Ercc6
entrez
319955
canonical
uniprot
F8VPZ5
canonical
ensembl
ENSMUSG00000054051
resolver
ensp
ENSMUSP00000066256
resolver
ensp
ENSMUSP00000162006
resolver
enst
ENSMUST00000066807
resolver
genesymbol
Ercc6
resolver
genesymbol_syn
Csb
resolver
uniprot
A3KMN2
resolver
uniprot_entry
ERCC6_MOUSE
resolver
uniprot_sec
A3KMN2
resolver
amino_acid_sequence
MFHEEVPNSTHPQEQDCLPSQHANAYKDMPVGQENGGVSEAGECLSSTSCEYGPSTSAEACVLAATRRGPTLLHIDRHQIPAVEPSAQALELQGLGVDVYDQAVLEQGVLQQVDSAMHEASCVAQLADAEKEYQSVLDDLMSCTTSLRQINKIIEQLSPQAASNRDINRKLDSVKRQKYNKEQQLKKITAKQKRLQAILGGAGVQVELDHASLEEDDAEPGPSCLGSMLMPAQETAWEELIRTGQMTPFGTPAPQKQEKKPRKIMLNEASGFEKYLAEQAQLSFERKKQAATKRTAKKAIVISESSRAAIETKADQRSQVLSQTDKRLKKHSRKLQRRALQFQGKVGLPSGKKPLEPEVRPEAEGDTEGEESGSSPTDGEEEEEQEEEEGVASLSSDDVSYELKPLRKRQKYQKKVPVQEIDDDFFPSSEEEDEAMEGRGGGRKVARRQDDGDEDYYKQRLRRWNRLRLQDKEKRLKLEDDSEESDAEFDEGFKVPGFLFKKLFKYQQTGVRWLWELHCQQAGGILGDEMGLGKTIQIIAFLAGLSYSKIRTRGSNYRFEGLGPTIIVCPTTVMHQWVKEFHTWWPPFRVAVLHETGSYTHKKERLIRDIVYCHGVLITSYSYIRLMQDDISRHDWHYVILDEGHKIRNPNAAVTLACKQFRTPHRIILSGSPMQNNLRELWSLFDFIFPGKLGTLPVFMEQFSVPITMGGYSNASPVQVKTAYKCACVLRDTINPYLLRRMKSDVKMSLSLPDKNEQVLFCRLTDEQHKVYQNFIDSKAVYRILNGENQIFSGLVALRKICNHPDLFSGGPKNASGPPEDELEEEQFGHWRRSGKMIVVESLLKIWHRQGQRVLLFSQSRQMLHILEVFLRAHKYSYLKMDGTTTIASRQPLITKYNEDTSIFVFLLTTRVGGLGVNLTGANRVIIYDPDWNPSTDTQARERAWRIGQKKQVTVYRLLTAGTIEEKIYHRQIFKQFLTNRVLKDPKQRRFFKSNDLYELFTLTSPDASQGTETSAIFAGTGSSIQTPKCQLKKRTSTVLGTDPKCKKPPVSDTPANAATLIGEKPKAAGATGRSVTSGESGPFKGDHDTNGNRASSVAFGEETDAGSTLEHLSVMSGDGKHSDSPTVDHTSRPPVEASTSEKQGSSYAGARCQAQTEPVPMSEQMEGQFSKYKSKRKHDASEEETTEKRPQPKQKAKNSKHCRDAKFEGTRVPHLVKKRRYRQQTSEQEGGAKDRSSDDYVLEKLFKKSVGVHSVVRHDAIIDGSSPDYVLVEAEANRVAQDALKALRLSRQQCLGAASGVPTWTGHRGISGAPTGVKNRFGQKRDSSLPVQHPSSLTEKTQNNMKKEGKAHTPEHFSGKEDGASVSGAPSSSSLLARMRARNHMILPERLESDSEHLAEAAAVPPCGTEHDDLLVDMRNFIAFQAQVDGQASTQEILQEFESKLSVAQSCVFRELLRNLCNFHRTPGGEGIWKLKPEYC
uniprot
proteins
ec_number
3.6.4.-
uniprot
proteins
function
FUNCTION: Essential factor involved in transcription-coupled nucleotide excision repair (TC-NER), a process during which RNA polymerase II-blocking lesions are rapidly removed from the transcribed strand of active genes. Plays a central role in the initiation of the TC-NER process: specifically recognizes and binds RNA polymerase II stalled at a lesion, and mediates recruitment of ERCC8/CSA, initiating DNA damage excision by TFIIH recruitment. 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. Acts as a chromatin remodeler at DSBs; DNA-dependent ATPase-dependent activity is essential for this function. 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. 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. Mediates the activation of the ATM- and CHEK2-dependent DNA damage responses thus preventing premature entry of cells into mitosis following the induction of DNA DSBs. Remodels chromatin by evicting histones from chromatin flanking DSBs, limiting RIF1 accumulation at DSBs thereby promoting BRCA1-mediated HR. Required for stable recruitment of ELOA and CUL5 to DNA damage sites. Also involved in UV-induced translocation of ERCC8 to the nuclear matrix. Essential for neuronal differentiation and neuritogenesis; regulates transcription and chromatin remodeling activities required during neurogenesis. {ECO:0000250|UniProtKB:Q03468}.
uniprot
proteins
mass_dalton
165958
uniprot
proteins
post_translational_modification
PTM: 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). {ECO:0000250|UniProtKB:Q03468}.; PTM: 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). {ECO:0000250|UniProtKB:Q03468}.
uniprot
proteins
protein_family
SNF2/RAD54 helicase family
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
21183079
uniprot
proteins
sequence_length
1481
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q03468}. Chromosome {ECO:0000250|UniProtKB:Q03468}. Note=Recognizes and binds RNA polymerase II stalled at DNA damage sites. {ECO:0000250|UniProtKB:Q03468}.
uniprot
proteins