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Protein
Submitted name:

Protein Ercc2

Gene

Ercc2

Organism
Rattus norvegicus (Rat)
Status
Unreviewed-Annotation score: Annotation score: 4 out of 5-Protein predictedi

Functioni

Catalytic activityi

ATP + H2O = ADP + phosphate.SAAS annotation

GO - Molecular functioni

  1. 5'-3' DNA helicase activity Source: Ensembl
  2. ATP binding Source: UniProtKB-KW
  3. ATP-dependent DNA helicase activity Source: InterPro
  4. DNA binding Source: InterPro
  5. RNA polymerase II carboxy-terminal domain kinase activity Source: Ensembl

GO - Biological processi

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

Keywords - Molecular functioni

HelicaseSAAS annotation, Hydrolase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_271824. RNA Polymerase II Promoter Escape.
REACT_273293. RNA Polymerase II Pre-transcription Events.
REACT_280841. RNA Polymerase I Transcription Initiation.
REACT_283793. Formation of RNA Pol II elongation complex.
REACT_290439. Dual incision reaction in GG-NER.
REACT_290496. RNA Polymerase I Chain Elongation.
REACT_291085. RNA Polymerase I Transcription Termination.
REACT_297910. Formation of transcription-coupled NER (TC-NER) repair complex.
REACT_319445. RNA Pol II CTD phosphorylation and interaction with CE.
REACT_320748. Cytosolic iron-sulfur cluster assembly.
REACT_323062. mRNA Capping.
REACT_323975. Dual incision reaction in TC-NER.
REACT_332743. Formation of incision complex in GG-NER.
REACT_338490. RNA Polymerase I Promoter Escape.
REACT_340454. RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
REACT_340969. Formation of the Early Elongation Complex.
REACT_343091. RNA Polymerase II Transcription Elongation.
REACT_343213. RNA Polymerase II Transcription Initiation And Promoter Clearance.
REACT_351677. RNA Polymerase II Transcription Initiation.

Names & Taxonomyi

Protein namesi
Submitted name:
Protein Ercc2Imported
Submitted name:
RCG54110Imported
Gene namesi
Name:Ercc2Imported
ORF Names:rCG_54110Imported
OrganismiRattus norvegicus (Rat)Imported
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494 Componenti: Chromosome 1

Organism-specific databases

RGDi1309109. Ercc2.

Subcellular locationi

GO - Cellular componenti

  1. core TFIIH complex Source: RGD
  2. cyclin-dependent protein kinase activating kinase holoenzyme complex Source: Ensembl
  3. cytoplasm Source: Ensembl
  4. MMXD complex Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

NucleusSAAS annotation

Family & Domainsi

Sequence similaritiesi

Contains helicase ATP-binding domain.SAAS annotation

Phylogenomic databases

GeneTreeiENSGT00550000075092.
InParanoidiD3ZEG9.
KOiK10844.
OMAiKKPLRFC.
OrthoDBiEOG70W3CM.
PhylomeDBiD3ZEG9.
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.

D3ZEG9-1 [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 FDTHGRQVPL PAGIYNLDDL KALGQRQGWC PYFLARYSIL
210 220 230 240 250
HANVVVYSYH YLLDPKIADL VSKELARKAV VVFDEAHNID NVCIDSMSVN
260 270 280 290 300
LTRRTLDRCQ SNLDTLQKTV LRIKETDEQR LRDEYRRLVE GLREASAARE
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 FDDRTPTITN PILHFSCMDA 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):86,814
Last modified:April 20, 2010 - v1
Checksum:iAC4316E1F21BCF67
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR06003883 Genomic DNA. No translation available.
CH473979 Genomic DNA. Translation: EDM08205.1.
RefSeqiNP_001166280.1. NM_001172809.1.
UniGeneiRn.41871.

Genome annotation databases

EnsembliENSRNOT00000024246; ENSRNOP00000024247; ENSRNOG00000017753.
GeneIDi308415.
KEGGirno:308415.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR06003883 Genomic DNA. No translation available.
CH473979 Genomic DNA. Translation: EDM08205.1.
RefSeqiNP_001166280.1. NM_001172809.1.
UniGeneiRn.41871.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000024246; ENSRNOP00000024247; ENSRNOG00000017753.
GeneIDi308415.
KEGGirno:308415.

Organism-specific databases

CTDi2068.
RGDi1309109. Ercc2.

Phylogenomic databases

GeneTreeiENSGT00550000075092.
InParanoidiD3ZEG9.
KOiK10844.
OMAiKKPLRFC.
OrthoDBiEOG70W3CM.
PhylomeDBiD3ZEG9.
TreeFamiTF101232.

Enzyme and pathway databases

ReactomeiREACT_271824. RNA Polymerase II Promoter Escape.
REACT_273293. RNA Polymerase II Pre-transcription Events.
REACT_280841. RNA Polymerase I Transcription Initiation.
REACT_283793. Formation of RNA Pol II elongation complex.
REACT_290439. Dual incision reaction in GG-NER.
REACT_290496. RNA Polymerase I Chain Elongation.
REACT_291085. RNA Polymerase I Transcription Termination.
REACT_297910. Formation of transcription-coupled NER (TC-NER) repair complex.
REACT_319445. RNA Pol II CTD phosphorylation and interaction with CE.
REACT_320748. Cytosolic iron-sulfur cluster assembly.
REACT_323062. mRNA Capping.
REACT_323975. Dual incision reaction in TC-NER.
REACT_332743. Formation of incision complex in GG-NER.
REACT_338490. RNA Polymerase I Promoter Escape.
REACT_340454. RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
REACT_340969. Formation of the Early Elongation Complex.
REACT_343091. RNA Polymerase II Transcription Elongation.
REACT_343213. RNA Polymerase II Transcription Initiation And Promoter Clearance.
REACT_351677. RNA Polymerase II Transcription Initiation.

Miscellaneous databases

NextBioi658821.

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. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
    Rat Genome Sequencing Project Consortium
    Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M.
    , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
    Nature 428:493-521(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown NorwayImported.
  2. Cited for: NUCLEOTIDE SEQUENCE.
    Strain: BNImported.
  3. Cited for: NUCLEOTIDE SEQUENCE.
    Strain: BNImported.
  4. Ensembl
    Submitted (JUN-2011) to UniProtKB
    Cited for: IDENTIFICATION.
    Strain: Brown NorwayImported.

Entry informationi

Entry nameiD3ZEG9_RAT
AccessioniPrimary (citable) accession number: D3ZEG9
Entry historyi
Integrated into UniProtKB/TrEMBL: April 20, 2010
Last sequence update: April 20, 2010
Last modified: April 1, 2015
This is version 43 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteomeImported

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.