D3ZEG9 (D3ZEG9_RAT) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Submitted name:
Protein Ercc2 Ensembl ENSRNOP00000024247

Submitted name:
RCG54110 EMBL EDM08205.1

Gene names

Name:	Ercc2 Ensembl ENSRNOP00000024247 RGD 1309109
ORF Names:	rCG_54110 EMBL EDM08205.1

Organism

Rattus norvegicus (Rat) [Reference proteome] Ensembl ENSRNOP00000024247

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	760 AA.
Sequence status	Complete.
Protein existence	Predicted

General annotation (Comments)

Catalytic activity	ATP + H2O = ADP + phosphate. SAAS SAAS013020
Sequence similarities	Contains 1 helicase ATP-binding domain. SAAS SAAS013020

Ontologies

Keywords
Cellular component	Nucleus SAAS SAAS013020
Ligand	ATP-binding Nucleotide-binding
Molecular function	Helicase SAAS SAAS013020 Hydrolase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	UV protection Inferred from electronic annotation. Source: Compara aging Inferred from electronic annotation. Source: Compara apoptotic process Inferred from electronic annotation. Source: Compara bone mineralization Inferred from electronic annotation. Source: Compara cell cycle checkpoint Inferred from electronic annotation. Source: Compara cell proliferation Inferred from electronic annotation. Source: Compara central nervous system myelin formation Inferred from electronic annotation. Source: Compara chromosome segregation Inferred from electronic annotation. Source: Compara embryonic cleavage Inferred from electronic annotation. Source: Compara erythrocyte maturation Inferred from electronic annotation. Source: Compara extracellular matrix organization Inferred from electronic annotation. Source: Compara hair cell differentiation Inferred from electronic annotation. Source: Compara hair follicle maturation Inferred from electronic annotation. Source: Compara hematopoietic stem cell differentiation Inferred from electronic annotation. Source: Compara in utero embryonic development Inferred from electronic annotation. Source: Compara induction of apoptosis Inferred from electronic annotation. Source: Compara multicellular organism growth Inferred from electronic annotation. Source: Compara negative regulation of apoptotic process Inferred from electronic annotation. Source: Compara nucleotide-excision repair, DNA incision Inferred from electronic annotation. Source: Compara positive regulation of DNA binding Inferred from electronic annotation. Source: Compara positive regulation of transcription from RNA polymerase II promoter Inferred from electronic annotation. Source: Compara post-embryonic development Inferred from electronic annotation. Source: Compara response to hypoxia Inferred from expression pattern PubMed 9763211. Source: RGD response to oxidative stress Inferred from electronic annotation. Source: Compara skin development Inferred from electronic annotation. Source: Compara spinal cord development Inferred from electronic annotation. Source: Compara transcription-coupled nucleotide-excision repair Inferred from electronic annotation. Source: Compara
Cellular_component	MMXD complex Inferred from electronic annotation. Source: Compara SSL2-core TFIIH complex Inferred from direct assay PubMed 8855220. Source: RGD cyclin-dependent protein kinase activating kinase holoenzyme complex Inferred from electronic annotation. Source: Compara cytoplasm Inferred from electronic annotation. Source: Compara
Molecular_function	5'-3' DNA helicase activity Inferred from electronic annotation. Source: Compara 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: InterPro RNA polymerase II carboxy-terminal domain kinase activity Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Sequences

	Sequence		Length	Mass (Da)
	D3ZEG9 [UniParc]. Last modified April 20, 2010. Version 1. Checksum: AC4316E1F21BCF67	FASTA	760	86,814
	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 FDTHGRQVPL PAGIYNLDDL 190 200 210 220 230 240 KALGQRQGWC PYFLARYSIL HANVVVYSYH YLLDPKIADL VSKELARKAV VVFDEAHNID 250 260 270 280 290 300 NVCIDSMSVN LTRRTLDRCQ SNLDTLQKTV LRIKETDEQR LRDEYRRLVE GLREASAARE 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 FDDRTPTITN PILHFSCMDA 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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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 Norway Ensembl ENSRNOP00000024247.
[2]	"Gene and alternative splicing annotation with AIR." Florea L., Di Francesco V., Miller J., Turner R., Yao A., Harris M., Walenz B., Mobarry C., Merkulov G.V., Charlab R., Dew I., Deng Z., Istrail S., Li P., Sutton G. Genome Res. 15:54-66(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE. Strain: BN EMBL EDM08205.1.
[3]	Mural R.J., Li P.W., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S.H., Dew I., Evans C.A., Ferriera S., Flanigan M., Fosler C., Glodek A., Gu Z., Holt R.A., Jennings D., Kraft C.L., Lu F. , Nguyen T., Nusskern D.R., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Wang Z., Woodage T., Zheng X.H., Zhong F. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE. Strain: BN EMBL EDM08205.1.
[4]	Ensembl Submitted (JUL-2011) to UniProtKB Cited for: IDENTIFICATION. Strain: Brown Norway Ensembl ENSRNOP00000024247.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AABR06003883 Genomic DNA. No translation available. CH473979 Genomic DNA. Translation: EDM08205.1.
IPI	IPI00367025.
RefSeq	NP_001166280.1. NM_001172809.1.
UniGene	Rn.41871.
3D structure databases
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSRNOT00000024246; ENSRNOP00000024247; ENSRNOG00000017753.
GeneID	308415.
KEGG	rno:308415.
Organism-specific databases
CTD	2068.
RGD	1309109. Ercc2.
Phylogenomic databases
GeneTree	ENSGT00550000075092.
KO	K10844.
OrthoDB	EOG4BVRT2.
Family and domain databases
InterPro	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]
Pfam	PF06733. DEAD_2. 1 hit. PF06777. DUF1227. 1 hit. PF13307. Helicase_C_2. 1 hit. [Graphical view]
PRINTS	PR00852. XRODRMPGMNTD.
SMART	SM00488. DEXDc2. 1 hit. SM00491. HELICc2. 1 hit. [Graphical view]
SUPFAM	SSF52540. SSF52540. 2 hits.
TIGRFAMs	TIGR00604. rad3. 1 hit.
PROSITE	PS00690. DEAH_ATP_HELICASE. 1 hit. PS51193. HELICASE_ATP_BIND_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	658821.

Entry information

Entry name

D3ZEG9_RAT

Accession

Primary (citable) accession number: D3ZEG9

Entry history

Integrated into UniProtKB/TrEMBL:	April 20, 2010
Last sequence update:	April 20, 2010
Last modified:	May 29, 2013
This is version 27 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)