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Protein Gawky

 GAWKY_DROME             Reviewed;        1384 AA.
Q8SY33; Q8MSF0; Q9V4F1;
21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
01-JUN-2002, sequence version 1.
28-FEB-2018, entry version 149.
RecName: Full=Protein Gawky {ECO:0000312|FlyBase:FBgn0051992};
Name=gw; Synonyms=GW182 {ECO:0000303|PubMed:16177138};
ORFNames=CG31992;
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 [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).
[2]
GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
STRAIN=Berkeley {ECO:0000269|PubMed:12537572};
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).
[3] {ECO:0000312|EMBL:AAL68245.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
STRAIN=Berkeley {ECO:0000312|EMBL:AAL68245.1};
TISSUE=Embryo {ECO:0000269|PubMed:12537569}, and
Ovary {ECO:0000269|PubMed:12537569};
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).
[4] {ECO:0000305}
FUNCTION.
PubMed=16177138; DOI=10.1261/rna.2191905;
Rehwinkel J., Behm-Ansmant I., Gatfield D., Izaurralde E.;
"A crucial role for GW182 and the DCP1:DCP2 decapping complex in
miRNA-mediated gene silencing.";
RNA 11:1640-1647(2005).
[5] {ECO:0000305}
FUNCTION, INTERACTION WITH AGO1, AND SUBCELLULAR LOCATION.
PubMed=16815998; DOI=10.1101/gad.1424106;
Behm-Ansmant I., Rehwinkel J., Doerks T., Stark A., Bork P.,
Izaurralde E.;
"mRNA degradation by miRNAs and GW182 requires both CCR4:NOT
deadenylase and DCP1:DCP2 decapping complexes.";
Genes Dev. 20:1885-1898(2006).
[6] {ECO:0000305}
FUNCTION, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
PubMed=16880270; DOI=10.1083/jcb.200512103;
Schneider M.D., Najand N., Chaker S., Pare J.M., Haskins J.,
Hughes S.C., Hobman T.C., Locke J., Simmonds A.J.;
"Gawky is a component of cytoplasmic mRNA processing bodies required
for early Drosophila development.";
J. Cell Biol. 174:349-358(2006).
[7] {ECO:0000305}
FUNCTION, AND INTERACTION WITH AGO1.
PubMed=18345015; DOI=10.1038/nsmb.1405;
Eulalio A., Huntzinger E., Izaurralde E.;
"GW182 interaction with Argonaute is essential for miRNA-mediated
translational repression and mRNA decay.";
Nat. Struct. Mol. Biol. 15:346-353(2008).
[8] {ECO:0000305}
FUNCTION, AND INTERACTION WITH PABP.
PubMed=19797087; DOI=10.1128/MCB.01081-09;
Zekri L., Huntzinger E., Heimstadt S., Izaurralde E.;
"The silencing domain of GW182 interacts with PABPC1 to promote
translational repression and degradation of microRNA targets and is
required for target release.";
Mol. Cell. Biol. 29:6220-6231(2009).
[9] {ECO:0000305}
REGIONS SUFFICIENT FOR MIRNA-MEDIATED SILENCING.
PubMed=19304924; DOI=10.1261/rna.1364909;
Chekulaeva M., Filipowicz W., Parker R.;
"Multiple independent domains of dGW182 function in miRNA-mediated
repression in Drosophila.";
RNA 15:794-803(2009).
[10] {ECO:0000305}
REGIONS REQUIRED FOR INTERACTION WITH AGO1 AND MIRNA-MEDIATED
SILENCING, AND ROLE OF UBA DOMAIN.
PubMed=19383769; DOI=10.1261/rna.1605509;
Eulalio A., Helms S., Fritzsch C., Fauser M., Izaurralde E.;
"A C-terminal silencing domain in GW182 is essential for miRNA
function.";
RNA 15:1067-1077(2009).
[11] {ECO:0000305}
REGIONS REQUIRED FOR INTERACTION WITH AGO1 AND MIRNA-MEDIATED
SILENCING.
PubMed=20530530; DOI=10.1093/nar/gkq501;
Chekulaeva M., Parker R., Filipowicz W.;
"The GW/WG repeats of Drosophila GW182 function as effector motifs for
miRNA-mediated repression.";
Nucleic Acids Res. 38:6673-6683(2010).
[12] {ECO:0000305}
FUNCTION, AND INTERACTION WITH CCR4-NOT AND PAN COMPLEXES.
PubMed=21981923; DOI=10.1016/j.molcel.2011.09.007;
Braun J.E., Huntzinger E., Fauser M., Izaurralde E.;
"GW182 proteins directly recruit cytoplasmic deadenylase complexes to
miRNA targets.";
Mol. Cell 44:120-133(2011).
[13] {ECO:0000305, ECO:0000312|PDB:2WBR}
STRUCTURE BY NMR OF 1114-1198, AND ROLE OF RRM DOMAIN.
PubMed=19295135; DOI=10.1093/nar/gkp173;
Eulalio A., Tritschler F., Buttner R., Weichenrieder O.,
Izaurralde E., Truffault V.;
"The RRM domain in GW182 proteins contributes to miRNA-mediated gene
silencing.";
Nucleic Acids Res. 37:2974-2983(2009).
-!- FUNCTION: Required for gene silencing mediated by micro-RNAs
(miRNAs). Silences both polyadenylated and deadenylated mRNAs.
Required for miRNA-mediated translational repression and mRNA
decay. Not required for miRNA target recognition. Necessary to
initiate but not to maintain silencing. Promotes mRNA
deadenylation through the recruitment of the CCR4-NOT and PAN
complexes and promotes decapping by the DCP1-DCP2 complex.
Dissociates from silenced mRNAs after deadenylation. Required for
completion of nuclear divisions during early embryonic
development. {ECO:0000269|PubMed:16177138,
ECO:0000269|PubMed:16815998, ECO:0000269|PubMed:16880270,
ECO:0000269|PubMed:18345015, ECO:0000269|PubMed:19797087,
ECO:0000269|PubMed:21981923}.
-!- SUBUNIT: Interacts (via N-terminal region) with AGO1 (via Piwi
domain); the interaction is essential for localization of AGO1 in
P-bodies and for miRNA-mediated silencing. Interacts with
pAbp/PABPC1; this interaction interferes with the binding of pAbp
to eIF4G and is required for miRNA-mediated silencing. Interacts
with CCR4-NOT complex members Not1, Rga/NOT2, twin/CCR4, Pop2 and
NOT3/5 and with PAN complex members CG8232/PAN2 and CG11486/PAN3.
{ECO:0000269|PubMed:16815998, ECO:0000269|PubMed:18345015,
ECO:0000269|PubMed:19797087, ECO:0000269|PubMed:21981923}.
-!- INTERACTION:
Q32KD4:AGO1; NbExp=4; IntAct=EBI-160693, EBI-105513;
D3DMN9:CG11486-RC; NbExp=2; IntAct=EBI-160693, EBI-6512959;
A8DY81:Not1; NbExp=2; IntAct=EBI-160693, EBI-3428401;
P21187:pAbp; NbExp=11; IntAct=EBI-160693, EBI-103658;
A1Z7K9:PAN2; NbExp=2; IntAct=EBI-160693, EBI-193297;
-!- SUBCELLULAR LOCATION: Cytoplasm, P-body
{ECO:0000269|PubMed:16815998, ECO:0000269|PubMed:16880270}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=A; Synonyms=B, E, F;
IsoId=Q8SY33-1; Sequence=Displayed;
Name=I;
IsoId=Q8SY33-2; Sequence=VSP_047895;
Note=No experimental confirmation available.;
Name=J;
IsoId=Q8SY33-3; Sequence=VSP_047896;
Note=No experimental confirmation available.;
-!- DEVELOPMENTAL STAGE: Highest levels are found during early
embryonic development until approximately 18 hours and during
pupariation. {ECO:0000269|PubMed:16880270}.
-!- DOMAIN: The UBA domain is not required for correct subcellular
location, gene silencing or interaction with pAbp.
{ECO:0000269|PubMed:19383769}.
-!- DOMAIN: The RRM domain lacks RNA-binding properties and does not
bind RNA in vitro. It is not required for P-body localization or
for interaction with AGO1 or miRNAs but is required for silencing.
May play a role in protein-protein interactions.
{ECO:0000269|PubMed:19295135, ECO:0000303|PubMed:19295135}.
-!- SIMILARITY: Belongs to the GW182 family. {ECO:0000255}.
-!- SEQUENCE CAUTION:
Sequence=AAM50720.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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EMBL; AE014135; AAF59322.2; -; Genomic_DNA.
EMBL; AE014135; AAF59323.2; -; Genomic_DNA.
EMBL; AE014135; AAN06507.2; -; Genomic_DNA.
EMBL; AE014135; AAN06508.1; -; Genomic_DNA.
EMBL; AE014135; AAN06509.1; -; Genomic_DNA.
EMBL; AE014135; AAX52511.2; -; Genomic_DNA.
EMBL; AY075429; AAL68245.1; -; mRNA.
EMBL; AY118860; AAM50720.1; ALT_INIT; mRNA.
RefSeq; NP_001014691.2; NM_001014691.2. [Q8SY33-3]
RefSeq; NP_726596.1; NM_166780.2. [Q8SY33-1]
RefSeq; NP_726597.1; NM_166781.2. [Q8SY33-1]
RefSeq; NP_726599.2; NM_166783.2. [Q8SY33-2]
RefSeq; NP_726600.1; NM_166784.2. [Q8SY33-1]
RefSeq; NP_726601.1; NM_166785.2. [Q8SY33-1]
UniGene; Dm.1403; -.
PDB; 2WBR; NMR; -; A=1114-1198.
PDBsum; 2WBR; -.
ProteinModelPortal; Q8SY33; -.
SMR; Q8SY33; -.
BioGrid; 68639; 20.
DIP; DIP-35525N; -.
ELM; Q8SY33; -.
IntAct; Q8SY33; 12.
MINT; Q8SY33; -.
STRING; 7227.FBpp0088165; -.
PaxDb; Q8SY33; -.
PRIDE; Q8SY33; -.
EnsemblMetazoa; FBtr0089096; FBpp0088165; FBgn0051992. [Q8SY33-1]
EnsemblMetazoa; FBtr0089097; FBpp0088166; FBgn0051992. [Q8SY33-1]
EnsemblMetazoa; FBtr0089100; FBpp0088169; FBgn0051992. [Q8SY33-1]
EnsemblMetazoa; FBtr0089101; FBpp0088170; FBgn0051992. [Q8SY33-1]
EnsemblMetazoa; FBtr0310542; FBpp0302679; FBgn0051992. [Q8SY33-2]
EnsemblMetazoa; FBtr0310543; FBpp0302680; FBgn0051992. [Q8SY33-3]
GeneID; 43808; -.
KEGG; dme:Dmel_CG31992; -.
UCSC; CG31992-RA; d. melanogaster. [Q8SY33-1]
CTD; 43808; -.
FlyBase; FBgn0051992; gw.
eggNOG; ENOG410IFAU; Eukaryota.
eggNOG; ENOG41110AX; LUCA.
GeneTree; ENSGT00410000025966; -.
InParanoid; Q8SY33; -.
KO; K18412; -.
OMA; GPLQNFH; -.
OrthoDB; EOG091G0JQM; -.
PhylomeDB; Q8SY33; -.
Reactome; R-DME-426496; Post-transcriptional silencing by small RNAs.
Reactome; R-DME-5578749; Transcriptional regulation by small RNAs.
ChiTaRS; gw; fly.
EvolutionaryTrace; Q8SY33; -.
GenomeRNAi; 43808; -.
PRO; PR:Q8SY33; -.
Proteomes; UP000000803; Chromosome 4.
Bgee; FBgn0051992; -.
Genevisible; Q8SY33; DM.
GO; GO:0000932; C:P-body; IDA:FlyBase.
GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
GO; GO:0001700; P:embryonic development via the syncytial blastoderm; IDA:FlyBase.
GO; GO:0035195; P:gene silencing by miRNA; IMP:UniProtKB.
GO; GO:0045475; P:locomotor rhythm; IMP:FlyBase.
GO; GO:0035278; P:miRNA mediated inhibition of translation; IEA:InterPro.
GO; GO:0006402; P:mRNA catabolic process; IMP:FlyBase.
GO; GO:0032880; P:regulation of protein localization; IMP:UniProtKB.
Gene3D; 3.30.70.330; -; 1.
InterPro; IPR019486; Argonaute_hook_dom.
InterPro; IPR033503; GW182.
InterPro; IPR026805; GW182_M_dom.
InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
InterPro; IPR035979; RBD_domain_sf.
InterPro; IPR015940; UBA.
InterPro; IPR009060; UBA-like_sf.
PANTHER; PTHR13020:SF25; PTHR13020:SF25; 1.
Pfam; PF10427; Ago_hook; 1.
Pfam; PF12938; M_domain; 1.
Pfam; PF00627; UBA; 1.
SUPFAM; SSF46934; SSF46934; 1.
SUPFAM; SSF54928; SSF54928; 1.
PROSITE; PS50030; UBA; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome; Cytoplasm;
Developmental protein; Reference proteome; RNA-binding;
RNA-mediated gene silencing; Translation regulation.
CHAIN 1 1384 Protein Gawky.
/FTId=PRO_0000415948.
DOMAIN 547 588 UBA. {ECO:0000255|PROSITE-
ProRule:PRU00212}.
DOMAIN 1117 1189 RRM. {ECO:0000255}.
REGION 1 605 Sufficient for miRNA-mediated silencing.
{ECO:0000269|PubMed:19304924}.
REGION 1 205 Required for interaction with AGO1.
{ECO:0000269|PubMed:20530530}.
REGION 205 490 Minimal N-terminal region required for
miRNA-mediated silencing.
{ECO:0000269|PubMed:20530530}.
REGION 605 830 Sufficient for miRNA-mediated silencing.
{ECO:0000269|PubMed:19304924}.
REGION 862 1115 Not required for interaction with AGO1 or
miRNAs or for localization to P-bodies
but necessary for miRNA-mediated
silencing and for interaction with pAbp.
{ECO:0000269|PubMed:19383769,
ECO:0000269|PubMed:19797087,
ECO:0000269|PubMed:20530530}.
REGION 940 1215 Sufficient for miRNA-mediated silencing.
{ECO:0000269|PubMed:19304924}.
REGION 1200 1384 Not required for interaction with AGO1 or
miRNAs or for localization to P-bodies
but necessary for miRNA-mediated
silencing, dissociation from AGO1 and
miRNAs and interaction with pAbp.
{ECO:0000269|PubMed:19383769,
ECO:0000269|PubMed:19797087,
ECO:0000269|PubMed:20530530}.
COMPBIAS 81 281 Gly-rich. {ECO:0000255}.
COMPBIAS 527 530 Poly-Gln. {ECO:0000255}.
COMPBIAS 713 824 Gln-rich. {ECO:0000255}.
COMPBIAS 1204 1366 Ser-rich. {ECO:0000255}.
VAR_SEQ 969 971 Missing (in isoform I). {ECO:0000305}.
/FTId=VSP_047895.
VAR_SEQ 1035 1036 Missing (in isoform J). {ECO:0000305}.
/FTId=VSP_047896.
STRAND 1118 1122 {ECO:0000244|PDB:2WBR}.
HELIX 1131 1140 {ECO:0000244|PDB:2WBR}.
STRAND 1143 1149 {ECO:0000244|PDB:2WBR}.
TURN 1150 1153 {ECO:0000244|PDB:2WBR}.
STRAND 1154 1161 {ECO:0000244|PDB:2WBR}.
HELIX 1162 1172 {ECO:0000244|PDB:2WBR}.
STRAND 1175 1177 {ECO:0000244|PDB:2WBR}.
STRAND 1180 1185 {ECO:0000244|PDB:2WBR}.
HELIX 1189 1196 {ECO:0000244|PDB:2WBR}.
SEQUENCE 1384 AA; 142973 MW; 4E87DFE49050883E CRC64;
MREALFSQDG WGCQHVNQDT NWEVPSSPEP ANKDAPGPPM WKPSINNGTD LWESNLRNGG
QPAAQQVPKP SWGHTPSSNL GGTWGEDDDG ADSSSVWTGG AVSNAGSGAA VGVNQAGVNV
GPGGVVSSGG PQWGQGVVGV GLGSTGGNGS SNITGSSGVA TGSSGNSSNA GNGWGDPREI
RPLGVGGSMD IRNVEHRGGN GSGATSSDPR DIRMIDPRDP IRGDPRGISG RLNGTSEMWG
HHPQMSHNQL QGINKMVGQS VATASTSVGT SGSGIGPGGP GPSTVSGNIP TQWGPAQPVS
VGVSGPKDMS KQISGWEEPS PPPQRRSIPN YDDGTSLWGQ QTRVPAASGH WKDMTDSIGR
SSHLMRGQSQ TGGIGIAGVG NSNVPVGANP SNPISSVVGP QARIPSVGGV QHKPDGGAMW
VHSGNVGGRN NVAAVTTWGD DTHSVNVGAP SSGSVSSNNW VDDKSNSTLA QNSWSDPAPV
GVSWGNKQSK PPSNSASSGW STAAGVVDGV DLGSEWNTHG GIIGKSQQQQ KLAGLNVGMV
NVINAEIIKQ SKQYRILVEN GFKKEDVERA LVIANMNIEE AADMLRANSS LSMDGWRRHD
ESLGSYADHN SSTSSGGFAG RYPVNSGQPS MSFPHNNLMN NMGGTAVTGG NNNTNMTALQ
VQKYLNQGQH GVAVGPQAVG NSSAVSVGFG QNTSNAAVAG AASVNIAANT NNQPSGQQIR
MLGQQIQLAI HSGFISSQIL TQPLTQTTLN LLNQLLSNIK HLQAAQQSLT RGGNVNPMAV
NVAISKYKQQ IQNLQNQINA QQAVYVKQQN MQPTSQQQQP QQQQLPSVHL SNSGNDYLRG
HDAINNLQSN FSELNINKPS GYQGASNQQS RLNQWKLPVL DKEINSDSTE FSRAPGATKQ
NLTANTSNIN SLGLQNDSTW STGRSIGDGW PDPSSDNENK DWSVAQPTSA ATAYTDLVQE
FEPGKPWKGS QIKSIEDDPS ITPGSVARSP LSINSTPKDA DIFANTGKNS PTDLPPLSLS
SSTWSFNPNQ NYPSHSWSDN SQQCTATSEL WTSPLNKSSS RGPPPGLTAN SNKSANSNAS
TPTTITGGAN GWLQPRSGGV QTTNTNWTGG NTTWGSSWLL LKNLTAQIDG PTLRTLCMQH
GPLVSFHPYL NQGIALCKYT TREEANKAQM ALNNCVLANT TIFAESPSEN EVQSIMQHLP
QTPSSTSSSG TSGGNVGGVG TSANNANSGS AACLSGNNSG NGNGSASGAG SGNNGNSSCN
NSAAGGGSSS NNTITTVANS NLVGSSGSVS NSSGVTANSS TVSVVSCTAS GNSINGAGTA
NSSGSKSSAN NLASGQSSAS NLTNSTNSTW RQTSQNQALQ SQSRPSGREA DFDYISLVYS
IVDD


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EIAAB25665 AML1T1,CBFA2T1,CDR,Cyclin-D-related protein,Eight twenty one protein,ETO,Homo sapiens,Human,MTG8,Protein CBFA2T1,Protein ETO,Protein MTG8,RUNX1T1,Zinc finger MYND domain-containing protein 2,ZMYND2
EIAAB46018 C6orf55,Dopamine-responsive gene 1 protein,DRG-1,Homo sapiens,HSPC228,Human,LIP5,LYST-interacting protein 5,My012,SBP1,SKD1-binding protein 1,Vacuolar protein sorting-associated protein VTA1 homolog,V
18-003-43690 Guanine nucleotide-binding protein subunit beta-like protein 1 - G protein subunit beta-like protein 1; WD40 repeat-containing protein deleted in VCFS; Protein WDVCF; WD repeat-containing protein 14; 0.1 mg Protein A
EIAAB32247 ADP-ribosylation factor-like protein 6-interacting protein 5,Aip-5,ARL-6-interacting protein 5,ARL6IP5,Cytoskeleton-related vitamin A-responsive protein,Dermal papilla-derived protein 11,DERP11,Glutam
E1773h ELISA kit G-CSF-induced gene 1 protein,GIG1,GIG-1 protein,GMP-17,Granule membrane protein of 17 kDa,Homo sapiens,Human,Natural killer cell protein 7,NKG7,p15-TIA-1,Protein NKG7 96T
U1773h CLIA G-CSF-induced gene 1 protein,GIG1,GIG-1 protein,GMP-17,Granule membrane protein of 17 kDa,Homo sapiens,Human,Natural killer cell protein 7,NKG7,p15-TIA-1,Protein NKG7 96T
E1773h ELISA G-CSF-induced gene 1 protein,GIG1,GIG-1 protein,GMP-17,Granule membrane protein of 17 kDa,Homo sapiens,Human,Natural killer cell protein 7,NKG7,p15-TIA-1,Protein NKG7 96T
EIAAB31034 Androgen receptor-interacting protein 3,ARIP3,DAB2-interacting protein,DIP,E3 SUMO-protein ligase PIAS2,Homo sapiens,Human,Miz1,Msx-interacting zinc finger protein,PIAS2,PIAS-NY protein,PIASX,Protein
EIAAB29586 Mouse,Mus musculus,p53-induced gene 11 protein,Pig11,Tp53i11,Transformation related protein 53 inducible protein 11,Trp53i11,Tumor protein p53-inducible protein 11
EIAAB43486 Mouse,Mus musculus,Protein TAP1,Protein TRUSS,Rabex-5_Rin2-interacting protein,Short transient receptor potential channel 4-associated protein,TNF-receptor ubiquitous scaffolding_signaling protein,Trp
10-663-45493 Heat Shock Protein 22kD (HSP22) Human - HspB8; Alpha crystallin C chain; Small stress protein-like protein HSP22; E2-induced gene 1 protein; Protein kinase H11 N_A 0.002 mg
10-663-45493 Heat Shock Protein 22kD (HSP22) Human - HspB8; Alpha crystallin C chain; Small stress protein-like protein HSP22; E2-induced gene 1 protein; Protein kinase H11 N_A 0.01 mg
10-663-45493 Heat Shock Protein 22kD (HSP22) Human - HspB8; Alpha crystallin C chain; Small stress protein-like protein HSP22; E2-induced gene 1 protein; Protein kinase H11 N_A 0.1 mg
EIAAB43485 C20orf188,Homo sapiens,Human,Protein TAP1,Protein TRUSS,Short transient receptor potential channel 4-associated protein,TNF-receptor ubiquitous scaffolding_signaling protein,Trp4-associated protein,TR
EIAAB33912 E3 ubiquitin-protein ligase RBBP6,Mouse,Mus musculus,P2pr,p53-associated cellular protein of testis,Pact,Proliferation potential-related protein,Protein P2P-R,Rbbp6,Retinoblastoma-binding protein 6
EIAAB38162 Homo sapiens,Human,MAP,Merlin-associated protein,RabGAPLP,RABGAPLP,Rab-GTPase-activating protein-like protein,RUN and TBC1 domain-containing protein 3,RUTBC3,SGSM3,Small G protein signaling modulator
EIAAB29908 Cap1,Contraception-associated protein 1,Fertility protein SP22,Park7,Parkinson disease protein 7 homolog,Protein CAP1,Protein DJ-1,Rat,Rattus norvegicus
EIAAB31031 DDXBP1,DEAD_H box-binding protein 1,E3 SUMO-protein ligase PIAS1,GBP,Gu-binding protein,Homo sapiens,Human,PIAS1,Protein inhibitor of activated STAT protein 1,RNA helicase II-binding protein


 

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