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Entry version 76 (22 Apr 2020)
Sequence version 1 (21 Sep 2011)
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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

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

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, 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.-)
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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000589 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 14

Organism-specific databases

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

More...
MGIi
MGI:1100494 Ercc6

<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

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

PeptideAtlas

More...
PeptideAtlasi
F8VPZ5

PRoteomics IDEntifications database

More...
PRIDEi
F8VPZ5

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 42 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 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

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

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
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 amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi356 – 393Asp/Glu-rich (acidic)Add BLAST38

<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
ENOG410XP4Z LUCA

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

KEGG Orthology (KO)

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KOi
K10841

Identification of Orthologs from Complete Genome Data

More...
OMAi
SVVKHDA

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

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_N, 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

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EMBLi

GenBank nucleotide sequence database

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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

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CCDSi
CCDS36868.1

NCBI Reference Sequences

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

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENSMUST00000066807; ENSMUSP00000066256; ENSMUSG00000054051

Database of genes from NCBI RefSeq genomes

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GeneIDi
319955

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
mmu:319955

UCSC genome browser

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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

SMRiF8VPZ5
ModBaseiSearch...

Protein-protein interaction databases

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

PTM databases

iPTMnetiF8VPZ5
PhosphoSitePlusiF8VPZ5

Proteomic databases

EPDiF8VPZ5
MaxQBiF8VPZ5
PaxDbiF8VPZ5
PeptideAtlasiF8VPZ5
PRIDEiF8VPZ5

Protocols and materials databases

Antibodypedia a portal for validated antibodies

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Antibodypediai
34972 386 antibodies

The DNASU plasmid repository

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DNASUi
319955

Genome annotation databases

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

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
2074
MGIiMGI:1100494 Ercc6

Phylogenomic databases

eggNOGiKOG0387 Eukaryota
ENOG410XP4Z LUCA
GeneTreeiENSGT00940000158057
HOGENOMiCLU_000315_7_2_1
InParanoidiF8VPZ5
KOiK10841
OMAiSVVKHDA
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

RNActiF8VPZ5 protein

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
Search...

Gene expression databases

BgeeiENSMUSG00000054051 Expressed in dorsal root ganglion and 42 other tissues
ExpressionAtlasiF8VPZ5 baseline and differential
GenevisibleiF8VPZ5 MM

Family and domain databases

Gene3Di3.40.50.10810, 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_N, 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

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

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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: April 22, 2020
This is version 76 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. SIMILARITY comments
    Index of protein domains and families
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
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