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La-related protein 1A (AtLARP1a)

 LRP1A_ARATH             Reviewed;         826 AA.
Q940X9; Q56WZ6;
16-APR-2014, integrated into UniProtKB/Swiss-Prot.
01-DEC-2001, sequence version 1.
16-JAN-2019, entry version 115.
RecName: Full=La-related protein 1A;
Short=AtLARP1a;
Name=LARP1A; OrderedLocusNames=At5g21160; ORFNames=T10F18.190;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130714; DOI=10.1038/35048507;
Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K.,
Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S.,
Nakazaki N., Naruo K., Okumura S., Shinpo S., Takeuchi C., Wada T.,
Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M.,
Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R.,
Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J.,
Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M.,
Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M.,
Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P.,
Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C.,
Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N.,
Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J.,
Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S.,
Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W.,
Ramsperger U., Wedler H., Balke K., Wedler E., Peters S.,
van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R.,
Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S.,
Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W.,
Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H.,
Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.;
"Sequence and analysis of chromosome 5 of the plant Arabidopsis
thaliana.";
Nature 408:823-826(2000).
[2]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 475-826.
STRAIN=cv. Columbia;
Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J.,
Hayashizaki Y., Shinozaki K.;
"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-378 AND SER-381, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Root;
PubMed=18433157; DOI=10.1021/pr8000173;
de la Fuente van Bentem S., Anrather D., Dohnal I., Roitinger E.,
Csaszar E., Joore J., Buijnink J., Carreri A., Forzani C.,
Lorkovic Z.J., Barta A., Lecourieux D., Verhounig A., Jonak C.,
Hirt H.;
"Site-specific phosphorylation profiling of Arabidopsis proteins by
mass spectrometry and peptide chip analysis.";
J. Proteome Res. 7:2458-2470(2008).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-465, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=cv. Columbia;
PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A.,
Andreasson E., Rathjen J.P., Peck S.C.;
"Phosphoproteomic analysis of nuclei-enriched fractions from
Arabidopsis thaliana.";
J. Proteomics 72:439-451(2009).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-378 AND SER-381, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19376835; DOI=10.1104/pp.109.138677;
Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
Grossmann J., Gruissem W., Baginsky S.;
"Large-scale Arabidopsis phosphoproteome profiling reveals novel
chloroplast kinase substrates and phosphorylation networks.";
Plant Physiol. 150:889-903(2009).
[8]
GENE FAMILY, AND NOMENCLATURE.
PubMed=19299548; DOI=10.1261/rna.1478709;
Bousquet-Antonelli C., Deragon J.M.;
"A comprehensive analysis of the La-motif protein superfamily.";
RNA 15:750-764(2009).
[9]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[10]
FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH XRN4, AND SUBCELLULAR
LOCATION.
PubMed=24332370; DOI=10.1016/j.celrep.2013.11.019;
Merret R., Descombin J., Juan Y.T., Favory J.J., Carpentier M.C.,
Chaparro C., Charng Y.Y., Deragon J.M., Bousquet-Antonelli C.;
"XRN4 and LARP1 are required for a heat-triggered mRNA decay pathway
involved in plant acclimation and survival during thermal stress.";
Cell Rep. 5:1279-1293(2013).
-!- FUNCTION: Required for acclimation and survival during thermal
stress. Heat-specific cofactor of XRN4 required for its targeting
to polysomes and subsequent rapid degradation of seedling
transcriptome during the early steps of the heat stress response.
{ECO:0000269|PubMed:24332370}.
-!- SUBUNIT: Interacts with XRN4 and facilitates its attachment to
polysomes upon heat stress. {ECO:0000269|PubMed:24332370}.
-!- SUBCELLULAR LOCATION: Cytoplasm, P-body
{ECO:0000269|PubMed:24332370}. Cytoplasm, cytosol
{ECO:0000269|PubMed:24332370}. Note=Translocates from cytosol to
P-bodies upon heat stress.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=1;
Comment=Additional isoforms seem to exist.;
Name=1;
IsoId=Q940X9-1; Sequence=Displayed;
-!- DISRUPTION PHENOTYPE: Reduced heat-induced fold reduction of mRNAs
and impaired attachment of XNR4 to polysomes.
{ECO:0000269|PubMed:24332370}.
-!- SIMILARITY: Belongs to the LARP family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AC140977; AAO73903.1; -; Genomic_DNA.
EMBL; CP002688; AED92941.1; -; Genomic_DNA.
EMBL; AY052365; AAK96556.1; -; mRNA.
EMBL; AY139801; AAM98107.1; -; mRNA.
EMBL; AK221883; BAD94211.1; -; mRNA.
RefSeq; NP_568409.1; NM_122123.3. [Q940X9-1]
UniGene; At.21994; -.
ProteinModelPortal; Q940X9; -.
SMR; Q940X9; -.
BioGrid; 17517; 3.
IntAct; Q940X9; 3.
STRING; 3702.AT5G21160.3; -.
iPTMnet; Q940X9; -.
PaxDb; Q940X9; -.
PRIDE; Q940X9; -.
EnsemblPlants; AT5G21160.1; AT5G21160.1; AT5G21160. [Q940X9-1]
GeneID; 832242; -.
Gramene; AT5G21160.1; AT5G21160.1; AT5G21160. [Q940X9-1]
KEGG; ath:AT5G21160; -.
Araport; AT5G21160; -.
eggNOG; KOG2590; Eukaryota.
eggNOG; COG5193; LUCA.
HOGENOM; HOG000082993; -.
KO; K18757; -.
OrthoDB; 258488at2759; -.
PhylomeDB; Q940X9; -.
PRO; PR:Q940X9; -.
Proteomes; UP000006548; Chromosome 5.
ExpressionAtlas; Q940X9; baseline and differential.
Genevisible; Q940X9; AT.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0000932; C:P-body; IDA:UniProtKB.
GO; GO:0005844; C:polysome; IDA:UniProtKB.
GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
GO; GO:0010286; P:heat acclimation; IMP:UniProtKB.
GO; GO:0006402; P:mRNA catabolic process; IMP:UniProtKB.
Gene3D; 1.10.10.10; -; 1.
InterPro; IPR006607; DM15.
InterPro; IPR006630; La_HTH.
InterPro; IPR036388; WH-like_DNA-bd_sf.
InterPro; IPR036390; WH_DNA-bd_sf.
Pfam; PF05383; La; 1.
SMART; SM00684; DM15; 3.
SMART; SM00715; LA; 1.
SUPFAM; SSF46785; SSF46785; 1.
PROSITE; PS50961; HTH_LA; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; Complete proteome; Cytoplasm;
Phosphoprotein; Reference proteome; RNA-binding.
CHAIN 1 826 La-related protein 1A.
/FTId=PRO_0000428666.
DOMAIN 272 361 HTH La-type RNA-binding.
{ECO:0000255|PROSITE-ProRule:PRU00332}.
COMPBIAS 58 273 Pro-rich.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000244|PubMed:22223895}.
MOD_RES 378 378 Phosphoserine.
{ECO:0000244|PubMed:18433157,
ECO:0000244|PubMed:19376835}.
MOD_RES 381 381 Phosphoserine.
{ECO:0000244|PubMed:18433157,
ECO:0000244|PubMed:19376835}.
MOD_RES 465 465 Phosphoserine.
{ECO:0000244|PubMed:19245862}.
SEQUENCE 826 AA; 91377 MW; 8D41922E5B609D9A CRC64;
MMAETEGSVA DDRELITREG GIGTKSPWKT TTSPVETIDA PVMGAHSWPA LADAAQQPRP
KNPPAPAPAP PSKNIPTSIP IPTPAVTGQA KSKGGGKANP GHKNPSGRHS KPGPRSNQNG
PPPPPYLVHA VPYHPPPFPP MVPLPHAAGP DFPYAPYPPY PVPVPPVTES GNEKQVQASP
LPPVLPAPQG DPGKPWPHQR GFDPRNMPQG AGPRNFGRPP FMGPAPGFLV GPGPGFPGPV
YYLPGPPPGA IRGPYPPRFA PYPVNQGPPI LSPEKLDLRD RVLKQVEYYF SDENLENDHY
LISLMDEEGW VPTKIIAGFK RVKAMTMDVD FIVYALGFSN SVEVQGDQIR KRDKWSDWIP
ASKKSTSAET IGDGDKDSPK SITSGDNFGN PSKGSSKPTV SDFSSEGAQS SRTNNYKSGN
LKSSADEKRN VEDLSNDFSN TFLLDEELDL EHRSPRKSGL SMSKSIEYED DDMAVDDQDI
QKLVIVTQNS GKSDGAGIGG TEAKNIPKEL ASTINDGLYY FEQELKKKRS GRRKNNSHLD
TKDGKIKSGE GLNTKLGENS AANDGGEEHG IITSRRKQNK GTHKHHTAHA RRFFSSNIRN
NGNISESPPS SSIGFFFGST PPDSHGPRLS KLSSSPQCTL SGSSPPVGSL PKSFPPFQHP
SHQLLEENGF KQEKYLKYRK RCLNERKKLG SGCSEEMNHL YRFWSYFLRD TFVLSMYDDF
QKFALEDAAG NYDYGLECLF RFYSYGLEKH FDEDLYKDFE KLSLDFYHKG NLYGLEKYWA
FHHYRGKEEP ITKHPELEKL LKEEFRSIDD FRAKETITNQ KENKSH


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Pathways :
WP2199: Seed Development
WP2272: Pathogenic Escherichia coli infection
WP731: Sterol regulatory element binding protein related
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
WP1497: Hedgehog-related genes
WP1502: Mitochondrial biogenesis
WP1531: Vitamin D synthesis
WP1559: TFs Regulate miRNAs related to cardiac hypertrophy
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
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Related Genes :
[] 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)]
[] 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); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[] 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); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[] 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); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[1a] Replicase polyprotein 1a (pp1a) (ORF1a polyprotein) [Cleaved into: Non-structural protein 1 (nsp1) (Leader protein); Non-structural protein 2 (nsp2) (p65 homolog); Non-structural protein 3 (nsp3) (EC 3.4.19.12) (EC 3.4.22.69) (PL2-PRO) (Papain-like proteinase) (PL-PRO) (SARS coronavirus main proteinase); Non-structural protein 4 (nsp4); 3C-like proteinase (3CL-PRO) (3CLp) (EC 3.4.22.-) (nsp5); Non-structural protein 6 (nsp6); Non-structural protein 7 (nsp7); Non-structural protein 8 (nsp8); Non-structural protein 9 (nsp9); Non-structural protein 10 (nsp10) (Growth factor-like peptide) (GFL); Non-structural protein 11 (nsp11)]
[al-2 B22I21.230 NCU00585] Bifunctional lycopene cyclase/phytoene synthase (Protein albino-2) [Includes: Lycopene beta-cyclase (EC 5.5.1.19) (Carotene cyclase) (Lycopene cyclase); Phytoene synthase (EC 2.5.1.32)]
[dim-5 29E8.110 NCU04402] Histone-lysine N-methyltransferase, H3 lysine-9 specific dim-5 (EC 2.1.1.43) (Histone H3-K9 methyltransferase dim-5) (H3-K9-HMTase dim-5) (HKMT)
[ARID1A BAF250 BAF250A C1orf4 OSA1 SMARCF1] AT-rich interactive domain-containing protein 1A (ARID domain-containing protein 1A) (B120) (BRG1-associated factor 250) (BAF250) (BRG1-associated factor 250a) (BAF250A) (Osa homolog 1) (hOSA1) (SWI-like protein) (SWI/SNF complex protein p270) (SWI/SNF-related, matrix-associated, actin-dependent regulator of chromatin subfamily F member 1) (hELD)
[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)]
[al-3 B8P8.010 NCU01427] Geranylgeranyl pyrophosphate synthase (GGPP synthase) (GGPPSase) (EC 2.5.1.-) ((2E,6E)-farnesyl diphosphate synthase) (Albino-3 protein) (Dimethylallyltranstransferase) (EC 2.5.1.1) (Farnesyl diphosphate synthase) (Farnesyltranstransferase) (EC 2.5.1.29) (Geranylgeranyl diphosphate synthase) (Geranyltranstransferase) (EC 2.5.1.10)
[1a] Replicase polyprotein 1a (pp1a) (ORF1a polyprotein) [Cleaved into: Non-structural protein 1 (nsp1) (Leader protein); Non-structural protein 2 (nsp2) (p65 homolog); Non-structural protein 3 (nsp3) (EC 3.4.19.12) (EC 3.4.22.69) (PL2-PRO) (Papain-like proteinase) (PL-PRO); Non-structural protein 4 (nsp4); 3C-like proteinase (3CL-PRO) (3CLp) (EC 3.4.22.-) (nsp5); Non-structural protein 6 (nsp6); Non-structural protein 7 (nsp7); Non-structural protein 8 (nsp8); Non-structural protein 9 (nsp9); Non-structural protein 10 (nsp10) (Growth factor-like peptide) (GFL); Non-structural protein 11 (nsp11)]
[1a] Replicase polyprotein 1a (pp1a) (ORF1a polyprotein) [Cleaved into: Non-structural protein 1 (nsp1) (Leader protein); Non-structural protein 2 (nsp2) (p65 homolog); Non-structural protein 3 (nsp3) (EC 3.4.19.12) (EC 3.4.22.69) (PL2-PRO) (Papain-like proteinase) (PL-PRO); Non-structural protein 4 (nsp4); 3C-like proteinase (3CL-PRO) (3CLp) (EC 3.4.22.-) (nsp5); Non-structural protein 6 (nsp6); Non-structural protein 7 (nsp7); Non-structural protein 8 (nsp8); Non-structural protein 9 (nsp9); Non-structural protein 10 (nsp10) (Growth factor-like peptide) (GFL); Non-structural protein 11 (nsp11)]
[1a] Replicase polyprotein 1a (pp1a) (ORF1a polyprotein) [Cleaved into: Non-structural protein 1 (nsp1) (Leader protein); Non-structural protein 2 (nsp2) (p65 homolog); Non-structural protein 3 (nsp3) (EC 3.4.19.12) (EC 3.4.22.69) (PL2-PRO) (Papain-like proteinase) (PL-PRO); Non-structural protein 4 (nsp4); 3C-like proteinase (3CL-PRO) (3CLp) (EC 3.4.22.-) (nsp5); Non-structural protein 6 (nsp6); Non-structural protein 7 (nsp7); Non-structural protein 8 (nsp8); Non-structural protein 9 (nsp9); Non-structural protein 10 (nsp10) (Growth factor-like peptide) (GFL); Non-structural protein 11 (nsp11)]
[AP1S1 AP19 CLAPS1] AP-1 complex subunit sigma-1A (Adaptor protein complex AP-1 subunit sigma-1A) (Adaptor-related protein complex 1 subunit sigma-1A) (Clathrin assembly protein complex 1 sigma-1A small chain) (Clathrin coat assembly protein AP19) (Golgi adaptor HA1/AP1 adaptin sigma-1A subunit) (HA1 19 kDa subunit) (Sigma 1a subunit of AP-1 clathrin) (Sigma-adaptin 1A) (Sigma1A-adaptin)
[] 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); Viroporin 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)]
[cat-1 NCU08791] Catalase-1 (EC 1.11.1.6)
[Arid1a Baf250 Baf250a Osa1 Smarcf1] AT-rich interactive domain-containing protein 1A (ARID domain-containing protein 1A) (BRG1-associated factor 250) (BAF250) (BRG1-associated factor 250a) (BAF250A) (Osa homolog 1) (SWI-like protein) (SWI/SNF complex protein p270) (SWI/SNF-related, matrix-associated, actin-dependent regulator of chromatin subfamily F member 1)
[fkr-2 9G6.180 NCU04140] FK506-binding protein 1A (FKBP-1A) (EC 5.2.1.8) (FK506-resistance protein 2) (NcFKBP13) (Peptidyl-prolyl cis-trans isomerase fkr-2) (PPIase fkr-2)
[KIF1A ATSV C2orf20] Kinesin-like protein KIF1A (Axonal transporter of synaptic vesicles) (Microtubule-based motor KIF1A) (Unc-104- and KIF1A-related protein) (hUnc-104)
[Ap1s1 Ap19] AP-1 complex subunit sigma-1A (Adaptor protein complex AP-1 subunit sigma-1A) (Adaptor-related protein complex 1 subunit sigma-1A) (Clathrin assembly protein complex 1 sigma-1A small chain) (Clathrin coat assembly protein AP19) (Golgi adaptor HA1/AP1 adaptin sigma-1A subunit) (HA1 19 kDa subunit) (Sigma 1a subunit of AP-1 clathrin) (Sigma-adaptin 1A) (Sigma1A-adaptin)
[MAP1LC3B MAP1ALC3] Microtubule-associated proteins 1A/1B light chain 3B (Autophagy-related protein LC3 B) (Autophagy-related ubiquitin-like modifier LC3 B) (MAP1 light chain 3-like protein 2) (MAP1A/MAP1B light chain 3 B) (MAP1A/MAP1B LC3 B) (Microtubule-associated protein 1 light chain 3 beta)
[frq B13D24.170 NCU02265] Frequency clock protein
[Htr1a Gpcr18] 5-hydroxytryptamine receptor 1A (5-HT-1A) (5-HT1A) (Serotonin receptor 1A)
[SMC1A DXS423E KIAA0178 SB1.8 SMC1 SMC1L1] Structural maintenance of chromosomes protein 1A (SMC protein 1A) (SMC-1-alpha) (SMC-1A) (Sb1.8)
[1a] Replicase polyprotein 1a (pp1a) (ORF1a polyprotein) [Cleaved into: Non-structural protein 1 (nsp1) (p28); Non-structural protein 2 (nsp2) (p65); Non-structural protein 3 (nsp3) (EC 3.4.19.12) (EC 3.4.22.69) (PL1-PRO/PL2-PRO) (PL1/PL2) (Papain-like proteinases 1/2) (p210); Non-structural protein 4 (nsp4) (Peptide HD2) (p44); 3C-like proteinase (3CL-PRO) (3CLp) (EC 3.4.22.-) (M-PRO) (nsp5) (p27); Non-structural protein 6 (nsp6); Non-structural protein 7 (nsp7) (p10); Non-structural protein 8 (nsp8) (p22); Non-structural protein 9 (nsp9) (p12); Non-structural protein 10 (nsp10) (Growth factor-like peptide) (GFL) (p15); Non-structural protein 11 (nsp11)]
[Smc1a Sb1.8 Smc1 Smc1l1 Smcb] Structural maintenance of chromosomes protein 1A (SMC protein 1A) (SMC-1-alpha) (SMC-1A) (Chromosome segregation protein SmcB) (Sb1.8)
[Siah1a] E3 ubiquitin-protein ligase SIAH1A (EC 2.3.2.27) (RING-type E3 ubiquitin transferase SIAH1A) (Seven in absentia homolog 1a) (Siah-1a) (Siah1a) (mSiah-1a)
[SMC1A SMC1 SMC1L1] Structural maintenance of chromosomes protein 1A (SMC protein 1A) (SMC-1A)
[aro-1 aro-2 aro-4 aro-5 aro-9 B14H13.20 NCU016321] Pentafunctional AROM polypeptide [Includes: 3-dehydroquinate synthase (DHQS) (EC 4.2.3.4); 3-phosphoshikimate 1-carboxyvinyltransferase (EC 2.5.1.19) (5-enolpyruvylshikimate-3-phosphate synthase) (EPSP synthase) (EPSPS); Shikimate kinase (SK) (EC 2.7.1.71); 3-dehydroquinate dehydratase (3-dehydroquinase) (EC 4.2.1.10); Shikimate dehydrogenase (EC 1.1.1.25)]
[stk-1 bur1 B20D17.070 NCU01435] Serine/threonine-protein kinase bur1 (EC 2.7.11.22) (EC 2.7.11.23) (Serine-threonine kinase 1)

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