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Developmental protein eyes absent (EC 3.1.3.48) (Protein Clift)

 EYA_DROME               Reviewed;         766 AA.
Q05201; Q961V4; Q9VMC1;
01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
01-JUN-1994, sequence version 1.
13-FEB-2019, entry version 168.
RecName: Full=Developmental protein eyes absent;
EC=3.1.3.48 {ECO:0000269|PubMed:14628052};
AltName: Full=Protein Clift;
Name=eya; Synonyms=cli; ORFNames=CG9554;
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, AND
SUBCELLULAR LOCATION.
TISSUE=Head;
PubMed=8431945; DOI=10.1016/0092-8674(93)90115-7;
Bonini N.M., Leiserson W.M., Benzer S.;
"The eyes absent gene: genetic control of cell survival and
differentiation in the developing Drosophila eye.";
Cell 72:379-395(1993).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[3]
GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
STRAIN=Berkeley;
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
STRAIN=Berkeley; TISSUE=Head;
PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M.,
George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H.,
Rubin G.M., Celniker S.E.;
"A Drosophila full-length cDNA resource.";
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
[5]
INTERACTION WITH SO.
PubMed=9428512; DOI=10.1016/S0092-8674(00)80480-8;
Pignoni F., Hu B., Zavitz K.H., Xiao J., Garrity P.A., Zipursky S.L.;
"The eye-specification proteins So and Eya form a complex and regulate
multiple steps in Drosophila eye development.";
Cell 91:881-891(1997).
[6]
INTERACTION WITH DAC.
PubMed=9428513; DOI=10.1016/S0092-8674(00)80481-X;
Chen R., Amoui M., Zhang Z., Mardon G.;
"Dachshund and eyes absent proteins form a complex and function
synergistically to induce ectopic eye development in Drosophila.";
Cell 91:893-903(1997).
[7]
FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF ASP-499.
PubMed=14628052; DOI=10.1038/nature02093;
Rayapureddi J.P., Kattamuri C., Steinmetz B.D., Frankfort B.J.,
Ostrin E.J., Mardon G., Hegde R.S.;
"Eyes absent represents a class of protein tyrosine phosphatases.";
Nature 426:295-298(2003).
[8]
3D-STRUCTURE MODELING OF 493-766, FUNCTION, AND MUTAGENESIS OF
ASP-499; SER-676; LYS-705; ASP-730 AND GLU-734.
PubMed=14628053; DOI=10.1038/nature02097;
Tootle T.L., Silver S.J., Davies E.L., Newman V., Latek R.R.,
Mills I.A., Selengut J.D., Parlikar B.E., Rebay I.;
"The transcription factor Eyes absent is a protein tyrosine
phosphatase.";
Nature 426:299-302(2003).
-!- FUNCTION: Tyrosine phosphatase thought to play a role in
transcription regulation during organogenesis through its
intrinsic protein phosphatase activity (PubMed:14628052,
PubMed:14628053). The phosphatase activity was shown in vitro.
Appears to function together with So and Dac in eye development
(PubMed:9428512, PubMed:9428513). Required for the survival of eye
progenitor cells at a critical stage in morphogenesis
(PubMed:8431945). {ECO:0000269|PubMed:14628052,
ECO:0000269|PubMed:14628053, ECO:0000269|PubMed:8431945,
ECO:0000269|PubMed:9428512, ECO:0000269|PubMed:9428513}.
-!- CATALYTIC ACTIVITY:
Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein]
+ phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136,
Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474,
ChEBI:CHEBI:46858, ChEBI:CHEBI:82620; EC=3.1.3.48;
Evidence={ECO:0000269|PubMed:14628052};
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000250|UniProtKB:O00167};
Note=Binds 1 Mg(2+) ion per subunit.
{ECO:0000250|UniProtKB:O00167};
-!- SUBUNIT: Interacts with Dac and So. {ECO:0000269|PubMed:9428512,
ECO:0000269|PubMed:9428513}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:8431945}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=I, A;
IsoId=Q05201-1; Sequence=Displayed;
Name=2; Synonyms=II, B;
IsoId=Q05201-2; Sequence=VSP_001500;
-!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily. EYA
family. {ECO:0000305}.
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EMBL; L08501; AAA28723.1; -; mRNA.
EMBL; L08502; AAA28310.1; -; mRNA.
EMBL; AE014134; AAF52400.1; -; Genomic_DNA.
EMBL; AE014134; AAN10587.1; -; Genomic_DNA.
EMBL; AY047539; AAK77271.1; -; mRNA.
PIR; A45174; A45174.
PIR; B45174; B45174.
RefSeq; NP_523492.1; NM_078768.4. [Q05201-2]
RefSeq; NP_723188.1; NM_164693.2. [Q05201-1]
UniGene; Dm.5293; -.
ProteinModelPortal; Q05201; -.
SMR; Q05201; -.
BioGrid; 60071; 35.
DIP; DIP-19253N; -.
IntAct; Q05201; 2.
STRING; 7227.FBpp0078964; -.
PaxDb; Q05201; -.
PRIDE; Q05201; -.
EnsemblMetazoa; FBtr0079334; FBpp0078963; FBgn0000320. [Q05201-2]
EnsemblMetazoa; FBtr0079335; FBpp0078964; FBgn0000320. [Q05201-1]
GeneID; 33916; -.
KEGG; dme:Dmel_CG9554; -.
CTD; 33916; -.
FlyBase; FBgn0000320; eya.
eggNOG; KOG3107; Eukaryota.
eggNOG; ENOG410XT12; LUCA.
GeneTree; ENSGT00940000156367; -.
InParanoid; Q05201; -.
KO; K15616; -.
PhylomeDB; Q05201; -.
Reactome; R-DME-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
ChiTaRS; eya; fly.
GenomeRNAi; 33916; -.
PRO; PR:Q05201; -.
Proteomes; UP000000803; Chromosome 2L.
Bgee; FBgn0000320; Expressed in 54 organ(s), highest expression level in eye disc (Drosophila).
ExpressionAtlas; Q05201; baseline and differential.
Genevisible; Q05201; DM.
GO; GO:0005737; C:cytoplasm; HDA:FlyBase.
GO; GO:0005829; C:cytosol; IDA:FlyBase.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004721; F:phosphoprotein phosphatase activity; IMP:FlyBase.
GO; GO:0004725; F:protein tyrosine phosphatase activity; IDA:FlyBase.
GO; GO:0030946; F:protein tyrosine phosphatase activity, metal-dependent; IDA:FlyBase.
GO; GO:0003713; F:transcription coactivator activity; IMP:FlyBase.
GO; GO:0008134; F:transcription factor binding; IPI:FlyBase.
GO; GO:0048856; P:anatomical structure development; IBA:GO_Central.
GO; GO:0007411; P:axon guidance; IGI:FlyBase.
GO; GO:0001746; P:Bolwig's organ morphogenesis; IMP:FlyBase.
GO; GO:0042675; P:compound eye cone cell differentiation; IMP:FlyBase.
GO; GO:0048749; P:compound eye development; IMP:FlyBase.
GO; GO:0042051; P:compound eye photoreceptor development; IMP:FlyBase.
GO; GO:0007455; P:eye-antennal disc morphogenesis; IMP:UniProtKB.
GO; GO:0008406; P:gonad development; IMP:FlyBase.
GO; GO:0016576; P:histone dephosphorylation; IBA:GO_Central.
GO; GO:0045087; P:innate immune response; IGI:FlyBase.
GO; GO:0007526; P:larval somatic muscle development; IMP:FlyBase.
GO; GO:0008584; P:male gonad development; IMP:FlyBase.
GO; GO:0007498; P:mesoderm development; IMP:FlyBase.
GO; GO:0009996; P:negative regulation of cell fate specification; IMP:FlyBase.
GO; GO:2001240; P:negative regulation of extrinsic apoptotic signaling pathway in absence of ligand; IBA:GO_Central.
GO; GO:0001744; P:optic lobe placode formation; IMP:FlyBase.
GO; GO:0030707; P:ovarian follicle cell development; IMP:FlyBase.
GO; GO:0072499; P:photoreceptor cell axon guidance; IMP:FlyBase.
GO; GO:0070285; P:pigment cell development; IMP:FlyBase.
GO; GO:0007280; P:pole cell migration; TAS:FlyBase.
GO; GO:0045739; P:positive regulation of DNA repair; IBA:GO_Central.
GO; GO:0010628; P:positive regulation of gene expression; IMP:FlyBase.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:FlyBase.
GO; GO:0006470; P:protein dephosphorylation; IDA:FlyBase.
GO; GO:0009416; P:response to light stimulus; IMP:FlyBase.
GO; GO:0007435; P:salivary gland morphogenesis; IMP:FlyBase.
GO; GO:0007283; P:spermatogenesis; IMP:FlyBase.
GO; GO:0006351; P:transcription, DNA-templated; TAS:FlyBase.
GO; GO:0007419; P:ventral cord development; IGI:FlyBase.
CDD; cd02601; HAD_Eya; 1.
Gene3D; 3.40.50.12350; -; 1.
InterPro; IPR006545; EYA_dom.
InterPro; IPR038102; EYA_dom_sf.
InterPro; IPR028472; EYA_fam.
PANTHER; PTHR10190; PTHR10190; 1.
TIGRFAMs; TIGR01658; EYA-cons_domain; 1.
1: Evidence at protein level;
Activator; Alternative splicing; Complete proteome;
Developmental protein; Hydrolase; Magnesium; Metal-binding; Nucleus;
Protein phosphatase; Reference proteome; Transcription;
Transcription regulation.
CHAIN 1 766 Developmental protein eyes absent.
/FTId=PRO_0000218655.
COMPBIAS 46 57 Poly-Gln.
COMPBIAS 60 68 Poly-Gln.
COMPBIAS 92 108 Poly-Gly.
COMPBIAS 253 260 Poly-Ala.
COMPBIAS 268 271 Poly-Tyr.
COMPBIAS 305 311 Poly-Ala.
COMPBIAS 428 434 Poly-Ala.
ACT_SITE 499 499 Nucleophile.
{ECO:0000250|UniProtKB:O00167}.
ACT_SITE 501 501 Proton donor.
{ECO:0000250|UniProtKB:O00167}.
METAL 499 499 Magnesium.
{ECO:0000250|UniProtKB:O00167}.
METAL 501 501 Magnesium; via carbonyl oxygen.
{ECO:0000250|UniProtKB:O00167}.
METAL 730 730 Magnesium.
{ECO:0000250|UniProtKB:O00167}.
VAR_SEQ 1 23 MVTLMPYNYAAPRCGLIDKMIEP -> MLYNVPCYQNFSTL
DYY (in isoform 2).
{ECO:0000303|PubMed:12537569,
ECO:0000303|PubMed:8431945}.
/FTId=VSP_001500.
MUTAGEN 499 499 D->N: Highly reduced ectopic eye
induction and diminishes degree of
ommatidial restoration in eyeless
phenotype rescue assay.
{ECO:0000269|PubMed:14628052,
ECO:0000269|PubMed:14628053}.
MUTAGEN 676 676 S->A: Highly reduced ectopic eye
induction and diminishes degree of
ommatidial restoration in eyeless
phenotype rescue assay.
{ECO:0000269|PubMed:14628053}.
MUTAGEN 705 705 K->Q: Highly reduced ectopic eye
induction and diminishes degree of
ommatidial restoration in eyeless
phenotype rescue assay.
{ECO:0000269|PubMed:14628053}.
MUTAGEN 730 730 D->N: Highly reduced ectopic eye
induction. {ECO:0000269|PubMed:14628053}.
MUTAGEN 734 734 E->Q: Highly reduced ectopic eye
induction. {ECO:0000269|PubMed:14628053}.
SEQUENCE 766 AA; 80657 MW; 3581C26AB1811E74 CRC64;
MVTLMPYNYA APRCGLIDKM IEPKVKRPKT DHTDTHERNR LCNLSQQQQQ QQPQQQQTHQ
QQQQQQQQSH QQSHSSTVLA SNGPSSAGAG MGVGVGGGGG SGGGVGGGVG QCSPLGLPPQ
SQPLQPTIGS LASLSGHYSN GNANPNVNSS SCSLATASSF AQSAGSSFST YQQAGGTSGG
VSGEDGVVGG ATVMSHWTHD GTGSSAAVKS ESRSPGQVHA SLDNGSVAGS NLYGCSSASN
PLDGGAVAVN SSAVAAAAAA VYDGKHDYYY YNSMQQYTPP PFYSGYGTPY AAATAARQAK
MEPGAAAAAA AYLTPSYAAS GNNNSQLYSS PYAGYNNFGQ QDYGGYYNEQ YGNYYSPANY
SPYAVSSPSS SASHGHGFHV AASSNLSESP TDTHSTTPVH QTTHSPHSPL PISPSTGSGI
GPLGNVSAAA AAAALNSSGG SSVGTAGSGG VATSKTTPTG KTGRARGRRH QQPSPTRSTA
SDTGNSEAVK PPERVFVWDL DETLIIFHTL LSGSYANRYT KDHSSLMTIA FRMEEMVFNM
ADTHFFFNEI EECDQVHIDD VSSDDNGQDL SAYNFATDGF HTNTPPGAPP NLCLPTGVRG
GVDWMRKLAF RYRKIKDIYN SYRGNVGTLL GPGKREAWLQ IRSEIEVATD NWATLALKCL
SMISQRENCV NVLVTSTQLA PALAKVLLFG LGGIFNIENI YSAHKIGHET CYERIVTRFG
RKSTYVVIGD GNEEETAAKA MNFPFWRISA HSDIRALYTA LDMGFL


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Kits Elisa; taq POLYMERASE

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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 :
[EYA1] Eyes absent homolog 1 (EC 3.1.3.16) (EC 3.1.3.48)
[EYA2 EAB1] Eyes absent homolog 2 (EC 3.1.3.48)
[Eya1] Eyes absent homolog 1 (EC 3.1.3.16) (EC 3.1.3.48)
[eya-1 C49A1.4] Eyes absent homolog 1 (EC 3.1.3.48)
[EYA3] Eyes absent homolog 3 (EC 3.1.3.48)
[Eya2 Eab1] Eyes absent homolog 2 (EC 3.1.3.48)
[EYA4] Eyes absent homolog 4 (EC 3.1.3.48)
[EYA At2g35320] Eyes absent homolog (AtEYA) (EC 3.1.3.48)
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; 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); P2; 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)]
[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)
[] Genome polyprotein [Cleaved into: Capsid protein C (Core protein); Protein prM; Peptide pr; Small envelope protein M (Matrix protein); Envelope protein E; Non-structural protein 1 (NS1); Non-structural protein 2A (NS2A); Serine protease subunit NS2B (Flavivirin protease NS2B regulatory subunit) (Non-structural protein 2B); Serine protease NS3 (EC 3.4.21.91) (EC 3.6.1.15) (EC 3.6.4.13) (Flavivirin protease NS3 catalytic subunit) (Non-structural protein 3); Non-structural protein 4A (NS4A); Peptide 2k; Non-structural protein 4B (NS4B); RNA-directed RNA polymerase NS5 (EC 2.1.1.56) (EC 2.1.1.57) (EC 2.7.7.48) (Non-structural protein 5)]
[] 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: 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)]
[pol] Genome polyprotein [Cleaved into: Capsid protein C (Core protein); Protein prM; Peptide pr; Small envelope protein M (Matrix protein); Envelope protein E; Non-structural protein 1 (NS1); Non-structural protein 2A (NS2A); Serine protease subunit NS2B (Flavivirin protease NS2B regulatory subunit) (Non-structural protein 2B); Serine protease NS3 (EC 3.4.21.91) (EC 3.6.1.15) (EC 3.6.4.13) (Flavivirin protease NS3 catalytic subunit) (Non-structural protein 3); Non-structural protein 4A (NS4A); Peptide 2k; Non-structural protein 4B (NS4B); RNA-directed RNA polymerase NS5 (EC 2.1.1.56) (EC 2.1.1.57) (EC 2.7.7.48) (Non-structural protein 5)]
[pteN ptenA DDB_G0286557] Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN (EC 3.1.3.16) (EC 3.1.3.48) (EC 3.1.3.67) (Pten 3-phosphoinositide phosphatase alpha)
[] 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) (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: 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: 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) (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) (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) (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) (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) (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) (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) (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: Capsid protein C (Core protein); Protein prM; Peptide pr; Small envelope protein M (Matrix protein); Envelope protein E; Non-structural protein 1 (NS1); Non-structural protein 2A (NS2A); Serine protease subunit NS2B (Flavivirin protease NS2B regulatory subunit) (Non-structural protein 2B); Serine protease NS3 (EC 3.4.21.91) (EC 3.6.1.15) (EC 3.6.4.13) (Flavivirin protease NS3 catalytic subunit) (Non-structural protein 3); Non-structural protein 4A (NS4A); Peptide 2k; Non-structural protein 4B (NS4B); RNA-directed RNA polymerase NS5 (EC 2.1.1.56) (EC 2.1.1.57) (EC 2.7.7.48) (Non-structural protein 5)]
[] Genome polyprotein [Cleaved into: Capsid protein C (Core protein); Protein prM; Peptide pr; Small envelope protein M (Matrix protein); Envelope protein E; Non-structural protein 1 (NS1); Non-structural protein 2A (NS2A); Serine protease subunit NS2B (Flavivirin protease NS2B regulatory subunit) (Non-structural protein 2B); Serine protease NS3 (EC 3.4.21.91) (EC 3.6.1.15) (EC 3.6.4.13) (Flavivirin protease NS3 catalytic subunit) (Non-structural protein 3); Non-structural protein 4A (NS4A); Peptide 2k; Non-structural protein 4B (NS4B); RNA-directed RNA polymerase NS5 (EC 2.1.1.56) (EC 2.1.1.57) (EC 2.7.7.48) (Non-structural protein 5)]
[pol] Genome polyprotein [Cleaved into: Capsid protein C (Core protein); Protein prM; Peptide pr; Small envelope protein M (Matrix protein); Envelope protein E; Non-structural protein 1 (NS1); Non-structural protein 2A (NS2A); Serine protease subunit NS2B (Flavivirin protease NS2B regulatory subunit) (Non-structural protein 2B); Serine protease NS3 (EC 3.4.21.91) (EC 3.6.1.15) (EC 3.6.4.13) (Flavivirin protease NS3 catalytic subunit) (Non-structural protein 3); Non-structural protein 4A (NS4A); Peptide 2k; Non-structural protein 4B (NS4B); RNA-directed RNA polymerase NS5 (EC 2.1.1.56) (EC 2.1.1.57) (EC 2.7.7.48) (Non-structural protein 5)]
[] Genome polyprotein [Cleaved into: Capsid protein C (Capsid protein) (Core protein); Protein prM (Precursor membrane protein); Peptide pr (Peptide precursor); Small envelope protein M (Matrix protein); Envelope protein E; Non-structural protein 1 (NS1); Non-structural protein 2A (NS2A); Serine protease subunit NS2B (Flavivirin protease NS2B regulatory subunit) (Non-structural protein 2B); Serine protease NS3 (EC 3.4.21.91) (EC 3.6.1.15) (EC 3.6.4.13) (Flavivirin protease NS3 catalytic subunit) (Non-structural protein 3); Non-structural protein 4A (NS4A); Peptide 2k; Non-structural protein 4B (NS4B); RNA-directed RNA polymerase NS5 (EC 2.1.1.56) (EC 2.1.1.57) (EC 2.7.7.48) (Non-structural protein 5)]

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