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Protein Dicer (Cell cycle control protein dcr1) (RNA interference pathway protein dcr1) [Includes: Endoribonuclease dcr1 (EC 3.1.26.-); ATP-dependent helicase dcr1 (EC 3.6.4.-)]

 DCR1_SCHPO              Reviewed;        1374 AA.
Q09884; Q9UUN1;
01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
01-FEB-1996, sequence version 1.
02-JUN-2021, entry version 169.
RecName: Full=Protein Dicer;
AltName: Full=Cell cycle control protein dcr1;
AltName: Full=RNA interference pathway protein dcr1;
Includes:
RecName: Full=Endoribonuclease dcr1;
EC=3.1.26.-;
Includes:
RecName: Full=ATP-dependent helicase dcr1;
EC=3.6.4.-;
Name=dcr1; ORFNames=SPCC188.13c, SPCC584.10c;
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
Schizosaccharomyces.
NCBI_TaxID=284812;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=972 / ATCC 24843;
PubMed=11859360; DOI=10.1038/nature724;
Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
Nurse P.;
"The genome sequence of Schizosaccharomyces pombe.";
Nature 415:871-880(2002).
[2]
FUNCTION, AND RNA CLEAVAGE.
PubMed=12482946; DOI=10.1073/pnas.212633199;
Provost P., Silverstein R.A., Dishart D., Walfridsson J., Djupedal I.,
Kniola B., Wright A., Samuelsson B., Raadmark O., Ekwall K.;
"Dicer is required for chromosome segregation and gene silencing in fission
yeast cells.";
Proc. Natl. Acad. Sci. U.S.A. 99:16648-16653(2002).
[3]
FUNCTION.
PubMed=12193640; DOI=10.1126/science.1074973;
Volpe T.A., Kidner C., Hall I.M., Teng G., Grewal S.I.S., Martienssen R.A.;
"Regulation of heterochromatic silencing and histone H3 lysine-9
methylation by RNAi.";
Science 297:1833-1837(2002).
[4]
FUNCTION.
PubMed=12215653; DOI=10.1126/science.1076466;
Hall I.M., Shankaranarayana G.D., Noma K., Ayoub N., Cohen A.,
Grewal S.I.S.;
"Establishment and maintenance of a heterochromatin domain.";
Science 297:2232-2237(2002).
[5]
FUNCTION.
PubMed=12733640; DOI=10.1023/a:1022815931524;
Volpe T., Schramke V., Hamilton G.L., White S.A., Teng G.,
Martienssen R.A., Allshire R.C.;
"RNA interference is required for normal centromere function in fission
yeast.";
Chromosome Res. 11:137-146(2003).
[6]
FUNCTION.
PubMed=12509501; DOI=10.1073/pnas.232688099;
Hall I.M., Noma K., Grewal S.I.S.;
"RNA interference machinery regulates chromosome dynamics during mitosis
and meiosis in fission yeast.";
Proc. Natl. Acad. Sci. U.S.A. 100:193-198(2003).
[7]
FUNCTION.
PubMed=15371329; DOI=10.1101/gad.1218004;
Sigova A., Rhind N., Zamore P.D.;
"A single Argonaute protein mediates both transcriptional and
posttranscriptional silencing in Schizosaccharomyces pombe.";
Genes Dev. 18:2359-2367(2004).
[8]
FUNCTION.
PubMed=14699070; DOI=10.1091/mbc.e03-06-0433;
Carmichael J.B., Provost P., Ekwall K., Hobman T.C.;
"ago1 and dcr1, two core components of the RNA interference pathway,
functionally diverge from rdp1 in regulating cell cycle events in
Schizosaccharomyces pombe.";
Mol. Biol. Cell 15:1425-1435(2004).
[9]
FUNCTION, AND RNA CLEAVAGE.
PubMed=15907173; DOI=10.2174/0929866053765590;
Qian Z., Xuan B., Hong J., Hao Z., Wang L., Huang W.;
"Expression and purification of the carboxyl terminus domain of
Schizosaccharomyces pombe dicer in Escherichia coli.";
Protein Pept. Lett. 12:311-314(2005).
[10]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
PubMed=16823372; DOI=10.1038/nbt1222;
Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
Yoshida M.;
"ORFeome cloning and global analysis of protein localization in the fission
yeast Schizosaccharomyces pombe.";
Nat. Biotechnol. 24:841-847(2006).
[11]
STRUCTURE BY NMR OF 1259-1358 IN COMPLEX WITH ZINC, DOMAIN, SUBCELLULAR
LOCATION, FUNCTION, AND MUTAGENESIS OF LYS-1265; CYS-1275;
1287-VAL--THR-1302; ARG-1322; ARG-1334; ASN-1344; TYR-1348; SER-1349;
CYS-1350 AND CYS-1352.
PubMed=21847092; DOI=10.1038/emboj.2011.300;
Barraud P., Emmerth S., Shimada Y., Hotz H.R., Allain F.H., Buehler M.;
"An extended dsRBD with a novel zinc-binding motif mediates nuclear
retention of fission yeast Dicer.";
EMBO J. 30:4223-4235(2011).
-!- FUNCTION: Required for G1 arrest and mating in response to nitrogen
starvation. Ago1 regulation of cytokinesis and cell cycle checkpoints
occurs downstream of dcr1. Required, indirectly, for regulated
hyperphosphorylation of cdc2.
-!- FUNCTION: Has a role in the RNA interference (RNAi) pathway which is
important for heterochromatin formation, accurate chromosome
segregation, centromere cohesion and telomere function during mitosis
and meiosis. Digests double-stranded RNA (dsRNA) producing 21 to 23 bp
dsRNAs, so-called interfering RNAs (siRNA). Required for both post-
transcriptional and transcriptional gene silencing. Required for
silencing at the centromeres and for initiation of transcriptionally
silent heterochromatin at the mating type locus. Promotes histone H3
'Lys-10' methylation necessary for centromere function. Required for
recruitment of swi6 and cohesin to an ectopic dg repeat.
{ECO:0000269|PubMed:12193640, ECO:0000269|PubMed:12215653,
ECO:0000269|PubMed:12482946, ECO:0000269|PubMed:12509501,
ECO:0000269|PubMed:12733640, ECO:0000269|PubMed:21847092}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
{ECO:0000269|PubMed:16823372, ECO:0000269|PubMed:21847092}.
-!- DOMAIN: The C-terminal dsRNA-binding fold contains a bound zinc ion and
is important for normal nuclear retention and function in RNAi-
dependent heterochromatin assembly. It binds double-stranded DNA and
RNA (in vitro). {ECO:0000269|PubMed:21847092}.
-!- SIMILARITY: Belongs to the helicase family. Dicer subfamily.
{ECO:0000255|PROSITE-ProRule:PRU00657}.
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EMBL; CU329672; CAB41233.1; -; Genomic_DNA.
PIR; T39130; S62524.
RefSeq; NP_588215.2; NM_001023205.2.
PDB; 2L6M; NMR; -; A=1259-1358.
PDBsum; 2L6M; -.
SMR; Q09884; -.
BioGRID; 275506; 210.
STRING; 4896.SPCC188.13c.1; -.
SwissPalm; Q09884; -.
PaxDb; Q09884; -.
PRIDE; Q09884; -.
EnsemblFungi; SPCC188.13c.1; SPCC188.13c.1:pep; SPCC188.13c.
GeneID; 2538930; -.
KEGG; spo:SPCC188.13c; -.
PomBase; SPCC188.13c; dcr1.
VEuPathDB; FungiDB:SPCC188.13c; -.
eggNOG; KOG0701; Eukaryota.
HOGENOM; CLU_000907_4_3_1; -.
InParanoid; Q09884; -.
OMA; ECSKPEN; -.
PhylomeDB; Q09884; -.
PRO; PR:Q09884; -.
Proteomes; UP000002485; Chromosome III.
GO; GO:0000785; C:chromatin; IDA:PomBase.
GO; GO:0005737; C:cytoplasm; IDA:PomBase.
GO; GO:0005829; C:cytosol; IDA:PomBase.
GO; GO:0000791; C:euchromatin; IDA:PomBase.
GO; GO:0034399; C:nuclear periphery; IDA:PomBase.
GO; GO:0005634; C:nucleus; IDA:PomBase.
GO; GO:0005721; C:pericentric heterochromatin; IDA:PomBase.
GO; GO:0016442; C:RISC complex; IBA:GO_Central.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0003690; F:double-stranded DNA binding; IDA:PomBase.
GO; GO:0003725; F:double-stranded RNA binding; IDA:PomBase.
GO; GO:1990188; F:euchromatin binding; IDA:PomBase.
GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
GO; GO:0004525; F:ribonuclease III activity; IDA:PomBase.
GO; GO:0003723; F:RNA binding; IBA:GO_Central.
GO; GO:0008270; F:zinc ion binding; IDA:PomBase.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0034613; P:cellular protein localization; IMP:PomBase.
GO; GO:0007059; P:chromosome segregation; IEA:UniProtKB-KW.
GO; GO:0033562; P:co-transcriptional gene silencing by RNA interference machinery; IMP:PomBase.
GO; GO:0031048; P:heterochromatin assembly by small RNA; IMP:PomBase.
GO; GO:0010629; P:negative regulation of gene expression; IMP:CACAO.
GO; GO:0031508; P:pericentric heterochromatin assembly; IMP:PomBase.
GO; GO:1904595; P:positive regulation of termination of RNA polymerase II transcription; IMP:PomBase.
GO; GO:0051570; P:regulation of histone H3-K9 methylation; IMP:PomBase.
GO; GO:0090501; P:RNA phosphodiester bond hydrolysis; IBA:GO_Central.
GO; GO:0006396; P:RNA processing; IEA:InterPro.
GO; GO:0030466; P:silent mating-type cassette heterochromatin assembly; IMP:PomBase.
CDD; cd00593; RIBOc; 2.
Gene3D; 1.10.1520.10; -; 2.
Gene3D; 3.30.160.380; -; 1.
InterPro; IPR038248; Dicer_dimer_sf.
InterPro; IPR005034; Dicer_dimerisation_dom.
InterPro; IPR006935; Helicase/UvrB_N.
InterPro; IPR014001; Helicase_ATP-bd.
InterPro; IPR001650; Helicase_C.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR000999; RNase_III_dom.
InterPro; IPR036389; RNase_III_sf.
Pfam; PF00271; Helicase_C; 1.
Pfam; PF04851; ResIII; 1.
Pfam; PF00636; Ribonuclease_3; 2.
SMART; SM00487; DEXDc; 1.
SMART; SM00490; HELICc; 1.
SMART; SM00535; RIBOc; 2.
SUPFAM; SSF52540; SSF52540; 1.
SUPFAM; SSF69065; SSF69065; 2.
PROSITE; PS51327; DICER_DSRBF; 1.
PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
PROSITE; PS51194; HELICASE_CTER; 1.
PROSITE; PS00517; RNASE_3_1; 1.
PROSITE; PS50142; RNASE_3_2; 2.
1: Evidence at protein level;
3D-structure; ATP-binding; Cell cycle; Chromosome partition; Cytoplasm;
Endonuclease; Helicase; Hydrolase; Magnesium; Manganese; Metal-binding;
Nuclease; Nucleotide-binding; Nucleus; Reference proteome; Repeat;
RNA-mediated gene silencing; Zinc.
CHAIN 1..1374
/note="Protein Dicer"
/id="PRO_0000102194"
DOMAIN 19..206
/note="Helicase ATP-binding"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
DOMAIN 340..517
/note="Helicase C-terminal"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
DOMAIN 537..628
/note="Dicer dsRNA-binding fold"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00657"
DOMAIN 916..1038
/note="RNase III 1"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00177"
DOMAIN 1083..1233
/note="RNase III 2"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00177"
NP_BIND 32..39
/note="ATP"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
REGION 1263..1355
/note="C-terminal dsRNA-binding fold"
/evidence="ECO:0000269|PubMed:21847092"
MOTIF 145..148
/note="DECH box"
/evidence="ECO:0000305"
METAL 1123
/note="Magnesium or manganese"
/evidence="ECO:0000250"
METAL 1219
/note="Magnesium or manganese"
/evidence="ECO:0000250"
METAL 1222
/note="Magnesium or manganese"
/evidence="ECO:0000250"
METAL 1275
/note="Zinc"
/evidence="ECO:0000269|PubMed:21847092,
ECO:0007744|PDB:2L6M"
METAL 1312
/note="Zinc; via tele nitrogen"
/evidence="ECO:0000269|PubMed:21847092,
ECO:0007744|PDB:2L6M"
METAL 1350
/note="Zinc"
/evidence="ECO:0000269|PubMed:21847092,
ECO:0007744|PDB:2L6M"
METAL 1352
/note="Zinc"
/evidence="ECO:0000269|PubMed:21847092,
ECO:0007744|PDB:2L6M"
SITE 1215
/note="Important for activity"
/evidence="ECO:0000250"
MUTAGEN 1265
/note="K->A: Abolishes binding to dsRNA and dsDNA. No
effect on retention in the nucleus, nor on function in
RNAi-dependent heterochromatin assembly."
/evidence="ECO:0000269|PubMed:21847092"
MUTAGEN 1275
/note="C->S: Abolishes retention in the nucleus and
function in RNAi-dependent heterochromatin assembly; when
associated with S-1350 and S-1352."
/evidence="ECO:0000269|PubMed:21847092"
MUTAGEN 1287..1302
/note="Missing: Abolishes binding to dsRNA and dsDNA. No
effect on retention in the nucleus, nor on function in
RNAi-dependent heterochromatin assembly."
/evidence="ECO:0000269|PubMed:21847092"
MUTAGEN 1322
/note="R->A: Abolishes binding to dsRNA and dsDNA. No
effect on retention in the nucleus, nor on function in
RNAi-dependent heterochromatin assembly."
/evidence="ECO:0000269|PubMed:21847092"
MUTAGEN 1334
/note="R->A: No effect on retention in the nucleus."
/evidence="ECO:0000269|PubMed:21847092"
MUTAGEN 1344
/note="N->A: Decreases location in the nucleus. Abolishes
retention in the nucleus; when associated with A-1348 and
A-1349."
/evidence="ECO:0000269|PubMed:21847092"
MUTAGEN 1348
/note="Y->A: Decreases location in the nucleus. Abolishes
retention in the nucleus; when associated with A-1344 and
A-1349."
/evidence="ECO:0000269|PubMed:21847092"
MUTAGEN 1349
/note="S->A: Decreases location in the nucleus. Abolishes
retention in the nucleus; when associated with A-1344 and
A-1348."
/evidence="ECO:0000269|PubMed:21847092"
MUTAGEN 1350
/note="C->S: Abolishes retention in the nucleus and
function in RNAi-dependent heterochromatin assembly; when
associated with S-1275 and S-1352."
/evidence="ECO:0000269|PubMed:21847092"
MUTAGEN 1352
/note="C->S: Abolishes retention in the nucleus and
function in RNAi-dependent heterochromatin assembly; when
associated with S-1275 and S-1350."
/evidence="ECO:0000269|PubMed:21847092"
HELIX 1262..1270
/evidence="ECO:0007829|PDB:2L6M"
TURN 1271..1274
/evidence="ECO:0007829|PDB:2L6M"
STRAND 1278..1286
/evidence="ECO:0007829|PDB:2L6M"
STRAND 1294..1297
/evidence="ECO:0007829|PDB:2L6M"
STRAND 1303..1311
/evidence="ECO:0007829|PDB:2L6M"
STRAND 1314..1323
/evidence="ECO:0007829|PDB:2L6M"
HELIX 1324..1341
/evidence="ECO:0007829|PDB:2L6M"
HELIX 1344..1347
/evidence="ECO:0007829|PDB:2L6M"
TURN 1351..1353
/evidence="ECO:0007829|PDB:2L6M"
SEQUENCE 1374 AA; 158040 MW; 89AE9EF8DE7966C6 CRC64;
MDISSFLLPQ LLRKYQQDVY NIASKQNTLL VMRTGAGKTL LAVKLIKQKL EEQILIQESN
LEHKKISVFL VNKVPLVFQQ AEYIRSQLPA KVGMFYGELS IEMSEQLLTN IILKYNVIVI
TADLFYLFLA RGFLSINDLN LIIFDECHHA IGNDAYARIM NDFYHRAKAV LSKKHFTLPR
IFGMTASPFT GKKGNLYHRL YQWEQLFDSK AHVVSENELA DYFCLPEESY VMYSNKLVVP
PSDSIIKKCE ETLQGCKLIS RAVKTALAET IDMGLWFGEQ VWLYLVDFVE TKRLKKKALG
KQLSDDEELA IDRLKIFVED WKNNKYSDNG PRIPVFDSTD VTDKVFKLLE LLKATYRKSD
SVRTVIFVER KATAFTLSLF MKTLNLPNIR AHSFIGHGPS DQGEFSMTFR RQKDTLHKFK
TGKYNVLIAT AVAEEGIDVP SCNLVIRFNI CRTVTQYVQS RGRARAMASK FLIFLNTEEL
LIHERILHEE KNLKFALSEL SNSNIFDSLV CEERERVTDD IVYEVGETGA LLTGLYAVSL
LYNFCNTLSR DVYTRYYPTF TAQPCLSGWY CFEVELPKAC KVPAAQGSPA KSIRKAKQNA
AFIMCLDLIR MGLIDKHLKP LDFRRKIADL ETLEEDELKD EGYIETYERY VPKSWMKVPE
DITRCFVSLL YTDANEGDNH IFHPLVFVQA HSFPKIDSFI LNSTVGPRVK IVLETIEDSF
KIDSHLLELL KKSTRYLLQF GLSTSLEQQI PTPYWLAPLN LSCTDYRFLE NLIDVDTIQN
FFKLPEPVQN VTDLQSDTVL LVNPQSIYEQ YAFEGFVNSE FMIPAKKKDK APSALCKKLP
LRLNYSLWGN RAKSIPKSQQ VRSFYINDLY ILPVSRHLKN SALLIPSILY HIENLLVASS
FIEHFRLDCK IDTACQALTS AESQLNFDYD RLEFYGDCFL KLGASITVFL KFPDTQEYQL
HFNRKKIISN CNLYKVAIDC ELPKYALSTP LEIRHWCPYG FQKSTSDKCR YAVLQKLSVK
RIADMVEASI GACLLDSGLD SALKICKSLS VGLLDISNWD EWNNYFDLNT YADSLRNVQF
PYSSYIEETI GYSFKNKKLL HLAFIHPSMM SQQGIYENYQ QLEFLGDAVL DYIIVQYLYK
KYPNATSGEL TDYKSFYVCN KSLSYIGFVL NLHKYIQHES AAMCDAIFEY QELIEAFRET
ASENPWFWFE IDSPKFISDT LEAMICAIFL DSGFSLQSLQ FVLPLFLNSL GDATHTKAKG
DIEHKVYQLL KDQGCEDFGT KCVIEEVKSS HKTLLNTELH LTKYYGFSFF RHGNIVAYGK
SRKVANAKYI MKQRLLKLLE DKSNLLLYSC NCKFSKKKPS DEQIKGDGKV KSLT


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WP1685: Peptidoglycan biosynthesis

Related Genes :
[dcr1 SPCC188.13c SPCC584.10c] Protein Dicer (Cell cycle control protein dcr1) (RNA interference pathway protein dcr1) [Includes: Endoribonuclease dcr1 (EC 3.1.26.-); ATP-dependent helicase dcr1 (EC 3.6.4.-)]
[Dcr-1 CG4792] Endoribonuclease Dcr-1 (Protein dicer-1) (EC 3.1.26.-)
[dcr-1 eri-4 let-740 K12H4.8] Endoribonuclease dcr-1 (EC 3.1.26.-) [Cleaved into: Death-promoting deoxyribonuclease (tDCR-1) (EC 3.1.21.-)]
[pyrG OJ16_08175] CTP synthase (EC 6.3.4.2) (Cytidine 5'-triphosphate synthase) (Cytidine triphosphate synthetase) (CTP synthetase) (CTPS) (UTP--ammonia ligase)
[gpt OJ16_03400] Xanthine-guanine phosphoribosyltransferase (XGPRT) (EC 2.4.2.22) (Xanthine phosphoribosyltransferase)
[cca OJ16_08165] Multifunctional CCA protein [Includes: CCA-adding enzyme (EC 2.7.7.72) (CCA tRNA nucleotidyltransferase) (tRNA CCA-pyrophosphorylase) (tRNA adenylyl-/cytidylyl-transferase) (tRNA nucleotidyltransferase) (tRNA-NT); 2'-nucleotidase (EC 3.1.3.-); 2',3'-cyclic phosphodiesterase (EC 3.1.4.-); Phosphatase]
[nudC OJ16_08710] NAD-capped RNA hydrolase NudC (DeNADding enzyme NudC) (EC 3.6.1.-) (NADH pyrophosphatase) (EC 3.6.1.22)
[Rag1] V(D)J recombination-activating protein 1 (EC 2.3.2.27) (EC 3.1.-.-) (Fragment)
[vas vasa CG46283] ATP-dependent RNA helicase vasa (EC 3.6.4.13) (Antigen Mab46F11)
[rbsK OJ16_17530] Ribokinase (RK) (EC 2.7.1.15)
[leuB OJ16_08355] 3-isopropylmalate dehydrogenase (EC 1.1.1.85) (3-IPM-DH) (Beta-IPM dehydrogenase) (IMDH)
[COI] Cytochrome c oxidase subunit 1 (EC 7.1.1.9) (Fragment)
[dapB OJ16_07755] 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8)
[Rm62 Dmp68 p62 CG10279] ATP-dependent RNA helicase p62 (EC 3.6.4.13)
[iscS OJ16_03205] Cysteine desulfurase IscS (EC 2.8.1.7)
[piwi CG6122] Protein piwi (EC 3.1.26.-)
[rbsK OJ16_17515] Ribokinase (RK) (EC 2.7.1.15)
[murQ OJ16_01585] N-acetylmuramic acid 6-phosphate etherase (MurNAc-6-P etherase) (EC 4.2.1.126) (N-acetylmuramic acid 6-phosphate hydrolase) (N-acetylmuramic acid 6-phosphate lyase)
[ribB OJ16_03440] 3,4-dihydroxy-2-butanone 4-phosphate synthase (DHBP synthase) (EC 4.1.99.12)
[recB OJ16_02545] RecBCD enzyme subunit RecB (EC 3.1.11.5) (Exonuclease V subunit RecB) (ExoV subunit RecB) (Helicase/nuclease RecBCD subunit RecB)
[katG OJ16_19185] Catalase-peroxidase (CP) (EC 1.11.1.21) (Peroxidase/catalase)
[pdxA OJ16_11850] 4-hydroxythreonine-4-phosphate dehydrogenase (EC 1.1.1.262) (4-(phosphohydroxy)-L-threonine dehydrogenase)
[murQ OJ16_06800] N-acetylmuramic acid 6-phosphate etherase (MurNAc-6-P etherase) (EC 4.2.1.126) (N-acetylmuramic acid 6-phosphate hydrolase) (N-acetylmuramic acid 6-phosphate lyase)
[dusC OJ16_05005] tRNA-dihydrouridine(16) synthase (EC 1.3.1.-) (U16-specific dihydrouridine synthase) (U16-specific Dus) (tRNA-dihydrouridine synthase C)
[OJ16_15830] Bifunctional protein PutA [Includes: Proline dehydrogenase (EC 1.5.5.2) (Proline oxidase); Delta-1-pyrroline-5-carboxylate dehydrogenase (P5C dehydrogenase) (EC 1.2.1.88) (L-glutamate gamma-semialdehyde dehydrogenase)]
[ced-3 C48D1.2] Cell death protein 3 (EC 3.4.22.60) (Caspase ced-3) [Cleaved into: Cell death protein 3 subunit p17; Cell death protein 3 subunit p15; Cell death protein 3 subunit p13]
[pdxH OJ16_15855] Pyridoxine/pyridoxamine 5'-phosphate oxidase (EC 1.4.3.5) (PNP/PMP oxidase) (PNPOx) (Pyridoxal 5'-phosphate synthase)
[ileS OJ16_11260] Isoleucine--tRNA ligase (EC 6.1.1.5) (Isoleucyl-tRNA synthetase) (IleRS)
[pir-1 T23G7.5] RNA/RNP complex-1-interacting phosphatase homolog (EC 3.1.3.-) (Dual specificity protein phosphatase 11 homolog) (Phosphatase interacting with RNA/RNP complex-1)
[queF OJ16_12545] NADPH-dependent 7-cyano-7-deazaguanine reductase (EC 1.7.1.13) (7-cyano-7-carbaguanine reductase) (NADPH-dependent nitrile oxidoreductase) (PreQ(0) reductase)

Bibliography :
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