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UniProtKB - P18074 (ERCC2_HUMAN)

Entry version 229 (18 Sep 2019)
Sequence version 1 (01 Nov 1990)
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Protein

General transcription and DNA repair factor IIH helicase subunit XPD

Gene

ERCC2

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

ATP-dependent 5'-3' DNA helicase, component of the general transcription and DNA repair factor IIH (TFIIH) core complex, which is involved in general and transcription-coupled nucleotide excision repair (NER) of damaged DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. In NER, TFIIH acts by opening DNA around the lesion to allow the excision of the damaged oligonucleotide and its replacement by a new DNA fragment. The ATP-dependent helicase activity of XPD/ERCC2 is required for DNA opening. In transcription, TFIIH has an essential role in transcription initiation. When the pre-initiation complex (PIC) has been established, TFIIH is required for promoter opening and promoter escape. Phosphorylation of the C-terminal tail (CTD) of the largest subunit of RNA polymerase II by the kinase module CAK controls the initiation of transcription. XPD/ERCC2 acts by forming a bridge between CAK and the core-TFIIH complex. Involved in the regulation of vitamin-D receptor activity. As part of the mitotic spindle-associated MMXD complex it plays a role in chromosome segregation. Might have a role in aging process and could play a causative role in the generation of skin cancers.4 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<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

Protein has several cofactor binding sites:

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 bindingi116Iron-sulfur (4Fe-4S)By similarity1
Metal bindingi134Iron-sulfur (4Fe-4S)By similarity1
Metal bindingi155Iron-sulfur (4Fe-4S)By similarity1
Metal bindingi190Iron-sulfur (4Fe-4S)Curated1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi42 – 49ATPPROSITE-ProRule annotation8

<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

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

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

Molecular functionDNA-binding, Helicase, Hydrolase
Biological processChromosome partition, DNA damage, DNA repair, Host-virus interaction, Transcription, Transcription regulation
Ligand4Fe-4S, ATP-binding, Iron, Iron-sulfur, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-HSA-112382 Formation of RNA Pol II elongation complex
R-HSA-113418 Formation of the Early Elongation Complex
R-HSA-167152 Formation of HIV elongation complex in the absence of HIV Tat
R-HSA-167158 Formation of the HIV-1 Early Elongation Complex
R-HSA-167160 RNA Pol II CTD phosphorylation and interaction with CE during HIV infection
R-HSA-167161 HIV Transcription Initiation
R-HSA-167162 RNA Polymerase II HIV Promoter Escape
R-HSA-167172 Transcription of the HIV genome
R-HSA-167200 Formation of HIV-1 elongation complex containing HIV-1 Tat
R-HSA-167246 Tat-mediated elongation of the HIV-1 transcript
R-HSA-2564830 Cytosolic iron-sulfur cluster assembly
R-HSA-427413 NoRC negatively regulates rRNA expression
R-HSA-5696395 Formation of Incision Complex in GG-NER
R-HSA-5696400 Dual Incision in GG-NER
R-HSA-674695 RNA Polymerase II Pre-transcription Events
R-HSA-6781823 Formation of TC-NER Pre-Incision Complex
R-HSA-6781827 Transcription-Coupled Nucleotide Excision Repair (TC-NER)
R-HSA-6782135 Dual incision in TC-NER
R-HSA-6782210 Gap-filling DNA repair synthesis and ligation in TC-NER
R-HSA-6796648 TP53 Regulates Transcription of DNA Repair Genes
R-HSA-72086 mRNA Capping
R-HSA-73762 RNA Polymerase I Transcription Initiation
R-HSA-73772 RNA Polymerase I Promoter Escape
R-HSA-73776 RNA Polymerase II Promoter Escape
R-HSA-73779 RNA Polymerase II Transcription Pre-Initiation And Promoter Opening
R-HSA-73863 RNA Polymerase I Transcription Termination
R-HSA-75953 RNA Polymerase II Transcription Initiation
R-HSA-75955 RNA Polymerase II Transcription Elongation
R-HSA-76042 RNA Polymerase II Transcription Initiation And Promoter Clearance
R-HSA-77075 RNA Pol II CTD phosphorylation and interaction with CE

SIGNOR Signaling Network Open Resource

More...SIGNORi		P18074

<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:
General transcription and DNA repair factor IIH helicase subunit XPD (EC:3.6.4.12)
Short name:
TFIIH subunit XPD
Alternative name(s):
Basic transcription factor 2 80 kDa subunit
Short name:
BTF2 p80
CXPD
DNA excision repair protein ERCC-2
DNA repair protein complementing XP-D cells
TFIIH basal transcription factor complex 80 kDa subunit
Short name:
TFIIH 80 kDa subunit
Short name:
TFIIH p80
Xeroderma pigmentosum group D-complementing protein
<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:ERCC2
Synonyms:XPD, XPDC
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 19

Organism-specific databases

Human Gene Nomenclature Database

More...HGNCi		HGNC:3434 ERCC2

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		126340 gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_P18074

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

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

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, 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 D (XP-D)7 Publications
The disease is caused by mutations 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-D patients present features of Cockayne syndrome, including 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_00818747G → R in XP-D. Corresponds to variant dbSNP:rs1360631927Ensembl.1
Natural variantiVAR_01728276T → A in XP-D. 1
Natural variantiVAR_003622112R → H in TTD1 and XP-D. 3 PublicationsCorresponds to variant dbSNP:rs121913020EnsemblClinVar.1
Natural variantiVAR_008188234D → N in XP-D. Corresponds to variant dbSNP:rs1340806384Ensembl.1
Natural variantiVAR_003623461L → V in XP-D and TTD1. 3 PublicationsCorresponds to variant dbSNP:rs121913016EnsemblClinVar.1
Natural variantiVAR_017283485L → P in XP-D; the corresponding mutation in fission yeast causes complete loss of activity. 1 PublicationCorresponds to variant dbSNP:rs121913025EnsemblClinVar.1
Natural variantiVAR_017285511R → Q in XP-D. Corresponds to variant dbSNP:rs772572683Ensembl.1
Natural variantiVAR_003625541S → R in XP-D; mild. 1 PublicationCorresponds to variant dbSNP:rs121913019EnsemblClinVar.1
Natural variantiVAR_008191542Y → C in XP-D. 1
Natural variantiVAR_017286582 – 583EK → VSE in XP-D. 1 Publication2
Natural variantiVAR_008192601R → L in XP-D. Corresponds to variant dbSNP:rs140522180Ensembl.1
Natural variantiVAR_017289601R → W in XP-D. Corresponds to variant dbSNP:rs753641926Ensembl.1
Natural variantiVAR_003627602G → D in XP-D; combined with features of Cockayne syndrome. Corresponds to variant dbSNP:rs771824813Ensembl.1
Natural variantiVAR_003626616R → P in XP-D and TTD1. 1 PublicationCorresponds to variant dbSNP:rs376556895EnsemblClinVar.1
Natural variantiVAR_008193616R → W in XP-D and COFS2. 1 PublicationCorresponds to variant dbSNP:rs121913024EnsemblClinVar.1
Natural variantiVAR_017292666R → W in XP-D. Corresponds to variant dbSNP:rs752510317Ensembl.1
Natural variantiVAR_017293681D → N in XP-D and COFS2. 1 PublicationCorresponds to variant dbSNP:rs121913023EnsemblClinVar.1
Natural variantiVAR_008197683R → Q in XP-D. Corresponds to variant dbSNP:rs758439420EnsemblClinVar.1
Natural variantiVAR_008198683R → W in XP-D; vitamin D-mediated activation of CYP24A1 is impaired in patient fibroblasts due to altered TFIIH-dependent phosphorylation of ETS1, subsequent impaired cooperation of ETS1 with VDR and altered VDR recruitment to CYP24A1 promoter. 1 PublicationCorresponds to variant dbSNP:rs41556519EnsemblClinVar.1
Natural variantiVAR_003629716 – 730Missing in XP-D and TTD1. 1 PublicationAdd BLAST15
Trichothiodystrophy 1, photosensitive (TTD1)6 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA form of trichothiodystrophy, an autosomal recessive disease characterized by sulfur-deficient brittle hair and multisystem variable abnormalities. The spectrum of clinical features varies from mild disease with only hair involvement to severe disease with cutaneous, neurologic and profound developmental defects. Ichthyosis, intellectual and developmental disabilities, decreased fertility, abnormal characteristics at birth, ocular abnormalities, short stature, and infections are common manifestations. There are both photosensitive and non-photosensitive forms of the disorder. TTD1 patients manifest cutaneous photosensitivity.
Related information in OMIM
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_003622112R → H in TTD1 and XP-D. 3 PublicationsCorresponds to variant dbSNP:rs121913020EnsemblClinVar.1
Natural variantiVAR_008189259C → Y in TTD1. 1 PublicationCorresponds to variant dbSNP:rs370454709EnsemblClinVar.1
Natural variantiVAR_003623461L → V in XP-D and TTD1. 3 PublicationsCorresponds to variant dbSNP:rs121913016EnsemblClinVar.1
Natural variantiVAR_008190482Missing in TTD1. 1 Publication1
Natural variantiVAR_017284487R → G in TTD1. 1
Natural variantiVAR_003624488 – 493Missing in TTD1; mild. 1 Publication6
Natural variantiVAR_017287592R → P in TTD1. 1
Natural variantiVAR_017288594A → P in TTD1. 1
Natural variantiVAR_003626616R → P in XP-D and TTD1. 1 PublicationCorresponds to variant dbSNP:rs376556895EnsemblClinVar.1
Natural variantiVAR_008194658R → C in TTD1. 2 PublicationsCorresponds to variant dbSNP:rs121913021EnsemblClinVar.1
Natural variantiVAR_017290658R → G in TTD1. 1
Natural variantiVAR_008195658R → H in TTD1. Corresponds to variant dbSNP:rs762141272Ensembl.1
Natural variantiVAR_017291663C → R in TTD1. Corresponds to variant dbSNP:rs770367713Ensembl.1
Natural variantiVAR_008196673D → G in TTD1. 1 Publication1
Natural variantiVAR_008199713G → R in TTD1. 2 PublicationsCorresponds to variant dbSNP:rs121913022EnsemblClinVar.1
Natural variantiVAR_003629716 – 730Missing in XP-D and TTD1. 1 PublicationAdd BLAST15
Natural variantiVAR_003630722R → W in TTD1. 2 PublicationsCorresponds to variant dbSNP:rs121913026EnsemblClinVar.1
Natural variantiVAR_003631725A → P in TTD1. 1 PublicationCorresponds to variant dbSNP:rs121913018EnsemblClinVar.1
Cerebro-oculo-facio-skeletal syndrome 2 (COFS2)1 Publication
The disease is caused by mutations 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
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_008193616R → W in XP-D and COFS2. 1 PublicationCorresponds to variant dbSNP:rs121913024EnsemblClinVar.1
Natural variantiVAR_017293681D → N in XP-D and COFS2. 1 PublicationCorresponds to variant dbSNP:rs121913023EnsemblClinVar.1

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>Mutagenesisi48K → R: Decreased transcriptional activity of the reconstituted TFIIH complex. 1 Publication1
Mutagenesisi190C → S: Reduced iron-sulfur-binding. Iron-sulfur-binding is further decreased in absence of MMS19. 1 Publication1

Keywords - Diseasei

Cataract, Cockayne syndrome, Deafness, Disease mutation, Dwarfism, Ichthyosis, Xeroderma pigmentosum

Organism-specific databases

DisGeNET

More...DisGeNETi		2068

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

More...GeneReviewsi		ERCC2

MalaCards human disease database

More...MalaCardsi		ERCC2
MIMi278730 phenotype
601675 phenotype
610756 phenotype

Open Targets

More...OpenTargetsi		ENSG00000104884

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

More...Orphaneti		1466 COFS syndrome
33364 Trichothiodystrophy
910 Xeroderma pigmentosum
220295 Xeroderma pigmentosum-Cockayne syndrome complex

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA27848

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL4105743

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		ERCC2

Domain mapping of disease mutations (DMDM)

More...DMDMi		119540

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

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001019801 – 760General transcription and DNA repair factor IIH helicase subunit XPDAdd BLAST760

<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

ISGylated.1 Publication

Keywords - PTMi

Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		P18074

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P18074

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...MassIVEi		P18074

MaxQB - The MaxQuant DataBase

More...MaxQBi		P18074

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

More...PaxDbi		P18074

PeptideAtlas

More...PeptideAtlasi		P18074

PRoteomics IDEntifications database

More...PRIDEi		P18074

ProteomicsDB human proteome resource

More...ProteomicsDBi		53542 [P18074-1]
53543 [P18074-2]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P18074

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

More...PhosphoSitePlusi		P18074

<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

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000104884 Expressed in 124 organ(s), highest expression level in right adrenal gland

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		P18074 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P18074 HS

Organism-specific databases

Human Protein Atlas

More...HPAi		CAB005375
HPA038057
HPA069266

<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

Component of the 7-subunit TFIIH core complex composed of XPB/ERCC3, XPD/ERCC2, GTF2H1, GTF2H2, GTF2H3, GTF2H4 and GTF2H5, which is active in NER. The core complex associates with the 3-subunit CDK-activating kinase (CAK) module composed of CCNH/cyclin H, CDK7 and MNAT1 to form the 10-subunit holoenzyme (holo-TFIIH) active in transcription. The interaction with GTF2H2 results in the stimulation of the 5'-->3' helicase activity (PubMed:9771713, PubMed:9852112).

Component of the MMXD complex, which includes CIAO1, ERCC2, CIAO2B, MMS19 and SLC25A5 (PubMed:20797633).

Interacts with CIAO1 and CIAO2B; the interaction WITH CIAO2B is direct (PubMed:23891004).

Interacts with ATF7IP (PubMed:19106100).

Interacts directly with MMS19 (PubMed:23585563).

6 Publications

(Microbial infection)

Interacts with Epstein-Barr virus EBNA2.

1 Publication

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		108380, 38 interactors

CORUM comprehensive resource of mammalian protein complexes

More...CORUMi		P18074

Database of interacting proteins

More...DIPi		DIP-644N

Protein interaction database and analysis system

More...IntActi		P18074, 48 interactors

Molecular INTeraction database

More...MINTi		P18074

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000375809

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

3D structure databases

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

More...SMRi		P18074

Database of comparative protein structure models

More...ModBasei		Search...

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

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini7 – 283Helicase ATP-bindingPROSITE-ProRule annotationAdd BLAST277

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>Regioni438 – 637Mediates interaction with MMS19Add BLAST200

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>Motifi234 – 237DEAH box4
Motifi682 – 695Nuclear localization signalSequence analysisAdd BLAST14

<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 helicase family. RAD3/XPD subfamily.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG1131 Eukaryota
COG1199 LUCA

Ensembl GeneTree

More...GeneTreei		ENSGT00950000182970

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000205390

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P18074

KEGG Orthology (KO)

More...KOi		K10844

Identification of Orthologs from Complete Genome Data

More...OMAi		KKPLRFC

Database of Orthologous Groups

More...OrthoDBi		1214165at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		P18074

TreeFam database of animal gene trees

More...TreeFami		TF101232

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR006555 ATP-dep_Helicase_C
IPR010614 DEAD_2
IPR002464 DNA/RNA_helicase_DEAH_CS
IPR010643 HBB
IPR014013 Helic_SF1/SF2_ATP-bd_DinG/Rad3
IPR006554 Helicase-like_DEXD_c2
IPR027417 P-loop_NTPase
IPR013020 Rad3/Chl1-like
IPR001945 RAD3/XPD

The PANTHER Classification System

More...PANTHERi		PTHR11472:SF1 PTHR11472:SF1, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF06733 DEAD_2, 1 hit
PF06777 HBB, 1 hit
PF13307 Helicase_C_2, 1 hit

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR00852 XRODRMPGMNTD

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00488 DEXDc2, 1 hit
SM00491 HELICc2, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF52540 SSF52540, 1 hit

TIGRFAMs; a protein family database

More...TIGRFAMsi		TIGR00604 rad3, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS00690 DEAH_ATP_HELICASE, 1 hit
PS51193 HELICASE_ATP_BIND_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_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 (2+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

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

This entry has 2 described isoforms and 6 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: P18074-1) [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
MKLNVDGLLV YFPYDYIYPE QFSYMRELKR TLDAKGHGVL EMPSGTGKTV 
        60         70         80         90        100
SLLALIMAYQ RAYPLEVTKL IYCSRTVPEI EKVIEELRKL LNFYEKQEGE 
       110        120        130        140        150
KLPFLGLALS SRKNLCIHPE VTPLRFGKDV DGKCHSLTAS YVRAQYQHDT 
       160        170        180        190        200
SLPHCRFYEE FDAHGREVPL PAGIYNLDDL KALGRRQGWC PYFLARYSIL 
       210        220        230        240        250
HANVVVYSYH YLLDPKIADL VSKELARKAV VVFDEAHNID NVCIDSMSVN 
       260        270        280        290        300
LTRRTLDRCQ GNLETLQKTV LRIKETDEQR LRDEYRRLVE GLREASAARE 
       310        320        330        340        350
TDAHLANPVL PDEVLQEAVP GSIRTAEHFL GFLRRLLEYV KWRLRVQHVV 
       360        370        380        390        400
QESPPAFLSG LAQRVCIQRK PLRFCAERLR SLLHTLEITD LADFSPLTLL 
       410        420        430        440        450
ANFATLVSTY AKGFTIIIEP FDDRTPTIAN PILHFSCMDA SLAIKPVFER 
       460        470        480        490        500
FQSVIITSGT LSPLDIYPKI LDFHPVTMAT FTMTLARVCL CPMIIGRGND 
       510        520        530        540        550
QVAISSKFET REDIAVIRNY GNLLLEMSAV VPDGIVAFFT SYQYMESTVA 
       560        570        580        590        600
SWYEQGILEN IQRNKLLFIE TQDGAETSVA LEKYQEACEN GRGAILLSVA 
       610        620        630        640        650
RGKVSEGIDF VHHYGRAVIM FGVPYVYTQS RILKARLEYL RDQFQIREND 
       660        670        680        690        700
FLTFDAMRHA AQCVGRAIRG KTDYGLMVFA DKRFARGDKR GKLPRWIQEH 
       710        720        730        740        750
LTDANLNLTV DEGVQVAKYF LRQMAQPFHR EDQLGLSLLS LEQLESEETL 
       760
KRIEQIAQQL
Length:760
Mass (Da):86,909
Last modified:November 1, 1990 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i746C0888CDF2E331
GO
Isoform 2 (identifier: P18074-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-24: Missing.
     414-429: FTIIIEPFDDRTPTIA → QAQHCGSSRNQKRSHP
     430-760: Missing.

Note: No experimental confirmation available.
Show »
Length:405
Mass (Da):46,274
Checksum:iD56A486AC3C9D222
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 6 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A8MX75A8MX75_HUMAN
General transcription and DNA repai...
ERCC2
706Annotation 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>
K7EIT8K7EIT8_HUMAN
General transcription and DNA repai...
ERCC2
292Annotation 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>
E7EVE9E7EVE9_HUMAN
General transcription and DNA repai...
ERCC2
682Annotation 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>
B4E0F6B4E0F6_HUMAN
General transcription and DNA repai...
ERCC2
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>
K7ENL1K7ENL1_HUMAN
General transcription and DNA repai...
ERCC2
109Annotation 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>
K7EKF3K7EKF3_HUMAN
General transcription and DNA repai...
ERCC2
202Annotation 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>

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence AAM45142 differs from that shown. Reason: Erroneous gene model prediction.Curated

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_00818747G → R in XP-D. Corresponds to variant dbSNP:rs1360631927Ensembl.1
Natural variantiVAR_01728276T → A in XP-D. 1
Natural variantiVAR_003622112R → H in TTD1 and XP-D. 3 PublicationsCorresponds to variant dbSNP:rs121913020EnsemblClinVar.1
Natural variantiVAR_011412199I → M. Corresponds to variant dbSNP:rs1799791Ensembl.1
Natural variantiVAR_011413201H → Y. Corresponds to variant dbSNP:rs1799792EnsemblClinVar.1
Natural variantiVAR_008188234D → N in XP-D. Corresponds to variant dbSNP:rs1340806384Ensembl.1
Natural variantiVAR_008189259C → Y in TTD1. 1 PublicationCorresponds to variant dbSNP:rs370454709EnsemblClinVar.1
Natural variantiVAR_011414312D → N4 PublicationsCorresponds to variant dbSNP:rs1799793EnsemblClinVar.1
Natural variantiVAR_003623461L → V in XP-D and TTD1. 3 PublicationsCorresponds to variant dbSNP:rs121913016EnsemblClinVar.1
Natural variantiVAR_008190482Missing in TTD1. 1 Publication1
Natural variantiVAR_017283485L → P in XP-D; the corresponding mutation in fission yeast causes complete loss of activity. 1 PublicationCorresponds to variant dbSNP:rs121913025EnsemblClinVar.1
Natural variantiVAR_017284487R → G in TTD1. 1
Natural variantiVAR_003624488 – 493Missing in TTD1; mild. 1 Publication6
Natural variantiVAR_017285511R → Q in XP-D. Corresponds to variant dbSNP:rs772572683Ensembl.1
Natural variantiVAR_003625541S → R in XP-D; mild. 1 PublicationCorresponds to variant dbSNP:rs121913019EnsemblClinVar.1
Natural variantiVAR_008191542Y → C in XP-D. 1
Natural variantiVAR_017286582 – 583EK → VSE in XP-D. 1 Publication2
Natural variantiVAR_017287592R → P in TTD1. 1
Natural variantiVAR_017288594A → P in TTD1. 1
Natural variantiVAR_008192601R → L in XP-D. Corresponds to variant dbSNP:rs140522180Ensembl.1
Natural variantiVAR_017289601R → W in XP-D. Corresponds to variant dbSNP:rs753641926Ensembl.1
Natural variantiVAR_003627602G → D in XP-D; combined with features of Cockayne syndrome. Corresponds to variant dbSNP:rs771824813Ensembl.1
Natural variantiVAR_011415616R → C1 Publication1
Natural variantiVAR_003626616R → P in XP-D and TTD1. 1 PublicationCorresponds to variant dbSNP:rs376556895EnsemblClinVar.1
Natural variantiVAR_008193616R → W in XP-D and COFS2. 1 PublicationCorresponds to variant dbSNP:rs121913024EnsemblClinVar.1
Natural variantiVAR_008194658R → C in TTD1. 2 PublicationsCorresponds to variant dbSNP:rs121913021EnsemblClinVar.1
Natural variantiVAR_017290658R → G in TTD1. 1
Natural variantiVAR_008195658R → H in TTD1. Corresponds to variant dbSNP:rs762141272Ensembl.1
Natural variantiVAR_017291663C → R in TTD1. Corresponds to variant dbSNP:rs770367713Ensembl.1
Natural variantiVAR_017292666R → W in XP-D. Corresponds to variant dbSNP:rs752510317Ensembl.1
Natural variantiVAR_008196673D → G in TTD1. 1 Publication1
Natural variantiVAR_003628675G → R in XP-D/CS; severe form. 1 Publication1
Natural variantiVAR_017293681D → N in XP-D and COFS2. 1 PublicationCorresponds to variant dbSNP:rs121913023EnsemblClinVar.1
Natural variantiVAR_008197683R → Q in XP-D. Corresponds to variant dbSNP:rs758439420EnsemblClinVar.1
Natural variantiVAR_008198683R → W in XP-D; vitamin D-mediated activation of CYP24A1 is impaired in patient fibroblasts due to altered TFIIH-dependent phosphorylation of ETS1, subsequent impaired cooperation of ETS1 with VDR and altered VDR recruitment to CYP24A1 promoter. 1 PublicationCorresponds to variant dbSNP:rs41556519EnsemblClinVar.1
Natural variantiVAR_008199713G → R in TTD1. 2 PublicationsCorresponds to variant dbSNP:rs121913022EnsemblClinVar.1
Natural variantiVAR_003629716 – 730Missing in XP-D and TTD1. 1 PublicationAdd BLAST15
Natural variantiVAR_003630722R → W in TTD1. 2 PublicationsCorresponds to variant dbSNP:rs121913026EnsemblClinVar.1
Natural variantiVAR_003631725A → P in TTD1. 1 PublicationCorresponds to variant dbSNP:rs121913018EnsemblClinVar.1
Natural variantiVAR_011416751K → Q Polymorphism; may be associated with increased susceptibility to DNA damage. 6 PublicationsCorresponds to variant dbSNP:rs13181EnsemblClinVar.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_0431321 – 24Missing in isoform 2. 1 PublicationAdd BLAST24
Alternative sequenceiVSP_043133414 – 429FTIII…TPTIA → QAQHCGSSRNQKRSHP in isoform 2. 1 PublicationAdd BLAST16
Alternative sequenceiVSP_043134430 – 760Missing in isoform 2. 1 PublicationAdd BLAST331

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
X52221 mRNA Translation: CAA36463.1
X52222 mRNA Translation: CAA36464.1
L47234 Genomic DNA Translation: AAL48323.1
AY092780 Genomic DNA Translation: AAM45142.1 Sequence problems.
BT006883 mRNA Translation: AAP35529.1
CH471126 Genomic DNA Translation: EAW57341.1
BC108255 mRNA Translation: AAI08256.1
BC110523 mRNA Translation: AAI10524.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS33049.1 [P18074-1]
CCDS46112.1 [P18074-2]

Protein sequence database of the Protein Information Resource

More...PIRi		S10888

NCBI Reference Sequences

More...RefSeqi		NP_000391.1, NM_000400.3 [P18074-1]
NP_001124339.1, NM_001130867.1 [P18074-2]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000391945; ENSP00000375809; ENSG00000104884 [P18074-1]
ENST00000485403; ENSP00000431229; ENSG00000104884 [P18074-2]

Database of genes from NCBI RefSeq genomes

More...GeneIDi		2068

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:2068

UCSC genome browser

More...UCSCi		uc002pbj.3 human [P18074-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

<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

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X52221 mRNA Translation: CAA36463.1
X52222 mRNA Translation: CAA36464.1
L47234 Genomic DNA Translation: AAL48323.1
AY092780 Genomic DNA Translation: AAM45142.1 Sequence problems.
BT006883 mRNA Translation: AAP35529.1
CH471126 Genomic DNA Translation: EAW57341.1
BC108255 mRNA Translation: AAI08256.1
BC110523 mRNA Translation: AAI10524.1
CCDSiCCDS33049.1 [P18074-1]
CCDS46112.1 [P18074-2]
PIRiS10888
RefSeqiNP_000391.1, NM_000400.3 [P18074-1]
NP_001124339.1, NM_001130867.1 [P18074-2]

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
5IVWelectron microscopy10.00W1-760[»]
5IY6electron microscopy7.20W1-760[»]
5IY7electron microscopy8.60W1-760[»]
5IY8electron microscopy7.90W1-760[»]
5IY9electron microscopy6.30W1-760[»]
5OF4electron microscopy4.40B1-760[»]
6NMIelectron microscopy3.70B1-760[»]
6O9Lelectron microscopy7.2001-760[»]
6O9Melectron microscopy4.4001-760[»]
6RO4electron microscopy3.50B1-760[»]
SMRiP18074
ModBaseiSearch...

Protein-protein interaction databases

BioGridi108380, 38 interactors
CORUMiP18074
DIPiDIP-644N
IntActiP18074, 48 interactors
MINTiP18074
STRINGi9606.ENSP00000375809

Chemistry databases

ChEMBLiCHEMBL4105743

PTM databases

iPTMnetiP18074
PhosphoSitePlusiP18074

Polymorphism and mutation databases

BioMutaiERCC2
DMDMi119540

Proteomic databases

EPDiP18074
jPOSTiP18074
MassIVEiP18074
MaxQBiP18074
PaxDbiP18074
PeptideAtlasiP18074
PRIDEiP18074
ProteomicsDBi53542 [P18074-1]
53543 [P18074-2]

Protocols and materials databases

The DNASU plasmid repository

More...DNASUi		2068
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000391945; ENSP00000375809; ENSG00000104884 [P18074-1]
ENST00000485403; ENSP00000431229; ENSG00000104884 [P18074-2]
GeneIDi2068
KEGGihsa:2068
UCSCiuc002pbj.3 human [P18074-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		2068
DisGeNETi2068

GeneCards: human genes, protein and diseases

More...GeneCardsi		ERCC2
GeneReviewsiERCC2
HGNCiHGNC:3434 ERCC2
HPAiCAB005375
HPA038057
HPA069266
MalaCardsiERCC2
MIMi126340 gene
278730 phenotype
601675 phenotype
610756 phenotype
neXtProtiNX_P18074
OpenTargetsiENSG00000104884
Orphaneti1466 COFS syndrome
33364 Trichothiodystrophy
910 Xeroderma pigmentosum
220295 Xeroderma pigmentosum-Cockayne syndrome complex
PharmGKBiPA27848

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG1131 Eukaryota
COG1199 LUCA
GeneTreeiENSGT00950000182970
HOGENOMiHOG000205390
InParanoidiP18074
KOiK10844
OMAiKKPLRFC
OrthoDBi1214165at2759
PhylomeDBiP18074
TreeFamiTF101232

Enzyme and pathway databases

ReactomeiR-HSA-112382 Formation of RNA Pol II elongation complex
R-HSA-113418 Formation of the Early Elongation Complex
R-HSA-167152 Formation of HIV elongation complex in the absence of HIV Tat
R-HSA-167158 Formation of the HIV-1 Early Elongation Complex
R-HSA-167160 RNA Pol II CTD phosphorylation and interaction with CE during HIV infection
R-HSA-167161 HIV Transcription Initiation
R-HSA-167162 RNA Polymerase II HIV Promoter Escape
R-HSA-167172 Transcription of the HIV genome
R-HSA-167200 Formation of HIV-1 elongation complex containing HIV-1 Tat
R-HSA-167246 Tat-mediated elongation of the HIV-1 transcript
R-HSA-2564830 Cytosolic iron-sulfur cluster assembly
R-HSA-427413 NoRC negatively regulates rRNA expression
R-HSA-5696395 Formation of Incision Complex in GG-NER
R-HSA-5696400 Dual Incision in GG-NER
R-HSA-674695 RNA Polymerase II Pre-transcription Events
R-HSA-6781823 Formation of TC-NER Pre-Incision Complex
R-HSA-6781827 Transcription-Coupled Nucleotide Excision Repair (TC-NER)
R-HSA-6782135 Dual incision in TC-NER
R-HSA-6782210 Gap-filling DNA repair synthesis and ligation in TC-NER
R-HSA-6796648 TP53 Regulates Transcription of DNA Repair Genes
R-HSA-72086 mRNA Capping
R-HSA-73762 RNA Polymerase I Transcription Initiation
R-HSA-73772 RNA Polymerase I Promoter Escape
R-HSA-73776 RNA Polymerase II Promoter Escape
R-HSA-73779 RNA Polymerase II Transcription Pre-Initiation And Promoter Opening
R-HSA-73863 RNA Polymerase I Transcription Termination
R-HSA-75953 RNA Polymerase II Transcription Initiation
R-HSA-75955 RNA Polymerase II Transcription Elongation
R-HSA-76042 RNA Polymerase II Transcription Initiation And Promoter Clearance
R-HSA-77075 RNA Pol II CTD phosphorylation and interaction with CE
SIGNORiP18074

Miscellaneous databases

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

More...ChiTaRSi		ERCC2 human

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		ERCC2

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

More...GenomeRNAii		2068

Pharos

More...Pharosi		P18074

Protein Ontology

More...PROi		PR:P18074

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000104884 Expressed in 124 organ(s), highest expression level in right adrenal gland
ExpressionAtlasiP18074 baseline and differential
GenevisibleiP18074 HS

Family and domain databases

InterProiView protein in InterPro
IPR006555 ATP-dep_Helicase_C
IPR010614 DEAD_2
IPR002464 DNA/RNA_helicase_DEAH_CS
IPR010643 HBB
IPR014013 Helic_SF1/SF2_ATP-bd_DinG/Rad3
IPR006554 Helicase-like_DEXD_c2
IPR027417 P-loop_NTPase
IPR013020 Rad3/Chl1-like
IPR001945 RAD3/XPD
PANTHERiPTHR11472:SF1 PTHR11472:SF1, 1 hit
PfamiView protein in Pfam
PF06733 DEAD_2, 1 hit
PF06777 HBB, 1 hit
PF13307 Helicase_C_2, 1 hit
PRINTSiPR00852 XRODRMPGMNTD
SMARTiView protein in SMART
SM00488 DEXDc2, 1 hit
SM00491 HELICc2, 1 hit
SUPFAMiSSF52540 SSF52540, 1 hit
TIGRFAMsiTIGR00604 rad3, 1 hit
PROSITEiView protein in PROSITE
PS00690 DEAH_ATP_HELICASE, 1 hit
PS51193 HELICASE_ATP_BIND_2, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

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 nameiERCC2_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: P18074
Secondary accession number(s): Q2TB78
, Q2YDY2, Q7KZU6, Q8N721
<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: November 1, 1990
Last sequence update: November 1, 1990
Last modified: September 18, 2019
This is version 229 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
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