DNA repair protein complementing XP-G cells homolog

Contribute

Send feedback

Read comments (?) or add your own

P35689 (ERCC5_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 114. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

text xml rdf/xml gff fasta

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

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 names

Name:	Ercc5
Synonyms:	Ercc-5, Xpg

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	1170 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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.
Cofactor	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.
Subunit structure	Interacts with PCNA By similarity.
Subcellular location	Nucleus By similarity.
Sequence similarities	Belongs to the XPG/RAD2 endonuclease family. XPG subfamily.

Ontologies

Keywords
Biological process	DNA damage DNA repair
Cellular component	Nucleus
Ligand	DNA-binding Magnesium Metal-binding
Molecular function	Endonuclease Hydrolase Nuclease
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	UV protection Inferred from direct assay Ref.3. Source: MGI determination of adult lifespan Inferred from mutant phenotype PubMed 15082767. Source: MGI multicellular organism growth Inferred from mutant phenotype PubMed 10022922. Source: MGI nucleic acid phosphodiester bond hydrolysis Inferred from electronic annotation. Source: GOC nucleotide-excision repair Inferred from mutant phenotype PubMed 10022922. Source: MGI
Cellular_component	nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	endonuclease activity Inferred from electronic annotation. Source: UniProtKB-KW metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW single-stranded DNA binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1170

1170

DNA repair protein complementing XP-G cells homolog

PRO_0000154032

Regions

Region

1 – 95

N-domain

Region

752 – 882

131

I-domain

Motif

1049 – 1065

Nuclear localization signal Potential

Sites

Metal binding

Magnesium 1 By similarity

Metal binding

Magnesium 1 By similarity

Metal binding

788

Magnesium 1 By similarity

Metal binding

790

Magnesium 1 By similarity

Metal binding

809

Magnesium 2 By similarity

Metal binding

811

Magnesium 2 By similarity

Metal binding

860

Magnesium 2 By similarity

Amino acid modifications

Modified residue

N6-acetyllysine By similarity

Modified residue

156

Phosphoserine By similarity

Modified residue

157

Phosphoserine By similarity

Modified residue

341

Phosphoserine By similarity

Modified residue

355

Phosphoserine By similarity

Modified residue

356

Phosphoserine By similarity

Modified residue

357

Phosphoserine By similarity

Modified residue

363

Phosphoserine By similarity

Modified residue

384

Phosphoserine By similarity

Modified residue

418

Phosphoserine By similarity

Modified residue

568

Phosphoserine By similarity

Modified residue

571

Phosphoserine By similarity

Modified residue

572

Phosphoserine By similarity

Modified residue

704

Phosphoserine Ref.5

Modified residue

705

Phosphoserine Ref.5

Experimental info

Sequence conflict

388

C → R in BAA03813. Ref.2

Sequence conflict

419

G → R in BAA03813. Ref.2

Sequence conflict

419

G → R in AAA91039. Ref.3

Sequence conflict

419

G → R in AAB17885. Ref.3

Sequence conflict

462

G → E in BAA03813. Ref.2

Sequence conflict

462

G → E in AAA91039. Ref.3

Sequence conflict

462

G → E in AAB17885. Ref.3

Sequence conflict

488

R → S in BAA03813. Ref.2

Sequence conflict

688

T → I in BAA03813. Ref.2

Sequence conflict

799

T → S in BAA03813. Ref.2

Sequence conflict

799

T → S in AAA91039. Ref.3

Sequence conflict

799

T → S in AAB17885. Ref.3

Sequence conflict

958 – 959

ST → RE in BAA03813. Ref.2

Sequence conflict

958 – 959

ST → RE in AAA91039. Ref.3

Sequence conflict

958 – 959

ST → RE in AAB17885. Ref.3

Sequence conflict

1015

N → S in BAA03813. Ref.2

Sequence conflict

1021

I → M in BAA03813. Ref.2

Sequence conflict

1110

S → G in BAA03813. Ref.2

Sequence conflict

1110

S → G in AAA91039. Ref.3

Sequence conflict

1110

S → G in AAB17885. Ref.3

Sequence conflict

1121

P → S in BAA03813. Ref.2

Sequence conflict

1138

D → G in BAA03813. Ref.2

Sequence conflict

1138

D → G in AAA91039. Ref.3

Sequence conflict

1138

D → G in AAB17885. Ref.3

Sequences

Sequence

Length

Mass (Da)

Tools

P35689 [UniParc].

Last modified October 3, 2012. Version 4.
Checksum: B4B9F93ACEBC3729
Show »

FASTA

1,170

130,715

        10         20         30         40         50         60 
MGVQGLWKLL ECSGHRVSPE ALEGKVLAVD ISIWLNQALK GVRDSHGNVI ENAHLLTLFH 

        70         80         90        100        110        120 
RLCKLLFFRI RPIFVFDGDA PLLKKQTLAK RRQRKDSASI DSRKTTEKLL KTFLKRQALK 

       130        140        150        160        170        180 
TAFRSSRHEA PPSLTQVQRQ DDIYVLPPLP EEEKHSSEEE DEKQWQARMD QKQALQEEFF 

       190        200        210        220        230        240 
HNPQAIDIES EDFSSLPPEV KHEILTDMKE FTKRRRTLFE AMPEESNDFS QYQLKGLLKK 

       250        260        270        280        290        300 
NYLNQHIENV QKEMNQQHSG QIQRQYQDEG GFLKEVESRR VVSEDTSHYI LIKGIQGKKV 

       310        320        330        340        350        360 
MDVDSESLPS SSNVHSVSSN LKSSPHEKVK PEREPEAAPP SPRTLLAIQA AMLGSSSEDE 

       370        380        390        400        410        420 
PESREGRQSK ERNSGATADA GSISPRTCAA IQKALDDDND EKVSGSSDDL AEKMLLGSGL 

       430        440        450        460        470        480 
EQEEHADETA ERGGGVPFDT APLTPSVTEV KECVTSGSSA NGQTDSAHSF TTASHRCDTP 

       490        500        510        520        530        540 
KETVSLARAV KEASQISSEC EVEGRPAALS PAFIGTPSSH VSGVLSEREP TLAPPTTRTH 

       550        560        570        580        590        600 
SDQGIDIHPE DPELQNGLYP LETKCNSSRL SSDDETEGGQ NPAPKACSTV HVPAEAMSNL 

       610        620        630        640        650        660 
ENALPSNAEE RGDFQETIQL REVPEAAARE LISAPKPMGP MEMESEESES DGSFIEVQSV 

       670        680        690        700        710        720 
VSNSELQTES SEASTHLSEK DAEEPRETLE EGTSRDTECL LQDSSDIEAM EGHREADIDA 

       730        740        750        760        770        780 
EDMPNEWQDI NLEELDALES NLLAEQNSLK AQKQQQDRIA ASVTGQMFLE SQELLRLFGV 

       790        800        810        820        830        840 
PYIQAPMEAE AQCAMLDLTD QTSGTITDDS DIWLFGARHV YKNFFNKNKF VEYYQYVDFY 

       850        860        870        880        890        900 
SQLGLDRNKL INLAYLLGSD YTEGIPTVGC VTAMEILNEF PGRGLDPLLK FSEWWHEAQN 

       910        920        930        940        950        960 
NKKVAENPYD TKVKKKLRKL QLTPGFPNPA VADAYLRPVV DDSRGSFLWG KPDVDKISTF 

       970        980        990       1000       1010       1020 
CQRYFGWNRM KTDESLYPVL KHLNAHQTQL RIDSFFRLAQ QEKQDAKLIK SHRLNRAVTC 

      1030       1040       1050       1060       1070       1080 
ILRKEREEKA PELTKVTEAL DDAKGKTQKR ELPYKKETSV PKRRRPSGNG GFLGDPYCSE 

      1090       1100       1110       1120       1130       1140 
SPQESSCEDG EGSSVMSARQ RSAAESSKIS CSDVPDLVRD PPHGRQGCVS TSSSSEDDED 

      1150       1160       1170 
KAKTVLVTAR PVFGKKKLKL KSMKRRKKKT

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	"Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. Ponting C.P. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6J.
[5]	"Large-scale phosphorylation analysis of mouse liver." Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-704 AND SER-705, MASS SPECTROMETRY. Tissue: Liver.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	D16306 mRNA. Translation: BAA03813.1. U40796 mRNA. Translation: AAA91039.1. U40795 U40794 Genomic DNA. Translation: AAB17885.1. AC123800 Genomic DNA. No translation available.
IPI	IPI00310463.
PIR	A57650.
UniGene	Mm.2213.
3D structure databases
ProteinModelPortal	P35689.
SMR	P35689. Positions 2-127, 733-998.
ModBase	Search...
PTM databases
PhosphoSite	P35689.
Proteomic databases
PRIDE	P35689.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Organism-specific databases
MGI	MGI:103582. Ercc5.
Phylogenomic databases
eggNOG	COG0258.
HOGENOM	HOG000131367.
HOVERGEN	HBG051501.
InParanoid	P35689.
OrthoDB	EOG4CNQQZ.
Gene expression databases
Genevestigator	P35689.
Family and domain databases
InterPro	IPR020045. 5-3_exonuclease_C. IPR008918. HhH2. IPR006086. XPG-I_dom. IPR006084. XPG/Rad2. IPR001044. XPG/Rad2_eukaryotes. IPR019974. XPG_CS. IPR006085. XPG_DNA_repair_N. [Graphical view]
PANTHER	PTHR11081. PTHR11081. 1 hit. PTHR11081:SF1. PTHR11081:SF1. 1 hit.
Pfam	PF00867. XPG_I. 1 hit. PF00752. XPG_N. 1 hit. [Graphical view]
PRINTS	PR00853. XPGRADSUPER. PR00066. XRODRMPGMNTG.
SMART	SM00279. HhH2. 1 hit. SM00484. XPGI. 1 hit. SM00485. XPGN. 1 hit. [Graphical view]
SUPFAM	SSF47807. 5_3_exo_C. 1 hit.
TIGRFAMs	TIGR00600. rad2. 1 hit.
PROSITE	PS00841. XPG_1. 1 hit. PS00842. XPG_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
SOURCE	Search...

Entry information

Entry name

ERCC5_MOUSE

Accession

Primary (citable) accession number: P35689
Secondary accession number(s): Q61528, Q64248

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	October 3, 2012
Last modified:	May 1, 2013
This is version 114 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

PTM databases

Proteomic databases

Protocols and materials databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents