Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
The new UniProt website is here! Take me to UniProt BETA

UniProtKB - F8VPZ5 (ERCC6_MOUSE)

Entry version 86 (25 May 2022)
Sequence version 1 (21 Sep 2011)
Previous versions | rss
Add a publicationFeedback
Protein

DNA excision repair protein ERCC-6

Gene

Ercc6

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

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

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

Essential factor involved in transcription-coupled nucleotide excision repair which allows RNA polymerase II-blocking lesions to be rapidly removed from the transcribed strand of active genes (By similarity).

Upon DNA-binding, it locally modifies DNA conformation by wrapping the DNA around itself, thereby modifying the interface between stalled RNA polymerase II and DNA (By similarity).

It is required for transcription-coupled repair complex formation. It recruits the CSA complex (DCX(ERCC8) complex), nucleotide excision repair proteins and EP300 to the sites of RNA polymerase II-blocking lesions (By similarity).

Plays an important role in regulating the choice of the DNA double-strand breaks (DSBs) repair pathway and G2/M checkpoint activation; DNA-dependent ATPase activity is essential for this function (By similarity).

Regulates the DNA repair pathway choice by inhibiting non-homologous end joining (NHEJ), thereby promoting the homologous recombination (HR)-mediated repair of DSBs during the S/G2 phases of the cell cycle (By similarity).

Mediates the activation of the ATM- and CHEK2-dependent DNA damage responses thus preventing the premature exit from the G2/M checkpoint (By similarity).

Acts as a chromatin remodeler at DSBs; DNA-dependent ATPase-dependent activity is essential for this function (By similarity).

Remodels chromatin by evicting histones from chromatin flanking DSBs, limiting RIF1 accumulation at DSBs thereby promoting BRCA1-mediated HR (By similarity).

Required for stable recruitment of ELOA and CUL5 to DNA damage sites (By similarity).

Involved in UV-induced translocation of ERCC8 to the nuclear matrix (By similarity).

Essential for neuronal differentiation and neuritogenesis; regulates transcription and chromatin remodeling activities required during neurogenesis (By similarity).

By similarity

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

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 bindingi528 – 535ATPPROSITE-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 processDNA damage, DNA repair, Neurogenesis, Transcription, Transcription regulation
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-MMU-5250924, B-WICH complex positively regulates rRNA expression
R-MMU-6781823, Formation of TC-NER Pre-Incision Complex
R-MMU-6782135, Dual incision in TC-NER
R-MMU-6782210, Gap-filling DNA repair synthesis and ligation in TC-NER
R-MMU-73762, RNA Polymerase I Transcription Initiation

<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-6 (EC:3.6.4.-By similarity)
Alternative name(s):
ATP-dependent helicase ERCC6
Cockayne syndrome protein CSB
<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:Ercc6
Synonyms:Csb
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiMus musculus (Mouse)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri10090 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000589 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 14

Organism-specific databases

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

More...MGIi		MGI:1100494, Ercc6

Eukaryotic Pathogen, Vector and Host Database Resources

More...VEuPathDBi		HostDB:ENSMUSG00000054051

<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

Nucleus

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

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00004482421 – 1481DNA excision repair protein ERCC-6Add BLAST1481

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 residuei158Phosphoserine; by CDK2By similarity1
Modified residuei170N6-methylated lysine; by EHMT2By similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki256Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei298N6-methylated lysine; by EHMT2By similarity1
Modified residuei428PhosphoserineBy similarity1
Modified residuei429PhosphoserineBy similarity1
Modified residuei444N6-methylated lysine; by EHMT2By similarity1
Modified residuei482PhosphoserineBy similarity1
Modified residuei485PhosphoserineBy similarity1
Modified residuei1047N6-methylated lysine; by EHMT2By similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Phosphorylated in a cell cycle-dependent manner at Ser-158 by cyclin A-CDK2 in response to DNA damage (By similarity). Phosphorylation at this site promotes the intramolecular interaction of the N-terminal domain with the helicase ATP-binding domain, thereby probably releasing the inhibitory effect of the N-terminal domain on its ATPase activity (By similarity). Phosphorylation is essential for its chromatin remodeling activity (By similarity).By similarity
Ubiquitinated at the C-terminus (By similarity). Ubiquitination by the CSA complex leads to ERCC6 proteasomal degradation in a UV-dependent manner (By similarity). Stabilized following interaction with KIAA1530/UVSSA, which promotes recruitment of deubiquitinating enzyme USP7, leading to deubiquitination of ERCC6 thereby preventing UV-induced degradation of ERCC6 by the proteasome (By similarity).By similarity

Keywords - PTMi

Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		F8VPZ5

MaxQB - The MaxQuant DataBase

More...MaxQBi		F8VPZ5

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

More...PaxDbi		F8VPZ5

PRoteomics IDEntifications database

More...PRIDEi		F8VPZ5

ProteomicsDB: a multi-organism proteome resource

More...ProteomicsDBi		363699

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		F8VPZ5

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

More...PhosphoSitePlusi		F8VPZ5

<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		ENSMUSG00000054051, Expressed in dorsal root ganglion and 90 other tissues

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		F8VPZ5, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		F8VPZ5, MM

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

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer (By similarity). Binds DNA (By similarity).

Interacts with ERCC8 (By similarity).

Interacts with RNA polymerase II; interaction is enhanced by UV irradiation (By similarity).

Component of the B-WICH complex, at least composed of SMARCA5/SNF2H, BAZ1B/WSTF, SF3B1, DEK, MYO1C, ERCC6, MYBBP1A and DDX21 (By similarity).

Interacts with KIAA1530/UVSSA (By similarity).

Interacts with ELOA and CUL5; the interaction is induced by DNA damaging agents or by inhibitors of RNA polymerase II elongation (By similarity).

Interacts (via WHD region) with RIF1 (By similarity).

Interacts with SMARCC2/BAF170, SMARCB1/BAF47 and the neuron-specific chromatin remodeling complex (nBAF complex) (By similarity).

Interacts with ERCC5/XPG (via C-terminus); the interaction stimulates ERCC6/CSB binding to DNA repair bubble and ERCC6/CSB ATPase activity (By similarity). 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 (By similarity).

Interacts with CAND1, CSTF1, DDX3X, DDX5, DDX17, DDX23, DHX36, HDAC1, HNRNPU, MTA2, PRPF3, PSMD3, RBBP4, SFPQ, SMARCA1, SMARCA2, TOP1, USP7 and XRCC5 (By similarity).

By similarity

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

ComplexPortal: manually curated resource of macromolecular complexes

More...ComplexPortali		CPX-1133, B-WICH chromatin remodelling complex

STRING: functional protein association networks

More...STRINGi		10090.ENSMUSP00000066256

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		F8VPZ5, protein

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

3D structure databases

AlphaFold Protein Structure Database

More...AlphaFoldDBi		F8VPZ5

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

More...SMRi		F8VPZ5

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%5Fand%5Fdomains%5Fsection">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>Domaini515 – 691Helicase ATP-bindingPROSITE-ProRule annotationAdd BLAST177
Domaini839 – 998Helicase C-terminalPROSITE-ProRule annotationAdd BLAST160

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 – 506N-terminal domain; essential for its chromatin remodeling activityBy similarityAdd BLAST506
Regioni309 – 452DisorderedSequence analysisAdd BLAST144
Regioni1040 – 1096DisorderedSequence analysisAdd BLAST57
Regioni1114 – 1238DisorderedSequence analysisAdd BLAST125
Regioni1307 – 1372DisorderedSequence analysisAdd BLAST66
Regioni1387 – 1416Ubiquitin-binding domain (UBD)By similarityAdd BLAST30
Regioni1417 – 1481Winged-helix domain (WHD)By similarityAdd BLAST65
Regioni1434 – 1481Essential for its interaction with RNA polymerase II, transcription-coupled nucleotide excision repair activity, association with chromatin after UV irradiation and for mediating the UV-induced translocation of ERRC8 to the nuclear matrixBy similarityAdd BLAST48

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>Motifi642 – 645DEAH boxPROSITE-ProRule annotation4

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 biasi363 – 393Acidic residuesSequence analysisAdd BLAST31
Compositional biasi401 – 421Basic and acidic residuesSequence analysisAdd BLAST21
Compositional biasi432 – 452Basic and acidic residuesSequence analysisAdd BLAST21
Compositional biasi1129 – 1164Polar residuesSequence analysisAdd BLAST36
Compositional biasi1170 – 1238Basic and acidic residuesSequence analysisAdd BLAST69
Compositional biasi1322 – 1343Polar residuesSequence analysisAdd BLAST22
Compositional biasi1344 – 1360Basic and acidic residuesSequence analysisAdd BLAST17

<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

A C-terminal ubiquitin-binding domain (UBD) is essential for transcription-coupled nucleotide excision repair activity, interaction with RNA polymerase II, association with chromatin after UV irradiation and for mediating the UV-induced translocation of ERRC8 to the nuclear matrix.By similarity
The N-terminal domain exerts an inhibitory effect on the helicase ATP-binding domain in such a manner that its ATPase activity is restricted (By similarity). Phosphorylation at Ser-158 promotes the intramolecular interaction of the N-terminal domain with the helicase ATP-binding domain, thereby probably releasing the inhibitory effect of the N-terminal domain on its ATPase activity (By similarity).By similarity

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

Belongs to the SNF2/RAD54 helicase family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG0387, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT00940000158057

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_000315_7_2_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		F8VPZ5

Identification of Orthologs from Complete Genome Data

More...OMAi		HSVVKHD

Database of Orthologous Groups

More...OrthoDBi		372069at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		F8VPZ5

TreeFam database of animal gene trees

More...TreeFami		TF101236

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		3.40.50.10810, 1 hit
3.40.50.300, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR014001, Helicase_ATP-bd
IPR001650, Helicase_C
IPR027417, P-loop_NTPase
IPR038718, SNF2-like_sf
IPR000330, SNF2_N

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00271, Helicase_C, 1 hit
PF00176, SNF2-rel_dom, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00487, DEXDc, 1 hit
SM00490, HELICc, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF52540, SSF52540, 2 hits

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS51192, HELICASE_ATP_BIND_1, 1 hit
PS51194, HELICASE_CTER, 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>Sequence (1+)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 has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All

F8VPZ5-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MFHEEVPNST HPQEQDCLPS QHANAYKDMP VGQENGGVSE AGECLSSTSC 
        60         70         80         90        100
EYGPSTSAEA CVLAATRRGP TLLHIDRHQI PAVEPSAQAL ELQGLGVDVY 
       110        120        130        140        150
DQAVLEQGVL QQVDSAMHEA SCVAQLADAE KEYQSVLDDL MSCTTSLRQI 
       160        170        180        190        200
NKIIEQLSPQ AASNRDINRK LDSVKRQKYN KEQQLKKITA KQKRLQAILG 
       210        220        230        240        250
GAGVQVELDH ASLEEDDAEP GPSCLGSMLM PAQETAWEEL IRTGQMTPFG 
       260        270        280        290        300
TPAPQKQEKK PRKIMLNEAS GFEKYLAEQA QLSFERKKQA ATKRTAKKAI 
       310        320        330        340        350
VISESSRAAI ETKADQRSQV LSQTDKRLKK HSRKLQRRAL QFQGKVGLPS 
       360        370        380        390        400
GKKPLEPEVR PEAEGDTEGE ESGSSPTDGE EEEEQEEEEG VASLSSDDVS 
       410        420        430        440        450
YELKPLRKRQ KYQKKVPVQE IDDDFFPSSE EEDEAMEGRG GGRKVARRQD 
       460        470        480        490        500
DGDEDYYKQR LRRWNRLRLQ DKEKRLKLED DSEESDAEFD EGFKVPGFLF 
       510        520        530        540        550
KKLFKYQQTG VRWLWELHCQ QAGGILGDEM GLGKTIQIIA FLAGLSYSKI 
       560        570        580        590        600
RTRGSNYRFE GLGPTIIVCP TTVMHQWVKE FHTWWPPFRV AVLHETGSYT 
       610        620        630        640        650
HKKERLIRDI VYCHGVLITS YSYIRLMQDD ISRHDWHYVI LDEGHKIRNP 
       660        670        680        690        700
NAAVTLACKQ FRTPHRIILS GSPMQNNLRE LWSLFDFIFP GKLGTLPVFM 
       710        720        730        740        750
EQFSVPITMG GYSNASPVQV KTAYKCACVL RDTINPYLLR RMKSDVKMSL 
       760        770        780        790        800
SLPDKNEQVL FCRLTDEQHK VYQNFIDSKA VYRILNGENQ IFSGLVALRK 
       810        820        830        840        850
ICNHPDLFSG GPKNASGPPE DELEEEQFGH WRRSGKMIVV ESLLKIWHRQ 
       860        870        880        890        900
GQRVLLFSQS RQMLHILEVF LRAHKYSYLK MDGTTTIASR QPLITKYNED 
       910        920        930        940        950
TSIFVFLLTT RVGGLGVNLT GANRVIIYDP DWNPSTDTQA RERAWRIGQK 
       960        970        980        990       1000
KQVTVYRLLT AGTIEEKIYH RQIFKQFLTN RVLKDPKQRR FFKSNDLYEL 
      1010       1020       1030       1040       1050
FTLTSPDASQ GTETSAIFAG TGSSIQTPKC QLKKRTSTVL GTDPKCKKPP 
      1060       1070       1080       1090       1100
VSDTPANAAT LIGEKPKAAG ATGRSVTSGE SGPFKGDHDT NGNRASSVAF 
      1110       1120       1130       1140       1150
GEETDAGSTL EHLSVMSGDG KHSDSPTVDH TSRPPVEAST SEKQGSSYAG 
      1160       1170       1180       1190       1200
ARCQAQTEPV PMSEQMEGQF SKYKSKRKHD ASEEETTEKR PQPKQKAKNS 
      1210       1220       1230       1240       1250
KHCRDAKFEG TRVPHLVKKR RYRQQTSEQE GGAKDRSSDD YVLEKLFKKS 
      1260       1270       1280       1290       1300
VGVHSVVRHD AIIDGSSPDY VLVEAEANRV AQDALKALRL SRQQCLGAAS 
      1310       1320       1330       1340       1350
GVPTWTGHRG ISGAPTGVKN RFGQKRDSSL PVQHPSSLTE KTQNNMKKEG 
      1360       1370       1380       1390       1400
KAHTPEHFSG KEDGASVSGA PSSSSLLARM RARNHMILPE RLESDSEHLA 
      1410       1420       1430       1440       1450
EAAAVPPCGT EHDDLLVDMR NFIAFQAQVD GQASTQEILQ EFESKLSVAQ 
      1460       1470       1480 
SCVFRELLRN LCNFHRTPGG EGIWKLKPEY C
Length:1,481
Mass (Da):165,958
Last modified:September 21, 2011 - 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:i8907FDB060B94B73
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 is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A2I3BQP1A0A2I3BQP1_MOUSE
DNA excision repair protein ERCC-6
Ercc6
48Annotation 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>

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
AC154412 Genomic DNA No translation available.
BC132447 mRNA Translation: AAI32448.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS36868.1

NCBI Reference Sequences

More...RefSeqi		NP_001074690.1, NM_001081221.1
XP_006519183.1, XM_006519120.3

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENSMUST00000066807; ENSMUSP00000066256; ENSMUSG00000054051

Database of genes from NCBI RefSeq genomes

More...GeneIDi		319955

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		mmu:319955

UCSC genome browser

More...UCSCi		uc007sze.1, mouse

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC154412 Genomic DNA No translation available.
BC132447 mRNA Translation: AAI32448.1
CCDSiCCDS36868.1
RefSeqiNP_001074690.1, NM_001081221.1
XP_006519183.1, XM_006519120.3

3D structure databases

AlphaFoldDBiF8VPZ5
SMRiF8VPZ5
ModBaseiSearch...

Protein-protein interaction databases

ComplexPortaliCPX-1133, B-WICH chromatin remodelling complex
STRINGi10090.ENSMUSP00000066256

PTM databases

iPTMnetiF8VPZ5
PhosphoSitePlusiF8VPZ5

Proteomic databases

EPDiF8VPZ5
MaxQBiF8VPZ5
PaxDbiF8VPZ5
PRIDEiF8VPZ5
ProteomicsDBi363699

Protocols and materials databases

Antibodypedia a portal for validated antibodies

More...Antibodypediai		34972, 404 antibodies from 35 providers

The DNASU plasmid repository

More...DNASUi		319955

Genome annotation databases

EnsembliENSMUST00000066807; ENSMUSP00000066256; ENSMUSG00000054051
GeneIDi319955
KEGGimmu:319955
UCSCiuc007sze.1, mouse

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		2074
MGIiMGI:1100494, Ercc6
VEuPathDBiHostDB:ENSMUSG00000054051

Phylogenomic databases

eggNOGiKOG0387, Eukaryota
GeneTreeiENSGT00940000158057
HOGENOMiCLU_000315_7_2_1
InParanoidiF8VPZ5
OMAiHSVVKHD
OrthoDBi372069at2759
PhylomeDBiF8VPZ5
TreeFamiTF101236

Enzyme and pathway databases

ReactomeiR-MMU-5250924, B-WICH complex positively regulates rRNA expression
R-MMU-6781823, Formation of TC-NER Pre-Incision Complex
R-MMU-6782135, Dual incision in TC-NER
R-MMU-6782210, Gap-filling DNA repair synthesis and ligation in TC-NER
R-MMU-73762, RNA Polymerase I Transcription Initiation

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...BioGRID-ORCSi		319955, 7 hits in 110 CRISPR screens

Protein Ontology

More...PROi		PR:F8VPZ5
RNActiF8VPZ5, protein

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSMUSG00000054051, Expressed in dorsal root ganglion and 90 other tissues
ExpressionAtlasiF8VPZ5, baseline and differential
GenevisibleiF8VPZ5, MM

Family and domain databases

Gene3Di3.40.50.10810, 1 hit
3.40.50.300, 1 hit
InterProiView protein in InterPro
IPR014001, Helicase_ATP-bd
IPR001650, Helicase_C
IPR027417, P-loop_NTPase
IPR038718, SNF2-like_sf
IPR000330, SNF2_N
PfamiView protein in Pfam
PF00271, Helicase_C, 1 hit
PF00176, SNF2-rel_dom, 1 hit
SMARTiView protein in SMART
SM00487, DEXDc, 1 hit
SM00490, HELICc, 1 hit
SUPFAMiSSF52540, SSF52540, 2 hits
PROSITEiView protein in PROSITE
PS51192, HELICASE_ATP_BIND_1, 1 hit
PS51194, HELICASE_CTER, 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 nameiERCC6_MOUSE
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: F8VPZ5
Secondary accession number(s): A3KMN2
<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: October 16, 2019
Last sequence update: September 21, 2011
Last modified: May 25, 2022
This is version 86 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

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

Keywords - Technical termi

Reference proteome

Documents

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

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

Do not show this banner again