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P07992 (ERCC1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 149. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
DNA excision repair protein ERCC-1
Gene names
Name:ERCC1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length297 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Isoform 1: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. Ref.12

Subunit structure

Heterodimer composed of ERCC1 isoform 1 and XPF/ERRC4. Ref.12 Ref.14 Ref.15

Subcellular location

Isoform 1: Nucleus Ref.12.

Isoform 2: Cytoplasm. Nucleus Ref.12.

Isoform 3: Nucleus Ref.12.

Isoform 4: Nucleus Ref.12.

Involvement in disease

Cerebro-oculo-facio-skeletal syndrome 4 (COFS4) [MIM:610758]: A disorder of prenatal onset characterized by microcephaly, congenital cataracts, facial dysmorphism, neurogenic arthrogryposis, growth failure and severe psychomotor retardation. COFS is considered to be part of the nucleotide-excision repair disorders spectrum that include also xeroderma pigmentosum, trichothiodystrophy and Cockayne syndrome.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.16 Ref.17

Sequence similarities

Belongs to the ERCC1/RAD10/SWI10 family.

Ontologies

Keywords
   Biological processDNA damage
DNA repair
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseCataract
   LigandDNA-binding
   Molecular functionEndonuclease
Hydrolase
Nuclease
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA catabolic process, endonucleolytic

Inferred from direct assay PubMed 7559382. Source: GOC

DNA recombination

Inferred from genetic interaction PubMed 11707424. Source: MGI

DNA repair

Traceable author statement. Source: Reactome

UV protection

Inferred from electronic annotation. Source: Ensembl

cell proliferation

Inferred from electronic annotation. Source: Ensembl

chromosome organization

Inferred from electronic annotation. Source: Ensembl

double-strand break repair

Inferred from electronic annotation. Source: Ensembl

embryonic organ development

Inferred from electronic annotation. Source: Ensembl

isotype switching

Inferred from electronic annotation. Source: Ensembl

male gonad development

Inferred from electronic annotation. Source: Ensembl

mitotic recombination

Inferred from mutant phenotype PubMed 8811092. Source: UniProtKB

multicellular organism growth

Inferred from electronic annotation. Source: Ensembl

multicellular organismal aging

Inferred from electronic annotation. Source: Ensembl

negative regulation of telomere maintenance

Inferred from mutant phenotype PubMed 17055345. Source: UniProtKB

nucleotide-excision repair

Inferred from direct assay PubMed 3290851. Source: MGI

nucleotide-excision repair, DNA damage removal

Traceable author statement. Source: Reactome

nucleotide-excision repair, DNA incision, 3'-to lesion

Inferred from mutant phenotype PubMed 7657672. Source: UniProtKB

nucleotide-excision repair, DNA incision, 5'-to lesion

Inferred from mutant phenotype PubMed 7657672. Source: UniProtKB

oogenesis

Inferred from electronic annotation. Source: Ensembl

post-embryonic hemopoiesis

Inferred from electronic annotation. Source: Ensembl

pyrimidine dimer repair by nucleotide-excision repair

Inferred from electronic annotation. Source: Ensembl

replicative cell aging

Inferred from electronic annotation. Source: Ensembl

response to X-ray

Inferred from electronic annotation. Source: Ensembl

response to nutrient

Inferred from electronic annotation. Source: Ensembl

response to oxidative stress

Inferred from mutant phenotype PubMed 17614221PubMed 9256505. Source: UniProtKB

response to sucrose

Inferred from electronic annotation. Source: Ensembl

spermatogenesis

Inferred from electronic annotation. Source: Ensembl

syncytium formation

Inferred from electronic annotation. Source: Ensembl

transcription-coupled nucleotide-excision repair

Traceable author statement. Source: Reactome

   Cellular_componentcytoplasm

Inferred from direct assay. Source: HPA

nuclear chromosome, telomeric region

Inferred from direct assay PubMed 14690602. Source: UniProtKB

nucleoplasm

Traceable author statement. Source: Reactome

nucleotide-excision repair complex

Inferred from direct assay PubMed 7559382PubMed 8197175. Source: UniProtKB

nucleus

Inferred from direct assay. Source: HPA

transcription factor TFIID complex

Inferred from electronic annotation. Source: Ensembl

   Molecular_functiondamaged DNA binding

Inferred from direct assay PubMed 17720715. Source: UniProtKB

endonuclease activity

Inferred from electronic annotation. Source: UniProtKB-KW

protein C-terminus binding

Inferred from physical interaction PubMed 9722633. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 14690602PubMed 14706347PubMed 16756962PubMed 7559382PubMed 8197175PubMed 9013642. Source: UniProtKB

protein domain specific binding

Inferred from physical interaction PubMed 17720715. Source: UniProtKB

single-stranded DNA binding

Inferred from direct assay Ref.14PubMed 17720715. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

SLX4Q8IY926EBI-750962,EBI-2370740

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P07992-1)

Also known as: 202;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P07992-2)

Also known as: 203;

The sequence of this isoform differs from the canonical sequence as follows:
     235-258: Missing.
Note: Not functional in the nucleotide excision repair pathway. Does not interact with XPF/ERCC4.
Isoform 3 (identifier: P07992-3)

Also known as: 201;

The sequence of this isoform differs from the canonical sequence as follows:
     282-297: ARRLFDVLHEPFLKVP → VRALGKNPRSWGKERAPNKHNLRPQSFKVKKEPKTRHSGFRL
Note: Not functional in the nucleotide excision repair pathway. Does not interact with XPF/ERCC4.
Isoform 4 (identifier: P07992-4)

Also known as: 204;

The sequence of this isoform differs from the canonical sequence as follows:
     36-107: Missing.
Note: Not functional in the nucleotide excision repair pathway. Does not interact with XPF/ERCC4.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 297297DNA excision repair protein ERCC-1
PRO_0000087006

Regions

DNA binding134 – 15623 Potential
Region220 – 29778HhH2, dimerization with ERCC4
Motif17 – 237Nuclear localization signal Potential

Amino acid modifications

Modified residue11N-acetylmethionine Ref.11

Natural variations

Alternative sequence36 – 10772Missing in isoform 4.
VSP_053474
Alternative sequence235 – 25824Missing in isoform 2.
VSP_042727
Alternative sequence282 – 29716ARRLF…FLKVP → VRALGKNPRSWGKERAPNKH NLRPQSFKVKKEPKTRHSGF RL in isoform 3.
VSP_043455
Natural variant2311F → L in COFS4; does not alter interaction with XPF/ERCC4 or GTF2H1. Ref.16 Ref.17
VAR_032776
Natural variant2661A → T. Ref.5
Corresponds to variant rs3212977 [ dbSNP | Ensembl ].
VAR_019167

Experimental info

Sequence conflict531A → P in BAG37398. Ref.6

Secondary structure

......................................... 297
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (202) [UniParc].

Last modified August 1, 1988. Version 1.
Checksum: 6FCE3615732349E5

FASTA29732,562
        10         20         30         40         50         60 
MDPGKDKEGV PQPSGPPARK KFVIPLDEDE VPPGVAKPLF RSTQSLPTVD TSAQAAPQTY 

        70         80         90        100        110        120 
AEYAISQPLE GAGATCPTGS EPLAGETPNQ ALKPGAKSNS IIVSPRQRGN PVLKFVRNVP 

       130        140        150        160        170        180 
WEFGDVIPDY VLGQSTCALF LSLRYHNLHP DYIHGRLQSL GKNFALRVLL VQVDVKDPQQ 

       190        200        210        220        230        240 
ALKELAKMCI LADCTLILAW SPEEAGRYLE TYKAYEQKPA DLLMEKLEQD FVSRVTECLT 

       250        260        270        280        290 
TVKSVNKTDS QTLLTTFGSL EQLIAASRED LALCPGLGPQ KARRLFDVLH EPFLKVP 

« Hide

Isoform 2 (203) [UniParc].

Checksum: 04DA21E774A33524
Show »

FASTA27329,993
Isoform 3 (201) [UniParc].

Checksum: D99BFAC9CE8E912E
Show »

FASTA32335,563
Isoform 4 (204) [UniParc].

Checksum: AF78F4C26AC7DA7E
Show »

FASTA22525,211

References

« Hide 'large scale' references
[1]"Molecular characterization of the human excision repair gene ERCC-1: cDNA cloning and amino acid homology with the yeast DNA repair gene RAD10."
van Duin M., de Wit J., Odijk H., Westerveld A., Yasui A., Koken M.H.M., Hoeijmakers J.H.J., Bootsma D.
Cell 44:913-923(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"Identification of DNA repair genes in the human genome."
Hoeijmakers J.H.J., van Duin M., Westerveld A., Yasui A., Bootsma D.
Cold Spring Harb. Symp. Quant. Biol. 51:91-101(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"A nucleotide polymorphism in ERCC1 in human ovarian cancer cell lines and tumor tissues."
Yu J.J., Mu C.J., Lee K.B., Okamoto A., Reed E.L., Bostick-Bruton F., Mitchell K.C., Reed E.
Mutat. Res. 382:13-20(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[4]"Human excision repair protein 1, transcript variant, mRNA."
Hisatomi H., Nagao K., Ishikawa H., Yokoyama Y., Ishihara Y., Hikiji K., Iizuka T.
Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[5]NIEHS SNPs program
Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT THR-266.
[6]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4).
Tissue: Cerebellum.
[7]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[8]"The DNA sequence and biology of human chromosome 19."
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V. expand/collapse author list , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[10]"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] (ISOFORMS 1 AND 3).
Tissue: Lung and Uterus.
[11]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"ERCC1 function in nuclear excision and interstrand crosslink repair pathways is mediated exclusively by the ERCC1-202 isoform."
Friboulet L., Postel-Vinay S., Sourisseau T., Adam J., Stoclin A., Ponsonnailles F., Dorvault N., Commo F., Saulnier P., Salome-Desmoulez S., Pottier G., Andre F., Kroemer G., Soria J.C., Olaussen K.A.
Cell Cycle 12:3298-3306(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION (ISOFORM 1), SUBCELLULAR LOCATION, SUBUNIT.
[13]"ERCC1 isoform expression and DNA repair in non-small-cell lung cancer."
Friboulet L., Olaussen K.A., Pignon J.P., Shepherd F.A., Tsao M.S., Graziano S., Kratzke R., Douillard J.Y., Seymour L., Pirker R., Filipits M., Andre F., Solary E., Ponsonnailles F., Robin A., Stoclin A., Dorvault N., Commo F. expand/collapse author list , Adam J., Vanhecke E., Saulnier P., Thomale J., Le Chevalier T., Dunant A., Rousseau V., Le Teuff G., Brambilla E., Soria J.C.
N. Engl. J. Med. 368:1101-1110(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ALTERNATIVE SPLICING.
[14]"Crystal structure and DNA binding functions of ERCC1, a subunit of the DNA structure-specific endonuclease XPF-ERCC1."
Tsodikov O.V., Enzlin J.H., Scharer O.D., Ellenberger T.
Proc. Natl. Acad. Sci. U.S.A. 102:11236-11241(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 96-227, X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 96-220-296 IN COMPLEX WIRH ERCC4, SUBUNIT.
[15]"The structure of the human ERCC1/XPF interaction domains reveals a complementary role for the two proteins in nucleotide excision repair."
Tripsianes K., Folkers G., Ab E., Das D., Odijk H., Jaspers N.G., Hoeijmakers J.H., Kaptein R., Boelens R.
Structure 13:1849-1858(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 220-297 IN COMPLEX WIRH ERCC4, SUBUNIT.
[16]"First reported patient with human ERCC1 deficiency has cerebro-oculo-facio-skeletal syndrome with a mild defect in nucleotide excision repair and severe developmental failure."
Jaspers N.G.J., Raams A., Silengo M.C., Wijgers N., Niedernhofer L.J., Robinson A.R., Giglia-Mari G., Hoogstraten D., Kleijer W.J., Hoeijmakers J.H.J., Vermeulen W.
Am. J. Hum. Genet. 80:457-466(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT COFS4 LEU-231.
[17]"Malfunction of nuclease ERCC1-XPF results in diverse clinical manifestations and causes Cockayne syndrome, xeroderma pigmentosum, and Fanconi anemia."
Kashiyama K., Nakazawa Y., Pilz D.T., Guo C., Shimada M., Sasaki K., Fawcett H., Wing J.F., Lewin S.O., Carr L., Li T.S., Yoshiura K., Utani A., Hirano A., Yamashita S., Greenblatt D., Nardo T., Stefanini M. expand/collapse author list , McGibbon D., Sarkany R., Fassihi H., Takahashi Y., Nagayama Y., Mitsutake N., Lehmann A.R., Ogi T.
Am. J. Hum. Genet. 92:807-819(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT COFS4 LEU-231, CHARACTERIZATION OF VARIANT COFS4 LEU-231.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M13194 mRNA. Translation: AAA52394.1.
M26163 Genomic DNA. Translation: AAA52395.1.
M28650 mRNA. Translation: AAA35810.1.
AF001925 mRNA. Translation: AAC16253.1.
AB069681 mRNA. Translation: BAB62810.1.
BT019806 mRNA. Translation: AAV38609.1.
AF512555 Genomic DNA. Translation: AAM34796.1.
AK092039 mRNA. Translation: BAG52472.1.
AK314884 mRNA. Translation: BAG37398.1.
AC092309 Genomic DNA. No translation available.
AC138128 Genomic DNA. No translation available.
AC138534 Genomic DNA. No translation available.
AC139353 Genomic DNA. No translation available.
CH471126 Genomic DNA. Translation: EAW57349.1.
BC008930 mRNA. Translation: AAH08930.1.
BC052813 mRNA. Translation: AAH52813.1.
CCDSCCDS12662.1. [P07992-1]
CCDS12663.1. [P07992-3]
CCDS54279.1. [P07992-2]
PIRA24781. A32875.
RefSeqNP_001159521.1. NM_001166049.1. [P07992-2]
NP_001974.1. NM_001983.3. [P07992-1]
NP_973730.1. NM_202001.2. [P07992-3]
XP_005258691.1. XM_005258634.1. [P07992-3]
XP_005258692.1. XM_005258635.1. [P07992-3]
XP_005258693.1. XM_005258636.2. [P07992-3]
UniGeneHs.435981.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1Z00NMR-A220-297[»]
2A1IX-ray1.90A96-227[»]
2A1JX-ray2.70B220-296[»]
2JNWNMR-A96-214[»]
2JPDNMR-A96-219[»]
ProteinModelPortalP07992.
SMRP07992. Positions 99-297.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108379. 16 interactions.
DIPDIP-24235N.
IntActP07992. 7 interactions.
MINTMINT-1457664.
STRING9606.ENSP00000013807.

PTM databases

PhosphoSiteP07992.

Polymorphism databases

DMDM119538.

Proteomic databases

MaxQBP07992.
PaxDbP07992.
PRIDEP07992.

Protocols and materials databases

DNASU2067.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000013807; ENSP00000013807; ENSG00000012061. [P07992-3]
ENST00000300853; ENSP00000300853; ENSG00000012061. [P07992-1]
ENST00000340192; ENSP00000345203; ENSG00000012061. [P07992-2]
ENST00000423698; ENSP00000394875; ENSG00000012061. [P07992-4]
ENST00000589165; ENSP00000468035; ENSG00000012061. [P07992-1]
GeneID2067.
KEGGhsa:2067.
UCSCuc002pbs.2. human. [P07992-1]
uc002pbt.2. human. [P07992-2]
uc002pbu.2. human.
uc002pbv.3. human. [P07992-3]

Organism-specific databases

CTD2067.
GeneCardsGC19M045912.
GeneReviewsERCC1.
HGNCHGNC:3433. ERCC1.
HPACAB004390.
HPA029773.
HPA050182.
MIM126380. gene.
610758. phenotype.
neXtProtNX_P07992.
Orphanet90322. Cockayne syndrome type 2.
1466. COFS syndrome.
PharmGKBPA155.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5241.
HOGENOMHOG000037440.
HOVERGENHBG051497.
KOK10849.
OMAHPDYIHQ.
OrthoDBEOG7XH6Q8.
PhylomeDBP07992.
TreeFamTF101231.

Enzyme and pathway databases

ReactomeREACT_216. DNA Repair.

Gene expression databases

ArrayExpressP07992.
BgeeP07992.
CleanExHS_ERCC1.
GenevestigatorP07992.

Family and domain databases

InterProIPR004579. DNA_repair_Rad10.
IPR000445. HhH_motif.
IPR003583. Hlx-hairpin-Hlx_DNA-bd_motif.
IPR011335. Restrct_endonuc-II-like.
IPR010994. RuvA_2-like.
[Graphical view]
PfamPF00633. HHH. 1 hit.
PF03834. Rad10. 1 hit.
[Graphical view]
ProDomPD013585. DNA_repair_Rad10. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00278. HhH1. 1 hit.
[Graphical view]
SUPFAMSSF47781. SSF47781. 1 hit.
SSF52980. SSF52980. 1 hit.
TIGRFAMsTIGR00597. rad10. 1 hit.
ProtoNetSearch...

Other

ChiTaRSERCC1. human.
EvolutionaryTraceP07992.
GeneWikiERCC1.
GenomeRNAi2067.
NextBio35469580.
PROP07992.
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Entry information

Entry nameERCC1_HUMAN
AccessionPrimary (citable) accession number: P07992
Secondary accession number(s): B2RC01 expand/collapse secondary AC list , B3KRR0, Q7Z7F5, Q96S40
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: August 1, 1988
Last modified: July 9, 2014
This is version 149 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM