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Protein

DNA repair protein complementing XP-G cells homolog

Gene

Ercc5

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Single-stranded structure-specific DNA endonuclease involved in DNA excision repair. Makes the 3'incision in DNA nucleotide excision repair (NER). Acts as a cofactor for a DNA glycosylase that removes oxidized pyrimidines from DNA. May also be involved in transcription-coupled repair of this kind of damage, in transcription by RNA polymerase II, and perhaps in other processes too (By similarity).By similarity

Cofactori

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi30 – 301Magnesium 1By similarity
Metal bindingi77 – 771Magnesium 1By similarity
Metal bindingi788 – 7881Magnesium 1By similarity
Metal bindingi790 – 7901Magnesium 1By similarity
Metal bindingi809 – 8091Magnesium 2By similarity
Metal bindingi811 – 8111Magnesium 2By similarity
Metal bindingi860 – 8601Magnesium 2By similarity

GO - Molecular functioni

  1. bubble DNA binding Source: MGI
  2. double-stranded DNA binding Source: MGI
  3. endodeoxyribonuclease activity Source: MGI
  4. metal ion binding Source: UniProtKB-KW
  5. protein homodimerization activity Source: MGI
  6. protein N-terminus binding Source: MGI
  7. single-stranded DNA binding Source: MGI

GO - Biological processi

  1. determination of adult lifespan Source: MGI
  2. DNA catabolic process, endonucleolytic Source: MGI
  3. DNA repair Source: MGI
  4. multicellular organism growth Source: MGI
  5. negative regulation of apoptotic process Source: MGI
  6. nucleotide-excision repair Source: MGI
  7. nucleotide-excision repair, DNA incision, 3'-to lesion Source: MGI
  8. response to UV Source: MGI
  9. response to UV-C Source: MGI
  10. transcription-coupled nucleotide-excision repair Source: MGI
  11. UV protection Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Endonuclease, Hydrolase, Nuclease

Keywords - Biological processi

DNA damage, DNA repair

Keywords - Ligandi

DNA-binding, Magnesium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
DNA repair protein complementing XP-G cells homolog (EC:3.1.-.-)
Alternative name(s):
DNA excision repair protein ERCC-5
Xeroderma pigmentosum group G-complementing protein homolog
Gene namesi
Name:Ercc5
Synonyms:Ercc-5, Xpg
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:103582. Ercc5.

Subcellular locationi

  1. Nucleus By similarity

GO - Cellular componenti

  1. intermediate filament cytoskeleton Source: MGI
  2. nucleoplasm Source: MGI
  3. nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11701170DNA repair protein complementing XP-G cells homologPRO_0000154032Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei8 – 81N6-acetyllysineBy similarity
Modified residuei384 – 3841Phosphoserine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP35689.
PRIDEiP35689.

PTM databases

PhosphoSiteiP35689.

Expressioni

Gene expression databases

GenevestigatoriP35689.

Interactioni

Subunit structurei

Interacts with PCNA.By similarity

Structurei

3D structure databases

ProteinModelPortaliP35689.
SMRiP35689. Positions 2-113, 753-980.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 9595N-domainAdd
BLAST
Regioni752 – 882131I-domainAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi1049 – 106517Nuclear localization signalSequence AnalysisAdd
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0258.
HOGENOMiHOG000131367.
HOVERGENiHBG051501.
InParanoidiP35689.

Family and domain databases

Gene3Di3.40.50.1010. 2 hits.
InterProiIPR020045. 5-3_exonuclease_C.
IPR008918. HhH2.
IPR029060. PIN_domain-like.
IPR006086. XPG-I_dom.
IPR006084. XPG/Rad2.
IPR001044. XPG/Rad2_eukaryotes.
IPR019974. XPG_CS.
IPR006085. XPG_DNA_repair_N.
[Graphical view]
PfamiPF00867. XPG_I. 1 hit.
PF00752. XPG_N. 1 hit.
[Graphical view]
PRINTSiPR00853. XPGRADSUPER.
PR00066. XRODRMPGMNTG.
SMARTiSM00279. HhH2. 1 hit.
SM00484. XPGI. 1 hit.
SM00485. XPGN. 1 hit.
[Graphical view]
SUPFAMiSSF47807. SSF47807. 1 hit.
SSF88723. SSF88723. 2 hits.
TIGRFAMsiTIGR00600. rad2. 1 hit.
PROSITEiPS00841. XPG_1. 1 hit.
PS00842. XPG_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P35689-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGVQGLWKLL ECSGHRVSPE ALEGKVLAVD ISIWLNQALK GVRDSHGNVI
60 70 80 90 100
ENAHLLTLFH RLCKLLFFRI RPIFVFDGDA PLLKKQTLAK RRQRKDSASI
110 120 130 140 150
DSRKTTEKLL KTFLKRQALK TAFRSSRHEA PPSLTQVQRQ DDIYVLPPLP
160 170 180 190 200
EEEKHSSEEE DEKQWQARMD QKQALQEEFF HNPQAIDIES EDFSSLPPEV
210 220 230 240 250
KHEILTDMKE FTKRRRTLFE AMPEESNDFS QYQLKGLLKK NYLNQHIENV
260 270 280 290 300
QKEMNQQHSG QIQRQYQDEG GFLKEVESRR VVSEDTSHYI LIKGIQGKKV
310 320 330 340 350
MDVDSESLPS SSNVHSVSSN LKSSPHEKVK PEREPEAAPP SPRTLLAIQA
360 370 380 390 400
AMLGSSSEDE PESREGRQSK ERNSGATADA GSISPRTCAA IQKALDDDND
410 420 430 440 450
EKVSGSSDDL AEKMLLGSGL EQEEHADETA ERGGGVPFDT APLTPSVTEV
460 470 480 490 500
KECVTSGSSA NGQTDSAHSF TTASHRCDTP KETVSLARAV KEASQISSEC
510 520 530 540 550
EVEGRPAALS PAFIGTPSSH VSGVLSEREP TLAPPTTRTH SDQGIDIHPE
560 570 580 590 600
DPELQNGLYP LETKCNSSRL SSDDETEGGQ NPAPKACSTV HVPAEAMSNL
610 620 630 640 650
ENALPSNAEE RGDFQETIQL REVPEAAARE LISAPKPMGP MEMESEESES
660 670 680 690 700
DGSFIEVQSV VSNSELQTES SEASTHLSEK DAEEPRETLE EGTSRDTECL
710 720 730 740 750
LQDSSDIEAM EGHREADIDA EDMPNEWQDI NLEELDALES NLLAEQNSLK
760 770 780 790 800
AQKQQQDRIA ASVTGQMFLE SQELLRLFGV PYIQAPMEAE AQCAMLDLTD
810 820 830 840 850
QTSGTITDDS DIWLFGARHV YKNFFNKNKF VEYYQYVDFY SQLGLDRNKL
860 870 880 890 900
INLAYLLGSD YTEGIPTVGC VTAMEILNEF PGRGLDPLLK FSEWWHEAQN
910 920 930 940 950
NKKVAENPYD TKVKKKLRKL QLTPGFPNPA VADAYLRPVV DDSRGSFLWG
960 970 980 990 1000
KPDVDKISTF CQRYFGWNRM KTDESLYPVL KHLNAHQTQL RIDSFFRLAQ
1010 1020 1030 1040 1050
QEKQDAKLIK SHRLNRAVTC ILRKEREEKA PELTKVTEAL DDAKGKTQKR
1060 1070 1080 1090 1100
ELPYKKETSV PKRRRPSGNG GFLGDPYCSE SPQESSCEDG EGSSVMSARQ
1110 1120 1130 1140 1150
RSAAESSKIS CSDVPDLVRD PPHGRQGCVS TSSSSEDDED KAKTVLVTAR
1160 1170
PVFGKKKLKL KSMKRRKKKT
Length:1,170
Mass (Da):130,715
Last modified:October 3, 2012 - v4
Checksum:iB4B9F93ACEBC3729
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti388 – 3881C → R in BAA03813 (PubMed:7590748).Curated
Sequence conflicti419 – 4191G → R in BAA03813 (PubMed:7590748).Curated
Sequence conflicti419 – 4191G → R in AAA91039 (PubMed:8703115).Curated
Sequence conflicti419 – 4191G → R in AAB17885 (PubMed:8703115).Curated
Sequence conflicti462 – 4621G → E in BAA03813 (PubMed:7590748).Curated
Sequence conflicti462 – 4621G → E in AAA91039 (PubMed:8703115).Curated
Sequence conflicti462 – 4621G → E in AAB17885 (PubMed:8703115).Curated
Sequence conflicti488 – 4881R → S in BAA03813 (PubMed:7590748).Curated
Sequence conflicti688 – 6881T → I in BAA03813 (PubMed:7590748).Curated
Sequence conflicti799 – 7991T → S in BAA03813 (PubMed:7590748).Curated
Sequence conflicti799 – 7991T → S in AAA91039 (PubMed:8703115).Curated
Sequence conflicti799 – 7991T → S in AAB17885 (PubMed:8703115).Curated
Sequence conflicti958 – 9592ST → RE in BAA03813 (PubMed:7590748).Curated
Sequence conflicti958 – 9592ST → RE in AAA91039 (PubMed:8703115).Curated
Sequence conflicti958 – 9592ST → RE in AAB17885 (PubMed:8703115).Curated
Sequence conflicti1015 – 10151N → S in BAA03813 (PubMed:7590748).Curated
Sequence conflicti1021 – 10211I → M in BAA03813 (PubMed:7590748).Curated
Sequence conflicti1110 – 11101S → G in BAA03813 (PubMed:7590748).Curated
Sequence conflicti1110 – 11101S → G in AAA91039 (PubMed:8703115).Curated
Sequence conflicti1110 – 11101S → G in AAB17885 (PubMed:8703115).Curated
Sequence conflicti1121 – 11211P → S in BAA03813 (PubMed:7590748).Curated
Sequence conflicti1138 – 11381D → G in BAA03813 (PubMed:7590748).Curated
Sequence conflicti1138 – 11381D → G in AAA91039 (PubMed:8703115).Curated
Sequence conflicti1138 – 11381D → G in AAB17885 (PubMed:8703115).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D16306 mRNA. Translation: BAA03813.1.
U40796 mRNA. Translation: AAA91039.1.
U40795
, U39892, U39893, U39894, U39896, U40073, U40431, U40432, U40668, U40669, U40670, U40792, U40793, U40794 Genomic DNA. Translation: AAB17885.1.
AC123800 Genomic DNA. No translation available.
CCDSiCCDS35553.1.
PIRiA57650.
UniGeneiMm.2213.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D16306 mRNA. Translation: BAA03813.1.
U40796 mRNA. Translation: AAA91039.1.
U40795
, U39892, U39893, U39894, U39896, U40073, U40431, U40432, U40668, U40669, U40670, U40792, U40793, U40794 Genomic DNA. Translation: AAB17885.1.
AC123800 Genomic DNA. No translation available.
CCDSiCCDS35553.1.
PIRiA57650.
UniGeneiMm.2213.

3D structure databases

ProteinModelPortaliP35689.
SMRiP35689. Positions 2-113, 753-980.
ModBaseiSearch...
MobiDBiSearch...

PTM databases

PhosphoSiteiP35689.

Proteomic databases

MaxQBiP35689.
PRIDEiP35689.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

MGIiMGI:103582. Ercc5.

Phylogenomic databases

eggNOGiCOG0258.
HOGENOMiHOG000131367.
HOVERGENiHBG051501.
InParanoidiP35689.

Miscellaneous databases

PROiP35689.
SOURCEiSearch...

Gene expression databases

GenevestigatoriP35689.

Family and domain databases

Gene3Di3.40.50.1010. 2 hits.
InterProiIPR020045. 5-3_exonuclease_C.
IPR008918. HhH2.
IPR029060. PIN_domain-like.
IPR006086. XPG-I_dom.
IPR006084. XPG/Rad2.
IPR001044. XPG/Rad2_eukaryotes.
IPR019974. XPG_CS.
IPR006085. XPG_DNA_repair_N.
[Graphical view]
PfamiPF00867. XPG_I. 1 hit.
PF00752. XPG_N. 1 hit.
[Graphical view]
PRINTSiPR00853. XPGRADSUPER.
PR00066. XRODRMPGMNTG.
SMARTiSM00279. HhH2. 1 hit.
SM00484. XPGI. 1 hit.
SM00485. XPGN. 1 hit.
[Graphical view]
SUPFAMiSSF47807. SSF47807. 1 hit.
SSF88723. SSF88723. 2 hits.
TIGRFAMsiTIGR00600. rad2. 1 hit.
PROSITEiPS00841. XPG_1. 1 hit.
PS00842. XPG_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "An ERCC5 gene with homology to yeast RAD2 is involved in group G Xeroderma pigmentosum."
    Shiomi T., Harada Y.-N., Saito T., Shiomi N., Okuno Y., Yamaizumi M.
    Mutat. Res. 314:167-175(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Complementary DNA sequence and chromosomal localization of xpg, the mouse counterpart of human repair gene XPG/ERCC5."
    Harada Y.N., Matsuda Y., Shiomi N., Shiomi T.
    Genomics 28:59-65(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: C57BL/10.
    Tissue: Liver.
  3. "Molecular cloning and structural analysis of the functional mouse genomic XPG gene."
    Ludwig D.L., Mudgett J.S., Park M.S., Perez-Castro A.V., Macinnes M.A.
    Mamm. Genome 7:644-649(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
    Strain: DBA/2.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-384, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiERCC5_MOUSE
AccessioniPrimary (citable) accession number: P35689
Secondary accession number(s): Q61528, Q64248
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: October 3, 2012
Last modified: April 29, 2015
This is version 129 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, 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

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.