GENTAUR Belgium BVBA BE0473327336 Voortstraat 49, 1910 Kampenhout BELGIUM Tel 0032 16 58 90 45
GENTAUR U.S.A Genprice Inc,Logistics 547 Yurok Circle, SanJose, CA 95123
Tel (408) 780-0908, Fax (408) 780-0908, [email protected]

Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, Gentaur another in time delivery

Decapping nuclease RAI1 (EC 3.6.1.-) (RAT1-interacting protein)

 DXO_YEAST               Reviewed;         387 AA.
P53063; D6VV89;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
13-FEB-2019, entry version 153.
RecName: Full=Decapping nuclease RAI1;
EC=3.6.1.-;
AltName: Full=RAT1-interacting protein;
Name=RAI1; OrderedLocusNames=YGL246C; ORFNames=NRE387;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 96604 / S288c / FY1679;
PubMed=8972578;
DOI=10.1002/(SICI)1097-0061(199612)12:15<1555::AID-YEA43>3.0.CO;2-Q;
Coissac E., Maillier E., Robineau S., Netter P.;
"Sequence of a 39,411 bp DNA fragment covering the left end of
chromosome VII of Saccharomyces cerevisiae.";
Yeast 12:1555-1562(1996).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169869;
Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M.,
Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J.,
Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E.,
Clemente M.L., Coblenz A., Coglievina M., Coissac E., Defoor E.,
Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B.,
Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L.,
Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M.,
Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M.,
Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B.,
Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W.,
Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A.,
Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S.,
Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L.,
Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S.,
Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J.,
Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M.,
Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B.,
Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J.,
Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M.,
van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M.,
Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H.,
Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M.,
Zollner A., Kleine K.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
Nature 387:81-84(1997).
[3]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=17322287; DOI=10.1101/gr.6037607;
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A.,
Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F.,
Williamson J., Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G.,
Kolodner R.D., LaBaer J.;
"Approaching a complete repository of sequence-verified protein-
encoding clones for Saccharomyces cerevisiae.";
Genome Res. 17:536-543(2007).
[5]
PROTEIN SEQUENCE OF 2-17, FUNCTION, AND INTERACTION WITH RAT1.
PubMed=10805743; DOI=10.1128/MCB.20.11.4006-4015.2000;
Xue Y., Bai X., Lee I., Kallstrom G., Ho J., Brown J., Stevens A.,
Johnson A.W.;
"Saccharomyces cerevisiae RAI1 (YGL246c) is homologous to human DOM3Z
and encodes a protein that binds the nuclear exoribonuclease Rat1p.";
Mol. Cell. Biol. 20:4006-4015(2000).
[6]
FUNCTION, INTERACTION WITH RAT1 AND PRE-60S RIBOSOMAL SUBUNITS, AND
SUBCELLULAR LOCATION.
PubMed=12612077; DOI=10.1128/MCB.23.6.2042-2054.2003;
Sydorskyy Y., Dilworth D.J., Yi E.C., Goodlett D.R., Wozniak R.W.,
Aitchison J.D.;
"Intersection of the Kap123p-mediated nuclear import and ribosome
export pathways.";
Mol. Cell. Biol. 23:2042-2054(2003).
[7]
FUNCTION.
PubMed=12897126; DOI=10.1128/MCB.23.16.5502-5515.2003;
Das B., Butler J.S., Sherman F.;
"Degradation of normal mRNA in the nucleus of Saccharomyces
cerevisiae.";
Mol. Cell. Biol. 23:5502-5515(2003).
[8]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[9]
FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN A
COMPLEX WITH RTT103.
PubMed=15565157; DOI=10.1038/nature03041;
Kim M., Krogan N.J., Vasiljeva L., Rando O.J., Nedea E.,
Greenblatt J.F., Buratowski S.;
"The yeast Rat1 exonuclease promotes transcription termination by RNA
polymerase II.";
Nature 432:517-522(2004).
[10]
ERRATUM.
Kim M., Krogan N.J., Vasiljeva L., Rando O.J., Nedea E.,
Greenblatt J.F., Buratowski S.;
Nature 433:661-661(2005).
[11]
FUNCTION.
PubMed=16131592; DOI=10.1261/rna.2900205;
Fang F., Phillips S., Butler J.S.;
"Rat1p and Rai1p function with the nuclear exosome in the processing
and degradation of rRNA precursors.";
RNA 11:1571-1578(2005).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-198, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth
phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
[13]
FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH RAT1, AND MUTAGENESIS
OF GLU-221 AND ASP-223.
PubMed=20802481; DOI=10.1038/nature09338;
Jiao X., Xiang S., Oh C., Martin C.E., Tong L., Kiledjian M.;
"Identification of a quality-control mechanism for mRNA 5'-end
capping.";
Nature 467:608-611(2010).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
-!- FUNCTION: Ribonuclease that specifically degrades pre-mRNAs with a
defective 5' end cap and is part of a pre-mRNA capping quality
control. Has decapping and pyrophosphohydrolase activities. Has
decapping activity toward incomplete 5' end cap mRNAs such as
unmethylated 5' end-capped RNA to release GpppN and 5' end
monophosphate RNA. Also possesses RNA 5'-pyrophosphohydrolase
activity by hydrolyzing the 5' end triphosphate to release
pyrophosphates. Stimulates exoribonuclease activity of RAT1,
allowing it to degrade RNAs with stable secondary structure more
effectively. Required for the processing of nuclear mRNA and rRNA
precursors. May promote termination of transcription by RNA
polymerase II. {ECO:0000269|PubMed:10805743,
ECO:0000269|PubMed:12612077, ECO:0000269|PubMed:12897126,
ECO:0000269|PubMed:15565157, ECO:0000269|PubMed:16131592,
ECO:0000269|PubMed:20802481}.
-!- COFACTOR:
Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
Evidence={ECO:0000250};
Note=Divalent metal cation. {ECO:0000250};
-!- SUBUNIT: Interacts with RAT1, RTT103 and pre-60S ribosomal
subunits. {ECO:0000269|PubMed:10805743,
ECO:0000269|PubMed:12612077, ECO:0000269|PubMed:15565157,
ECO:0000269|PubMed:20802481}.
-!- INTERACTION:
Q02792:RAT1; NbExp=4; IntAct=EBI-24206, EBI-14845;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12612077}.
-!- MISCELLANEOUS: Present with 4030 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the DXO/Dom3Z family. {ECO:0000305}.
-!- CAUTION: In contrast to canonical decapping enzymes, which release
m(7)pppG (m(7)GDP), the decapping activity releases the entire cap
structure GpppN and a 5' end monophosphate RNA.
{ECO:0000305|PubMed:20802481}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; X94357; CAA64141.1; -; Genomic_DNA.
EMBL; Z72768; CAA96966.1; -; Genomic_DNA.
EMBL; AY693165; AAT93184.1; -; Genomic_DNA.
EMBL; BK006941; DAA07873.1; -; Genomic_DNA.
PIR; S61615; S61615.
RefSeq; NP_011268.1; NM_001181112.1.
ProteinModelPortal; P53063; -.
SMR; P53063; -.
BioGrid; 33033; 71.
ComplexPortal; CPX-1332; RAT1-RAI1 RNA polymerase II termination complex.
DIP; DIP-6807N; -.
IntAct; P53063; 13.
MINT; P53063; -.
STRING; 4932.YGL246C; -.
iPTMnet; P53063; -.
MaxQB; P53063; -.
PaxDb; P53063; -.
PRIDE; P53063; -.
EnsemblFungi; YGL246C_mRNA; YGL246C_mRNA; YGL246C.
GeneID; 852646; -.
KEGG; sce:YGL246C; -.
EuPathDB; FungiDB:YGL246C; -.
SGD; S000003215; RAI1.
GeneTree; ENSGT00390000006425; -.
HOGENOM; HOG000200647; -.
InParanoid; P53063; -.
KO; K14845; -.
OMA; MAYWGYK; -.
BioCyc; YEAST:G3O-30717-MONOMER; -.
PRO; PR:P53063; -.
Proteomes; UP000002311; Chromosome VII.
GO; GO:0005829; C:cytosol; IDA:SGD.
GO; GO:0005634; C:nucleus; IDA:SGD.
GO; GO:0030234; F:enzyme regulator activity; IDA:SGD.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
GO; GO:1990174; F:phosphodiesterase decapping endonuclease activity; IDA:SGD.
GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
GO; GO:0034353; F:RNA pyrophosphohydrolase activity; IDA:SGD.
GO; GO:0000448; P:cleavage in ITS2 between 5.8S rRNA and LSU-rRNA of tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IDA:SGD.
GO; GO:0031087; P:deadenylation-independent decapping of nuclear-transcribed mRNA; IDA:SGD.
GO; GO:0000466; P:maturation of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
GO; GO:0000463; P:maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
GO; GO:0071035; P:nuclear polyadenylation-dependent rRNA catabolic process; IMP:SGD.
GO; GO:0000956; P:nuclear-transcribed mRNA catabolic process; IMP:SGD.
GO; GO:0030846; P:termination of RNA polymerase II transcription, poly(A)-coupled; IMP:SGD.
InterPro; IPR013961; RAI1.
InterPro; IPR039039; RAI1-like_fam.
PANTHER; PTHR12395; PTHR12395; 1.
Pfam; PF08652; RAI1; 1.
1: Evidence at protein level;
Complete proteome; Direct protein sequencing; Hydrolase;
Metal-binding; mRNA processing; Nuclease; Nucleotide-binding; Nucleus;
Phosphoprotein; Reference proteome; RNA-binding; rRNA processing;
Transcription; Transcription regulation; Transcription termination.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:10805743}.
CHAIN 2 387 Decapping nuclease RAI1.
/FTId=PRO_0000202708.
REGION 273 387 Interaction with RAT1.
METAL 172 172 Divalent metal cation. {ECO:0000250}.
METAL 223 223 Divalent metal cation. {ECO:0000250}.
METAL 241 241 Divalent metal cation. {ECO:0000250}.
METAL 242 242 Divalent metal cation; via carbonyl
oxygen. {ECO:0000250}.
BINDING 105 105 Substrate. {ECO:0000250}.
BINDING 221 221 Substrate. {ECO:0000250}.
BINDING 267 267 Substrate. {ECO:0000250}.
MOD_RES 198 198 Phosphoserine.
{ECO:0000244|PubMed:18407956}.
MUTAGEN 221 221 E->A: Abolishes the decapping activity.
{ECO:0000269|PubMed:20802481}.
MUTAGEN 223 223 D->A: Abolishes the decapping activity.
{ECO:0000269|PubMed:20802481}.
CONFLICT 8 8 F -> S (in Ref. 5; AA sequence).
{ECO:0000305}.
SEQUENCE 387 AA; 44510 MW; E4A6565AF690A3E1 CRC64;
MGVSANLFVK QRGSTTALKQ PKEIGFYSRT KDEEYLISDD TNLNYYYLPD AELDRKLDLS
SGFQKFKDYY KDFEDRCSLR GLLETIESSE RHKGKKINAD IITFRGIARK LISCAFDSPS
FNTVDLRIVS FNGQLFIKEV PEAVNAAKAS SATEAGRNIN QDLNVFTGYK FETLATLSNP
LQYTPREVIE KRTKRIVSHG DEYISVVRTG VGNCKLILGA EVDCIFDFKE NGRDNLKHYA
ELKCTQQVAN ISDTHKFERK LFRTWLQCFL VGIPRIIYGF KDDHYVLKTV EEFSTEEVPV
LLKNNNPQVG SACLEAIKWY GLLTEWLLKM IPRDEDPHSQ IRAFKLVFEN NHLRLSEIEE
SDEEYSGLID GEHILSNGFK EWRKSLK


Related products :

Catalog number Product name Quantity
28-134 Decapping is a key step in general and regulated mRNA decay. The protein encoded by this gene is a decapping enzyme. This protein and another decapping enzyme form a decapping complex, which interacts 0.1 mg
29-052 Decapping is a key step in general and regulated mRNA decay. The protein encoded by this gene is a decapping enzyme. This protein and another decapping enzyme form a decapping complex, which interacts 0.1 mg
RAI1 RAI1 Gene retinoic acid induced 1
EIAAB10631 Dcp1a,MAD homolog 4-interacting transcription coactivator 1,Mitc1,Mouse,mRNA-decapping enzyme 1A,Mus musculus,Smad4-interacting transcriptional co-activator,Smif,Transcription factor SMIF
27-634 SND1 was originally characterized as a transcriptional coactivator for Epstein-Barr virus nuclear antigen 2. It is a STAT6 TAD interacting protein containing staphylococcal nuclease (SN)-like domain a 0.1 mg
EIAAB14410 Fan1,FANCD2_FANCI-associated nuclease 1,Fanconi-associated nuclease 1,Kiaa1018,Mouse,Mtmr15,Mus musculus,Myotubularin-related protein 15
EIAAB14411 FAN1,FANCD2_FANCI-associated nuclease 1,Fanconi-associated nuclease 1,Homo sapiens,Human,KIAA1018,MTMR15,Myotubularin-related protein 15
EIAAB27017 45 kDa NF-AT-interacting protein,45 kDa NFAT-interacting protein,Homo sapiens,Human,NFATC2-interacting protein,NFATC2IP,NIP45,Nuclear factor of activated T-cells, cytoplasmic 2-interacting protein
EIAAB27018 45 kDa NF-AT-interacting protein,45 kDa NFAT-interacting protein,Mouse,Mus musculus,NFATC2-interacting protein,Nfatc2ip,Nip45,Nuclear factor of activated T-cells, cytoplasmic 2-interacting protein
60B340 Polyclonal Antibodies: RAI1-(N-terminal); Specificity: RAI1-(N-terminal) ; Application: IHC 0.1mg
60B341 Polyclonal Antibodies: RAI1-(C-terminal); Specificity: RAI1-(C-terminal) ; Application: IHC 0.1mg
18-003-43271 mRNA decapping enzyme 1A - EC 3.-.-.-; Transcription factor SMIF; Smad4-interacting transcriptional co-activator Polyclonal 0.1 mg Protein A
18-003-42557 mRNA decapping enzyme 1A - EC 3.-.-.-; Transcription factor SMIF; Smad4-interacting transcriptional co-activator Polyclonal 0.1 mg Protein A
EIAAB31218 Homo sapiens,hPIP1,Human,p21-activated protein kinase-interacting protein 1,PAK_PLC-interacting protein 1,PAK1-interacting protein 1,PAK1IP1,PIP1,WD repeat-containing protein 84,WDR84
EIAAB46349 Homo sapiens,Human,Protein PRPL-2,WAS_WASL-interacting protein family member 1,WASP-interacting protein,WASPIP,WIP,WIPF1,Wiskott-Aldrich syndrome protein-interacting protein
EIAAB39347 Mouse,Mus musculus,Spata24,Spermatogenesis-associated protein 24,TATA-binding protein-like factor-interacting protein,Testis protein T6441 homolog,Tipt,Tipt2,TLF-interacting protein,TRF2-interacting p
EIAAB07420 Cdc42-interacting protein 4,CIP4,Homo sapiens,hSTP,Human,Protein Felic,Salt tolerant protein,STOT,STP,Thyroid receptor-interacting protein 10,TR-interacting protein 10,TRIP10,TRIP-10
EIAAB39604 54 kDa VacA-interacting protein,54 kDa vimentin-interacting protein,90 kDa SH3 protein interacting with Nck,AF3p21,AF3P21,Dia-interacting protein 1,Diaphanous protein-interacting protein,DIP-1,Homo sa
EIAAB39603 54 kDa VacA-interacting protein,90 kDa N-WASP-interacting protein,90 kDa SH3 protein interacting with Nck,Mouse,Mus musculus,NCK-interacting protein with SH3 domain,Nckipsd,N-WASP-binding protein,SH3
EIAAB46351 Rat,Rattus norvegicus,WAS_WASL-interacting protein family member 1,WASP-interacting protein,Waspip,Wip,Wipf1,Wiskott-Aldrich syndrome protein-interacting protein
EIAAB46350 Mouse,Mus musculus,WAS_WASL-interacting protein family member 1,WASP-interacting protein,Waspip,Wip,Wipf1,Wiskott-Aldrich syndrome protein-interacting protein
EIAAB30253 Aip1,ALG-2-interacting protein 1,ALG-2-interacting protein X,Alix,E2F1-inducible protein,Eig2,Mouse,Mus musculus,Pdcd6ip,Programmed cell death 6-interacting protein
EIAAB32252 Addicsin,ADP-ribosylation factor-like protein 6-interacting protein 5,Aip5,Aip-5,ARL-6-interacting protein 5,Arl6ip5,Glutamate transporter EAAC1-interacting protein,GTRAP3-18,Jwa,Mouse,Mus musculus,PR
EIAAB07421 Cdc42-interacting protein 4,Cip4,Rat,Rattus norvegicus,Salt tolerant protein,Stp,Thyroid receptor-interacting protein 10,TR-interacting protein 10,Trip10,TRIP-10
EIAAB44012 Homo sapiens,Human,OIP1,OIP-1,Opa-interacting protein 1,Thyroid receptor-interacting protein 6,TR-interacting protein 6,TRIP6,TRIP-6,ZRP-1,Zyxin-related protein 1

Kits Elisa; taq POLYMERASE

Search in Google:

google

Share this page:
share on twitter rss feedsfacebookgoogle gentaur



Quick order!
Enter catalog number :


Gentaur; yes we can

Pathways :
WP1049: G Protein Signaling Pathways
WP1165: G Protein Signaling Pathways
WP1371: G Protein Signaling Pathways
WP1438: Influenza A virus infection
WP1493: Carbon assimilation C4 pathway
WP1502: Mitochondrial biogenesis
WP1531: Vitamin D synthesis
WP1566: Citrate cycle (TCA cycle)
WP1613: 1,4-Dichlorobenzene degradation
WP1616: ABC transporters
WP1624: Bacterial secretion system
WP1625: Base excision repair
WP1644: DNA replication
WP1650: Fluorobenzoate degradation
WP1654: gamma-Hexachlorocyclohexane degradation
WP1657: Glycerolipid metabolism
WP1659: Glycine, serine and threonine metabolism
WP1661: Glyoxylate and dicarboxylate metabolism
WP1663: Homologous recombination
WP1665: Limonene and pinene degradation
WP1672: Mismatch repair
WP1673: Naphthalene and anthracene degradation
WP1675: Nitrogen metabolism
WP1676: Non-homologous end-joining
WP1678: Nucleotide excision repair

Related Genes :
[rai1 B13O20.160 NCU04191] Decapping nuclease rai1 (EC 3.6.1.-)
[exr-1 rat1 B7K22.110 NCU01643] 5'-3' exoribonuclease 2 (EC 3.1.13.-) (Exoribonuclease 1)
[CYP26A1 CYP26 P450RAI1] Cytochrome P450 26A1 (EC 1.14.13.-) (Cytochrome P450 retinoic acid-inactivating 1) (Cytochrome P450RAI) (hP450RAI) (Retinoic acid 4-hydroxylase) (Retinoic acid-metabolizing cytochrome)
[XRN1 DST2 KEM1 RAR5 SEP1 SKI1 YGL173C G1645] 5'-3' exoribonuclease 1 (EC 3.1.13.-) (DNA strand transfer protein beta) (STP-beta) (KAR(-)-enhancing mutation protein) (Strand exchange protein 1) (p175)
[XRN4 AIN1 EIN5 At1g54490 F20D21.30] 5'-3' exoribonuclease 4 (EC 3.1.13.-) (Protein ACC INSENSITIVE 1) (Protein ETHYLENE INSENSITIVE 5) (Protein EXORIBONUCLEASE 4)
[Nudt16] U8 snoRNA-decapping enzyme (EC 3.6.1.62) (IDP phosphatase) (IDPase) (EC 3.6.1.64) (Inosine diphosphate phosphatase) (Nucleoside diphosphate-linked moiety X motif 16) (Nudix motif 16) (m7GpppN-mRNA hydrolase)
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C) (EC 3.4.22.28); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[DCPS DCS1 HINT5 HSPC015] m7GpppX diphosphatase (EC 3.6.1.59) (DCS-1) (Decapping scavenger enzyme) (Hint-related 7meGMP-directed hydrolase) (Histidine triad nucleotide-binding protein 5) (Histidine triad protein member 5) (HINT-5) (Scavenger mRNA-decapping enzyme DcpS)
[Inppl1 Ship2] Phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 2 (EC 3.1.3.86) (Inositol polyphosphate phosphatase-like protein 1) (INPPL-1) (SH2 domain-containing inositol 5'-phosphatase 2) (SH2 domain-containing inositol phosphatase 2) (SHIP-2)
[NUDT16] U8 snoRNA-decapping enzyme (EC 3.6.1.62) (IDP phosphatase) (IDPase) (EC 3.6.1.64) (Inosine diphosphate phosphatase) (Nucleoside diphosphate-linked moiety X motif 16) (Nudix motif 16) (Nudix hydrolase 16) (U8 snoRNA-binding protein H29K) (m7GpppN-mRNA hydrolase)
[Apex1 Ape Apex Ref1] DNA-(apurinic or apyrimidinic site) lyase (EC 3.1.-.-) (EC 4.2.99.18) (APEX nuclease) (APEN) (Apurinic-apyrimidinic endonuclease 1) (AP endonuclease 1) (REF-1) (Redox factor-1) [Cleaved into: DNA-(apurinic or apyrimidinic site) lyase, mitochondrial]
[Arl6ip5 Aip5 Jwa Pra2 Praf3] PRA1 family protein 3 (ADP-ribosylation factor-like protein 6-interacting protein 5) (ARL-6-interacting protein 5) (Aip-5) (Addicsin) (GTRAP3-18) (Glutamate transporter EAAC1-interacting protein) (Prenylated Rab acceptor protein 2) (Protein JWa)
[nudt16] U8 snoRNA-decapping enzyme (EC 3.6.1.62) (IDP phosphatase) (IDPase) (EC 3.6.1.64) (Inosine diphosphate phosphatase) (Nucleoside diphosphate-linked moiety X motif 16) (Nudix motif 16) (U8 snoRNA-binding protein X29) (m7GpppN-mRNA hydrolase)
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C) (EC 3.4.22.28); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[Dcp1a Mitc1 Smif] mRNA-decapping enzyme 1A (EC 3.-.-.-) (MAD homolog 4-interacting transcription coactivator 1) (Smad4-interacting transcriptional co-activator) (Transcription factor SMIF)
[DCP2 TDT At5g13570 MSH12.3] mRNA-decapping enzyme subunit 2 (AtDCP2) (Protein DECAPPING 2) (EC 3.6.1.62) (M(7)GpppN-mRNA hydrolase DCP2) (Protein TRIDENT)
[] Genome polyprotein [Cleaved into: Core protein p21 (Capsid protein C) (p21); Core protein p19; Envelope glycoprotein E1 (gp32) (gp35); Envelope glycoprotein E2 (NS1) (gp68) (gp70); p7; Protease NS2-3 (p23) (EC 3.4.22.-); Serine protease NS3 (EC 3.4.21.98) (EC 3.6.1.15) (EC 3.6.4.13) (Hepacivirin) (NS3P) (p70); Non-structural protein 4A (NS4A) (p8); Non-structural protein 4B (NS4B) (p27); Non-structural protein 5A (NS5A) (p56); RNA-directed RNA polymerase (EC 2.7.7.48) (NS5B) (p68)]
[] Genome polyprotein [Cleaved into: Core protein p21 (Capsid protein C) (p21); Core protein p19; Envelope glycoprotein E1 (gp32) (gp35); Envelope glycoprotein E2 (NS1) (gp68) (gp70); p7; Protease NS2-3 (p23) (EC 3.4.22.-); Serine protease NS3 (EC 3.4.21.98) (EC 3.6.1.15) (EC 3.6.4.13) (Hepacivirin) (NS3P) (p70); Non-structural protein 4A (NS4A) (p8); Non-structural protein 4B (NS4B) (p27); Non-structural protein 5A (NS5A) (p56); RNA-directed RNA polymerase (EC 2.7.7.48) (NS5B) (p68)]
[Mical1 Mical Nical] [F-actin]-monooxygenase MICAL1 (EC 1.14.13.225) (Molecule interacting with CasL protein 1) (MICAL-1) (mMical1) (NEDD9-interacting protein with calponin homology and LIM domains)
[rep 1a-1b] Replicase polyprotein 1ab (ORF1ab polyprotein) [Cleaved into: Nsp1 (EC 3.4.22.-); Nsp1-alpha papain-like cysteine proteinase (EC 3.4.22.-) (PCP1-alpha); Nsp1-beta papain-like cysteine proteinase (EC 3.4.22.-) (PCP1-beta); Nsp2 cysteine proteinase (EC 3.4.19.12) (EC 3.4.22.-) (CP2) (CP); Non-structural protein 3 (Nsp3); Serine protease nsp4 (3CLSP) (EC 3.4.21.-) (3C-like serine proteinase) (Nsp4); Non-structural protein 5-6-7 (Nsp5-6-7); Non-structural protein 5 (Nsp5); Non-structural protein 6 (Nsp6); Non-structural protein 7-alpha (Nsp7-alpha); Non-structural protein 7-beta (Nsp7-beta); Non-structural protein 8 (Nsp8); RNA-directed RNA polymerase (Pol) (RdRp) (EC 2.7.7.48) (Nsp9); Helicase nsp10 (Hel) (EC 3.6.4.12) (EC 3.6.4.13) (Nsp10); Non-structural protein 11 (Nsp11); Non-structural protein 12 (Nsp12)]
[Apex2 Ape2] DNA-(apurinic or apyrimidinic site) lyase 2 (EC 3.1.-.-) (EC 4.2.99.18) (APEX nuclease 2) (Apurinic-apyrimidinic endonuclease 2) (AP endonuclease 2)
[hchA A8C65_13880 A9R57_25255 AKG99_20940 AMK83_16550 B7C53_22525 B9M99_11580 B9T59_01945 BJJ90_15205 BMT49_12710 BMT53_00170 BUE81_10670 BW690_17225 BZL69_29425 C2U48_24800 C5715_19445 C5N07_21380 C6669_19295 C7B06_02290 C7B07_03930 CDL37_00765 CG691_19145 CG705_13560 CG706_14580 CIJ94_05515 COD46_23180 CRD98_26150 D3I61_11545 DL800_09215 DNQ41_14245 DQE83_22775 DTL43_21780 DTL84_23375 DTM25_06080 EC95NR1_00961 ERS085379_01273 ERS085386_05041 HMPREF3040_01583 HW43_13705 NCTC10082_04431 NCTC10418_03071 NCTC10767_03558 NCTC11022_01867 NCTC11126_04427 NCTC11181_05650 NCTC12950_02263 NCTC13462_05714 NCTC8985_00529 NCTC9111_05933 NCTC9703_00277 PU06_24500 SAMEA3472055_03589 SAMEA3472056_01268 SAMEA3472070_00654 SAMEA3472080_04213 SAMEA3472090_03376 SAMEA3472110_00060 SAMEA3472112_00448 SAMEA3752372_00752 SAMEA3753106_00003 SAMEA3753391_00513 UN91_23615 WQ89_10695] Protein/nucleic acid deglycase HchA (EC 3.1.2.-) (EC 3.5.1.-) (EC 3.5.1.124) (Maillard deglycase)
[DCS1 YLR270W] m7GpppX diphosphatase (EC 3.6.1.59) (DCS-1) (Hint-related 7meGMP-directed hydrolase 1) (Protein Dcs1p) (Scavenger mRNA-decapping enzyme DcpS)
[gag-pol] Gag-Pol polyprotein (Pr160Gag-Pol) [Cleaved into: Matrix protein p17 (MA); Capsid protein p24 (CA); Spacer peptide 1 (SP1) (p2); Nucleocapsid protein p7 (NC); Transframe peptide (TF); p6-pol (p6*); Protease (EC 3.4.23.16) (PR) (Retropepsin); Reverse transcriptase/ribonuclease H (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.13) (Exoribonuclease H) (EC 3.1.13.2) (p66 RT); p51 RT; p15; Integrase (IN) (EC 2.7.7.-) (EC 3.1.-.-)]
[GRIN2B NMDAR2B] Glutamate receptor ionotropic, NMDA 2B (GluN2B) (Glutamate [NMDA] receptor subunit epsilon-2) (N-methyl D-aspartate receptor subtype 2B) (NMDAR2B) (NR2B) (N-methyl-D-aspartate receptor subunit 3) (NR3) (hNR3)
[APEX1 APE APE1 APEX APX HAP1 REF1] DNA-(apurinic or apyrimidinic site) lyase (EC 3.1.-.-) (EC 4.2.99.18) (APEX nuclease) (APEN) (Apurinic-apyrimidinic endonuclease 1) (AP endonuclease 1) (APE-1) (REF-1) (Redox factor-1) [Cleaved into: DNA-(apurinic or apyrimidinic site) lyase, mitochondrial]
[Mapk8ip3 Jip3 Jsap1 Syd2] C-Jun-amino-terminal kinase-interacting protein 3 (JIP-3) (JNK-interacting protein 3) (JNK MAP kinase scaffold protein 3) (JNK/SAPK-associated protein 1) (JSAP1) (Mitogen-activated protein kinase 8-interacting protein 3) (Sunday driver 2)
[] Genome polyprotein [Cleaved into: Core protein p21 (Capsid protein C) (p21); Core protein p19; Envelope glycoprotein E1 (gp32) (gp35); Envelope glycoprotein E2 (NS1) (gp68) (gp70); p7; Protease NS2-3 (p23) (EC 3.4.22.-); Serine protease NS3 (EC 3.4.21.98) (EC 3.6.1.15) (EC 3.6.4.13) (Hepacivirin) (NS3P) (p70); Non-structural protein 4A (NS4A) (p8); Non-structural protein 4B (NS4B) (p27); Non-structural protein 5A (NS5A) (p56); RNA-directed RNA polymerase (EC 2.7.7.48) (NS5B) (p68)]
[] Genome polyprotein [Cleaved into: Core protein p21 (Capsid protein C) (p21); Core protein p19; Envelope glycoprotein E1 (gp32) (gp35); Envelope glycoprotein E2 (NS1) (gp68) (gp70); p7; Protease NS2-3 (p23) (EC 3.4.22.-); Serine protease NS3 (EC 3.4.21.98) (EC 3.6.1.15) (EC 3.6.4.13) (Hepacivirin) (NS3P) (p70); Non-structural protein 4A (NS4A) (p8); Non-structural protein 4B (NS4B) (p27); Non-structural protein 5A (NS5A) (p56); RNA-directed RNA polymerase (EC 2.7.7.48) (NS5B) (p68)]
[APEX1 APE APEX BAP1 REF1] DNA-(apurinic or apyrimidinic site) lyase (EC 3.1.-.-) (EC 4.2.99.18) (APEX nuclease) (APEN) (Apurinic-apyrimidinic endonuclease 1) (AP endonuclease 1) (REF-1) (Redox factor-1) [Cleaved into: DNA-(apurinic or apyrimidinic site) lyase, mitochondrial]

Bibliography :
?>