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Cadherin-related tumor suppressor (Protein fat) [Cleaved into: Ft-mito]

 FAT_DROME               Reviewed;        5147 AA.
P33450; Q9VQX5;
01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
21-FEB-2001, sequence version 3.
22-NOV-2017, entry version 163.
RecName: Full=Cadherin-related tumor suppressor;
AltName: Full=Protein fat;
Contains:
RecName: Full=Ft-mito {ECO:0000305|PubMed:25215488};
Flags: Precursor;
Name=ft {ECO:0000312|FlyBase:FBgn0001075};
ORFNames=CG3352 {ECO:0000312|FlyBase:FBgn0001075};
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 [GENOMIC DNA].
PubMed=1959133; DOI=10.1016/0092-8674(91)90359-7;
Mahoney P.A., Weber U., Onofrechuk P., Biessmann H., Bryant P.J.,
Goodman C.S.;
"The fat tumor suppressor gene in Drosophila encodes a novel member of
the cadherin gene superfamily.";
Cell 67:853-868(1991).
[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.
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]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=11893338; DOI=10.1016/S0092-8674(02)00658-X;
Yang C.H., Axelrod J.D., Simon M.A.;
"Regulation of Frizzled by fat-like cadherins during planar polarity
signaling in the Drosophila compound eye.";
Cell 108:675-688(2002).
[5]
FUNCTION.
PubMed=12540853; DOI=10.1038/nature01366;
Ma D., Yang C.H., McNeill H., Simon M.A., Axelrod J.D.;
"Fidelity in planar cell polarity signalling.";
Nature 421:543-547(2003).
[6]
FUNCTION.
PubMed=15240556; DOI=10.1242/dev.01254;
Matakatsu H., Blair S.S.;
"Interactions between Fat and Dachsous and the regulation of planar
cell polarity in the Drosophila wing.";
Development 131:3785-3794(2004).
[7]
FUNCTION.
PubMed=15548581; DOI=10.1242/dev.01550;
Simon M.A.;
"Planar cell polarity in the Drosophila eye is directed by graded
Four-jointed and Dachsous expression.";
Development 131:6175-6184(2004).
[8]
DOMAIN.
PubMed=16687445; DOI=10.1242/dev.02401;
Matakatsu H., Blair S.S.;
"Separating the adhesive and signaling functions of the Fat and
Dachsous protocadherins.";
Development 133:2315-2324(2006).
[9]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=16996265; DOI=10.1016/j.cub.2006.09.005;
Willecke M., Hamaratoglu F., Kango-Singh M., Udan R., Chen C.L.,
Tao C., Zhang X., Halder G.;
"The fat cadherin acts through the hippo tumor-suppressor pathway to
regulate tissue size.";
Curr. Biol. 16:2090-2100(2006).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4843; SER-5054 AND
SER-5061, 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).
[11]
PHOSPHORYLATION.
PubMed=18635802; DOI=10.1126/science.1158159;
Ishikawa H.O., Takeuchi H., Haltiwanger R.S., Irvine K.D.;
"Four-jointed is a Golgi kinase that phosphorylates a subset of
cadherin domains.";
Science 321:401-404(2008).
[12]
PHOSPHORYLATION, AND CLEAVAGE.
PubMed=19574458; DOI=10.1073/pnas.0811540106;
Feng Y., Irvine K.D.;
"Processing and phosphorylation of the Fat receptor.";
Proc. Natl. Acad. Sci. U.S.A. 106:11989-11994(2009).
[13]
FUNCTION, PHOSPHORYLATION, AND MUTAGENESIS OF SER-273.
PubMed=20434335; DOI=10.1016/j.cub.2010.04.016;
Simon M.A., Xu A., Ishikawa H.O., Irvine K.D.;
"Modulation of fat:dachsous binding by the cadherin domain kinase
four-jointed.";
Curr. Biol. 20:811-817(2010).
[14]
FUNCTION.
PubMed=23667559; DOI=10.1371/journal.pone.0062998;
Zhao X., Yang C.H., Simon M.A.;
"The Drosophila Cadherin Fat regulates tissue size and planar cell
polarity through different domains.";
PLoS ONE 8:E62998-E62998(2013).
[15]
FUNCTION, SUBCELLULAR LOCATION, CLEAVAGE, DISRUPTION PHENOTYPE, AND
INTERACTION WITH ATPSYNC AND ND-24.
PubMed=25215488; DOI=10.1016/j.cell.2014.07.036;
Sing A., Tsatskis Y., Fabian L., Hester I., Rosenfeld R.,
Serricchio M., Yau N., Bietenhader M., Shanbhag R., Jurisicova A.,
Brill J.A., McQuibban G.A., McNeill H.;
"The atypical cadherin fat directly regulates mitochondrial function
and metabolic state.";
Cell 158:1293-1308(2014).
[16]
SUBCELLULAR LOCATION, INTERACTION WITH FBXL7, AND MUTAGENESIS OF
THR-4854.
PubMed=25107277; DOI=10.7554/eLife.03383;
Bosch J.A., Sumabat T.M., Hafezi Y., Pellock B.J., Gandhi K.D.,
Hariharan I.K.;
"The Drosophila F-box protein Fbxl7 binds to the protocadherin fat and
regulates Dachs localization and Hippo signaling.";
Elife 3:E03383-E03383(2014).
-!- FUNCTION: Involved in regulation of planar cell polarity in the
compound eye where it is required for correct specification of the
R3 and R4 photoreceptor cells by regulating Fz activity in the
R3/R4 precursor cells (PubMed:11893338). This is likely to occur
through creation of an ft gradient so that the equatorial R3/R4
precursor cell has a higher level of ft function than its polar
neighbor (PubMed:15548581). Also required for planar cell polarity
of wing hairs (PubMed:12540853, PubMed:15240556). Mediates
heterophilic cell adhesion in vitro and is required to stabilize
ds on the cell surface (PubMed:15240556). Involved in regulation
of eye imaginal disk size (PubMed:23667559). Upstream component of
the Hippo pathway where it is likely to act as a cell surface
receptor involved in regulation of tissue size and is required for
the localization and stability of ex (PubMed:16996265). Probably
acts as a cell surface receptor for ds (PubMed:20434335).
{ECO:0000269|PubMed:11893338, ECO:0000269|PubMed:12540853,
ECO:0000269|PubMed:15240556, ECO:0000269|PubMed:15548581,
ECO:0000269|PubMed:16996265, ECO:0000269|PubMed:20434335,
ECO:0000269|PubMed:23667559}.
-!- FUNCTION: Ft-mito: Regulates mitochondrial electron transport
chain integrity and promotes oxidative phosphorylation.
{ECO:0000269|PubMed:25215488}.
-!- SUBUNIT: Interacts with Fbxl7 (PubMed:25107277). Ft-mito interacts
with NADH dehydrogenase subunit ND-24 and with ATP synthase
subunit ATPsynC (PubMed:25215488). {ECO:0000269|PubMed:25107277,
ECO:0000269|PubMed:25215488}.
-!- INTERACTION:
Q6NN09:ATPsynC; NbExp=2; IntAct=EBI-135374, EBI-153383;
Q8IQA6:Gug; NbExp=3; IntAct=EBI-135374, EBI-153156;
Q9VX36:ND-24; NbExp=4; IntAct=EBI-135374, EBI-189196;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11893338};
Single-pass type I membrane protein {ECO:0000250}. Apical cell
membrane {ECO:0000269|PubMed:25107277}.
-!- SUBCELLULAR LOCATION: Ft-mito: Mitochondrion
{ECO:0000269|PubMed:25215488}.
-!- DOMAIN: The extracellular domain is required for correct
subcellular localization and for cell adhesion.
{ECO:0000269|PubMed:16687445}.
-!- DOMAIN: The intracellular domain is sufficient for viability,
growth control and planar cell polarity.
{ECO:0000269|PubMed:16687445}.
-!- PTM: Phosphorylated by fj on Ser/Thr of cadherin domains
(PubMed:18635802). Phosphorylation by fj enhances binding to ds
(PubMed:20434335). Phosphorylated in the cytoplasmic domain in a
dco-dependent manner which is promoted by ds (PubMed:19574458).
{ECO:0000269|PubMed:18635802, ECO:0000269|PubMed:19574458,
ECO:0000269|PubMed:20434335}.
-!- PTM: Proteolytically cleaved to yield stably associated N- and C-
terminal fragments (PubMed:19574458). The C-terminal fragment is
processed further to release a 68 kDa mitochondrial fragment, Ft-
mito (PubMed:25215488). {ECO:0000269|PubMed:19574458,
ECO:0000269|PubMed:25215488}.
-!- DISRUPTION PHENOTYPE: Severe overgrown imaginal disk derivatives
and pupal death (PubMed:16996265). Overall larval growth is
reduced (PubMed:25215488). Cells are round, swollen and have
abnormal mitochondrial cristae due to defects in assembly of the
mitochondrial electron chain complexes I and V (CI and CV)
(PubMed:25215488). Loss of CI activity results in a switch to
aerobic glycosis which increases lactate levels (PubMed:25215488).
RNAi-mediated knockdown results in dorsal-ventral inversions in
ommatidia planar cell polarity (PubMed:25215488).
{ECO:0000269|PubMed:16996265, ECO:0000269|PubMed:25215488}.
-!- MISCELLANEOUS: The name 'fat' originates from weak mutant alleles
that exhibit a broadening of the abdomen. {ECO:0000305}.
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EMBL; M80537; AAA28530.1; -; Genomic_DNA.
EMBL; AE014134; AAF51036.1; -; Genomic_DNA.
PIR; A41087; IJFFTM.
RefSeq; NP_477497.1; NM_058149.4.
UniGene; Dm.293; -.
ProteinModelPortal; P33450; -.
SMR; P33450; -.
BioGrid; 59824; 75.
DIP; DIP-21094N; -.
IntAct; P33450; 52.
MINT; MINT-1746562; -.
STRING; 7227.FBpp0077167; -.
iPTMnet; P33450; -.
PaxDb; P33450; -.
PRIDE; P33450; -.
EnsemblMetazoa; FBtr0077478; FBpp0077167; FBgn0001075.
GeneID; 33627; -.
KEGG; dme:Dmel_CG3352; -.
CTD; 33627; -.
FlyBase; FBgn0001075; ft.
eggNOG; KOG1219; Eukaryota.
eggNOG; ENOG410XPEI; LUCA.
HOGENOM; HOG000107041; -.
InParanoid; P33450; -.
KO; K16669; -.
OMA; HALLLYN; -.
OrthoDB; EOG091G000B; -.
PhylomeDB; P33450; -.
Reactome; R-DME-350379; Homo-/heterophilic binding of transmembrane components.
Reactome; R-DME-390023; Subcellular localisation of D.
Reactome; R-DME-451850; Positive regulation of FT and DS.
GenomeRNAi; 33627; -.
PRO; PR:P33450; -.
Proteomes; UP000000803; Chromosome 2L.
Bgee; FBgn0001075; -.
ExpressionAtlas; P33450; differential.
Genevisible; P33450; DM.
GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0016327; C:apicolateral plasma membrane; IDA:FlyBase.
GO; GO:0016021; C:integral component of membrane; TAS:FlyBase.
GO; GO:0005887; C:integral component of plasma membrane; IDA:FlyBase.
GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
GO; GO:0045296; F:cadherin binding; IPI:FlyBase.
GO; GO:0005509; F:calcium ion binding; IDA:FlyBase.
GO; GO:0050839; F:cell adhesion molecule binding; ISS:FlyBase.
GO; GO:0004872; F:receptor activity; ISS:FlyBase.
GO; GO:0016339; P:calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules; IDA:FlyBase.
GO; GO:0000904; P:cell morphogenesis involved in differentiation; IMP:UniProtKB.
GO; GO:0008283; P:cell proliferation; IMP:UniProtKB.
GO; GO:0098609; P:cell-cell adhesion; IMP:FlyBase.
GO; GO:0044331; P:cell-cell adhesion mediated by cadherin; IDA:FlyBase.
GO; GO:0045317; P:equator specification; IMP:UniProtKB.
GO; GO:0048105; P:establishment of body hair planar orientation; IMP:FlyBase.
GO; GO:0045198; P:establishment of epithelial cell apical/basal polarity; IMP:FlyBase.
GO; GO:0001737; P:establishment of imaginal disc-derived wing hair orientation; IMP:FlyBase.
GO; GO:0042067; P:establishment of ommatidial planar polarity; IMP:UniProtKB.
GO; GO:0001736; P:establishment of planar polarity; IMP:FlyBase.
GO; GO:0007164; P:establishment of tissue polarity; IMP:FlyBase.
GO; GO:0016336; P:establishment or maintenance of polarity of larval imaginal disc epithelium; IMP:UniProtKB.
GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; IPI:FlyBase.
GO; GO:0035329; P:hippo signaling; IGI:FlyBase.
GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; ISS:FlyBase.
GO; GO:0007446; P:imaginal disc growth; IMP:FlyBase.
GO; GO:0007447; P:imaginal disc pattern formation; IMP:UniProtKB.
GO; GO:0007476; P:imaginal disc-derived wing morphogenesis; IMP:FlyBase.
GO; GO:0090176; P:microtubule cytoskeleton organization involved in establishment of planar polarity; IMP:FlyBase.
GO; GO:0008285; P:negative regulation of cell proliferation; IMP:FlyBase.
GO; GO:0010629; P:negative regulation of gene expression; IMP:UniProtKB.
GO; GO:0045926; P:negative regulation of growth; IMP:FlyBase.
GO; GO:0035331; P:negative regulation of hippo signaling; IMP:FlyBase.
GO; GO:0045571; P:negative regulation of imaginal disc growth; IMP:FlyBase.
GO; GO:0030178; P:negative regulation of Wnt signaling pathway; TAS:FlyBase.
GO; GO:0016318; P:ommatidial rotation; TAS:FlyBase.
GO; GO:0018149; P:peptide cross-linking; IPI:UniProtKB.
GO; GO:0090251; P:protein localization involved in establishment of planar polarity; IMP:FlyBase.
GO; GO:0035209; P:pupal development; IMP:UniProtKB.
GO; GO:0040008; P:regulation of growth; IMP:FlyBase.
GO; GO:0045570; P:regulation of imaginal disc growth; IMP:UniProtKB.
GO; GO:0046620; P:regulation of organ growth; IGI:FlyBase.
GO; GO:0032880; P:regulation of protein localization; IMP:FlyBase.
GO; GO:0035159; P:regulation of tube length, open tracheal system; IMP:FlyBase.
GO; GO:0009888; P:tissue development; IMP:UniProtKB.
GO; GO:0035220; P:wing disc development; IMP:UniProtKB.
Gene3D; 4.10.900.10; -; 1.
InterPro; IPR002126; Cadherin.
InterPro; IPR015919; Cadherin-like.
InterPro; IPR020894; Cadherin_CS.
InterPro; IPR027397; Catenin_binding_dom_sf.
InterPro; IPR013320; ConA-like_dom_sf.
InterPro; IPR001881; EGF-like_Ca-bd_dom.
InterPro; IPR013032; EGF-like_CS.
InterPro; IPR000742; EGF-like_dom.
InterPro; IPR001791; Laminin_G.
Pfam; PF00028; Cadherin; 33.
Pfam; PF00008; EGF; 2.
Pfam; PF00054; Laminin_G_1; 1.
Pfam; PF02210; Laminin_G_2; 1.
PRINTS; PR00205; CADHERIN.
SMART; SM00112; CA; 34.
SMART; SM00181; EGF; 5.
SMART; SM00179; EGF_CA; 3.
SMART; SM00282; LamG; 2.
SUPFAM; SSF49313; SSF49313; 34.
SUPFAM; SSF49899; SSF49899; 3.
PROSITE; PS00232; CADHERIN_1; 22.
PROSITE; PS50268; CADHERIN_2; 34.
PROSITE; PS00022; EGF_1; 4.
PROSITE; PS01186; EGF_2; 2.
PROSITE; PS50026; EGF_3; 4.
PROSITE; PS50025; LAM_G_DOMAIN; 2.
1: Evidence at protein level;
Calcium; Cell adhesion; Cell membrane; Complete proteome;
Disulfide bond; EGF-like domain; Glycoprotein; Membrane;
Mitochondrion; Phosphoprotein; Receptor; Reference proteome; Repeat;
Signal; Transmembrane; Transmembrane helix.
SIGNAL 1 35 {ECO:0000255}.
CHAIN 36 5147 Cadherin-related tumor suppressor.
/FTId=PRO_0000004015.
CHAIN ? 5147 Ft-mito. {ECO:0000269|PubMed:25215488}.
/FTId=PRO_0000434022.
TOPO_DOM 36 4583 Extracellular. {ECO:0000255}.
TRANSMEM 4584 4609 Helical. {ECO:0000255}.
TOPO_DOM 4610 5147 Cytoplasmic. {ECO:0000255}.
DOMAIN 36 156 Cadherin 1. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 157 270 Cadherin 2. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 271 382 Cadherin 3. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 383 494 Cadherin 4. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 495 599 Cadherin 5. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 600 708 Cadherin 6. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 709 820 Cadherin 7. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 821 942 Cadherin 8. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 943 1049 Cadherin 9. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 1050 1153 Cadherin 10. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 1154 1278 Cadherin 11. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 1279 1384 Cadherin 12. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 1385 1489 Cadherin 13. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 1490 1601 Cadherin 14. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 1602 1713 Cadherin 15. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 1714 1823 Cadherin 16. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 1824 1922 Cadherin 17. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 1923 2027 Cadherin 18. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 2028 2167 Cadherin 19. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 2168 2278 Cadherin 20. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 2279 2385 Cadherin 21. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 2386 2491 Cadherin 22. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 2492 2596 Cadherin 23. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 2597 2703 Cadherin 24. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 2704 2810 Cadherin 25. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 2811 2913 Cadherin 26. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 2914 3013 Cadherin 27. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 3014 3124 Cadherin 28. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 3125 3229 Cadherin 29. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 3230 3334 Cadherin 30. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 3335 3439 Cadherin 31. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 3440 3545 Cadherin 32. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 3546 3651 Cadherin 33. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 3652 3756 Cadherin 34. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 3950 4011 EGF-like 1. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 4013 4049 EGF-like 2. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 4052 4090 EGF-like 3. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 4092 4128 EGF-like 4. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 4129 4320 Laminin G-like 1. {ECO:0000255|PROSITE-
ProRule:PRU00122}.
DOMAIN 4321 4362 EGF-like 5. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 4402 4569 Laminin G-like 2. {ECO:0000255|PROSITE-
ProRule:PRU00122}.
REGION 4744 4771 Essential for stability of mitochondrial
electron chain complexes I and V, and
promotes interaction with ND-24.
{ECO:0000269|PubMed:25215488}.
MOD_RES 4843 4843 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 5054 5054 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 5061 5061 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
CARBOHYD 239 239 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 257 257 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 276 276 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 280 280 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 402 402 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 461 461 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 605 605 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 631 631 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1155 1155 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1367 1367 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1458 1458 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1751 1751 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1831 1831 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1880 1880 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2080 2080 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2171 2171 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2247 2247 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2290 2290 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2437 2437 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2581 2581 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2799 2799 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2920 2920 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2946 2946 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2967 2967 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3167 3167 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3303 3303 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3386 3386 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3389 3389 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3525 3525 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3852 3852 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3865 3865 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3905 3905 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 4306 4306 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 4414 4414 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 4471 4471 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 4487 4487 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 4539 4539 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 4550 4550 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 3954 3966 {ECO:0000250}.
DISULFID 3960 3999 {ECO:0000250}.
DISULFID 4001 4010 {ECO:0000250}.
DISULFID 4017 4028 {ECO:0000250}.
DISULFID 4022 4037 {ECO:0000250}.
DISULFID 4039 4048 {ECO:0000250}.
DISULFID 4056 4067 {ECO:0000250}.
DISULFID 4061 4078 {ECO:0000250}.
DISULFID 4080 4089 {ECO:0000250}.
DISULFID 4096 4107 {ECO:0000250}.
DISULFID 4101 4116 {ECO:0000250}.
DISULFID 4118 4127 {ECO:0000250}.
DISULFID 4294 4320 {ECO:0000250}.
DISULFID 4325 4341 {ECO:0000250}.
DISULFID 4334 4350 {ECO:0000250}.
DISULFID 4352 4361 {ECO:0000250}.
DISULFID 4536 4569 {ECO:0000250}.
VARIANT 1229 1229 S -> G.
VARIANT 1233 1233 G -> S.
MUTAGEN 273 273 S->A,D: Blocks ability of fj to enhance
binding to ds.
{ECO:0000269|PubMed:20434335}.
MUTAGEN 4854 4854 T->I: In ft61; strong overgrowth of eye
imaginal disks. Binding to Fbxl7 is not
affected. {ECO:0000269|PubMed:25107277}.
CONFLICT 676 676 S -> P (in Ref. 1; AAA28530).
{ECO:0000305}.
CONFLICT 718 718 A -> T (in Ref. 1; AAA28530).
{ECO:0000305}.
CONFLICT 889 889 T -> S (in Ref. 1; AAA28530).
{ECO:0000305}.
CONFLICT 1298 1298 T -> M (in Ref. 1; AAA28530).
{ECO:0000305}.
CONFLICT 1338 1338 G -> A (in Ref. 1; AAA28530).
{ECO:0000305}.
CONFLICT 1366 1366 S -> T (in Ref. 1; AAA28530).
{ECO:0000305}.
CONFLICT 1408 1408 A -> G (in Ref. 1; AAA28530).
{ECO:0000305}.
CONFLICT 1755 1755 T -> V (in Ref. 1; AAA28530).
{ECO:0000305}.
CONFLICT 2168 2168 I -> V (in Ref. 1; AAA28530).
{ECO:0000305}.
CONFLICT 2266 2266 I -> V (in Ref. 1; AAA28530).
{ECO:0000305}.
CONFLICT 2665 2665 H -> T (in Ref. 1; AAA28530).
{ECO:0000305}.
CONFLICT 2712 2712 A -> T (in Ref. 1; AAA28530).
{ECO:0000305}.
CONFLICT 2816 2816 N -> T (in Ref. 1; AAA28530).
{ECO:0000305}.
CONFLICT 2893 2893 M -> L (in Ref. 1; AAA28530).
{ECO:0000305}.
CONFLICT 3359 3359 A -> T (in Ref. 1; AAA28530).
{ECO:0000305}.
CONFLICT 3674 3674 I -> M (in Ref. 1; AAA28530).
{ECO:0000305}.
CONFLICT 3722 3722 I -> V (in Ref. 1; AAA28530).
{ECO:0000305}.
CONFLICT 3869 3869 Y -> N (in Ref. 1; AAA28530).
{ECO:0000305}.
CONFLICT 4187 4187 G -> D (in Ref. 1; AAA28530).
{ECO:0000305}.
CONFLICT 4309 4309 L -> S (in Ref. 1; AAA28530).
{ECO:0000305}.
SEQUENCE 5147 AA; 564791 MW; 6A5A4743FC7E07D0 CRC64;
MERLLLLFFL LLAGRESLCQ TGDTKLELLA PRGRSYATTY EQYAAFPRRR SSSSSPSGEM
QSRAVDTSAD FEVLEGQPRG TTVGFIPTKP KFSYRFNEPP REFTLDPVTG EVKTNVVLDR
EGMRDHYDLV VLSSQPTYPI EVRIKVLDVN DNSPEFPEPS IAISFSESAT SGTRLLLDAA
TDADVGENGV TDQYEIVAGN VDNKFRLVTT ANPSGDTSYL HLETTGNLDR ESRGSYQLNI
SARDGGSPPR FGYLQVNVTI LDVNDNPPIF DHSDYNVSLN ETALPGTPVV TVMASDNDLG
DNSKITYYLA ETEHQFTVNP ETGVISTTER VNCPQQTNVK SSASQKSCVF TVFARDHGSP
RQDGRTYVTV NLLDTNDHDP IISFRFFPDG GKVATVDENA VNGTVVAAVA VKDSDSGLNG
RTSVRIVSGN ELGHFRLEEA ADLHIVRVNG VLDREEIGKY NLTVVAMDQG TPARTTTAHL
IIDVNDVNDH EPVFEKSEYS AVLSELAPTG SFVASITATD EDTGVNAQVH YDILSGNELK
WFSMDPLTGL IVTTGPLDRE IRDTVELSIS ARDGGPNPKF AYTQLKVIIL DENDEAPQFS
QREQNVTLGE DAPPQTIVAL MTATDHDQGT NGSVTFALAP SVERLYPLQF ALDALTGQLT
TRRPLDREKM SQYEISVIAR DQGAPTPQSA TATVWLNVAD VNDNDPQFYP RHYIYSLADD
DDDIKLKKEV EKERILLHVT ASDKDDGDNA LIEYRLESGG EGLFQLDARS GAISLRGDAP
ASMHWKPHYK LLVSARDAGQ RRSQQDAIVE IVLKSKLEML ECGQAQAGGY EFQMVEDHEQ
QRNSQPNREV GIVQVKSTNG KANSHIEYDI IQGDRAQNFR IDTRSGRITT ARPLDREEQA
NYRLTILASS SSSSSAAASS VSYGQCIVNI AIIDLNDNAP VFALDRESEP TISLPENAAV
GQEIYLSRVR DRDAGVNSRI SYSLTNNPNQ QFRIGPVTGV LYLQRPIRAE PGSLIHVELM
ATDAGSPPLS SKLSLSVLIA DVNDHTPVFD HTSYETSLPE TTKVNTRFFA LAATDIDLGD
NGRISYEIIE GNTERMFGVF PDGYLFVRAP LDREERDYYA LTVSCRDAGQ PSRSSVVPVV
IHVIDENDNA PQFTNSTFTF SIPENAPADT FVGKLTAVDR DIGRNAELSF TLSSQTQDFT
IDTRNGFIKT LRPFDREALV KVSRNAEASG EDGSLRGSMA GNYMLLEATV SDNGIPRLQD
KVKVKVIVTD VNDNAPEFLR APYHVTISEG ASEGTHITHV FTQDADEGLN GDVYYSLAKG
NEAGQFNLDS ATGQLSLGRR LDRESQEIHH LIVVAKDAAL KHPLSSNASI TIVVLDENDN
APEFTQSSSE VSVLETSPTG TELMRFRASD ADQGVNSQVV FSISAGNRRD TFHIDSITGS
LYLHKPLDYE DITSYTLNIT ASDCGTPSLS TTVLYNVLVV DDNDNPPIFP STAIVRQIKE
GIPLKTPIVT VTADDPDSGL NGKVSYAISK QEPQLPQGRH FGINTETGVI HTLREIDRES
IDTFRLTVVA TDRAQPSERQ LSTEKLVTVI VEDINDNAPV FVSMNAAILP PKFSTSKGSS
TAVMQVHAKD ADSSSNGLVT YEIVSGPQEL FKLQRNTGII TFTPGPQFKQ EVRYQLTLKS
TDEAVQSERR SSEVYITIIT PGSGGSESSV PQFEQRSKLS GSVYENEPIG TSILTVTAHL
ASAEIEYFVT NVTATGSRGQ VDRLFDIDAK LGILSTAAEL DREAGPEEYE VEVYAIALGG
QPRTSRTKVR VTVLDKNDSP PQFLDTPFVY NVSEDLQIGH TISTLRAHDP DTLGSVTFLL
MDGHDGKFLL EPSTGKLILN DTLDRETKSK YELRIRVSDG VQYTEAYATI QVSDTNDNPP
LFEDTVYSFD IPENAQRGYQ VGQIVARDAD LGQNAQLSYG VVSDWANDVF SLNPQTGMLT
LTARLDYEEV QHYILIVQAQ DNGQPSLSTT ITVYCNVLDL NDNAPIFDPM SYSSEVFENV
PIATEVVTVS AKDIDSGNNG LIEYSITAGD VDSEFGIDSN GTIRTRRNLD REHRSTYTLT
VTARDCADEF ASFSELEETQ LKLKYRSPRK YQQTRQEFLA HQKQQRLSST VKVTILIKDV
NDEVPVFISA NETAIMENVA INTVVIAVKA VDNDEGRNGY IDYLMKEARD EDMGQSDPLP
FSLNPTDGQL RVVDALDREL RSSYLLNITA RDRGEPPQST ESQLLIRILD ENDNSPVFDP
KQYSASVAEN ASIGAMVLQV SATDVDEGAN GRIRYSIVLG DQNHDFSISE DTGVVRVAKN
LNYERLSRYS LTVRAEDCAL ENPAGDTAEL TINILDINDN RPTFLDSPYL ARVMENTVPP
NGGYVLTVNA YDADTPPLNS QVRYFLKEGD SDLFRINASS GDIALLKPLD REQQSEYTLT
LVAMDTGSPP LTGTGIVRVE VQDINDNDPV FELQSYHATV RENLPSGTHV LTPRATDKDE
GLNAKLRFNL LGEHMHRFHI DSETGEISTA TTLDREETSV YHLTLMAQDS SITEPRASSV
NLTISVSDVN DNIPKFDSTT YNVAVPERIS KGEFVFGARA LDLDDGENAV VHYTISGRDQ
HYFDINTKTG VVSTKLELKT KTKSHDDLTY TIVISAMDQG EQSLSSKAEL TVILRPPELF
PTFAYMANSH FAMSEDVRPG KMITKVSATS PKKGLVGKIR YAIAGGIMGD SLRVDPNSGL
LSVGQDGLDY ELTHLYEIWI EAADGDTPSL RSVTLITLNV TDANDNAPVM EQLIYNAEVL
EEESPPQLIA VVKASDRDSG DNGNVIYRLQ NDFDGTFEIT ESGEIYTRMR LDREEIGDYA
FVVEAVDQGV PHMTGTASVL LHLLDKNDNP PKFTRLFSLN VTENAEIGSF VIRVTSSDLD
LGANANASYS FSENPGEKFR IEPQSGNITV AGHLDREQQD EYILKVVASD GAWRAETPIT
ITIQDQNDNA PEFEHSFYSF SFPELQQSIA LVGQIIATDR DKQGPNSVIS YSLQQPSPMF
SIDPATGEVF SKKAVRFKHS QYVRSPENMY ALTVLATDNG KPPLYSECLV NINIVDAHNN
PPKFEQAEYL APLPQDAVRG QRIVRVHAND KQDLGTNEMD YSLMTFNLSS IFSVGRHDGW
ITLVKPIQVP PNTRYELVVR ATDRGVPPQS DETRVVIVVT GENMDTPRFS VNSYQVIVPE
NEPVGSTILT VGATDDDTGP NGMLRYSISG GNERQDFSVD ERTGGIVIQQ QLDYDLIQEY
HLNITVQDLG YHPLSSVAML TIILTDVNDN PPVFNHKEYH CYIPENKPVG TFVFQAHAAD
KDSPKNAIIH YAFLPSGPDR HFFIMNQSNG TISSAVSFDY EERRIYTLQI KAKNPDSSME
SYANLYVHVL GVNEFYPQFL QPVFHFDVSE TSAVGTRVGA VQATDKDSGE DGRVYYLLVG
SSNDKGFRID TNTGLIYVAR HLDRETQNRV VLTVMAKNYG SIRGNDTDEA QVIISIQDGN
DPPEFIKHYY TSTISEAAPV GTKVTTVKAI DKDVRTQNNQ FSYSIINGNL KQSFKIDVQT
GEISTASRLD REETSTYNLV IGAIDTGLPP QTGSATVHIE LEDVNDNGPT FTPEGLNGYI
SENEPAGTSI MTLIASDPDL PRNGGPFTYQ LIGGKHKSWL SVDRNSGVVR STTSFDREMT
PILEAIIEVE DSGKPKQKSQ HLLTITVLDQ NDNPSTTRSL HIAVSLFNGD LPSNVKLADV
RPNDIDIVGD YRCRLQKNPA QSQLQLAIPR ACDLITTSHT TPIASVFSYT GNDGKHGDVS
SKVSVAFQSF NNETLANSVS IMVRNMTAYH FLANHYRPIL EMIKSRMSNE DEVILYSLLE
GGSGNSTNLQ LLMAVRLAKT SYQQPKYLIE RLREKRSAFS ELLQKEVIVG YEPCSEPDVC
ENGGVCSATM RLLDAHSFVI QDSPALVLSG PRVVHDYSCQ CTSGFSGEQC SRRQDPCLPN
PCHSQVQCRR LGSDFQCMCP ANRDGKHCEK ERSDVCYSKP CRNGGSCQRS PDGSSYFCLC
RPGFRGNQCE SVSDSCRPNP CLHGGLCVSL KPGYKCNCTP GRYGRHCERF SYGFQPLSYM
TFPALDVTTN DISIVFATTK PNSLLLYNYG MQSGGRSDFL AIELVHGRAY FSSGGARTAI
STVIAGRNLA DGGWHKVTAT RNGRVMSLSV AKCADSGDVC TECLPGDSSC YADEVGPVGT
LNFNKQPLMI GGLSSADPIL ERPGQVHSDD LVGCLHSVHI GGRALNLSLP LQQKGILAGC
NRQACQPALA AERCGGFAGQ CIDRWSSSLC QCGGHLQSPD CSDSLEPITL GEGAFVEFRI
SEIYRRMQLL DNLYNSKSAW LDNQQMRERR AVSNFSTASQ IYEAPKMLSM LFRTYKDQGQ
ILYAATNQMF TSLSLREGRL VYYSKQHLTI NMTVQETSTL NDGKWHNVSL FSESRSLRLI
VDGRQVGDEL DIAGVHDFLD PYLTILNVGG EAFVGCLANV TVNNELQPLN GSGSIFPEVR
YHGKIESGCR GDIGQDAAQV ADPLSIGFTL VIVFFVILVV AILGSYVIYR FRGKQEKIGS
LSCGVPGFKI KHPGGPVTQS QVDHVLVRNL HPSEAPSPPV GAGDHMRPPV GSHHLVGPEL
LTKKFKEPTA EMPQPQQQQQ RPQRPDIIER ESPLIREDHH LPIPPLHPLP LEHASSVDMG
SEYPEHYDLE NASSIAPSDI DIVYHYKGYR EAAGLRKYKA SVPPVSAYTH HKHQNSGSQQ
QQQQHRHTAP FVTRNQGGQP PPPPTSASRT HQSTPLARLS PSSELSSQQP RILTLHDISG
KPLQSALLAT TSSSGGVGKD VHSNSERSLN SPVMSQLSGQ SSSASRQKPG VPQQQAQQTS
MGLTAEEIER LNGRPRTCSL ISTLDAVSSS SEAPRVSSSA LHMSLGGDVD AHSSTSTDES
GNDSFTCSEI EYDNNSLSGD GKYSTSKSLL DGRSPVSRAL SGGETSRNPP TTVVKTPPIP
PHAYDGFESS FRGSLSTLVA SDDDIANHLS GIYRKANGAA SPSATTLGWE YLLNWGPSYE
NLMGVFKDIA ELPDTNGPSQ QQQQQTQVVS TLRMPSSNGP AAPEEYV


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