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D3ZEG9

- D3ZEG9_RAT

UniProt

D3ZEG9 - D3ZEG9_RAT

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Protein
Submitted name:

Protein Ercc2

Gene

Ercc2

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

Display
All None

  • Function
  • Names & Taxonomy
  • Subcellular locationSubcell. location
  • Pathology & BiotechPathol./Biotech
  • PTM / Processing
  • Expression
  • Interaction
  • Structure
  • Family & Domains
  • Sequence
  • Cross-references
  • Publications
  • Entry information
  • Miscellaneous
  • Similar proteins
Top

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_198290. Cytosolic iron-sulfur cluster assembly.
REACT_206206. RNA Polymerase I Transcription Initiation.
REACT_214635. Dual incision reaction in GG-NER.
REACT_216241. RNA Polymerase II Pre-transcription Events.
REACT_218876. RNA Polymerase I Promoter Escape.
REACT_219180. Formation of incision complex in GG-NER.
REACT_231914. RNA Polymerase I Transcription Termination.
REACT_234724. mRNA Capping.
REACT_240071. RNA Polymerase II Transcription Initiation And Promoter Clearance.
REACT_245552. RNA Polymerase II Transcription Elongation.
REACT_247742. RNA Polymerase II Transcription Initiation.
REACT_253548. RNA Pol II CTD phosphorylation and interaction with CE.
REACT_253844. Formation of transcription-coupled NER (TC-NER) repair complex.
REACT_254690. Dual incision reaction in TC-NER.
REACT_255888. RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
REACT_258114. RNA Polymerase II Promoter Escape.
REACT_259307. RNA Polymerase I Chain Elongation.
REACT_262325. Formation of the Early Elongation Complex.

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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus
ProteomesiUP000002494: 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.
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 .
RefSeqi NP_001166280.1. NM_001172809.1.
UniGenei Rn.41871.

3D structure databases

ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000024246 ; ENSRNOP00000024247 ; ENSRNOG00000017753 .
GeneIDi 308415.
KEGGi rno:308415.

Organism-specific databases

CTDi 2068.
RGDi 1309109. Ercc2.

Phylogenomic databases

GeneTreei ENSGT00550000075092.
KOi K10844.
OMAi KKPLRFC.
OrthoDBi EOG70W3CM.
PhylomeDBi D3ZEG9.
TreeFami TF101232.

Enzyme and pathway databases

Reactomei REACT_198290. Cytosolic iron-sulfur cluster assembly.
REACT_206206. RNA Polymerase I Transcription Initiation.
REACT_214635. Dual incision reaction in GG-NER.
REACT_216241. RNA Polymerase II Pre-transcription Events.
REACT_218876. RNA Polymerase I Promoter Escape.
REACT_219180. Formation of incision complex in GG-NER.
REACT_231914. RNA Polymerase I Transcription Termination.
REACT_234724. mRNA Capping.
REACT_240071. RNA Polymerase II Transcription Initiation And Promoter Clearance.
REACT_245552. RNA Polymerase II Transcription Elongation.
REACT_247742. RNA Polymerase II Transcription Initiation.
REACT_253548. RNA Pol II CTD phosphorylation and interaction with CE.
REACT_253844. Formation of transcription-coupled NER (TC-NER) repair complex.
REACT_254690. Dual incision reaction in TC-NER.
REACT_255888. RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
REACT_258114. RNA Polymerase II Promoter Escape.
REACT_259307. RNA Polymerase I Chain Elongation.
REACT_262325. Formation of the Early Elongation Complex.

Miscellaneous databases

NextBioi 658821.

Family and domain databases

Gene3Di 3.40.50.300. 2 hits.
InterProi IPR006555. 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 ]
Pfami PF06733. DEAD_2. 1 hit.
PF06777. DUF1227. 1 hit.
PF13307. Helicase_C_2. 1 hit.
[Graphical view ]
PRINTSi PR00852. XRODRMPGMNTD.
SMARTi SM00488. DEXDc2. 1 hit.
SM00491. HELICc2. 1 hit.
[Graphical view ]
SUPFAMi SSF52540. SSF52540. 4 hits.
TIGRFAMsi TIGR00604. rad3. 1 hit.
PROSITEi PS00690. DEAH_ATP_HELICASE. 1 hit.
PS51193. HELICASE_ATP_BIND_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

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(2004) [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 (JUL-2011) to UniProtKB
    Cited for: IDENTIFICATION.
    Strain: Brown NorwayImported.
+Additional computationally mapped references.

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: January 7, 2015
This is version 40 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.
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