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Modifier of mdg4

 MMD4_DROME              Reviewed;         610 AA.
Q86B87; A1A725; A8JR64; A8JR66; P91932; Q24099; Q24100; Q24101;
Q24482; Q24483; Q86B84; Q86B85; Q86B86; Q8IN28; Q8IN29; Q8IN30;
Q8IN31; Q8IN32; Q8IN33; Q8IN34; Q8WTI9; Q8WTJ0; Q8WTJ1; Q95R78;
Q95ZF4; Q95ZF5; Q95ZF6; Q95ZF7; Q95ZF8; Q9N6U6; Q9N6U7; Q9N6U8;
Q9N6U9; Q9N6V0; Q9N6V1; Q9N6V2; Q9N6V3; Q9N6V4; Q9N6V5; Q9N6V6;
Q9N6V7; Q9N6V8; Q9N6V9; Q9N6W0; Q9N6W1; Q9N6W2; Q9N6W3; Q9N6W4;
Q9N6W5; Q9VDA9; Q9VDB2; Q9VDB3; Q9VDB4; Q9VDB5;
13-APR-2004, integrated into UniProtKB/Swiss-Prot.
01-JUN-2003, sequence version 1.
25-OCT-2017, entry version 136.
RecName: Full=Modifier of mdg4;
Name=mod(mdg4) {ECO:0000312|FlyBase:FBgn0002781};
Synonyms=bpd, doom {ECO:0000312|FlyBase:FBgn0002781},
E(var)3-93D {ECO:0000312|FlyBase:FBgn0002781};
ORFNames=CG32491 {ECO:0000312|FlyBase:FBgn0002781};
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}
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS C AND MOD2.2),
FUNCTION, AND SUBCELLULAR LOCATION.
STRAIN=Oregon-R {ECO:0000269|PubMed:8248257};
TISSUE=Embryo {ECO:0000269|PubMed:8248257};
PubMed=8248257; DOI=10.1073/pnas.90.23.11376;
Dorn R., Krauss V., Reuter G., Saumweber H.;
"The enhancer of position-effect variegation of Drosophila, E(var)3-
93D, codes for a chromatin protein containing a conserved domain
common to several transcriptional regulators.";
Proc. Natl. Acad. Sci. U.S.A. 90:11376-11380(1993).
[2] {ECO:0000305}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS MOD1.8; MOD1.9 AND MOD2.2),
FUNCTION, AND INTERACTION WITH SU(HW).
PubMed=7664338; DOI=10.1016/0092-8674(95)90031-4;
Gerasimova T.I., Gdula D.A., Gerasimov D.V., Simonova O., Corces V.G.;
"A Drosophila protein that imparts directionality on a chromatin
insulator is an enhancer of position-effect variegation.";
Cell 82:587-597(1995).
[3] {ECO:0000305}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM H), AND FUNCTION.
STRAIN=Canton-S {ECO:0000269|PubMed:9111355};
PubMed=9111355; DOI=10.1128/MCB.17.5.2835;
Harvey A.J., Bidwai A.P., Miller L.K.;
"Doom, a product of the Drosophila mod(mdg4) gene, induces apoptosis
and binds to baculovirus inhibitor-of-apoptosis proteins.";
Mol. Cell. Biol. 17:2835-2843(1997).
[4] {ECO:0000305}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 53.1; 53.6; 55.6; 59.0; 62.3; B;
C; D; E; F; G; H; I; J; K; M; N; O; Q; R AND S), FUNCTION, SUBCELLULAR
LOCATION, AND DEVELOPMENTAL STAGE.
PubMed=10790390;
Buechner K., Roth P., Schotta G., Krauss V., Saumweber H., Reuter G.,
Dorn R.;
"Genetic and molecular complexity of the position effect variegation
modifier mod(mdg4) in Drosophila.";
Genetics 155:141-157(2000).
[5] {ECO:0000305}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A; L; P; 53.6 AND 54.7).
PubMed=11493677; DOI=10.1073/pnas.151268698;
Dorn R., Reuter G., Loewendorf A.;
"Transgene analysis proves mRNA trans-splicing at the complex
mod(mdg4) locus in Drosophila.";
Proc. Natl. Acad. Sci. U.S.A. 98:9724-9729(2001).
[6] {ECO:0000305}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley {ECO:0000269|PubMed:10731132};
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).
[7] {ECO:0000305}
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).
[8] {ECO:0000305}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 55.6; AA; E AND P).
STRAIN=Berkeley {ECO:0000305}; TISSUE=Embryo {ECO:0000305};
Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W.,
Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E.,
George R.A., Gonzalez M., Guarin H., Kapadia B., Kronmiller B.,
Li P.W., Liao G., Miranda A., Mungall C.J., Nunoo J., Pacleb J.M.,
Paragas V., Park S., Patel S., Phouanenavong S., Wan K.H., Yu C.,
Lewis S.E., Rubin G.M., Celniker S.E.;
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 458-610 (ISOFORM MOD2.2), AND
FUNCTION.
STRAIN=Oregon-R;
PubMed=11604507; DOI=10.1128/MCB.21.22.7714-7720.2001;
Wei W., Brennan M.D.;
"The gypsy insulator can act as a promoter-specific transcriptional
stimulator.";
Mol. Cell. Biol. 21:7714-7720(2001).
[10]
FUNCTION.
PubMed=7761470; DOI=10.1073/pnas.92.11.5184;
Georgiev P.G., Corces V.G.;
"The su(Hw) protein bound to gypsy sequences in one chromosome can
repress enhancer-promoter interactions in the paired gene located in
the other homolog.";
Proc. Natl. Acad. Sci. U.S.A. 92:5184-5188(1995).
[11]
FUNCTION.
PubMed=8852842;
Georgiev P.G., Kozycina M.;
"Interaction between mutations in the suppressor of Hairy wing and
modifier of mdg4 genes of Drosophila melanogaster affecting the
phenotype of gypsy-induced mutations.";
Genetics 142:425-436(1996).
[12]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=9491892; DOI=10.1016/S0092-8674(00)80944-7;
Gerasimova T.I., Corces V.G.;
"Polycomb and trithorax group proteins mediate the function of a
chromatin insulator.";
Cell 92:511-521(1998).
[13]
FUNCTION.
PubMed=10363916;
DOI=10.1002/(SICI)1097-4695(19990605)39:3<447::AID-NEU10>3.0.CO;2-Q;
Gorczyca M., Popova E., Jia X.-X., Budnik V.;
"The gene mod(mdg4) affects synapse specificity and structure in
Drosophila.";
J. Neurobiol. 39:447-460(1999).
[14]
SUBCELLULAR LOCATION.
PubMed=11106742; DOI=10.1016/S1097-2765(00)00101-5;
Gerasimova T.I., Byrd K., Corces V.G.;
"A chromatin insulator determines the nuclear localization of DNA.";
Mol. Cell 6:1025-1035(2000).
[15]
CHARACTERIZATION OF MUTANT MOD(MDG4)351.
PubMed=11024164; DOI=10.1093/nar/28.20.3864;
Read D., Butte M.J., Dernburg A.F., Frasch M., Kornberg T.B.;
"Functional studies of the BTB domain in the Drosophila GAGA and
Mod(mdg4) proteins.";
Nucleic Acids Res. 28:3864-3870(2000).
[16]
SELF-ASSOCIATION, INTERACTION WITH SU(HW), AND SUBCELLULAR LOCATION.
PubMed=11350941; DOI=10.1093/emboj/20.10.2518;
Ghosh D., Gerasimova T.I., Corces V.G.;
"Interactions between the Su(Hw) and Mod(mdg4) proteins required for
gypsy insulator function.";
EMBO J. 20:2518-2527(2001).
[17]
FUNCTION.
PubMed=11779804;
Chen S., Corces V.G.;
"The gypsy insulator of Drosophila affects chromatin structure in a
directional manner.";
Genetics 159:1649-1658(2001).
[18]
FUNCTION, SELF-ASSOCIATION, AND INTERACTION WITH CHI AND SU(HW).
PubMed=11416154; DOI=10.1128/MCB.21.14.4807-4817.2001;
Gause M., Morcillo P., Dorsett D.;
"Insulation of enhancer-promoter communication by a gypsy transposon
insert in the Drosophila cut gene: cooperation between suppressor of
hairy-wing and modifier of mdg4 proteins.";
Mol. Cell. Biol. 21:4807-4817(2001).
[19]
INTERACTION WITH CP190; SU(HW) AND TRL, AND SUBCELLULAR LOCATION.
PubMed=15574329; DOI=10.1016/j.molcel.2004.11.004;
Pai C.-Y., Lei E.P., Ghosh D., Corces V.G.;
"The centrosomal protein CP190 is a component of the gypsy chromatin
insulator.";
Mol. Cell 16:737-748(2004).
[20]
INTERACTION WITH TRL.
PubMed=15465920; DOI=10.1073/pnas.0403959101;
Melnikova L., Juge F., Gruzdeva N., Mazur A., Cavalli G.,
Georgiev P.G.;
"Interaction between the GAGA factor and Mod(mdg4) proteins promotes
insulator bypass in Drosophila.";
Proc. Natl. Acad. Sci. U.S.A. 101:14806-14811(2004).
[21]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=16286005; DOI=10.1016/j.cell.2005.08.043;
Thomas S.E., Soltani-Bejnood M., Roth P., Dorn R., Logsdon J.M. Jr.,
McKee B.D.;
"Identification of two proteins required for conjunction and regular
segregation of achiasmate homologs in Drosophila male meiosis.";
Cell 123:555-568(2005).
[22]
INTERACTION WITH TOPORS, AND SUBCELLULAR LOCATION.
PubMed=16209949; DOI=10.1016/j.molcel.2005.08.031;
Capelson M., Corces V.G.;
"The ubiquitin ligase dTopors directs the nuclear organization of a
chromatin insulator.";
Mol. Cell 20:105-116(2005).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-230, AND IDENTIFICATION
BY MASS SPECTROMETRY.
TISSUE=Embryo;
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).
[24]
INTERACTION WITH TOP2, AND SUBCELLULAR LOCATION.
PubMed=21304601; DOI=10.1371/journal.pone.0016562;
Ramos E., Torre E.A., Bushey A.M., Gurudatta B.V., Corces V.G.;
"DNA topoisomerase II modulates insulator function in Drosophila.";
PLoS ONE 6:E16562-E16562(2011).
-!- FUNCTION: Component of the gypsy chromatin insulator complex which
is required for the function of the gypsy chromatin insulator and
other endogenous chromatin insulators. Chromatin insulators are
regulatory elements which establish independent domains of
transcriptional activity within eukaryotic genomes. Insulators
have two defining properties; they can block the communication
between an enhancer and a promoter when placed between them and
can also buffer transgenes from position effect variegation (PEV).
Insulators are proposed to structure the chromatin fiber into
independent domains of differing transcriptional potential by
promoting the formation of distinct chromatin loops. This
chromatin looping may involve the formation of insulator bodies,
where homotypic interactions between individual subunits of the
insulator complex could promote the clustering of widely spaced
insulators at the nuclear periphery. Within the gypsy insulator
complex, this protein may control the nature of the repressive
effect of su(Hw): in the absence of mod(mdg4) protein, su(Hw)
exerts a bidirectional silencing effect, whereas in the presence
of mod(mdg4), the silencing effect is unidirectional. Isoform H is
specifically required to maintain the pairing of achiasmate
homologs in male meiosis I which is mediated by the rDNA repeats
on the achiasmate X-Y bivalents. Isoform H also plays a role in
apoptotic regulatory pathways. {ECO:0000269|PubMed:10363916,
ECO:0000269|PubMed:10790390, ECO:0000269|PubMed:11416154,
ECO:0000269|PubMed:11604507, ECO:0000269|PubMed:11779804,
ECO:0000269|PubMed:16286005, ECO:0000269|PubMed:7664338,
ECO:0000269|PubMed:7761470, ECO:0000269|PubMed:8248257,
ECO:0000269|PubMed:8852842, ECO:0000269|PubMed:9111355,
ECO:0000269|PubMed:9491892}.
-!- SUBUNIT: Can self-associate (PubMed:11350941, PubMed:11416154).
Interacts with Chi (PubMed:11416154). Interacts with Top2
(PubMed:21304601). Isoform mod2.2: Component of the gypsy
chromatin insulator complex, composed of Cp190, mod(mdg4) and
su(Hw) (PubMed:7664338, PubMed:11350941, PubMed:11416154,
PubMed:15574329). The gypsy chromatin insulator complex interacts
with Topors via mod(mdg4) and su(Hw) (PubMed:16209949). Isoform
mod2.2 interacts with Trl/GAGA and interaction with this protein
may bypass the repressive effects of the su(Hw) insulator
(PubMed:15465920). {ECO:0000269|PubMed:11350941,
ECO:0000269|PubMed:11416154, ECO:0000269|PubMed:15465920,
ECO:0000269|PubMed:15574329, ECO:0000269|PubMed:16209949,
ECO:0000269|PubMed:21304601, ECO:0000269|PubMed:7664338}.
-!- INTERACTION:
Q24478:Cp190; NbExp=4; IntAct=EBI-1433422, EBI-868840;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10790390,
ECO:0000269|PubMed:11106742, ECO:0000269|PubMed:11350941,
ECO:0000269|PubMed:15574329, ECO:0000269|PubMed:16209949,
ECO:0000269|PubMed:16286005, ECO:0000269|PubMed:21304601,
ECO:0000269|PubMed:8248257, ECO:0000269|PubMed:9491892}.
Chromosome {ECO:0000269|PubMed:10790390,
ECO:0000269|PubMed:11106742, ECO:0000269|PubMed:11350941,
ECO:0000269|PubMed:15574329, ECO:0000269|PubMed:16209949,
ECO:0000269|PubMed:16286005, ECO:0000269|PubMed:21304601,
ECO:0000269|PubMed:8248257, ECO:0000269|PubMed:9491892}.
Note=Colocalizes with other elements of the gypsy chromatin
insulator complex at multiple sites on polytene chromosomes and at
nuclear insulator bodies (PubMed:9491892, PubMed:11106742,
PubMed:11350941, PubMed:15574329, PubMed:16209949). The unique C-
termini of individual isoforms may specify binding to particular
chromosomal locations (PubMed:11350941). During the G2 phase of
male meiosis isoform H localizes to the nucleolus
(PubMed:16286005). It subsequently localizes to the rDNA repeats
of the X-Y bivalent and to multiple autosomal loci, where it
remains until anaphase I (PubMed:16286005). Localization to the
rDNA repeats requires SA-2, while localization to autosomal loci
requires SA-2 and tef (PubMed:16286005).
{ECO:0000269|PubMed:11106742, ECO:0000269|PubMed:11350941,
ECO:0000269|PubMed:15574329, ECO:0000269|PubMed:16209949,
ECO:0000269|PubMed:16286005, ECO:0000269|PubMed:9491892}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=31;
Name=mod2.2; Synonyms=67.2 {ECO:0000269|PubMed:10790390},
E(VAR)3-93D;
IsoId=Q86B87-1; Sequence=Displayed;
Note=C-terminal exons are translated from the opposite DNA
strand. This may be due to a trans-splicing event.;
Name=53.1 {ECO:0000269|PubMed:10790390};
IsoId=Q86B87-16; Sequence=VSP_050724;
Note=C-terminal exons are translated from the opposite DNA
strand. This may be due to a trans-splicing event.;
Name=53.6; Synonyms=X;
IsoId=Q86B87-28; Sequence=VSP_010286;
Note=C-terminal exons are translated from the opposite DNA
strand. This may be due to a trans-splicing event.;
Name=54.7; Synonyms=Y;
IsoId=Q86B87-23; Sequence=VSP_010287;
Note=C-terminal exons are translated from the opposite DNA
strand. This may be due to a trans-splicing event. Ref.5
(CAC51489) sequence is in conflict in position: 458:N->D.
{ECO:0000305};
Name=55.6 {ECO:0000269|PubMed:10790390};
IsoId=Q86B87-13; Sequence=VSP_050725;
Note=C-terminal exons are translated from the opposite DNA
strand. This may be due to a trans-splicing event.;
Name=59.0; Synonyms=Z;
IsoId=Q86B87-25; Sequence=VSP_010288;
Note=C-terminal exons are translated from the opposite DNA
strand. This may be due to a trans-splicing event.;
Name=62.3 {ECO:0000269|PubMed:10790390};
IsoId=Q86B87-4; Sequence=VSP_050701;
Note=C-terminal exons are translated from the opposite DNA
strand. This may be due to a trans-splicing event.;
Name=A {ECO:0000269|PubMed:11493677}; Synonyms=54.2
{ECO:0000269|PubMed:11493677};
IsoId=Q86B87-17; Sequence=VSP_050713;
Name=AA;
IsoId=Q86B87-29; Sequence=VSP_034704;
Note=No experimental confirmation available.;
Name=AC;
IsoId=Q86B87-30; Sequence=VSP_034706;
Note=No experimental confirmation available.;
Name=AB;
IsoId=Q86B87-31; Sequence=VSP_034705;
Note=No experimental confirmation available.;
Name=B; Synonyms=54.6;
IsoId=Q86B87-27; Sequence=VSP_010284;
Note=No experimental confirmation available.;
Name=C {ECO:0000269|PubMed:10790390, ECO:0000269|PubMed:8248257};
Synonyms=58.0 {ECO:0000269|PubMed:10790390}, 3
{ECO:0000269|PubMed:8248257};
IsoId=Q86B87-9; Sequence=VSP_050714;
Note=Ref.1 (CAA53215) sequence is in conflict in position:
422:V->A. {ECO:0000305};
Name=D; Synonyms=57.4;
IsoId=Q86B87-24; Sequence=VSP_010285;
Name=E {ECO:0000269|PubMed:10790390}; Synonyms=65.0
{ECO:0000269|PubMed:10790390};
IsoId=Q86B87-2; Sequence=VSP_050699;
Name=F {ECO:0000269|PubMed:10790390}; Synonyms=58.6
{ECO:0000269|PubMed:10790390};
IsoId=Q86B87-8; Sequence=VSP_050704;
Note=Ref.4 (CAB85480) sequence is in conflict in position:
521:S->T. {ECO:0000305};
Name=G {ECO:0000269|PubMed:10790390}; Synonyms=54.2
{ECO:0000269|PubMed:10790390};
IsoId=Q86B87-15; Sequence=VSP_050715;
Name=H {ECO:0000269|PubMed:10790390, ECO:0000269|PubMed:9111355};
Synonyms=56.3 {ECO:0000269|PubMed:10790390}, Doom, MNM;
IsoId=Q86B87-10; Sequence=VSP_050716;
Note=Ref.4 (CAB85478) sequence is in conflict in position:
447:D->A. {ECO:0000305};
Name=I {ECO:0000269|PubMed:10790390}; Synonyms=59.1
{ECO:0000269|PubMed:10790390};
IsoId=Q86B87-6; Sequence=VSP_050703;
Name=J {ECO:0000269|PubMed:10790390}; Synonyms=51.4
{ECO:0000269|PubMed:10790390};
IsoId=Q86B87-19; Sequence=VSP_050717;
Name=K {ECO:0000269|PubMed:10790390}; Synonyms=55.7
{ECO:0000269|PubMed:10790390};
IsoId=Q86B87-11; Sequence=VSP_050718;
Note=Ref.4 (CAB85477) sequence is in conflict in position:
484:A->P. {ECO:0000305};
Name=L {ECO:0000269|PubMed:11493677}; Synonyms=52.2
{ECO:0000269|PubMed:11493677};
IsoId=Q86B87-18; Sequence=VSP_050719;
Note=Ref.5 (CAC51387) sequence is in conflict in position:
469:A->T. {ECO:0000305};
Name=M {ECO:0000269|PubMed:10790390}; Synonyms=55.3
{ECO:0000269|PubMed:10790390};
IsoId=Q86B87-14; Sequence=VSP_050720;
Name=N {ECO:0000269|PubMed:10790390}; Synonyms=64.2
{ECO:0000269|PubMed:10790390};
IsoId=Q86B87-3; Sequence=VSP_050700;
Name=O {ECO:0000269|PubMed:10790390}; Synonyms=60.1
{ECO:0000269|PubMed:10790390};
IsoId=Q86B87-5; Sequence=VSP_050702;
Note=Ref.4 (CAB85483) sequence is in conflict in position:
543:M->I. {ECO:0000305};
Name=P {ECO:0000303|PubMed:10731132}; Synonyms=58.6;
IsoId=Q86B87-7; Sequence=VSP_050705;
Name=Q {ECO:0000269|PubMed:10790390}; Synonyms=46.3
{ECO:0000269|PubMed:10790390};
IsoId=Q86B87-21; Sequence=VSP_050721;
Name=R {ECO:0000269|PubMed:10790390}; Synonyms=52.0
{ECO:0000269|PubMed:10790390};
IsoId=Q86B87-20; Sequence=VSP_050722;
Name=S {ECO:0000269|PubMed:10790390}; Synonyms=55.1
{ECO:0000269|PubMed:10790390};
IsoId=Q86B87-12; Sequence=VSP_050723;
Name=mod1.8;
IsoId=Q86B87-26; Sequence=VSP_010289;
Name=mod1.9;
IsoId=Q86B87-22; Sequence=VSP_010283;
-!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
Zygotic expression is high in pupae and adult females but low in
other stages of development. {ECO:0000269|PubMed:10790390}.
-!- DOMAIN: Homotypic interactions mediated by the BTB (POZ) domain of
this protein may promote the clustering of distant insulator
complexes into nuclear insulator bodies.
-!- SEQUENCE CAUTION:
Sequence=AAA82990.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
Sequence=AAL29128.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
Sequence=AAN13870.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; X75498; CAA53215.1; -; Genomic_DNA.
EMBL; X75499; CAA53216.1; -; mRNA.
EMBL; U30905; AAA82988.1; -; mRNA.
EMBL; U30913; AAA82989.1; -; mRNA.
EMBL; U30914; AAA82990.1; ALT_SEQ; mRNA.
EMBL; U62802; AAC17459.1; -; mRNA.
EMBL; AJ277174; CAB85469.1; -; mRNA.
EMBL; AJ277175; CAB85470.1; -; mRNA.
EMBL; AJ277176; CAB85471.1; -; mRNA.
EMBL; AJ277177; CAB85472.1; -; mRNA.
EMBL; AJ277178; CAB85473.1; -; mRNA.
EMBL; AJ277179; CAB85474.1; -; mRNA.
EMBL; AJ277180; CAB85475.1; -; mRNA.
EMBL; AJ277181; CAB85476.1; -; mRNA.
EMBL; AJ277182; CAB85477.1; -; mRNA.
EMBL; AJ277183; CAB85478.1; -; mRNA.
EMBL; AJ277184; CAB85479.1; -; mRNA.
EMBL; AJ277185; CAB85480.1; -; mRNA.
EMBL; AJ277186; CAB85481.1; -; mRNA.
EMBL; AJ277187; CAB85482.1; -; mRNA.
EMBL; AJ277188; CAB85483.1; -; mRNA.
EMBL; AJ277189; CAB85484.1; -; mRNA.
EMBL; AJ277190; CAB85485.1; -; mRNA.
EMBL; AJ277191; CAB85486.1; -; mRNA.
EMBL; AJ277192; CAB85487.1; -; mRNA.
EMBL; AJ277193; CAB85488.1; -; mRNA.
EMBL; AJ277194; CAB85489.1; -; mRNA.
EMBL; AJ320161; CAC51387.1; -; mRNA.
EMBL; AJ320162; CAC51487.1; -; mRNA.
EMBL; AJ320163; CAC51488.1; -; mRNA.
EMBL; AJ320164; CAC51489.1; -; mRNA.
EMBL; AJ320165; CAC51388.1; -; mRNA.
EMBL; AE014297; AAF55882.2; -; Genomic_DNA.
EMBL; AE014297; AAF55883.2; -; Genomic_DNA.
EMBL; AE014297; AAF55884.1; -; Genomic_DNA.
EMBL; AE014297; AAF55885.2; -; Genomic_DNA.
EMBL; AE014297; AAF55888.1; -; Genomic_DNA.
EMBL; AE014297; AAN13862.1; -; Genomic_DNA.
EMBL; AE014297; AAN13863.1; -; Genomic_DNA.
EMBL; AE014297; AAN13864.1; -; Genomic_DNA.
EMBL; AE014297; AAN13865.1; -; Genomic_DNA.
EMBL; AE014297; AAN13866.1; -; Genomic_DNA.
EMBL; AE014297; AAN13867.1; -; Genomic_DNA.
EMBL; AE014297; AAN13868.1; -; Genomic_DNA.
EMBL; AE014297; AAN13869.1; -; Genomic_DNA.
EMBL; AE014297; AAN13870.1; ALT_INIT; Genomic_DNA.
EMBL; AE014297; AAN13871.1; -; Genomic_DNA.
EMBL; AE014297; AAN13872.1; -; Genomic_DNA.
EMBL; AE014297; AAN13873.1; -; Genomic_DNA.
EMBL; AE014297; AAN13874.1; -; Genomic_DNA.
EMBL; AE014297; AAN13875.1; -; Genomic_DNA.
EMBL; AE014297; AAO41581.1; -; Genomic_DNA.
EMBL; AE014297; AAO41582.1; -; Genomic_DNA.
EMBL; AE014297; AAO41583.1; -; Genomic_DNA.
EMBL; AE014297; ABW08718.1; -; Genomic_DNA.
EMBL; AE014297; ABW08719.1; -; Genomic_DNA.
EMBL; AE014297; ABW08720.1; -; Genomic_DNA.
EMBL; AY061580; AAL29128.1; ALT_SEQ; mRNA.
EMBL; BT003484; AAO39487.1; -; mRNA.
EMBL; BT003579; AAO39583.1; -; mRNA.
EMBL; BT029698; ABL75755.1; -; mRNA.
EMBL; AF214648; AAL33873.1; -; Genomic_DNA.
EMBL; AF214649; AAL33874.1; -; Genomic_DNA.
EMBL; AF214650; AAL33875.1; -; Genomic_DNA.
RefSeq; NP_001097856.1; NM_001104386.2. [Q86B87-29]
RefSeq; NP_001097857.1; NM_001104387.2. [Q86B87-31]
RefSeq; NP_001097858.1; NM_001104388.2. [Q86B87-30]
RefSeq; NP_524936.2; NM_080197.3. [Q86B87-8]
RefSeq; NP_732619.1; NM_163877.2. [Q86B87-20]
RefSeq; NP_732620.1; NM_163878.2. [Q86B87-17]
RefSeq; NP_732621.1; NM_163879.2. [Q86B87-24]
RefSeq; NP_732622.1; NM_163880.2. [Q86B87-15]
RefSeq; NP_732623.2; NM_163881.2.
RefSeq; NP_732624.1; NM_163882.2. [Q86B87-10]
RefSeq; NP_732625.1; NM_163883.2. [Q86B87-27]
RefSeq; NP_732626.1; NM_163884.2. [Q86B87-6]
RefSeq; NP_732627.1; NM_163885.2. [Q86B87-19]
RefSeq; NP_732628.1; NM_163886.2. [Q86B87-7]
RefSeq; NP_732629.1; NM_163887.2. [Q86B87-18]
RefSeq; NP_732630.1; NM_163888.2. [Q86B87-11]
RefSeq; NP_732631.1; NM_163889.2. [Q86B87-14]
RefSeq; NP_732632.1; NM_163890.2. [Q86B87-2]
RefSeq; NP_732633.1; NM_163891.2. [Q86B87-9]
RefSeq; NP_732634.1; NM_163892.2. [Q86B87-12]
RefSeq; NP_732635.1; NM_163893.2. [Q86B87-5]
RefSeq; NP_732636.1; NM_163894.2. [Q86B87-3]
RefSeq; NP_788698.1; NM_176521.1. [Q86B87-1]
RefSeq; NP_788699.1; NM_176522.1. [Q86B87-25]
RefSeq; NP_788700.1; NM_176523.1. [Q86B87-23]
RefSeq; NP_788701.1; NM_176524.1. [Q86B87-28]
RefSeq; NP_788702.1; NM_176525.1. [Q86B87-13]
RefSeq; NP_788703.1; NM_176526.1. [Q86B87-4]
RefSeq; NP_788704.1; NM_176527.1. [Q86B87-16]
UniGene; Dm.20407; -.
ProteinModelPortal; Q86B87; -.
SMR; Q86B87; -.
BioGrid; 72097; 72.
IntAct; Q86B87; 28.
MINT; MINT-298823; -.
STRING; 7227.FBpp0292464; -.
iPTMnet; Q86B87; -.
PeptideAtlas; Q86B87; -.
PRIDE; Q86B87; -.
EnsemblMetazoa; FBtr0084060; FBpp0083459; FBgn0002781. [Q86B87-17]
EnsemblMetazoa; FBtr0084061; FBpp0083460; FBgn0002781. [Q86B87-27]
EnsemblMetazoa; FBtr0084062; FBpp0083461; FBgn0002781. [Q86B87-9]
EnsemblMetazoa; FBtr0084063; FBpp0083462; FBgn0002781. [Q86B87-24]
EnsemblMetazoa; FBtr0084064; FBpp0083463; FBgn0002781. [Q86B87-2]
EnsemblMetazoa; FBtr0084065; FBpp0083464; FBgn0002781. [Q86B87-8]
EnsemblMetazoa; FBtr0084066; FBpp0083465; FBgn0002781. [Q86B87-15]
EnsemblMetazoa; FBtr0084067; FBpp0083466; FBgn0002781. [Q86B87-10]
EnsemblMetazoa; FBtr0084068; FBpp0083467; FBgn0002781. [Q86B87-6]
EnsemblMetazoa; FBtr0084069; FBpp0083468; FBgn0002781. [Q86B87-19]
EnsemblMetazoa; FBtr0084070; FBpp0083469; FBgn0002781. [Q86B87-11]
EnsemblMetazoa; FBtr0084071; FBpp0083470; FBgn0002781. [Q86B87-18]
EnsemblMetazoa; FBtr0084072; FBpp0083471; FBgn0002781. [Q86B87-14]
EnsemblMetazoa; FBtr0084073; FBpp0083472; FBgn0002781. [Q86B87-3]
EnsemblMetazoa; FBtr0084074; FBpp0083473; FBgn0002781. [Q86B87-5]
EnsemblMetazoa; FBtr0084075; FBpp0083474; FBgn0002781. [Q86B87-7]
EnsemblMetazoa; FBtr0084077; FBpp0083476; FBgn0002781. [Q86B87-20]
EnsemblMetazoa; FBtr0084078; FBpp0083477; FBgn0002781. [Q86B87-12]
EnsemblMetazoa; FBtr0084079; FBpp0083478; FBgn0002781. [Q86B87-1]
EnsemblMetazoa; FBtr0084080; FBpp0083479; FBgn0002781. [Q86B87-16]
EnsemblMetazoa; FBtr0084081; FBpp0083480; FBgn0002781. [Q86B87-4]
EnsemblMetazoa; FBtr0084082; FBpp0083481; FBgn0002781. [Q86B87-13]
EnsemblMetazoa; FBtr0084083; FBpp0083482; FBgn0002781. [Q86B87-28]
EnsemblMetazoa; FBtr0084084; FBpp0083483; FBgn0002781. [Q86B87-23]
EnsemblMetazoa; FBtr0084085; FBpp0083484; FBgn0002781. [Q86B87-25]
EnsemblMetazoa; FBtr0114359; FBpp0112908; FBgn0002781. [Q86B87-29]
EnsemblMetazoa; FBtr0114360; FBpp0112909; FBgn0002781. [Q86B87-31]
EnsemblMetazoa; FBtr0114361; FBpp0112910; FBgn0002781. [Q86B87-30]
GeneID; 49228; -.
KEGG; dme:Dmel_CG32491; -.
UCSC; CG32491-RAA; d. melanogaster.
UCSC; CG32491-RAB; d. melanogaster.
UCSC; CG32491-RAC; d. melanogaster.
CTD; 49228; -.
FlyBase; FBgn0002781; mod(mdg4).
InParanoid; Q86B87; -.
OMA; QITVQTA; -.
OrthoDB; EOG091G0A8U; -.
SignaLink; Q86B87; -.
ChiTaRS; mod(mdg4); fly.
GenomeRNAi; 49228; -.
PRO; PR:Q86B87; -.
Proteomes; UP000000803; Chromosome 3R.
Bgee; FBgn0002781; -.
ExpressionAtlas; Q86B87; differential.
Genevisible; Q86B87; DM.
GO; GO:0000785; C:chromatin; IMP:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:FlyBase.
GO; GO:0005886; C:plasma membrane; ISS:FlyBase.
GO; GO:0005700; C:polytene chromosome; IDA:FlyBase.
GO; GO:0005704; C:polytene chromosome band; IDA:FlyBase.
GO; GO:0003682; F:chromatin binding; IMP:UniProtKB.
GO; GO:0003677; F:DNA binding; IDA:FlyBase.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0008195; F:phosphatidate phosphatase activity; ISS:FlyBase.
GO; GO:0031208; F:POZ domain binding; IDA:FlyBase.
GO; GO:0042803; F:protein homodimerization activity; IDA:FlyBase.
GO; GO:0006915; P:apoptotic process; IMP:UniProtKB.
GO; GO:0016569; P:covalent chromatin modification; IEA:UniProtKB-KW.
GO; GO:0008354; P:germ cell migration; IMP:FlyBase.
GO; GO:0007060; P:male meiosis chromosome segregation; IMP:FlyBase.
GO; GO:0007141; P:male meiosis I; IMP:FlyBase.
GO; GO:0010032; P:meiotic chromosome condensation; IMP:FlyBase.
GO; GO:0048477; P:oogenesis; IMP:FlyBase.
GO; GO:0001672; P:regulation of chromatin assembly or disassembly; IMP:UniProtKB.
GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; IBA:GO_Central.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
InterPro; IPR000210; BTB/POZ_dom.
InterPro; IPR011333; SKP1/BTB/POZ.
InterPro; IPR007588; Znf_FLYWCH.
Pfam; PF00651; BTB; 1.
Pfam; PF04500; FLYWCH; 1.
SMART; SM00225; BTB; 1.
SUPFAM; SSF54695; SSF54695; 1.
PROSITE; PS50097; BTB; 1.
1: Evidence at protein level;
Alternative splicing; Apoptosis; Chromatin regulator; Chromosome;
Complete proteome; Metal-binding; Nucleus; Phosphoprotein;
Reference proteome; Transcription; Transcription regulation; Zinc;
Zinc-finger.
CHAIN 1 610 Modifier of mdg4.
/FTId=PRO_0000096505.
DOMAIN 32 98 BTB. {ECO:0000255|PROSITE-
ProRule:PRU00037}.
ZN_FING 452 512 FLYWCH-type.
REGION 1 308 Interaction with Chi.
REGION 1 160 Self-association.
REGION 551 610 Interaction with su(Hw).
COMPBIAS 139 209 Gln-rich.
MOD_RES 230 230 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
VAR_SEQ 360 449 Missing (in isoform mod1.9).
{ECO:0000303|PubMed:7664338}.
/FTId=VSP_010283.
VAR_SEQ 403 610 AATSASATKIPPRKRGRPKTKVEDQTPKPKLLEKLQAATLN
EEASEPAVYASTTKGGVKLIFNGHLFKFSFRKADYSVFQCC
YREHGEECKVRVVCDQKRVFPYEGEHVHFMQASDKSCLPSQ
FMPGESGVISSLSPSKELLMKNTTKLEEADDKEDEDFEEFE
IQEIDEIELDEPEKTPAKEEEVDPNDFREKIKRRLQKALQN
KKK -> GDATQFFFTKGQRESVKLNYCGHSYVKFMENGRG
TKWICATRSTTKCRARIRTTKNNYLEVLYASHNHGFPPQKK
DRGRASQRM (in isoform 53.1).
{ECO:0000303|PubMed:10790390}.
/FTId=VSP_050724.
VAR_SEQ 403 610 AATSASATKIPPRKRGRPKTKVEDQTPKPKLLEKLQAATLN
EEASEPAVYASTTKGGVKLIFNGHLFKFSFRKADYSVFQCC
YREHGEECKVRVVCDQKRVFPYEGEHVHFMQASDKSCLPSQ
FMPGESGVISSLSPSKELLMKNTTKLEEADDKEDEDFEEFE
IQEIDEIELDEPEKTPAKEEEVDPNDFREKIKRRLQKALQN
KKK -> EQEDDFKLHLPLLVTRRKKTPGGSRKQSFDHLEV
SFTRSNRGNNLLTIDGKPFTLNRRIKDVCYWECVKLRCKYI
KCSARVVTKSNRISALSGLHNHP (in isoform
54.7). {ECO:0000303|PubMed:11493677}.
/FTId=VSP_010287.
VAR_SEQ 403 610 AATSASATKIPPRKRGRPKTKVEDQTPKPKLLEKLQAATLN
EEASEPAVYASTTKGGVKLIFNGHLFKFSFRKADYSVFQCC
YREHGEECKVRVVCDQKRVFPYEGEHVHFMQASDKSCLPSQ
FMPGESGVISSLSPSKELLMKNTTKLEEADDKEDEDFEEFE
IQEIDEIELDEPEKTPAKEEEVDPNDFREKIKRRLQKALQN
KKK -> GHLSTLRHLPVEAIFDADGKQMDFIPNIRVIRSQ
RKTIKLMFKKYAYSKTNEHDTTTYWHCRSRRNGRPACKARF
STKKLKNGSYKVYLTQPEHNHPPKKRRL (in isoform
55.6). {ECO:0000303|PubMed:10790390,
ECO:0000303|Ref.8}.
/FTId=VSP_050725.
VAR_SEQ 403 610 AATSASATKIPPRKRGRPKTKVEDQTPKPKLLEKLQAATLN
EEASEPAVYASTTKGGVKLIFNGHLFKFSFRKADYSVFQCC
YREHGEECKVRVVCDQKRVFPYEGEHVHFMQASDKSCLPSQ
FMPGESGVISSLSPSKELLMKNTTKLEEADDKEDEDFEEFE
IQEIDEIELDEPEKTPAKEEEVDPNDFREKIKRRLQKALQN
KKK -> VTQHVRNCGPQMFLISRKGGTLLTINNFVYRSNL
KFFGKSNNILYWECVQNRSVKCRSRLKTIGDDLYVTNDVHN
HMGDNKRIEAAKAAGMLIHKKLSSLTAADKIQGSWKMDTEG
NPDHLPKM (in isoform 59.0).
{ECO:0000303|PubMed:10790390}.
/FTId=VSP_010288.
VAR_SEQ 403 610 AATSASATKIPPRKRGRPKTKVEDQTPKPKLLEKLQAATLN
EEASEPAVYASTTKGGVKLIFNGHLFKFSFRKADYSVFQCC
YREHGEECKVRVVCDQKRVFPYEGEHVHFMQASDKSCLPSQ
FMPGESGVISSLSPSKELLMKNTTKLEEADDKEDEDFEEFE
IQEIDEIELDEPEKTPAKEEEVDPNDFREKIKRRLQKALQN
KKK -> ESSVAIYSATSRGRMQLIYGGQPFIFEKTLKLSS
GEEKRFWRCNQWWNQKCRSRVFTINDVVCPLNRFHTHEEIV
RRKKRVRRVPPVETIAKVVATTPRHPQHQQTTQQQQEIQLT
SDAIAGAILDDESPATIDVSELGMHLKYEEIVADVTGIVGG
TRVVSRRK (in isoform 62.3).
{ECO:0000303|PubMed:10790390}.
/FTId=VSP_050701.
VAR_SEQ 403 610 AATSASATKIPPRKRGRPKTKVEDQTPKPKLLEKLQAATLN
EEASEPAVYASTTKGGVKLIFNGHLFKFSFRKADYSVFQCC
YREHGEECKVRVVCDQKRVFPYEGEHVHFMQASDKSCLPSQ
FMPGESGVISSLSPSKELLMKNTTKLEEADDKEDEDFEEFE
IQEIDEIELDEPEKTPAKEEEVDPNDFREKIKRRLQKALQN
KKK -> EKQFEYVVSQKGHVLLLHKKFPFIREKCINGKTY
WRCTQYTTKTKCHGRLHVLNGKIVHIKTHNHSPLDQERKQY
MKLQLNNV (in isoform A).
{ECO:0000303|PubMed:11493677}.
/FTId=VSP_050713.
VAR_SEQ 403 610 AATSASATKIPPRKRGRPKTKVEDQTPKPKLLEKLQAATLN
EEASEPAVYASTTKGGVKLIFNGHLFKFSFRKADYSVFQCC
YREHGEECKVRVVCDQKRVFPYEGEHVHFMQASDKSCLPSQ
FMPGESGVISSLSPSKELLMKNTTKLEEADDKEDEDFEEFE
IQEIDEIELDEPEKTPAKEEEVDPNDFREKIKRRLQKALQN
KKK -> VLTYDDRGKLVHEGFTFSCYSRNPGKCLAFWRCS
MYKKMHCTSALTTHIKSIKSIRGFHNHKPPERLKTFVPRVL
DCPPRPHKEDY (in isoform AA).
{ECO:0000303|Ref.8}.
/FTId=VSP_034704.
VAR_SEQ 403 610 AATSASATKIPPRKRGRPKTKVEDQTPKPKLLEKLQAATLN
EEASEPAVYASTTKGGVKLIFNGHLFKFSFRKADYSVFQCC
YREHGEECKVRVVCDQKRVFPYEGEHVHFMQASDKSCLPSQ
FMPGESGVISSLSPSKELLMKNTTKLEEADDKEDEDFEEFE
IQEIDEIELDEPEKTPAKEEEVDPNDFREKIKRRLQKALQN
KKK -> GVIQSLKALFEGKTTGASIQYTTTQRGRVMLVYE
GYRYVVNRQSLKNVFWRCSRYVKHSCRATLVTSKVQEVTLR
IAGTPHTHAPEVSSMDLTTDLLDEFPELQ (in isoform
AB). {ECO:0000305}.
/FTId=VSP_034705.
VAR_SEQ 403 610 AATSASATKIPPRKRGRPKTKVEDQTPKPKLLEKLQAATLN
EEASEPAVYASTTKGGVKLIFNGHLFKFSFRKADYSVFQCC
YREHGEECKVRVVCDQKRVFPYEGEHVHFMQASDKSCLPSQ
FMPGESGVISSLSPSKELLMKNTTKLEEADDKEDEDFEEFE
IQEIDEIELDEPEKTPAKEEEVDPNDFREKIKRRLQKALQN
KKK -> VTFDVLTDPIVKPDQHQLMKRVRLSKSMEGVHYV
RTPAGNVVLHCGEHRYLRNAAYKDKVYWKCSKWRKQCRSRV
ITHILPNGQSRYAVSGVHNHP (in isoform B).
{ECO:0000303|PubMed:10790390}.
/FTId=VSP_010284.
VAR_SEQ 403 610 AATSASATKIPPRKRGRPKTKVEDQTPKPKLLEKLQAATLN
EEASEPAVYASTTKGGVKLIFNGHLFKFSFRKADYSVFQCC
YREHGEECKVRVVCDQKRVFPYEGEHVHFMQASDKSCLPSQ
FMPGESGVISSLSPSKELLMKNTTKLEEADDKEDEDFEEFE
IQEIDEIELDEPEKTPAKEEEVDPNDFREKIKRRLQKALQN
KKK -> DGPSKDTAIPKPAEHPRKPVTDSVQKSPRDADAI
PLFDGSRVFVSKVALAKAYIPMPMIYTCRVMDLVIGKDKLV
RIAQHEETTDKDLIQDIITHVCKVFALRGNQLTPSAVQEFI
DHKLSTLKLMPIKEGK (in isoform C).
{ECO:0000303|PubMed:10790390,
ECO:0000303|PubMed:8248257}.
/FTId=VSP_050714.
VAR_SEQ 403 610 AATSASATKIPPRKRGRPKTKVEDQTPKPKLLEKLQAATLN
EEASEPAVYASTTKGGVKLIFNGHLFKFSFRKADYSVFQCC
YREHGEECKVRVVCDQKRVFPYEGEHVHFMQASDKSCLPSQ
FMPGESGVISSLSPSKELLMKNTTKLEEADDKEDEDFEEFE
IQEIDEIELDEPEKTPAKEEEVDPNDFREKIKRRLQKALQN
KKK -> EFDYGHGQYRGNNPQIQFSVSKRGGQLLWLDGMK
FFRNNINRTNLYWRCHWYYRHTKCPVLICMSKTNSNDFRQI
HDHCHIRPKRKENSGTGDGPKIRTPVVSNVRSLPQSMAHMF
DM (in isoform D).
{ECO:0000303|PubMed:10790390}.
/FTId=VSP_010285.
VAR_SEQ 403 610 AATSASATKIPPRKRGRPKTKVEDQTPKPKLLEKLQAATLN
EEASEPAVYASTTKGGVKLIFNGHLFKFSFRKADYSVFQCC
YREHGEECKVRVVCDQKRVFPYEGEHVHFMQASDKSCLPSQ
FMPGESGVISSLSPSKELLMKNTTKLEEADDKEDEDFEEFE
IQEIDEIELDEPEKTPAKEEEVDPNDFREKIKRRLQKALQN
KKK -> VKIKMEPSPTPGHSSDAAVAALAVTYLSDEESFR
KPFTLPKLLDGKFYKNIQPNQKTPGAIQATCTTCHGLISGT
TKSTGNFLSHIKRRHKELLPLCQLYCQAKANGTVPAVKSSP
PNPNHVLTSATPTPAMEMMTQVAQMPPTAAYATGPTHLGMP
VTVPVPVSMSLAMPISLPHVQTPQMMALMQQHQAHGAVFIS
KDY (in isoform E).
{ECO:0000303|PubMed:10790390,
ECO:0000303|Ref.8}.
/FTId=VSP_050699.
VAR_SEQ 403 610 AATSASATKIPPRKRGRPKTKVEDQTPKPKLLEKLQAATLN
EEASEPAVYASTTKGGVKLIFNGHLFKFSFRKADYSVFQCC
YREHGEECKVRVVCDQKRVFPYEGEHVHFMQASDKSCLPSQ
FMPGESGVISSLSPSKELLMKNTTKLEEADDKEDEDFEEFE
IQEIDEIELDEPEKTPAKEEEVDPNDFREKIKRRLQKALQN
KKK -> VVLANDEVPNPEDVLVFFTQSLRGRPAIMANGIR
FLIMSENKKKILWRCSSMATKKLKCPARITMLKETPPKFII
NKAEHLHAELKRNKYSSSKAQTLRDPHQMATKLDCEMEGAG
GVSFDLHEEELNELTHDV (in isoform F).
{ECO:0000303|PubMed:10790390}.
/FTId=VSP_050704.
VAR_SEQ 403 610 AATSASATKIPPRKRGRPKTKVEDQTPKPKLLEKLQAATLN
EEASEPAVYASTTKGGVKLIFNGHLFKFSFRKADYSVFQCC
YREHGEECKVRVVCDQKRVFPYEGEHVHFMQASDKSCLPSQ
FMPGESGVISSLSPSKELLMKNTTKLEEADDKEDEDFEEFE
IQEIDEIELDEPEKTPAKEEEVDPNDFREKIKRRLQKALQN
KKK -> ELAVFGTGQRGRTVLLFQNEKFVKNRCSASRTYW
ICSKKDVTVCRARVVTAVDKNSQERIIKCTYEHDHSRKFPS
NNVNLPVLIKREKALSLDAS (in isoform G).
{ECO:0000303|PubMed:10790390}.
/FTId=VSP_050715.
VAR_SEQ 403 610 AATSASATKIPPRKRGRPKTKVEDQTPKPKLLEKLQAATLN
EEASEPAVYASTTKGGVKLIFNGHLFKFSFRKADYSVFQCC
YREHGEECKVRVVCDQKRVFPYEGEHVHFMQASDKSCLPSQ
FMPGESGVISSLSPSKELLMKNTTKLEEADDKEDEDFEEFE
IQEIDEIELDEPEKTPAKEEEVDPNDFREKIKRRLQKALQN
KKK -> DLGELNPSNLADFGNESFLPKTKGKRPQNVRCGL
APDQKCVRTLDDWDRIRYDRTRSGDVLVYDGYRYDRRANYN
DIIYWGCAKKRLSCNVYMITHKNKPTYVAISGVHNHL (in
isoform H). {ECO:0000303|PubMed:10790390,
ECO:0000303|PubMed:9111355}.
/FTId=VSP_050716.
VAR_SEQ 403 610 AATSASATKIPPRKRGRPKTKVEDQTPKPKLLEKLQAATLN
EEASEPAVYASTTKGGVKLIFNGHLFKFSFRKADYSVFQCC
YREHGEECKVRVVCDQKRVFPYEGEHVHFMQASDKSCLPSQ
FMPGESGVISSLSPSKELLMKNTTKLEEADDKEDEDFEEFE
IQEIDEIELDEPEKTPAKEEEVDPNDFREKIKRRLQKALQN
KKK -> VCDDLDDMKGAIKHSLLTFIRGQRGCKLLAFNGH
NYVRNRRSNLKTYWICSKKGSTKCNARVVTNVVEGVHKIVL
ESCHHTCLNTERKKRLSVTNVVGKARSKSEKSVSTGFIKEE
GDEDLTLELRTLNLSIEDLNNLQ (in isoform I).
{ECO:0000303|PubMed:10790390}.
/FTId=VSP_050703.
VAR_SEQ 403 610 AATSASATKIPPRKRGRPKTKVEDQTPKPKLLEKLQAATLN
EEASEPAVYASTTKGGVKLIFNGHLFKFSFRKADYSVFQCC
YREHGEECKVRVVCDQKRVFPYEGEHVHFMQASDKSCLPSQ
FMPGESGVISSLSPSKELLMKNTTKLEEADDKEDEDFEEFE
IQEIDEIELDEPEKTPAKEEEVDPNDFREKIKRRLQKALQN
KKK -> GSVAYYSYITGFRGSRKLKIGEFSFTRNKTSGLK
TYWSCARAGVHKCKARVVTAQDHDVTIKCGQHNHPPY (in
isoform J).
{ECO:0000303|PubMed:10790390}.
/FTId=VSP_050717.
VAR_SEQ 403 610 AATSASATKIPPRKRGRPKTKVEDQTPKPKLLEKLQAATLN
EEASEPAVYASTTKGGVKLIFNGHLFKFSFRKADYSVFQCC
YREHGEECKVRVVCDQKRVFPYEGEHVHFMQASDKSCLPSQ
FMPGESGVISSLSPSKELLMKNTTKLEEADDKEDEDFEEFE
IQEIDEIELDEPEKTPAKEEEVDPNDFREKIKRRLQKALQN
KKK -> GQFIGDIPRGQWIDKHEYFFLKNQKQGFNLVFNG
YMYKKEASFRATVNWICSDGNGKRLNENKCSARAITKFDGG
IKLGKNAHNHPPRFLGGKVPAKLMPKDAFYPQY (in
isoform K).
{ECO:0000303|PubMed:10790390}.
/FTId=VSP_050718.
VAR_SEQ 403 610 AATSASATKIPPRKRGRPKTKVEDQTPKPKLLEKLQAATLN
EEASEPAVYASTTKGGVKLIFNGHLFKFSFRKADYSVFQCC
YREHGEECKVRVVCDQKRVFPYEGEHVHFMQASDKSCLPSQ
FMPGESGVISSLSPSKELLMKNTTKLEEADDKEDEDFEEFE
IQEIDEIELDEPEKTPAKEEEVDPNDFREKIKRRLQKALQN
KKK -> DRKRYSKKFLNFDGPAEFSLAAHRRPRLIIANKH
FIVHRILGKDNLIGSWRCMYHHKGCKARATTFMVDSEVKYR
STCSSHNHKNVRSQQQSLKMPWVFTD (in isoform
M). {ECO:0000303|PubMed:10790390}.
/FTId=VSP_050720.
VAR_SEQ 403 610 AATSASATKIPPRKRGRPKTKVEDQTPKPKLLEKLQAATLN
EEASEPAVYASTTKGGVKLIFNGHLFKFSFRKADYSVFQCC
YREHGEECKVRVVCDQKRVFPYEGEHVHFMQASDKSCLPSQ
FMPGESGVISSLSPSKELLMKNTTKLEEADDKEDEDFEEFE
IQEIDEIELDEPEKTPAKEEEVDPNDFREKIKRRLQKALQN
KKK -> DTEISFIRSQKKNAQLVFRNYIYNKKLTQANGQT
TWRCADVLKLRCKAVVITRDGHFIDARRQHNHESHASRIGQ
RQLYKVEQELEEYIEICTSNPKISQYLGSSNIIVTAKDGKD
CKLFLPAAEATEIEMQALVDAAEEELDEEERHAEERIRDRQ
RVGRWRTEEAKHRSLLKSEHP (in isoform N).
{ECO:0000303|PubMed:10790390}.
/FTId=VSP_050700.
VAR_SEQ 403 610 AATSASATKIPPRKRGRPKTKVEDQTPKPKLLEKLQAATLN
EEASEPAVYASTTKGGVKLIFNGHLFKFSFRKADYSVFQCC
YREHGEECKVRVVCDQKRVFPYEGEHVHFMQASDKSCLPSQ
FMPGESGVISSLSPSKELLMKNTTKLEEADDKEDEDFEEFE
IQEIDEIELDEPEKTPAKEEEVDPNDFREKIKRRLQKALQN
KKK -> EDELVFIESPWSTPCLVLNGYMYNCHSRKSNKQY
WRCHNYSKKAHEMRCRSRCVLENGRLKSVTGGLHNHQPHTE
KIDKIIQRNKMAAIGTGRKLSRTHSFTQLQLQEQKQEFIDE
HQLTSDAATLQLTDQELMHASMMLMHE (in isoform
O). {ECO:0000303|PubMed:10790390}.
/FTId=VSP_050702.
VAR_SEQ 403 610 AATSASATKIPPRKRGRPKTKVEDQTPKPKLLEKLQAATLN
EEASEPAVYASTTKGGVKLIFNGHLFKFSFRKADYSVFQCC
YREHGEECKVRVVCDQKRVFPYEGEHVHFMQASDKSCLPSQ
FMPGESGVISSLSPSKELLMKNTTKLEEADDKEDEDFEEFE
IQEIDEIELDEPEKTPAKEEEVDPNDFREKIKRRLQKALQN
KKK -> GCDGLQGSCRDRGGQKLTGANHQMHLRA (in
isoform Q).
{ECO:0000303|PubMed:10790390}.
/FTId=VSP_050721.
VAR_SEQ 403 610 AATSASATKIPPRKRGRPKTKVEDQTPKPKLLEKLQAATLN
EEASEPAVYASTTKGGVKLIFNGHLFKFSFRKADYSVFQCC
YREHGEECKVRVVCDQKRVFPYEGEHVHFMQASDKSCLPSQ
FMPGESGVISSLSPSKELLMKNTTKLEEADDKEDEDFEEFE
IQEIDEIELDEPEKTPAKEEEVDPNDFREKIKRRLQKALQN
KKK -> GTSHLATFSCTRKKKRKLVIDRHEFVMDRKLKSS
INWRCARYRSSNCKVRATTHVQKNGLEVYRLKYAKHSHL
(in isoform R).
{ECO:0000303|PubMed:10790390}.
/FTId=VSP_050722.
VAR_SEQ 403 610 AATSASATKIPPRKRGRPKTKVEDQTPKPKLLEKLQAATLN
EEASEPAVYASTTKGGVKLIFNGHLFKFSFRKADYSVFQCC
YREHGEECKVRVVCDQKRVFPYEGEHVHFMQASDKSCLPSQ
FMPGESGVISSLSPSKELLMKNTTKLEEADDKEDEDFEEFE
IQEIDEIELDEPEKTPAKEEEVDPNDFREKIKRRLQKALQN
KKK -> GLIFKAARHIAPIQKVRQVRDDKFLATIIKLEPA
GRLNLKNPDNIIRTSSNEHNFVYVGLPRMKGKCVNCLKKNR
TGLRRINTLCNTCPGSNWMCEPCFEELHS (in isoform
S). {ECO:0000303|PubMed:10790390}.
/FTId=VSP_050723.
VAR_SEQ 404 610 ATSASATKIPPRKRGRPKTKVEDQTPKPKLLEKLQAATLNE
EASEPAVYASTTKGGVKLIFNGHLFKFSFRKADYSVFQCCY
REHGEECKVRVVCDQKRVFPYEGEHVHFMQASDKSCLPSQF
MPGESGVISSLSPSKELLMKNTTKLEEADDKEDEDFEEFEI
QEIDEIELDEPEKTPAKEEEVDPNDFREKIKRRLQKALQNK
KK -> CYQLVPNRRGGKNLIFQGHMYSVERKYRNSINWVC
SKNSNSVLRCPARCVTNPESGNGIKLSHRRHNHPADAFKPH
KRCRKRPGDRK (in isoform 53.6).
{ECO:0000303|PubMed:10790390,
ECO:0000303|PubMed:11493677}.
/FTId=VSP_010286.
VAR_SEQ 404 610 ATSASATKIPPRKRGRPKTKVEDQTPKPKLLEKLQAATLNE
EASEPAVYASTTKGGVKLIFNGHLFKFSFRKADYSVFQCCY
REHGEECKVRVVCDQKRVFPYEGEHVHFMQASDKSCLPSQF
MPGESGVISSLSPSKELLMKNTTKLEEADDKEDEDFEEFEI
QEIDEIELDEPEKTPAKEEEVDPNDFREKIKRRLQKALQNK
KK -> FHIDFADSKKNGGKLLVINGFRFFRNKKRGHLQYW
KCRNYYKERCPAIAIHDESTLILRLCHQHQHTESNDIEIKP
LPGSETKLAESAEDEAQAEPEAELDNETDPDTNHEPARVPP
LIMEPPPLLEIKSKLRNQDF (in isoform AC).
{ECO:0000305}.
/FTId=VSP_034706.
VAR_SEQ 404 610 ATSASATKIPPRKRGRPKTKVEDQTPKPKLLEKLQAATLNE
EASEPAVYASTTKGGVKLIFNGHLFKFSFRKADYSVFQCCY
REHGEECKVRVVCDQKRVFPYEGEHVHFMQASDKSCLPSQF
MPGESGVISSLSPSKELLMKNTTKLEEADDKEDEDFEEFEI
QEIDEIELDEPEKTPAKEEEVDPNDFREKIKRRLQKALQNK
KK -> KDQNKGVLLKRTAQGEFLVVNGKSYKKTRAMQYRT
YFHCLTRNCPTYYVLVELSRRPRLTRHHEHAQHCLQCY
(in isoform L).
{ECO:0000303|PubMed:11493677}.
/FTId=VSP_050719.
VAR_SEQ 404 610 ATSASATKIPPRKRGRPKTKVEDQTPKPKLLEKLQAATLNE
EASEPAVYASTTKGGVKLIFNGHLFKFSFRKADYSVFQCCY
REHGEECKVRVVCDQKRVFPYEGEHVHFMQASDKSCLPSQF
MPGESGVISSLSPSKELLMKNTTKLEEADDKEDEDFEEFEI
QEIDEIELDEPEKTPAKEEEVDPNDFREKIKRRLQKALQNK
KK -> KFDYQISVDVGEATMQLANASSAGVVNSNSPFFIV
SKYGTKQIMLKQHTFNRHICRDDVTYWRCSQFAVLRCRARL
KTKLDTLTILNSEHNHEVITKARKYGSLKRQRAEAEAAARA
ERRQDPLETAATSAPATTT (in isoform P).
{ECO:0000303|PubMed:10731132,
ECO:0000303|PubMed:11493677,
ECO:0000303|Ref.8}.
/FTId=VSP_050705.
VAR_SEQ 459 610 GVKLIFNGHLFKFSFRKADYSVFQCCYREHGEECKVRVVCD
QKRVFPYEGEHVHFMQASDKSCLPSQFMPGESGVISSLSPS
KELLMKNTTKLEEADDKEDEDFEEFEIQEIDEIELDEPEKT
PAKEEEVDPNDFREKIKRRLQKALQNKKK -> DPTRPQLW
SSDVPDQPQATLLTINNFVYRANLKFFGKSNNILYWECVKT
DRLSAAVALKTIGDDLYVTNGSYSAVSKCKGHLMASFHLQM
CTITWATTSVLRRPRRLDADPQEVEFPHSRRQNPGFLENGH
RGQPRPSAQDVAASILPTQTFVFC (in isoform
mod1.8). {ECO:0000303|PubMed:7664338}.
/FTId=VSP_010289.
MUTAGEN 33 33 D->N: In allele mod(mdg4)351; embryonic
lethal; when associated with S-92.
MUTAGEN 92 92 G->S: In allele mod(mdg4)351; embryonic
lethal; when associated with N-33.
CONFLICT 151 152 QQ -> HE (in Ref. 2; AAA82988/AAA82989/
AAA82990 and 3; AAC17459). {ECO:0000305}.
CONFLICT 466 466 G -> V (in Ref. 9; AAL33875).
{ECO:0000305}.
CONFLICT 507 507 E -> K (in Ref. 1; CAA53216 and 4;
CAB85487). {ECO:0000305}.
SEQUENCE 610 AA; 67171 MW; 79CC78E52D2ADAF5 CRC64;
MADDEQFSLC WNNFNTNLSA GFHESLCRGD LVDVSLAAEG QIVKAHRLVL SVCSPFFRKM
FTQMPSNTHA IVFLNNVSHS ALKDLIQFMY CGEVNVKQDA LPAFISTAES LQIKGLTDND
PAPQPPQESS PPPAAPHVQQ QQIPAQRVQR QQPRASARYK IETVDDGLGD EKQSTTQIVI
QTTAAPQATI VQQQQPQQAA QQIQSQQLQT GTTTTATLVS TNKRSAQRSS LTPASSSAGV
KRSKTSTSAN VMDPLDSTTE TGATTTAQLV PQQITVQTSV VSAAEAKLHQ QSPQQVRQEE
AEYIDLPMEL PTKSEPDYSE DHGDAAGDAE GTYVEDDTYG DMRYDDSYFT ENEDAGNQTA
ANTSGGGVTA TTSKAVVKQQ SQNYSESSFV DTSGDQGNTE AQAATSASAT KIPPRKRGRP
KTKVEDQTPK PKLLEKLQAA TLNEEASEPA VYASTTKGGV KLIFNGHLFK FSFRKADYSV
FQCCYREHGE ECKVRVVCDQ KRVFPYEGEH VHFMQASDKS CLPSQFMPGE SGVISSLSPS
KELLMKNTTK LEEADDKEDE DFEEFEIQEI DEIELDEPEK TPAKEEEVDP NDFREKIKRR
LQKALQNKKK


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