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P07903

- ERCC1_MOUSE

UniProt

P07903 - ERCC1_MOUSE

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Protein

DNA excision repair protein ERCC-1

Gene

Ercc1

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

Functioni

Non-catalytic component of a structure-specific DNA repair endonuclease responsible for the 5'-incision during DNA repair. Responsible, in conjunction with SLX4, for the first step in the repair of interstrand cross-links (ICL). Participates in the processing of anaphase bridge-generating DNA structures, which consist in incompletely processed DNA lesions arising during S or G2 phase, and can result in cytokinesis failure. Also required for homology-directed repair (HDR) of DNA double-strand breaks, in conjunction with SLX4 (By similarity).By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi134 – 15623Sequence AnalysisAdd
BLAST

GO - Molecular functioni

  1. damaged DNA binding Source: InterPro
  2. single-stranded DNA binding Source: Ensembl
  3. single-stranded DNA endodeoxyribonuclease activity Source: Ensembl
  4. TBP-class protein binding Source: MGI
  5. TFIID-class transcription factor binding Source: MGI

GO - Biological processi

  1. cell development Source: MGI
  2. cell proliferation Source: MGI
  3. cellular response to DNA damage stimulus Source: MGI
  4. chromosome organization Source: MGI
  5. DNA recombination Source: MGI
  6. DNA repair Source: MGI
  7. double-strand break repair Source: MGI
  8. embryonic organ development Source: Ensembl
  9. germ cell development Source: MGI
  10. interstrand cross-link repair Source: MGI
  11. isotype switching Source: MGI
  12. male gonad development Source: MGI
  13. mitotic recombination Source: Ensembl
  14. multicellular organismal aging Source: MGI
  15. multicellular organism growth Source: MGI
  16. negative regulation of telomere maintenance Source: Ensembl
  17. nucleotide-excision repair Source: UniProtKB
  18. nucleotide-excision repair, DNA incision, 3'-to lesion Source: Ensembl
  19. nucleotide-excision repair, DNA incision, 5'-to lesion Source: Ensembl
  20. oogenesis Source: MGI
  21. post-embryonic hemopoiesis Source: MGI
  22. pyrimidine dimer repair by nucleotide-excision repair Source: MGI
  23. replicative cell aging Source: MGI
  24. response to nutrient Source: Ensembl
  25. response to oxidative stress Source: Ensembl
  26. response to sucrose Source: Ensembl
  27. response to X-ray Source: MGI
  28. spermatogenesis Source: MGI
  29. syncytium formation Source: MGI
  30. UV protection Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Endonuclease, Hydrolase, Nuclease

Keywords - Biological processi

DNA damage, DNA repair

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiREACT_223654. Formation of transcription-coupled NER (TC-NER) repair complex.
REACT_224562. Dual incision reaction in TC-NER.
REACT_240507. Dual incision reaction in GG-NER.
REACT_252106. Formation of incision complex in GG-NER.

Names & Taxonomyi

Protein namesi
Recommended name:
DNA excision repair protein ERCC-1
Gene namesi
Name:Ercc1
Synonyms:Ercc-1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 7

Organism-specific databases

MGIiMGI:95412. Ercc1.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: Ensembl
  2. nuclear chromosome, telomeric region Source: Ensembl
  3. nucleotide-excision repair complex Source: UniProtKB
  4. transcription factor TFIID complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 298298DNA excision repair protein ERCC-1PRO_0000087007Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP07903.
PRIDEiP07903.

PTM databases

PhosphoSiteiP07903.

Expressioni

Gene expression databases

ExpressionAtlasiP07903. baseline and differential.
GenevestigatoriP07903.

Interactioni

Subunit structurei

Heterodimer composed of ERCC1 and XPF/ERRC4.

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000003645.

Structurei

3D structure databases

ProteinModelPortaliP07903.
SMRiP07903. Positions 99-297.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni220 – 29879HhH2, dimerization with ERCC4By similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi17 – 237Nuclear localization signalSequence Analysis

Sequence similaritiesi

Belongs to the ERCC1/RAD10/SWI10 family.Curated

Phylogenomic databases

eggNOGiCOG5241.
GeneTreeiENSGT00390000011275.
HOGENOMiHOG000037440.
HOVERGENiHBG051497.
InParanoidiP07903.
KOiK10849.
OMAiHPDYIHQ.
OrthoDBiEOG7XH6Q8.
TreeFamiTF101231.

Family and domain databases

InterProiIPR004579. DNA_repair_Rad10.
IPR000445. HhH_motif.
IPR003583. Hlx-hairpin-Hlx_DNA-bd_motif.
IPR011335. Restrct_endonuc-II-like.
IPR010994. RuvA_2-like.
[Graphical view]
PfamiPF00633. HHH. 1 hit.
PF03834. Rad10. 1 hit.
[Graphical view]
ProDomiPD013585. DNA_repair_Rad10. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00278. HhH1. 1 hit.
[Graphical view]
SUPFAMiSSF47781. SSF47781. 1 hit.
SSF52980. SSF52980. 1 hit.
TIGRFAMsiTIGR00597. rad10. 1 hit.

Sequencei

Sequence statusi: Complete.

P07903-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MDPGKDEESR PQPSGPPTRR KFVIPLEEEE VPCAGVKPLF RSSRNPTIPA
60 70 80 90 100
TSAHVAPQTY AEYAITQPPG GAGATVPTGS EPAAGENPSQ TLKTGAKSNS
110 120 130 140 150
IIVSPRQRGN PVLKFVRNVP WEFGEVIPDY VLGQSTCALF LSLRYHNLHP
160 170 180 190 200
DYIHERLQSL GKNFALRVLL VQVDVKDPQQ ALKELAKMCI LADCTLVLAW
210 220 230 240 250
SAEEAGRYLE TYKAYEQKPA DLLMEKLEQN FLSRATECLT TVKSVNKTDS
260 270 280 290
QTLLATFGSL EQLFTASRED LALCPGLGPQ KARRLFEVLH EPFLKVPR
Length:298
Mass (Da):32,910
Last modified:October 3, 2012 - v2
Checksum:i264DF6865A3ED847
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti55 – 551V → M in CAA30310. (PubMed:3290851)Curated
Sequence conflicti213 – 2131K → R in CAA30310. (PubMed:3290851)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X07414 mRNA. Translation: CAA30310.1.
X07413 Genomic DNA. No translation available.
AK088271 mRNA. Translation: BAC40249.1.
AK136733 mRNA. Translation: BAE23112.1.
AC148988 Genomic DNA. No translation available.
CH466639 Genomic DNA. Translation: EDL23137.1.
BC011224 mRNA. Translation: AAH11224.1.
CCDSiCCDS20898.1.
PIRiS01202.
RefSeqiNP_001120796.1. NM_001127324.1.
NP_031974.2. NM_007948.2.
UniGeneiMm.280913.

Genome annotation databases

EnsembliENSMUST00000003645; ENSMUSP00000003645; ENSMUSG00000003549.
GeneIDi13870.
KEGGimmu:13870.
UCSCiuc009flm.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X07414 mRNA. Translation: CAA30310.1 .
X07413 Genomic DNA. No translation available.
AK088271 mRNA. Translation: BAC40249.1 .
AK136733 mRNA. Translation: BAE23112.1 .
AC148988 Genomic DNA. No translation available.
CH466639 Genomic DNA. Translation: EDL23137.1 .
BC011224 mRNA. Translation: AAH11224.1 .
CCDSi CCDS20898.1.
PIRi S01202.
RefSeqi NP_001120796.1. NM_001127324.1.
NP_031974.2. NM_007948.2.
UniGenei Mm.280913.

3D structure databases

ProteinModelPortali P07903.
SMRi P07903. Positions 99-297.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 10090.ENSMUSP00000003645.

PTM databases

PhosphoSitei P07903.

Proteomic databases

PaxDbi P07903.
PRIDEi P07903.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000003645 ; ENSMUSP00000003645 ; ENSMUSG00000003549 .
GeneIDi 13870.
KEGGi mmu:13870.
UCSCi uc009flm.2. mouse.

Organism-specific databases

CTDi 2067.
MGIi MGI:95412. Ercc1.

Phylogenomic databases

eggNOGi COG5241.
GeneTreei ENSGT00390000011275.
HOGENOMi HOG000037440.
HOVERGENi HBG051497.
InParanoidi P07903.
KOi K10849.
OMAi HPDYIHQ.
OrthoDBi EOG7XH6Q8.
TreeFami TF101231.

Enzyme and pathway databases

Reactomei REACT_223654. Formation of transcription-coupled NER (TC-NER) repair complex.
REACT_224562. Dual incision reaction in TC-NER.
REACT_240507. Dual incision reaction in GG-NER.
REACT_252106. Formation of incision complex in GG-NER.

Miscellaneous databases

NextBioi 284784.
PROi P07903.
SOURCEi Search...

Gene expression databases

ExpressionAtlasi P07903. baseline and differential.
Genevestigatori P07903.

Family and domain databases

InterProi IPR004579. DNA_repair_Rad10.
IPR000445. HhH_motif.
IPR003583. Hlx-hairpin-Hlx_DNA-bd_motif.
IPR011335. Restrct_endonuc-II-like.
IPR010994. RuvA_2-like.
[Graphical view ]
Pfami PF00633. HHH. 1 hit.
PF03834. Rad10. 1 hit.
[Graphical view ]
ProDomi PD013585. DNA_repair_Rad10. 1 hit.
[Graphical view ] [Entries sharing at least one domain ]
SMARTi SM00278. HhH1. 1 hit.
[Graphical view ]
SUPFAMi SSF47781. SSF47781. 1 hit.
SSF52980. SSF52980. 1 hit.
TIGRFAMsi TIGR00597. rad10. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J and NOD.
    Tissue: Epididymis and Thymus.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  4. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: FVB/N.
    Tissue: Mammary tumor.

Entry informationi

Entry nameiERCC1_MOUSE
AccessioniPrimary (citable) accession number: P07903
Secondary accession number(s): Q91VP3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: October 3, 2012
Last modified: November 26, 2014
This is version 121 of the entry and version 2 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