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AF4/FMR2 family member 4 (Protein lilliputian) (Suppressor of Raf at 2A) (Suppressor of sina 2-1)

 AFF4_DROME              Reviewed;        1673 AA.
Q9VQI9; B7YZZ6; C9QPD1; Q95RP2; Q9BH66;
15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
01-OCT-2002, sequence version 2.
10-OCT-2018, entry version 132.
RecName: Full=AF4/FMR2 family member 4 {ECO:0000303|PubMed:11171403};
AltName: Full=Protein lilliputian {ECO:0000303|PubMed:11171403};
AltName: Full=Suppressor of Raf at 2A {ECO:0000303|PubMed:8770593};
AltName: Full=Suppressor of sina 2-1 {ECO:0000303|PubMed:9475739};
Name=lilli {ECO:0000312|EMBL:AAF51180.2,
ECO:0000312|FlyBase:FBgn0041111};
Synonyms=l(2)00632 {ECO:0000303|PubMed:8978055},
SS2-1 {ECO:0000303|PubMed:9475739},
Su(Raf)2A {ECO:0000303|PubMed:8770593}; ORFNames=CG8817;
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227;
[1] {ECO:0000305, ECO:0000312|EMBL:AAG53639.1}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, SUBCELLULAR
LOCATION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
PubMed=11171403;
Wittwer F., van der Straten A., Keleman K., Dickson B.J., Hafen E.;
"Lilliputian: an AF4/FMR2-related protein that controls cell identity
and cell growth.";
Development 128:791-800(2001).
[2] {ECO:0000305, ECO:0000312|EMBL:AAK18163.1}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, DEVELOPMENTAL STAGE,
AND DISRUPTION PHENOTYPE.
PubMed=11171404;
Tang A.H., Neufeld T.P., Rubin G.M., Muller H.A.;
"Transcriptional regulation of cytoskeletal functions and segmentation
by a novel maternal pair-rule gene, lilliputian.";
Development 128:801-813(2001).
[3] {ECO:0000312|EMBL:AAF51180.2}
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).
[4] {ECO:0000305, ECO:0000312|EMBL:AAF51180.2}
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).
[5] {ECO:0000305, ECO:0000312|EMBL:ACX54921.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM D).
STRAIN=Berkeley; TISSUE=Testis;
Carlson J.W., Booth B., Frise E., Park S., Wan K.H., Yu C.,
Celniker S.E.;
Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
[6] {ECO:0000305, ECO:0000312|EMBL:AAL28786.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1374-1673 (ISOFORMS A/D).
STRAIN=Berkeley {ECO:0000312|EMBL:AAL28786.1};
TISSUE=Embryo {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).
[7] {ECO:0000305}
FUNCTION.
PubMed=8770593;
Dickson B.J., van der Straten A., Dominguez M., Hafen E.;
"Mutations Modulating Raf signaling in Drosophila eye development.";
Genetics 142:163-171(1996).
[8] {ECO:0000305}
FUNCTION.
PubMed=8978055;
Perrimon N., Lanjuin A., Arnold C., Noll E.;
"Zygotic lethal mutations with maternal effect phenotypes in
Drosophila melanogaster. II. Loci on the second and third chromosomes
identified by P-element-induced mutations.";
Genetics 144:1681-1692(1996).
[9] {ECO:0000305}
FUNCTION.
PubMed=9475739;
Neufeld T.P., Tang A.H., Rubin G.M.;
"A genetic screen to identify components of the sina signaling pathway
in Drosophila eye development.";
Genetics 148:277-286(1998).
[10] {ECO:0000305}
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-420; SER-450; SER-452;
SER-821; SER-822; SER-871; SER-873; SER-1362 AND THR-1364, AND
IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Embryo {ECO:0000269|PubMed:18327897};
PubMed=18327897; DOI=10.1021/pr700696a;
Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
"Phosphoproteome analysis of Drosophila melanogaster embryos.";
J. Proteome Res. 7:1675-1682(2008).
[11]
IDENTIFICATION IN THE SEC COMPLEX, AND SUBCELLULAR LOCATION.
PubMed=22195968; DOI=10.1016/j.molcel.2011.12.008;
Smith E.R., Lin C., Garrett A.S., Thornton J., Mohaghegh N., Hu D.,
Jackson J., Saraf A., Swanson S.K., Seidel C., Florens L.,
Washburn M.P., Eissenberg J.C., Shilatifard A.;
"The little elongation complex regulates small nuclear RNA
transcription.";
Mol. Cell 44:954-965(2011).
-!- FUNCTION: Has a role in transcriptional regulation. Acts in
parallel with the Ras/MAPK and the PI3K/PKB pathways in the
control of cell identity and cellular growth. Essential for
regulation of the cytoskeleton and cell growth but not for cell
proliferation or growth rate. Required specifically for the
microtubule-based basal transport of lipid droplets. Plays a
partially redundant function downstream of Raf in cell fate
specification in the developing eye. Pair-rule protein that
regulates embryonic cellularization, gastrulation and
segmentation. {ECO:0000269|PubMed:11171403,
ECO:0000269|PubMed:11171404, ECO:0000269|PubMed:8770593,
ECO:0000269|PubMed:8978055, ECO:0000269|PubMed:9475739}.
-!- SUBUNIT: Component of the super elongation complex (SEC), at least
composed of Ell, Cdk9, cyclin-T (CycT), lilli and ear.
{ECO:0000269|PubMed:22195968}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11171403,
ECO:0000269|PubMed:22195968}. Note=Associates to transcriptionally
active chromatin.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=A {ECO:0000269|PubMed:10731132}; Synonyms=B
{ECO:0000269|PubMed:10731132}, C {ECO:0000269|PubMed:10731132}, G
{ECO:0000269|PubMed:10731132};
IsoId=Q9VQI9-1; Sequence=Displayed;
Name=D {ECO:0000269|PubMed:10731132}; Synonyms=E
{ECO:0000269|PubMed:10731132}, F {ECO:0000269|PubMed:10731132};
IsoId=Q9VQI9-2; Sequence=VSP_039294;
Note=No experimental confirmation available. {ECO:0000305};
-!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
{ECO:0000269|PubMed:11171403, ECO:0000269|PubMed:11171404}.
-!- DISRUPTION PHENOTYPE: Embryos lacking maternal lilli show specific
defects in the establishment of a functional cytoskeleton during
cellularization, and exhibit a pair-rule segmentation phenotype.
Adults lacking lilli exhibit reduction in cell and organ size and
partial suppression of the increased growth associated with loss
of PTEN function. {ECO:0000269|PubMed:11171403,
ECO:0000269|PubMed:11171404}.
-!- SIMILARITY: Belongs to the AF4 family. {ECO:0000255}.
-!- SEQUENCE CAUTION:
Sequence=AAL28786.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=ACX54921.1; Type=Frameshift; Positions=1210; Evidence={ECO:0000305};
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EMBL; AF293971; AAG53639.1; -; mRNA.
EMBL; AF289034; AAK18163.1; -; mRNA.
EMBL; AE014134; AAF51180.2; -; Genomic_DNA.
EMBL; AE014134; AAN10399.1; -; Genomic_DNA.
EMBL; AE014134; AAN10400.1; -; Genomic_DNA.
EMBL; AE014134; ACL82979.1; -; Genomic_DNA.
EMBL; AE014134; ACL82980.1; -; Genomic_DNA.
EMBL; AE014134; ACL82981.1; -; Genomic_DNA.
EMBL; AE014134; ACL82982.1; -; Genomic_DNA.
EMBL; BT100013; ACX54921.1; ALT_FRAME; mRNA.
EMBL; AY061238; AAL28786.1; ALT_INIT; mRNA.
RefSeq; NP_001137772.1; NM_001144300.2. [Q9VQI9-2]
RefSeq; NP_001137773.1; NM_001144301.1. [Q9VQI9-2]
RefSeq; NP_001137774.1; NM_001144302.2. [Q9VQI9-2]
RefSeq; NP_001137775.1; NM_001144303.1. [Q9VQI9-1]
RefSeq; NP_001259973.1; NM_001273044.1. [Q9VQI9-2]
RefSeq; NP_523464.1; NM_078740.3. [Q9VQI9-1]
RefSeq; NP_722863.1; NM_164516.2. [Q9VQI9-1]
RefSeq; NP_722864.1; NM_164517.1. [Q9VQI9-1]
UniGene; Dm.2778; -.
BioGrid; 59717; 35.
IntAct; Q9VQI9; 5.
STRING; 7227.FBpp0077318; -.
iPTMnet; Q9VQI9; -.
PaxDb; Q9VQI9; -.
PRIDE; Q9VQI9; -.
EnsemblMetazoa; FBtr0077632; FBpp0077317; FBgn0041111. [Q9VQI9-1]
EnsemblMetazoa; FBtr0077633; FBpp0077318; FBgn0041111. [Q9VQI9-1]
EnsemblMetazoa; FBtr0077634; FBpp0077319; FBgn0041111. [Q9VQI9-1]
EnsemblMetazoa; FBtr0290038; FBpp0288477; FBgn0041111. [Q9VQI9-2]
EnsemblMetazoa; FBtr0290039; FBpp0288478; FBgn0041111. [Q9VQI9-2]
EnsemblMetazoa; FBtr0290040; FBpp0288479; FBgn0041111. [Q9VQI9-2]
EnsemblMetazoa; FBtr0290041; FBpp0288480; FBgn0041111. [Q9VQI9-1]
EnsemblMetazoa; FBtr0332458; FBpp0304731; FBgn0041111. [Q9VQI9-2]
GeneID; 33496; -.
KEGG; dme:Dmel_CG8817; -.
UCSC; CG8817-RA; d. melanogaster. [Q9VQI9-1]
CTD; 33496; -.
FlyBase; FBgn0041111; lilli.
eggNOG; ENOG410IGJB; Eukaryota.
eggNOG; ENOG410XRXU; LUCA.
GeneTree; ENSGT00530000063217; -.
InParanoid; Q9VQI9; -.
KO; K15194; -.
OrthoDB; EOG091G0KKW; -.
PhylomeDB; Q9VQI9; -.
Reactome; R-DME-112382; Formation of RNA Pol II elongation complex.
Reactome; R-DME-674695; RNA Polymerase II Pre-transcription Events.
Reactome; R-DME-75955; RNA Polymerase II Transcription Elongation.
ChiTaRS; lilli; fly.
GenomeRNAi; 33496; -.
PRO; PR:Q9VQI9; -.
Proteomes; UP000000803; Chromosome 2L.
Bgee; FBgn0041111; Expressed in 22 organ(s), highest expression level in testis.
ExpressionAtlas; Q9VQI9; baseline and differential.
Genevisible; Q9VQI9; DM.
GO; GO:0032783; C:ELL-EAF complex; IPI:FlyBase.
GO; GO:0005634; C:nucleus; IDA:FlyBase.
GO; GO:0008023; C:transcription elongation factor complex; IDA:UniProtKB.
GO; GO:0035327; C:transcriptionally active chromatin; IDA:UniProtKB.
GO; GO:0003677; F:DNA binding; ISS:FlyBase.
GO; GO:0003700; F:DNA-binding transcription factor activity; IMP:UniProtKB.
GO; GO:0061629; F:RNA polymerase II sequence-specific DNA-binding transcription factor binding; IPI:FlyBase.
GO; GO:0000915; P:actomyosin contractile ring assembly; NAS:FlyBase.
GO; GO:0042051; P:compound eye photoreceptor development; IGI:FlyBase.
GO; GO:0007611; P:learning or memory; IMP:FlyBase.
GO; GO:0097150; P:neuronal stem cell population maintenance; IMP:FlyBase.
GO; GO:0007365; P:periodic partitioning; IMP:FlyBase.
GO; GO:0007366; P:periodic partitioning by pair rule gene; IMP:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:FlyBase.
GO; GO:0008361; P:regulation of cell size; IMP:FlyBase.
GO; GO:0051493; P:regulation of cytoskeleton organization; IMP:UniProtKB.
GO; GO:0032368; P:regulation of lipid transport; IMP:UniProtKB.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:UniProtKB.
GO; GO:0007379; P:segment specification; HMP:FlyBase.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0048190; P:wing disc dorsal/ventral pattern formation; IGI:FlyBase.
InterPro; IPR007797; TF_AF4/FMR2.
PANTHER; PTHR10528; PTHR10528; 1.
Pfam; PF05110; AF-4; 1.
PROSITE; PS00354; HMGI_Y; 1.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Developmental protein;
DNA-binding; Nucleus; Pair-rule protein; Phosphoprotein;
Reference proteome; Transcription; Transcription regulation.
CHAIN 1 1673 AF4/FMR2 family member 4.
/FTId=PRO_0000394675.
DNA_BIND 851 863 A.T hook. {ECO:0000255}.
COMPBIAS 3 48 Gln-rich. {ECO:0000255}.
COMPBIAS 463 484 Ser-rich. {ECO:0000255}.
COMPBIAS 489 525 Gln-rich. {ECO:0000255}.
COMPBIAS 720 743 Ser-rich. {ECO:0000255}.
COMPBIAS 941 1060 Ser-rich. {ECO:0000255}.
MOD_RES 420 420 Phosphothreonine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 450 450 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 452 452 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 821 821 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 822 822 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 871 871 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 873 873 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 1362 1362 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 1364 1364 Phosphothreonine.
{ECO:0000269|PubMed:18327897}.
VAR_SEQ 1 59 Missing (in isoform D).
{ECO:0000303|PubMed:10731132,
ECO:0000303|Ref.5}.
/FTId=VSP_039294.
CONFLICT 235 235 V -> A (in Ref. 5; ACX54921).
{ECO:0000305}.
CONFLICT 254 254 L -> M (in Ref. 5; ACX54921).
{ECO:0000305}.
CONFLICT 614 614 A -> T (in Ref. 5; ACX54921).
{ECO:0000305}.
CONFLICT 1201 1201 D -> I (in Ref. 5; ACX54921).
{ECO:0000305}.
SEQUENCE 1673 AA; 180089 MW; 7D32A4E81C55B752 CRC64;
MAQQQQQQMQ QQQQHHTSSI NNNNSSSIVL LQQQQPQQQQ QQLDQLQQYN NNLYSQNYNM
EEYERRKRRE REKIERQQGI QIDDRETSLF GEPRRLTEGD AEITAALGEF FEAREYINNQ
TVGISRSAPG AGNPRLQPNL APQAKSLGHS PSSASSAAGP TAASATTSLP GQQQHYQQQQ
RPPTYVKQAD NKPPYNGRGG YPGQPMKNDI PSSSGMAPPR GPPRTSSSNS NSSSVTNNAS
SGGVPASTPL GPPLSTQMPN GREKSFLGPP APALHNGTGG RFVPPAASKR PGVGQQPPPP
EKDVNKIISD IANIFTVQPL TLIAATPHAP TRENYNLLAP NRQKYAMDIP SSPPSAEPSS
LMTPLFAPIT SPIAPLVTTP PQASQMPLGG ATSGTILAGE ALAPLHQLPP TMPKAASGVT
SPGPVKPLKT EKNHSLEKQD SCLENDLELS ESEDEQRKKE GRSGGNSSNS SESDSSESGS
ESSSKNDLQH HPNHQQHHHQ LQQQQQQQQA TMQQQQVLQQ QHRSQPLTSN GAQNKKFRHE
IIARGSNTIT GLLSSSGFGS GGNVGPAGVN SNAVVGTGSG SGGTLSSGGS SSNKTPSPTE
SNKWNLSRFF HKPANQTNSE SVSPGNVSMK VPGILPGGAQ IIPESIDVTT AIVKNEKNDM
AMEEGEEEDD DEEQQLRYGG GLSVTPVAVK KEAIDAVSEM ALGAIPKTQI KRESAETLLS
ARLSDSGTSA SGSSSSSSSS SDSAMGGEVV PMPGPGETLQ LPGVPAAITT VMRVQPTQSQ
KAPPSNSVTL TPILPLPTSP KQRQKKPRKK KAITSAPILD SSDDDEPPPK HPGLDHTAVS
VQTQPATDTV KKGRGRPRKQ QQSGGSGNLS SASAGSSSQT KGPTLTAAKK PLAKTPLAMS
RARKREHSSQ SSSNGNTPTK KVATPQLVAA PLKPTSNTAG SSSSDEDSSS SAESSSKSSS
SSSSSDDTET QNTNCRIVKL NKTGAVQKKA LLGSGSSSPS SSGSEAEDQT TRSQVGSGQA
LAQQLPPYKQ LPISQHSQHL SSSDCSSSSG GCTAVCSSSS GEEDEGRREK ERERKPKSDK
NKINTLTRIF NPKEGGAKKQ GQVVIVDLQE EQQQGKLDAA AQPSAPQAPP AAPAAIMAKP
RMTPTQQQQL GAGLASPART TTPHLTSLIC KIDLSKLSRE RIMRLKKLTP AQQNGHLTPK
DQATNAVHVP NGYAGDTNPA AKVKHEHPVK PEPELDAGYE AKFKPGNVKQ EFQLKQERDR
DRERERERER ERERDREREQ PPGRRRKRSS SSSSSPYKEK KRKKEKADQL QMGKELLPVP
VLLPSNNHER MPNHDRLSYD KLQLLHEDAA AVIGDVSAPN GSPTKKLLAM SPLPPPPTVT
VAPATCNEAV QTTPPSATAT SAIAPPVPAT RLIYRSYFDR DVEHPSDDPR KNNQFLQEAI
NRKHAADLER DSFNQVTLYL EAVVYFLLTA DAMERCSSEQ ATNTMYKDTL SLIKFISTKF
RPYQQQSTTN IQHETHNKVA ILSLRCQSLI SLKLYKLRRK DCRAIINSLT DFFRVGRGDI
ANGNTPSSIS PSNSVGSQGS GSNTPPGRIV PPDIHNMLCK QNEFLSYLNS AHELWDQADR
LVRTGNHIDF IRELDHENGP LTLHSTMHEV FRYVQAGLKT LRDAVSHPTH QSQ


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HRCT1 HRASLS5 Gene HRAS-like suppressor family, member 5
201-20-2620 HRASLS5{HRAS-like suppressor family, member 5}rabbit.pAb 0.2ml
28-786 E2F3 is a member of the E2F family of transcription factors. The E2F family plays a crucial role in the control of cell cycle and action of tumor suppressor proteins and is also a target of the transf 0.05 mg
31-226 E2F5 is a member of the E2F family of transcription factors. The E2F family plays a crucial role in the control of cell cycle and action of tumor suppressor proteins and is also a target of the transf 0.05 mg
27-375 E2F2 is a member of the E2F family of transcription factors. The E2F family plays a crucial role in the control of cell cycle and action of tumor suppressor proteins and is also a target of the transf 0.05 mg
30-622 ING1 is a tumor suppressor protein that can induce cell growth arrest and apoptosis. The protein is a nuclear protein that physically interacts with the tumor suppressor protein TP53 and is a componen 0.1 mg
EIAAB11279 Diras1,Distinct subgroup of the Ras family member 1,Gbts1,GTP-binding protein Di-Ras1,Mouse,Mus musculus,Small GTP-binding tumor suppressor 1
EIAAB40138 HCCS1,HCCS-1,Homo sapiens,Human,Human cervical cancer suppressor gene 1 protein,ST20,Suppressor of tumorigenicity 20 protein
EIAAB14459 Cadherin family member 14,CDHF14,FAT tumor suppressor homolog 4,FAT4,FATJ,Fat-like cadherin protein FAT-J,hFat4,Homo sapiens,Human,Nbla00548,Protocadherin Fat 4
20-272-191330 DCC - Mouse monoclonal [AF5] to DCC; Tumor suppressor protein DCC; Colorectal cancer suppressor Monoclonal 0.05 mg
EIAAB08209 CNK homolog protein 3,CNK3,CNKSR family member 3,Cnksr3,Connector enhancer of kinase suppressor of ras 3,Connector enhancer of KSR 3,Maguin-like protein,Mouse,Mus musculus
27-407 SSBP2 is a member of a closely related, evolutionarily conserved, and ubiquitously expressed gene family. It is also a potential tumor suppressor. 0.05 mg
EIAAB08207 CNK homolog protein 3,CNK3,CNKSR family member 3,CNKSR3,Connector enhancer of kinase suppressor of ras 3,Connector enhancer of KSR 3,Homo sapiens,Human,MAGI1,Maguin-like protein
EIAAB11278 DIRAS1,Distinct subgroup of the Ras family member 1,GBTS1,GTP-binding protein Di-Ras1,Homo sapiens,Human,Ras-related inhibitor of cell growth,Rig,RIG,Small GTP-binding tumor suppressor 1
EIAAB38475 Bos taurus,Bovine,SIKE,SIKE1,Suppressor of IKBKE 1,Suppressor of IKK-epsilon


 

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