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Protein

TFIIH basal transcription factor complex helicase XPD subunit

Gene

Ercc2

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

Functioni

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).By similarity

Catalytic activityi

ATP + H2O = ADP + phosphate.

Cofactori

Protein has several cofactor binding sites:

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi116 – 1161Iron-sulfur (4Fe-4S)By similarity
Metal bindingi134 – 1341Iron-sulfur (4Fe-4S)By similarity
Metal bindingi155 – 1551Iron-sulfur (4Fe-4S)By similarity
Metal bindingi190 – 1901Iron-sulfur (4Fe-4S)By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi42 – 498ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. 4 iron, 4 sulfur cluster binding Source: UniProtKB-KW
  2. 5'-3' DNA helicase activity Source: UniProtKB
  3. ATP binding Source: UniProtKB-KW
  4. ATP-dependent DNA helicase activity Source: InterPro
  5. DNA binding Source: UniProtKB-KW
  6. metal ion binding Source: UniProtKB-KW
  7. protein C-terminus binding Source: MGI
  8. protein N-terminus binding Source: MGI
  9. RNA polymerase II carboxy-terminal domain kinase activity Source: Ensembl

GO - Biological processi

  1. aging Source: MGI
  2. apoptotic process Source: UniProtKB
  3. ATP catabolic process Source: MGI
  4. bone mineralization Source: MGI
  5. cell proliferation Source: MGI
  6. central nervous system myelin formation Source: MGI
  7. chromosome segregation Source: UniProtKB
  8. DNA duplex unwinding Source: MGI
  9. DNA repair Source: MGI
  10. embryonic cleavage Source: MGI
  11. erythrocyte maturation Source: MGI
  12. extracellular matrix organization Source: MGI
  13. hair cell differentiation Source: MGI
  14. hair cycle process Source: MGI
  15. hair follicle maturation Source: MGI
  16. hematopoietic stem cell differentiation Source: MGI
  17. in utero embryonic development Source: MGI
  18. multicellular organism growth Source: MGI
  19. nucleotide-excision repair Source: MGI
  20. nucleotide-excision repair, DNA incision Source: MGI
  21. positive regulation of DNA binding Source: MGI
  22. positive regulation of transcription, DNA-templated Source: MGI
  23. positive regulation of transcription from RNA polymerase II promoter Source: MGI
  24. post-embryonic development Source: MGI
  25. protein phosphorylation Source: MGI
  26. regulation of mitotic cell cycle phase transition Source: MGI
  27. response to hypoxia Source: Ensembl
  28. response to oxidative stress Source: MGI
  29. response to UV Source: MGI
  30. skin development Source: MGI
  31. spinal cord development Source: MGI
  32. transcription-coupled nucleotide-excision repair Source: UniProtKB
  33. transcription from RNA polymerase II promoter Source: UniProtKB
  34. UV protection Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Helicase, Hydrolase

Keywords - Biological processi

Chromosome partition, DNA damage, DNA repair, Transcription, Transcription regulation

Keywords - Ligandi

4Fe-4S, ATP-binding, DNA-binding, Iron, Iron-sulfur, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_196637. Cytosolic iron-sulfur cluster assembly.
REACT_203462. Formation of the Early Elongation Complex.
REACT_223654. Formation of transcription-coupled NER (TC-NER) repair complex.
REACT_224562. Dual incision reaction in TC-NER.
REACT_226490. RNA Polymerase II Transcription Elongation.
REACT_230204. RNA Polymerase II Transcription Initiation And Promoter Clearance.
REACT_232235. RNA Polymerase I Promoter Escape.
REACT_232708. RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
REACT_235780. RNA Polymerase I Transcription Initiation.
REACT_240507. Dual incision reaction in GG-NER.
REACT_244380. RNA Polymerase II Transcription Initiation.
REACT_252106. Formation of incision complex in GG-NER.
REACT_255009. RNA Polymerase II Pre-transcription Events.
REACT_255334. RNA Polymerase II Promoter Escape.
REACT_257165. RNA Polymerase I Transcription Termination.
REACT_257596. RNA Pol II CTD phosphorylation and interaction with CE.
REACT_258231. mRNA Capping.
REACT_259097. RNA Polymerase I Chain Elongation.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:Ercc2
Synonyms:Xpd
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 7

Organism-specific databases

MGIiMGI:95413. Ercc2.

Subcellular locationi

Nucleus. Cytoplasmcytoskeletonspindle By similarity

GO - Cellular componenti

  1. core TFIIH complex Source: Ensembl
  2. cyclin-dependent protein kinase activating kinase holoenzyme complex Source: Ensembl
  3. cytoplasm Source: UniProtKB
  4. holo TFIIH complex Source: UniProtKB
  5. MMXD complex Source: UniProtKB
  6. nucleus Source: MGI
  7. spindle Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 760760TFIIH basal transcription factor complex helicase XPD subunitPRO_0000101981Add
BLAST

Post-translational modificationi

ISGylated.By similarity

Keywords - PTMi

Ubl conjugation

Proteomic databases

MaxQBiO08811.
PaxDbiO08811.
PRIDEiO08811.

PTM databases

PhosphoSiteiO08811.

Expressioni

Gene expression databases

BgeeiO08811.
ExpressionAtlasiO08811. baseline and differential.
GenevestigatoriO08811.

Interactioni

Subunit structurei

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).By similarity

Protein-protein interaction databases

IntActiO08811. 1 interaction.
MINTiMINT-4114299.
STRINGi10090.ENSMUSP00000054380.

Structurei

3D structure databases

ProteinModelPortaliO08811.
SMRiO08811. Positions 26-258.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini7 – 283277Helicase ATP-bindingPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni438 – 637200Mediates interaction with MMS19By similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi234 – 2374DEAH box

Sequence similaritiesi

Belongs to the helicase family. RAD3/XPD subfamily.Curated
Contains 1 helicase ATP-binding domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG1199.
GeneTreeiENSGT00550000075092.
HOGENOMiHOG000205390.
HOVERGENiHBG051498.
InParanoidiO08811.
KOiK10844.
OMAiKKPLRFC.
OrthoDBiEOG70W3CM.
TreeFamiTF101232.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR006555. 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]
PfamiPF06733. DEAD_2. 1 hit.
PF06777. DUF1227. 1 hit.
PF13307. Helicase_C_2. 1 hit.
[Graphical view]
PRINTSiPR00852. XRODRMPGMNTD.
SMARTiSM00488. DEXDc2. 1 hit.
SM00491. HELICc2. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 4 hits.
TIGRFAMsiTIGR00604. rad3. 1 hit.
PROSITEiPS00690. DEAH_ATP_HELICASE. 1 hit.
PS51193. HELICASE_ATP_BIND_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O08811-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKLNVDGLLV YFPYDYIYPE QFSYMLELKR TLDAKGHGVL EMPSGTGKTV
60 70 80 90 100
SLLALIVAYQ RAYPLEVTKL IYCSRTVPEI EKVIEELRKL LSFYEQQEGE
110 120 130 140 150
KLPFLGLALS SRKNLCIHPE VTPLRFGKDV DGKCHSLTAS YVRAQYQQDA
160 170 180 190 200
SLPHCRFYEE FDIHGRQMPL PAGIYNLDDL KALGQRQGWC PYFLARYSIL
210 220 230 240 250
HANVVVYSYH YLLDPKIADL VSKELARKAV VVFDEAHNID NVCIDSMSVN
260 270 280 290 300
LTRRTLDRCQ SNLDTLQKTV LRIKETDEQR LRDEYRRLVE GLREASVARE
310 320 330 340 350
TDAHLANPVL PDEVLQEAVP GSIRTAEHFL GFLRRLLEYV KWRLRVQHVV
360 370 380 390 400
QESPPAFLSG LAQRVCIQRK PLRFCAERLR SLLHTLEIAD LADFSPLTLL
410 420 430 440 450
ANFATLVSTY AKGFTIIIEP FDDRTPTIAN PVLHFSCMDA SLAIKPVFER
460 470 480 490 500
FQSVIITSGT LSPLDIYPKI LDFHPVTMAT FTMTLARVCL CPMIIGRGND
510 520 530 540 550
QVAISSKFET REDIAVIRNY GNLLLEMSAV VPDGIVAFFT SYQYMESTVA
560 570 580 590 600
SWYEQGILEN IQRNKLLFIE TQDGAETSVA LEKYQEACEN GRGAILLSVA
610 620 630 640 650
RGKVSEGIDF VHHYGRAVIM FGVPYVYTQS RILKARLEYL RDQFQIREND
660 670 680 690 700
FLTFDAMRHA AQCVGRAIRG KTDYGLMVFA DKRFARADKR GKLPRWIQEH
710 720 730 740 750
LTDSNLNLTV DEGVQVAKYF LRQMAQPFHR EDQLGLSLLS LEQLQSEETL
760
QRIEQIAQQL
Length:760
Mass (Da):86,842
Last modified:July 27, 2011 - v2
Checksum:i02B2E116792D4E44
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti285 – 2851Y → C in BAB23443. (PubMed:16141072)Curated
Sequence conflicti595 – 5951I → V in AAB58296. (PubMed:9426063)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U97572 mRNA. Translation: AAB58296.1.
AK004652 mRNA. Translation: BAB23443.1. Different initiation.
AK082761 mRNA. Translation: BAC38607.1.
CH466639 Genomic DNA. Translation: EDL23140.1.
CCDSiCCDS20900.1.
RefSeqiNP_031975.2. NM_007949.4.
UniGeneiMm.36524.

Genome annotation databases

EnsembliENSMUST00000062831; ENSMUSP00000054380; ENSMUSG00000030400.
GeneIDi13871.
KEGGimmu:13871.
UCSCiuc009flq.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U97572 mRNA. Translation: AAB58296.1.
AK004652 mRNA. Translation: BAB23443.1. Different initiation.
AK082761 mRNA. Translation: BAC38607.1.
CH466639 Genomic DNA. Translation: EDL23140.1.
CCDSiCCDS20900.1.
RefSeqiNP_031975.2. NM_007949.4.
UniGeneiMm.36524.

3D structure databases

ProteinModelPortaliO08811.
SMRiO08811. Positions 26-258.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiO08811. 1 interaction.
MINTiMINT-4114299.
STRINGi10090.ENSMUSP00000054380.

PTM databases

PhosphoSiteiO08811.

Proteomic databases

MaxQBiO08811.
PaxDbiO08811.
PRIDEiO08811.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000062831; ENSMUSP00000054380; ENSMUSG00000030400.
GeneIDi13871.
KEGGimmu:13871.
UCSCiuc009flq.1. mouse.

Organism-specific databases

CTDi2068.
MGIiMGI:95413. Ercc2.

Phylogenomic databases

eggNOGiCOG1199.
GeneTreeiENSGT00550000075092.
HOGENOMiHOG000205390.
HOVERGENiHBG051498.
InParanoidiO08811.
KOiK10844.
OMAiKKPLRFC.
OrthoDBiEOG70W3CM.
TreeFamiTF101232.

Enzyme and pathway databases

ReactomeiREACT_196637. Cytosolic iron-sulfur cluster assembly.
REACT_203462. Formation of the Early Elongation Complex.
REACT_223654. Formation of transcription-coupled NER (TC-NER) repair complex.
REACT_224562. Dual incision reaction in TC-NER.
REACT_226490. RNA Polymerase II Transcription Elongation.
REACT_230204. RNA Polymerase II Transcription Initiation And Promoter Clearance.
REACT_232235. RNA Polymerase I Promoter Escape.
REACT_232708. RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
REACT_235780. RNA Polymerase I Transcription Initiation.
REACT_240507. Dual incision reaction in GG-NER.
REACT_244380. RNA Polymerase II Transcription Initiation.
REACT_252106. Formation of incision complex in GG-NER.
REACT_255009. RNA Polymerase II Pre-transcription Events.
REACT_255334. RNA Polymerase II Promoter Escape.
REACT_257165. RNA Polymerase I Transcription Termination.
REACT_257596. RNA Pol II CTD phosphorylation and interaction with CE.
REACT_258231. mRNA Capping.
REACT_259097. RNA Polymerase I Chain Elongation.

Miscellaneous databases

NextBioi284788.
PROiO08811.
SOURCEiSearch...

Gene expression databases

BgeeiO08811.
ExpressionAtlasiO08811. baseline and differential.
GenevestigatoriO08811.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR006555. 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]
PfamiPF06733. DEAD_2. 1 hit.
PF06777. DUF1227. 1 hit.
PF13307. Helicase_C_2. 1 hit.
[Graphical view]
PRINTSiPR00852. XRODRMPGMNTD.
SMARTiSM00488. DEXDc2. 1 hit.
SM00491. HELICc2. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 4 hits.
TIGRFAMsiTIGR00604. rad3. 1 hit.
PROSITEiPS00690. DEAH_ATP_HELICASE. 1 hit.
PS51193. HELICASE_ATP_BIND_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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].

Entry informationi

Entry nameiERCC2_MOUSE
AccessioniPrimary (citable) accession number: O08811
Secondary accession number(s): Q8C487, Q9DC01
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 27, 2011
Last modified: February 4, 2015
This is version 128 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

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.