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O08811 (ERCC2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 122. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
TFIIH basal transcription factor complex helicase XPD subunit

EC=3.6.4.12
Alternative name(s):
CXPD
DNA excision repair protein ERCC-2
DNA repair protein complementing XP-D cells
Xeroderma pigmentosum group D-complementing protein
Gene names
Name:Ercc2
Synonyms:Xpd
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length760 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

ATP-dependent 5'-3' DNA helicase, component of the core-TFIIH basal transcription factor. Involved in nucleotide excision repair (NER) of DNA by opening DNA around the damage, and in RNA transcription by RNA polymerase II by anchoring the CDK-activating kinase (CAK) complex, composed of CDK7, cyclin H and MAT1, to the core-TFIIH complex. Involved in the regulation of vitamin-D receptor activity. As part of the mitotic spindle-associated MMXD complex it plays a role in chromosome segregation. Might have a role in aging process and could play a causative role in the generation of skin cancers By similarity.

Catalytic activity

ATP + H2O = ADP + phosphate.

Cofactor

Magnesium By similarity.

Binds 1 4Fe-4S cluster By similarity.

Subunit structure

One of the six subunits forming the core-TFIIH basal transcription factor which associates with the CAK complex composed of CDK7, CCNH/cyclin H and MNAT1 to form the TFIIH basal transcription factor. The interaction with GTF2H2 results in the stimulation of the 5'-->3' helicase activity. Component of the MMXD complex, which includes CIAO1, ERCC2, FAM96B, MMS19 and SLC25A5. Interacts with FAM196B; the interaction is direct By similarity. Interacts with ATF7IP By similarity.

Subcellular location

Nucleus. Cytoplasmcytoskeletonspindle By similarity.

Post-translational modification

ISGylated By similarity.

Sequence similarities

Belongs to the helicase family. RAD3/XPD subfamily.

Contains 1 helicase ATP-binding domain.

Sequence caution

The sequence BAB23443.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
   Biological processChromosome partition
DNA damage
DNA repair
Transcription
Transcription regulation
   Cellular componentCytoplasm
Cytoskeleton
Nucleus
   Ligand4Fe-4S
ATP-binding
DNA-binding
Iron
Iron-sulfur
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionHelicase
Hydrolase
   PTMUbl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processATP catabolic process

Inferred from sequence or structural similarity. Source: GOC

DNA duplex unwinding

Inferred from sequence or structural similarity. Source: GOC

DNA repair

Inferred from mutant phenotype PubMed 11950998. Source: MGI

UV protection

Inferred from mutant phenotype PubMed 9651581. Source: MGI

aging

Inferred from mutant phenotype PubMed 11950998PubMed 17020410PubMed 18545656. Source: MGI

apoptotic process

Inferred from sequence or structural similarity. Source: UniProtKB

bone mineralization

Inferred from mutant phenotype PubMed 17020410. Source: MGI

cell proliferation

Inferred from mutant phenotype PubMed 17554309. Source: MGI

central nervous system myelin formation

Inferred from mutant phenotype PubMed 17952069. Source: MGI

chromosome segregation

Inferred from sequence or structural similarity. Source: UniProtKB

embryonic cleavage

Inferred from mutant phenotype Ref.1. Source: MGI

erythrocyte maturation

Inferred from mutant phenotype PubMed 17020410. Source: MGI

extracellular matrix organization

Inferred from mutant phenotype PubMed 9651581. Source: MGI

hair cell differentiation

Inferred from mutant phenotype PubMed 17020410. Source: MGI

hair cycle process

Inferred from mutant phenotype PubMed 17020410. Source: MGI

hair follicle maturation

Inferred from mutant phenotype PubMed 9651581. Source: MGI

hematopoietic stem cell differentiation

Inferred from mutant phenotype PubMed 17554309. Source: MGI

in utero embryonic development

Inferred from mutant phenotype PubMed 17020410. Source: MGI

multicellular organism growth

Inferred from mutant phenotype PubMed 17020410. Source: MGI

nucleotide-excision repair

Inferred from mutant phenotype PubMed 11950998PubMed 9651581. Source: MGI

nucleotide-excision repair, DNA incision

Inferred from electronic annotation. Source: Ensembl

positive regulation of DNA binding

Inferred from mutant phenotype PubMed 17952069. Source: MGI

positive regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

post-embryonic development

Inferred from mutant phenotype PubMed 11950998PubMed 17020410. Source: MGI

regulation of mitotic cell cycle phase transition

Inferred from electronic annotation. Source: Ensembl

response to UV

Inferred from mutant phenotype PubMed 17020410. Source: MGI

response to hypoxia

Inferred from electronic annotation. Source: Ensembl

response to oxidative stress

Inferred from mutant phenotype PubMed 11950998. Source: MGI

skin development

Inferred from mutant phenotype PubMed 17020410PubMed 9651581. Source: MGI

spinal cord development

Inferred from mutant phenotype PubMed 17020410. Source: MGI

transcription from RNA polymerase II promoter

Inferred from sequence or structural similarity. Source: UniProtKB

transcription-coupled nucleotide-excision repair

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentMMXD complex

Inferred from sequence or structural similarity. Source: UniProtKB

cyclin-dependent protein kinase activating kinase holoenzyme complex

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

holo TFIIH complex

Inferred from sequence or structural similarity. Source: UniProtKB

nucleus

Inferred from direct assay PubMed 17952069. Source: MGI

spindle

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_function4 iron, 4 sulfur cluster binding

Inferred from electronic annotation. Source: UniProtKB-KW

5'-3' DNA helicase activity

Inferred from sequence or structural similarity. Source: UniProtKB

ATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

ATP-dependent DNA helicase activity

Inferred from electronic annotation. Source: InterPro

DNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

RNA polymerase II carboxy-terminal domain kinase activity

Inferred from electronic annotation. Source: Ensembl

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 760760TFIIH basal transcription factor complex helicase XPD subunit
PRO_0000101981

Regions

Domain7 – 283277Helicase ATP-binding
Nucleotide binding42 – 498ATP By similarity
Region438 – 637200Mediates interaction with MMS19 By similarity
Motif234 – 2374DEAH box

Sites

Metal binding1161Iron-sulfur (4Fe-4S) By similarity
Metal binding1341Iron-sulfur (4Fe-4S) By similarity
Metal binding1551Iron-sulfur (4Fe-4S) By similarity
Metal binding1901Iron-sulfur (4Fe-4S) By similarity

Experimental info

Sequence conflict2851Y → C in BAB23443. Ref.2
Sequence conflict5951I → V in AAB58296. Ref.1

Sequences

Sequence LengthMass (Da)Tools
O08811 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: 02B2E116792D4E44

FASTA76086,842
        10         20         30         40         50         60 
MKLNVDGLLV YFPYDYIYPE QFSYMLELKR TLDAKGHGVL EMPSGTGKTV SLLALIVAYQ 

        70         80         90        100        110        120 
RAYPLEVTKL IYCSRTVPEI EKVIEELRKL LSFYEQQEGE KLPFLGLALS SRKNLCIHPE 

       130        140        150        160        170        180 
VTPLRFGKDV DGKCHSLTAS YVRAQYQQDA SLPHCRFYEE FDIHGRQMPL PAGIYNLDDL 

       190        200        210        220        230        240 
KALGQRQGWC PYFLARYSIL HANVVVYSYH YLLDPKIADL VSKELARKAV VVFDEAHNID 

       250        260        270        280        290        300 
NVCIDSMSVN LTRRTLDRCQ SNLDTLQKTV LRIKETDEQR LRDEYRRLVE GLREASVARE 

       310        320        330        340        350        360 
TDAHLANPVL PDEVLQEAVP GSIRTAEHFL GFLRRLLEYV KWRLRVQHVV QESPPAFLSG 

       370        380        390        400        410        420 
LAQRVCIQRK PLRFCAERLR SLLHTLEIAD LADFSPLTLL ANFATLVSTY AKGFTIIIEP 

       430        440        450        460        470        480 
FDDRTPTIAN PVLHFSCMDA SLAIKPVFER FQSVIITSGT LSPLDIYPKI LDFHPVTMAT 

       490        500        510        520        530        540 
FTMTLARVCL CPMIIGRGND QVAISSKFET REDIAVIRNY GNLLLEMSAV VPDGIVAFFT 

       550        560        570        580        590        600 
SYQYMESTVA SWYEQGILEN IQRNKLLFIE TQDGAETSVA LEKYQEACEN GRGAILLSVA 

       610        620        630        640        650        660 
RGKVSEGIDF VHHYGRAVIM FGVPYVYTQS RILKARLEYL RDQFQIREND FLTFDAMRHA 

       670        680        690        700        710        720 
AQCVGRAIRG KTDYGLMVFA DKRFARADKR GKLPRWIQEH LTDSNLNLTV DEGVQVAKYF 

       730        740        750        760 
LRQMAQPFHR EDQLGLSLLS LEQLQSEETL QRIEQIAQQL 

« Hide

References

« Hide 'large scale' references
[1]"Disruption of the mouse xeroderma pigmentosum group D DNA repair/basal transcription gene results in preimplantation lethality."
de Boer J., Donker I., de Wit J., Hoeijmakers J.H.J., Weeda G.
Cancer Res. 58:89-94(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [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. expand/collapse author list , 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.
Tissue: Lung.
[3]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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U97572 mRNA. Translation: AAB58296.1.
AK004652 mRNA. Translation: BAB23443.1. Different initiation.
AK082761 mRNA. Translation: BAC38607.1.
CH466639 Genomic DNA. Translation: EDL23140.1.
CCDSCCDS20900.1.
RefSeqNP_031975.2. NM_007949.4.
UniGeneMm.36524.

3D structure databases

ProteinModelPortalO08811.
SMRO08811. Positions 26-258.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActO08811. 1 interaction.
MINTMINT-4114299.
STRING10090.ENSMUSP00000054380.

PTM databases

PhosphoSiteO08811.

Proteomic databases

PaxDbO08811.
PRIDEO08811.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000062831; ENSMUSP00000054380; ENSMUSG00000030400.
GeneID13871.
KEGGmmu:13871.
UCSCuc009flq.1. mouse.

Organism-specific databases

CTD2068.
MGIMGI:95413. Ercc2.

Phylogenomic databases

eggNOGCOG1199.
GeneTreeENSGT00550000075092.
HOGENOMHOG000205390.
HOVERGENHBG051498.
InParanoidQ8C487.
KOK10844.
OMADEVWKYK.
OrthoDBEOG70W3CM.
TreeFamTF101232.

Gene expression databases

BgeeO08811.
GenevestigatorO08811.

Family and domain databases

Gene3D3.40.50.300. 2 hits.
InterProIPR006555. ATP-dep_Helicase_C.
IPR010614. DEAD_2.
IPR002464. DNA/RNA_helicase_DEAH_CS.
IPR013020. DNA_helicase_DNA-repair_Rad3.
IPR010643. DUF1227.
IPR014013. Helic_SF1/SF2_ATP-bd_DinG/Rad3.
IPR006554. Helicase-like_DEXD_c2.
IPR027417. P-loop_NTPase.
IPR001945. XPGD_DNA_repair.
[Graphical view]
PfamPF06733. DEAD_2. 1 hit.
PF06777. DUF1227. 1 hit.
PF13307. Helicase_C_2. 1 hit.
[Graphical view]
PRINTSPR00852. XRODRMPGMNTD.
SMARTSM00488. DEXDc2. 1 hit.
SM00491. HELICc2. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 4 hits.
TIGRFAMsTIGR00604. rad3. 1 hit.
PROSITEPS00690. DEAH_ATP_HELICASE. 1 hit.
PS51193. HELICASE_ATP_BIND_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio284788.
PROO08811.
SOURCESearch...

Entry information

Entry nameERCC2_MOUSE
AccessionPrimary (citable) accession number: O08811
Secondary accession number(s): Q8C487, Q9DC01
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 27, 2011
Last modified: July 9, 2014
This is version 122 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

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