSequence analysisAdd BLAST19

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

Both nuclear localization signals 1 and 2 act as a monopartite signal which binds to the high affinity site on KPNA2/importin-alpha.1 Publication
Both the spacer region (also known as the recognition (R) domain) and C-terminal domain are required for stable binding to the DNA repair bubble (PubMed:16246722). However, both domains are dispensable for incision of DNA bubble structures (PubMed:16246722, PubMed:32821917, PubMed:32522879).3 Publications

<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

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG2520, Eukaryota

Ensembl GeneTree

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GeneTreei
ENSGT00510000048601

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
CLU_003018_2_0_1

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P28715

Identification of Orthologs from Complete Genome Data

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OMAi
RNRQDRM

Database of Orthologous Groups

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OrthoDBi
1094524at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
P28715

TreeFam database of animal gene trees

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TreeFami
TF101235

Family and domain databases

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR036279, 5-3_exonuclease_C_sf
IPR008918, HhH2
IPR029060, PIN-like_dom_sf
IPR006086, XPG-I_dom
IPR006084, XPG/Rad2
IPR001044, XPG/Rad2_eukaryotes
IPR019974, XPG_CS
IPR006085, XPG_DNA_repair_N

Pfam protein domain database

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Pfami
View protein in Pfam
PF00867, XPG_I, 1 hit
PF00752, XPG_N, 1 hit

Protein Motif fingerprint database; a protein domain database

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PRINTSi
PR00853, XPGRADSUPER
PR00066, XRODRMPGMNTG

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00279, HhH2, 1 hit
SM00484, XPGI, 1 hit
SM00485, XPGN, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF47807, SSF47807, 1 hit
SSF88723, SSF88723, 1 hit

TIGRFAMs; a protein family database

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TIGRFAMsi
TIGR00600, rad2, 1 hit

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS00841, XPG_1, 1 hit
PS00842, XPG_2, 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 (3+)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.

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

This entry has 3 described isoforms and 4 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: P28715-1) [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
MGVQGLWKLL ECSGRQVSPE ALEGKILAVD ISIWLNQALK GVRDRHGNSI
60 70 80 90 100
ENPHLLTLFH RLCKLLFFRI RPIFVFDGDA PLLKKQTLVK RRQRKDLASS
110 120 130 140 150
DSRKTTEKLL KTFLKRQAIK TAFRSKRDEA LPSLTQVRRE NDLYVLPPLQ
160 170 180 190 200
EEEKHSSEEE DEKEWQERMN QKQALQEEFF HNPQAIDIES EDFSSLPPEV
210 220 230 240 250
KHEILTDMKE FTKRRRTLFE AMPEESDDFS QYQLKGLLKK NYLNQHIEHV
260 270 280 290 300
QKEMNQQHSG HIRRQYEDEG GFLKEVESRR VVSEDTSHYI LIKGIQAKTV
310 320 330 340 350
AEVDSESLPS SSKMHGMSFD VKSSPCEKLK TEKEPDATPP SPRTLLAMQA
360 370 380 390 400
ALLGSSSEEE LESENRRQAR GRNAPAAVDE GSISPRTLSA IKRALDDDED
410 420 430 440 450
VKVCAGDDVQ TGGPGAEEMR INSSTENSDE GLKVRDGKGI PFTATLASSS
460 470 480 490 500
VNSAEEHVAS TNEGREPTDS VPKEQMSLVH VGTEAFPISD ESMIKDRKDR
510 520 530 540 550
LPLESAVVRH SDAPGLPNGR ELTPASPTCT NSVSKNETHA EVLEQQNELC
560 570 580 590 600
PYESKFDSSL LSSDDETKCK PNSASEVIGP VSLQETSSIV SVPSEAVDNV
610 620 630 640 650
ENVVSFNAKE HENFLETIQE QQTTESAGQD LISIPKAVEP MEIDSEESES
660 670 680 690 700
DGSFIEVQSV ISDEELQAEF PETSKPPSEQ GEEELVGTRE GEAPAESESL
710 720 730 740 750
LRDNSERDDV DGEPQEAEKD AEDSLHEWQD INLEELETLE SNLLAQQNSL
760 770 780 790 800
KAQKQQQERI AATVTGQMFL ESQELLRLFG IPYIQAPMEA EAQCAILDLT
810 820 830 840 850
DQTSGTITDD SDIWLFGARH VYRNFFNKNK FVEYYQYVDF HNQLGLDRNK
860 870 880 890 900
LINLAYLLGS DYTEGIPTVG CVTAMEILNE FPGHGLEPLL KFSEWWHEAQ
910 920 930 940 950
KNPKIRPNPH DTKVKKKLRT LQLTPGFPNP AVAEAYLKPV VDDSKGSFLW
960 970 980 990 1000
GKPDLDKIRE FCQRYFGWNR TKTDESLFPV LKQLDAQQTQ LRIDSFFRLA
1010 1020 1030 1040 1050
QQEKEDAKRI KSQRLNRAVT CMLRKEKEAA ASEIEAVSVA MEKEFELLDK
1060 1070 1080 1090 1100
AKGKTQKRGI TNTLEESSSL KRKRLSDSKG KNTCGGFLGE TCLSESSDGS
1110 1120 1130 1140 1150
SSEDAESSSL MNVQRRTAAK EPKTSASDSQ NSVKEAPVKN GGATTSSSSD
1160 1170 1180
SDDDGGKEKM VLVTARSVFG KKRRKLRRAR GRKRKT
Length:1,186
Mass (Da):133,108
Last modified:September 2, 2008 - v3
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iB0A844D617C53F2E
GO
Isoform 2 (identifier: P28715-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-767: Missing.

Show »
Length:419
Mass (Da):47,319
Checksum:iA26C01C3C1DFAC28
GO
Isoform 3 (identifier: P28715-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     225-232: ESDDFSQY → VYLPLLQP
     233-1186: Missing.

Note: Includes a cryptic exon found in intron 6.Curated
Show »
Length:232
Mass (Da):27,259
Checksum:iE2808BE7528D94F1
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
A0A494C0S2A0A494C0S2_HUMAN
DNA repair protein-complementing XP...
ERCC5
904Annotation 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>
A0A090HNM7A0A090HNM7_HUMAN
DNA repair protein-complementing XP...
ERCC5 ERCC5-201
1,018Annotation 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>
A0A494C113A0A494C113_HUMAN
DNA repair protein-complementing XP...
ERCC5
127Annotation 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>
F2Z2A1F2Z2A1_HUMAN
DNA repair protein-complementing XP...
ERCC5
43Annotation 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 conflicti55L → P in BAA03812 (PubMed:7510366).Curated1
Sequence conflicti120 – 122KTA → QTS in BAA03812 (PubMed:7510366).Curated3
Sequence conflicti126K → Q in BAA03812 (PubMed:7510366).Curated1
Sequence conflicti264 – 266RQY → SSH in BAA03812 (PubMed:7510366).Curated3
Sequence conflicti760I → F in BAA03812 (PubMed:7510366).Curated1
Sequence conflicti796I → V in BAA03812 (PubMed:7510366).Curated1
Sequence conflicti864 – 872EGIPTVGCV → GNTNCGLC in BAA03812 (PubMed:7510366).Curated9
Sequence conflicti959R → S in BAA03812 (PubMed:7510366).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_07577328A → D in XP-G; patient cells show a strong DNA repair defect in response to UV light but not in response to oxidative stress; decreased nucleotide-excision repair activity. 1 PublicationCorresponds to variant dbSNP:rs267607281Ensembl.1
Natural variantiVAR_01528072P → H in XP-G; combined with features of Cockayne syndrome. 1 PublicationCorresponds to variant dbSNP:rs121434574EnsemblClinVar.1
Natural variantiVAR_020431145V → I. Corresponds to variant dbSNP:rs4987063EnsemblClinVar.1
Natural variantiVAR_023120181H → R1 PublicationCorresponds to variant dbSNP:rs4150295EnsemblClinVar.1
Natural variantiVAR_007732254M → V4 PublicationsCorresponds to variant dbSNP:rs1047769EnsemblClinVar.1
Natural variantiVAR_020432256Q → R1 PublicationCorresponds to variant dbSNP:rs4150313EnsemblClinVar.1
Natural variantiVAR_014829311S → C1 PublicationCorresponds to variant dbSNP:rs2307491Ensembl.1
Natural variantiVAR_023121399E → K1 PublicationCorresponds to variant dbSNP:rs4150315Ensembl.1
Natural variantiVAR_020433529C → S1 PublicationCorresponds to variant dbSNP:rs2227869EnsemblClinVar.1
Natural variantiVAR_023122590V → I1 PublicationCorresponds to variant dbSNP:rs4150318EnsemblClinVar.1
Natural variantiVAR_023123597V → L1 PublicationCorresponds to variant dbSNP:rs4150319EnsemblClinVar.1
Natural variantiVAR_046373670F → L. Corresponds to variant dbSNP:rs1803542Ensembl.1
Natural variantiVAR_020434680Q → R. Corresponds to variant dbSNP:rs4987168Ensembl.1
Natural variantiVAR_007733792A → V in XP-G; mild form. 1 PublicationCorresponds to variant dbSNP:rs121434571EnsemblClinVar.1
Natural variantiVAR_017097858L → P in XP-G; reduced stability and greatly impaired endonuclease activity. 1 PublicationCorresponds to variant dbSNP:rs121434575EnsemblClinVar.1
Natural variantiVAR_017096874A → T in XP-G; mild form; residual activity. 1 PublicationCorresponds to variant dbSNP:rs121434576EnsemblClinVar.1
Natural variantiVAR_020435879N → S1 PublicationCorresponds to variant dbSNP:rs4150342EnsemblClinVar.1
Natural variantiVAR_075774968W → C in XP-G; patient cells show a strong DNA repair defect in response to UV light but not in response to oxidative stress; decreased nucleotide-excision repair activity. 1 PublicationCorresponds to variant dbSNP:rs267607280EnsemblClinVar.1
Natural variantiVAR_0231241009R → H1 PublicationCorresponds to variant dbSNP:rs4150387EnsemblClinVar.1
Natural variantiVAR_0463741053G → R6 PublicationsCorresponds to variant dbSNP:rs9514066Ensembl.1
Natural variantiVAR_0231251080G → Q Requires 2 nucleotide substitutions. 1 PublicationCorresponds to variant dbSNP:rs587778291Ensembl.1
Natural variantiVAR_0463751080G → R6 PublicationsCorresponds to variant dbSNP:rs9514067Ensembl.1
Natural variantiVAR_0077341104D → H1 PublicationCorresponds to variant dbSNP:rs17655EnsemblClinVar.1
Natural variantiVAR_0204361119A → V. Corresponds to variant dbSNP:rs2227871EnsemblClinVar.1

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_0353801 – 767Missing in isoform 2. CuratedAdd BLAST767
Alternative sequenceiVSP_053828225 – 232ESDDFSQY → VYLPLLQP in isoform 3. Curated8
Alternative sequenceiVSP_053829233 – 1186Missing in isoform 3. CuratedAdd BLAST954

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
X69978 mRNA Translation: CAA49598.1
D16305 mRNA Translation: BAA03812.1
L20046 mRNA Translation: AAC37533.1
AF255436 AF255435 Genomic DNA Translation: AAF89178.1
AF255442 AF255441 Genomic DNA Translation: AAF89179.1
AF462447 mRNA Translation: AAP97715.1
AF550128 Genomic DNA Translation: AAN46091.1
AL157769 Genomic DNA No translation available.
BC031522 mRNA Translation: AAH31522.1
X71341, X71342 Genomic DNA Translation: CAA50481.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS32004.1 [P28715-1]

Protein sequence database of the Protein Information Resource

More...
PIRi
I58009
S35993

NCBI Reference Sequences

More...
RefSeqi
NP_000114.2, NM_000123.3 [P28715-1]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000652225; ENSP00000498881; ENSG00000134899 [P28715-1]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
2073

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:2073

UCSC genome browser

More...
UCSCi
uc001vpw.4, human [P28715-1]

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%5Freferences%5Fsection">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

Atlas of Genetics and Cytogenetics in Oncology and Haematology
NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X69978 mRNA Translation: CAA49598.1
D16305 mRNA Translation: BAA03812.1
L20046 mRNA Translation: AAC37533.1
AF255436 AF255435 Genomic DNA Translation: AAF89178.1
AF255442 AF255441 Genomic DNA Translation: AAF89179.1
AF462447 mRNA Translation: AAP97715.1
AF550128 Genomic DNA Translation: AAN46091.1
AL157769 Genomic DNA No translation available.
BC031522 mRNA Translation: AAH31522.1
X71341, X71342 Genomic DNA Translation: CAA50481.1
CCDSiCCDS32004.1 [P28715-1]
PIRiI58009
S35993
RefSeqiNP_000114.2, NM_000123.3 [P28715-1]

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
5EKFX-ray2.00B/C1054-1077[»]
5EKGX-ray2.80B/C1168-1186[»]
6TURX-ray2.90AAA/BBB/CCC/DDD1-747[»]
AAA/BBB/CCC/DDD750-990[»]
6TUSX-ray2.50A/B1-747[»]
A/B750-990[»]
6TUWX-ray3.50A1-747[»]
A750-990[»]
6TUXX-ray3.10A/B1-747[»]
A/B750-986[»]
6VBHX-ray2.00A766-987[»]
SMRiP28715
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi108385, 30 interactors
DIPiDIP-750N
ELMiP28715
IntActiP28715, 13 interactors
STRINGi9606.ENSP00000347978

Chemistry databases

BindingDBiP28715
ChEMBLiCHEMBL4736

PTM databases

iPTMnetiP28715
PhosphoSitePlusiP28715

Genetic variation databases

BioMutaiERCC5
DMDMi205371791

Proteomic databases

EPDiP28715
jPOSTiP28715
MassIVEiP28715
MaxQBiP28715
PaxDbiP28715
PeptideAtlasiP28715
PRIDEiP28715
ProteomicsDBi54495 [P28715-1]
54496 [P28715-2]
81837

Protocols and materials databases

Antibodypedia a portal for validated antibodies

More...
Antibodypediai
11224, 372 antibodies

The DNASU plasmid repository

More...
DNASUi
2073

Genome annotation databases

EnsembliENST00000652225; ENSP00000498881; ENSG00000134899 [P28715-1]
GeneIDi2073
KEGGihsa:2073
UCSCiuc001vpw.4, human [P28715-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
2073
DisGeNETi2073

GeneCards: human genes, protein and diseases

More...
GeneCardsi
ERCC5
GeneReviewsiERCC5
HGNCiHGNC:3437, ERCC5
HPAiENSG00000134899, Low tissue specificity
MalaCardsiERCC5
MIMi133530, gene
278780, phenotype
616570, phenotype
neXtProtiNX_P28715
OpenTargetsiENSG00000134899
Orphaneti1466, COFS syndrome
910, Xeroderma pigmentosum
220295, Xeroderma pigmentosum-Cockayne syndrome complex
PharmGKBiPA27851
VEuPathDBiHostDB:ENSG00000134899.17

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG2520, Eukaryota
GeneTreeiENSGT00510000048601
HOGENOMiCLU_003018_2_0_1
InParanoidiP28715
OMAiRNRQDRM
OrthoDBi1094524at2759
PhylomeDBiP28715
TreeFamiTF101235

Enzyme and pathway databases

PathwayCommonsiP28715
ReactomeiR-HSA-5696395, Formation of Incision Complex in GG-NER
R-HSA-5696400, Dual Incision in GG-NER
R-HSA-6782135, Dual incision in TC-NER
SIGNORiP28715

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...
BioGRID-ORCSi
2073, 18 hits in 995 CRISPR screens

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
ERCC5

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

More...
GenomeRNAii
2073
PharosiP28715, Tchem

Protein Ontology

More...
PROi
PR:P28715
RNActiP28715, protein

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000134899, Expressed in tendon of biceps brachii and 237 other tissues
ExpressionAtlasiP28715, baseline and differential
GenevisibleiP28715, HS

Family and domain databases

InterProiView protein in InterPro
IPR036279, 5-3_exonuclease_C_sf
IPR008918, HhH2
IPR029060, PIN-like_dom_sf
IPR006086, XPG-I_dom
IPR006084, XPG/Rad2
IPR001044, XPG/Rad2_eukaryotes
IPR019974, XPG_CS
IPR006085, XPG_DNA_repair_N
PfamiView protein in Pfam
PF00867, XPG_I, 1 hit
PF00752, XPG_N, 1 hit
PRINTSiPR00853, XPGRADSUPER
PR00066, XRODRMPGMNTG
SMARTiView protein in SMART
SM00279, HhH2, 1 hit
SM00484, XPGI, 1 hit
SM00485, XPGN, 1 hit
SUPFAMiSSF47807, SSF47807, 1 hit
SSF88723, SSF88723, 1 hit
TIGRFAMsiTIGR00600, rad2, 1 hit
PROSITEiView protein in PROSITE
PS00841, XPG_1, 1 hit
PS00842, XPG_2, 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 nameiERCC5_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: P28715
Secondary accession number(s): A6NGT4
, Q5JUS4, Q5JUS5, Q7Z2V3, Q8IZL6, Q8N1B7, Q9HD59, Q9HD60
<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: April 1, 1993
Last sequence update: September 2, 2008
Last modified: June 2, 2021
This is version 228 of the entry and version 3 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

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

Keywords - Technical termi

3D-structure, Reference proteome

Documents

  1. Human chromosome 13
    Human chromosome 13: 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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