Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Actin cytoskeleton-regulatory complex protein END3 (Endocytosis protein 3)

 END3_YEAST              Reviewed;         349 AA.
P39013; D6W195; Q8TFC4; Q8TFD0; Q8TG51;
01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
01-FEB-1995, sequence version 1.
05-DEC-2018, entry version 162.
RecName: Full=Actin cytoskeleton-regulatory complex protein END3;
AltName: Full=Endocytosis protein 3;
Name=END3; OrderedLocusNames=YNL084C; ORFNames=N2307;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=7841519; DOI=10.1091/mbc.5.9.1023;
Benedetti H., Raths S., Crausaz F., Riezman H.;
"The END3 gene encodes a protein that is required for the
internalization step of endocytosis and for actin cytoskeleton
organization in yeast.";
Mol. Biol. Cell 5:1023-1037(1994).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS GLU-245; ASN-258 AND
ASN-268.
STRAIN=ATCC 200060 / W303, S96, SK1, YJM 1129, YJM 269, YJM 270,
YJM 280, YJM 320, YJM 326, YJM 339, YJM 421, YJM 627, and YJM 789;
PubMed=11907579; DOI=10.1038/416326a;
Steinmetz L.M., Sinha H., Richards D.R., Spiegelman J.I., Oefner P.J.,
McCusker J.H., Davis R.W.;
"Dissecting the architecture of a quantitative trait locus in yeast.";
Nature 416:326-330(2002).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ASN-268.
STRAIN=SK1;
PubMed=16273108; DOI=10.1038/ng1674;
Deutschbauer A.M., Davis R.W.;
"Quantitative trait loci mapped to single-nucleotide resolution in
yeast.";
Nat. Genet. 37:1333-1340(2005).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 96604 / S288c / FY1679;
PubMed=8740422;
DOI=10.1002/(SICI)1097-0061(199604)12:5<485::AID-YEA928>3.0.CO;2-U;
Soler-Mira A., Saiz J.E., Ballesta J.P.G., Remacha M.A.;
"The sequence of a 17,933 bp segment of Saccharomyces cerevisiae
chromosome XIV contains the RHO2, TOP2, MKT1 and END3 genes and five
new open reading frames.";
Yeast 12:485-491(1996).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169873;
Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F.,
Doignon F., Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M.,
Fritz C., Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N.,
Goffeau A., Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D.,
Hilbert H., Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A.,
Jonniaux J.-L., Karpfinger-Hartl L., Lanfranchi G., Lepingle A.,
Levesque H., Lyck R., Maftahi M., Mallet L., Maurer C.T.C.,
Messenguy F., Mewes H.-W., Moestl D., Nasr F., Nicaud J.-M.,
Niedenthal R.K., Pandolfo D., Pierard A., Piravandi E., Planta R.J.,
Pohl T.M., Purnelle B., Rebischung C., Remacha M.A., Revuelta J.L.,
Rinke M., Saiz J.E., Sartorello F., Scherens B., Sen-Gupta M.,
Soler-Mira A., Urbanus J.H.M., Valle G., Van Dyck L., Verhasselt P.,
Vierendeels F., Vissers S., Voet M., Volckaert G., Wach A.,
Wambutt R., Wedler H., Zollner A., Hani J.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV
and its evolutionary implications.";
Nature 387:93-98(1997).
[6]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[7]
FUNCTION.
PubMed=8380177; DOI=10.1083/jcb.120.1.55;
Raths S., Rohrer J., Crausaz F., Riezman H.;
"END3 and END4: two mutants defective in receptor-mediated and fluid-
phase endocytosis in Saccharomyces cerevisiae.";
J. Cell Biol. 120:55-65(1993).
[8]
FUNCTION.
PubMed=8144575;
Volland C., Urban-Grimal D., Geraud G., Haguenauer-Tsapis R.;
"Endocytosis and degradation of the yeast uracil permease under
adverse conditions.";
J. Biol. Chem. 269:9833-9841(1994).
[9]
FUNCTION.
PubMed=7865884; DOI=10.1091/mbc.5.11.1185;
Berkower C., Loayza D., Michaelis S.;
"Metabolic instability and constitutive endocytosis of STE6, the a-
factor transporter of Saccharomyces cerevisiae.";
Mol. Biol. Cell 5:1185-1198(1994).
[10]
FUNCTION.
PubMed=7852314; DOI=10.1074/jbc.270.6.2525;
Lai K., Bolognese C.P., Swift S., McGraw P.;
"Regulation of inositol transport in Saccharomyces cerevisiae involves
inositol-induced changes in permease stability and endocytic
degradation in the vacuole.";
J. Biol. Chem. 270:2525-2534(1995).
[11]
FUNCTION.
PubMed=8991091; DOI=10.1083/jcb.135.6.1789;
Tan P.K., Howard J.P., Payne G.S.;
"The sequence NPFXD defines a new class of endocytosis signal in
Saccharomyces cerevisiae.";
J. Cell Biol. 135:1789-1800(1996).
[12]
FUNCTION.
PubMed=8741841; DOI=10.1091/mbc.7.1.81;
Robinson K.S., Lai K., Cannon T.A., McGraw P.;
"Inositol transport in Saccharomyces cerevisiae is regulated by
transcriptional and degradative endocytic mechanisms during the growth
cycle that are distinct from inositol-induced regulation.";
Mol. Biol. Cell 7:81-89(1996).
[13]
FUNCTION.
PubMed=9128251; DOI=10.1083/jcb.137.2.399;
Ayscough K.R., Stryker J., Pokala N., Sanders M., Crews P.,
Drubin D.G.;
"High rates of actin filament turnover in budding yeast and roles for
actin in establishment and maintenance of cell polarity revealed using
the actin inhibitor latrunculin-A.";
J. Cell Biol. 137:399-416(1997).
[14]
FUNCTION.
PubMed=9243513; DOI=10.1091/mbc.8.7.1361;
Moreau V., Galan J.-M., Devilliers G., Haguenauer-Tsapis R.,
Winsor B.;
"The yeast actin-related protein Arp2p is required for the
internalization step of endocytosis.";
Mol. Biol. Cell 8:1361-1375(1997).
[15]
FUNCTION, AND IDENTIFICATION IN THE PAN1 COMPLEX.
PubMed=9234686; DOI=10.1128/MCB.17.8.4294;
Tang H.-Y., Munn A., Cai M.;
"EH domain proteins Pan1p and End3p are components of a complex that
plays a dual role in organization of the cortical actin cytoskeleton
and endocytosis in Saccharomyces cerevisiae.";
Mol. Cell. Biol. 17:4294-4304(1997).
[16]
DOMAINS.
PubMed=9822599; DOI=10.1093/emboj/17.22.6541;
Paoluzi S., Castagnoli L., Lauro I., Salcini A.E., Coda L., Fre' S.,
Confalonieri S., Pelicci P.G., Di Fiore P.P., Cesareni G.;
"Recognition specificity of individual EH domains of mammals and
yeast.";
EMBO J. 17:6541-6550(1998).
[17]
FUNCTION.
PubMed=9436999; DOI=10.1091/mbc.9.1.173;
Prescianotto-Baschong C., Riezman H.;
"Morphology of the yeast endocytic pathway.";
Mol. Biol. Cell 9:173-189(1998).
[18]
FUNCTION.
PubMed=9885245; DOI=10.1083/jcb.144.1.71;
Zeng G., Cai M.;
"Regulation of the actin cytoskeleton organization in yeast by a novel
serine/threonine kinase Prk1p.";
J. Cell Biol. 144:71-82(1999).
[19]
FUNCTION.
PubMed=10954428;
Gagny B., Wiederkehr A., Dumoulin P., Winsor B., Riezman H.,
Haguenauer-Tsapis R.;
"A novel EH domain protein of Saccharomyces cerevisiae, Ede1p,
involved in endocytosis.";
J. Cell Sci. 113:3309-3319(2000).
[20]
FUNCTION, AND IDENTIFICATION IN THE PAN1 COMPLEX.
PubMed=10594004; DOI=10.1128/MCB.20.1.12-25.2000;
Tang H.-Y., Xu J., Cai M.;
"Pan1p, End3p, and Sla1p, three yeast proteins required for normal
cortical actin cytoskeleton organization, associate with each other
and play essential roles in cell wall morphogenesis.";
Mol. Cell. Biol. 20:12-25(2000).
[21]
FUNCTION.
PubMed=10972812; DOI=10.1046/j.1365-2958.2000.02063.x;
Eisfeld K., Riffer F., Mentges J., Schmitt M.J.;
"Endocytotic uptake and retrograde transport of a virally encoded
killer toxin in yeast.";
Mol. Microbiol. 37:926-940(2000).
[22]
INTERACTION WITH PAN1, AND IDENTIFICATION IN THE PAN1 COMPLEX.
PubMed=11739778; DOI=10.1091/mbc.12.12.3759;
Zeng G., Yu X., Cai M.;
"Regulation of yeast actin cytoskeleton-regulatory complex
Pan1p/Sla1p/End3p by serine/threonine kinase Prk1p.";
Mol. Biol. Cell 12:3759-3772(2001).
[23]
INTERACTION WITH YAP1802.
PubMed=11940605; DOI=10.1083/jcb.200110027;
Howard J.P., Hutton J.L., Olson J.M., Payne G.S.;
"Sla1p serves as the targeting signal recognition factor for
NPFX(1,2)D-mediated endocytosis.";
J. Cell Biol. 157:315-326(2002).
[24]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
PubMed=14562095; DOI=10.1038/nature02026;
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
Weissman J.S., O'Shea E.K.;
"Global analysis of protein localization in budding yeast.";
Nature 425:686-691(2003).
[25]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[26]
FUNCTION.
PubMed=15248838; DOI=10.1042/BJ20040392;
Aouida M., Leduc A., Wang H., Ramotar D.;
"Characterization of a transport and detoxification pathway for the
antitumour drug bleomycin in Saccharomyces cerevisiae.";
Biochem. J. 384:47-58(2004).
[27]
FUNCTION.
PubMed=15944351; DOI=10.1534/genetics.105.041459;
Morishita M., Engebrecht J.;
"End3p-mediated endocytosis is required for spore wall formation in
Saccharomyces cerevisiae.";
Genetics 170:1561-1574(2005).
[28]
FUNCTION.
PubMed=16914733; DOI=10.1128/MCB.00117-06;
Gourlay C.W., Ayscough K.R.;
"Actin-induced hyperactivation of the Ras signaling pathway leads to
apoptosis in Saccharomyces cerevisiae.";
Mol. Cell. Biol. 26:6487-6501(2006).
[29]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=ADR376;
PubMed=17330950; DOI=10.1021/pr060559j;
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
Elias J.E., Gygi S.P.;
"Large-scale phosphorylation analysis of alpha-factor-arrested
Saccharomyces cerevisiae.";
J. Proteome Res. 6:1190-1197(2007).
[30]
INTERACTION WITH SLA2.
PubMed=17151356; DOI=10.1091/mbc.E06-09-0788;
Toshima J., Toshima J.Y., Duncan M.C., Cope M.J.T.V., Sun Y.,
Martin A.C., Anderson S., Yates J.R. III, Mizuno K., Drubin D.G.;
"Negative regulation of yeast Eps15-like Arp2/3 complex activator,
Pan1p, by the Hip1R-related protein, Sla2p, during endocytosis.";
Mol. Biol. Cell 18:658-668(2007).
[31]
INTERACTION WITH SCD5.
PubMed=17898076; DOI=10.1091/mbc.E07-06-0607;
Zeng G., Huang B., Neo S.P., Wang J., Cai M.;
"Scd5p mediates phosphoregulation of actin and endocytosis by the type
1 phosphatase Glc7p in yeast.";
Mol. Biol. Cell 18:4885-4898(2007).
[32]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-276, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth
phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
[33]
SUBCELLULAR LOCATION.
PubMed=18298676; DOI=10.1111/j.1600-0854.2008.00726.x;
Toret C.P., Lee L., Sekiya-Kawasaki M., Drubin D.G.;
"Multiple pathways regulate endocytic coat disassembly in
Saccharomyces cerevisiae for optimal downstream trafficking.";
Traffic 9:848-859(2008).
[34]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19779198; DOI=10.1126/science.1172867;
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
"Global analysis of Cdk1 substrate phosphorylation sites provides
insights into evolution.";
Science 325:1682-1686(2009).
-!- FUNCTION: Component of the PAN1 actin cytoskeleton-regulatory
complex required for the internalization of endosomes during
actin-coupled endocytosis. The complex links the site of
endocytosis to the cell membrane-associated actin cytoskeleton.
Mediates uptake of external molecules and vacuolar degradation of
plasma membrane proteins. Plays a role in the proper organization
of the cell membrane-associated actin cytoskeleton and promotes
its destabilization. END3 regulates PAN1 function by preventing
phosphorylation of PAN1 by PKR1 and is also involved in the
correct localization of SLA1 to the cell cortex, in the bipolar
budding of diploid cells and the correct distribution of chitin at
the cell surface. {ECO:0000269|PubMed:10594004,
ECO:0000269|PubMed:10954428, ECO:0000269|PubMed:10972812,
ECO:0000269|PubMed:15248838, ECO:0000269|PubMed:15944351,
ECO:0000269|PubMed:16914733, ECO:0000269|PubMed:7841519,
ECO:0000269|PubMed:7852314, ECO:0000269|PubMed:7865884,
ECO:0000269|PubMed:8144575, ECO:0000269|PubMed:8380177,
ECO:0000269|PubMed:8741841, ECO:0000269|PubMed:8991091,
ECO:0000269|PubMed:9128251, ECO:0000269|PubMed:9234686,
ECO:0000269|PubMed:9243513, ECO:0000269|PubMed:9436999,
ECO:0000269|PubMed:9885245}.
-!- SUBUNIT: Component of the PAN1 actin cytoskeleton-regulatory
complex composed of at least END3, PAN1, and SLA1. Interacts with
SCD5, SLA2 and YAP1802. Interacts directly with PAN1; the
interaction with PAN1 is prevented by PAN1 phosphorylation by
PKR1. {ECO:0000269|PubMed:10594004, ECO:0000269|PubMed:11739778,
ECO:0000269|PubMed:11940605, ECO:0000269|PubMed:17151356,
ECO:0000269|PubMed:17898076, ECO:0000269|PubMed:9234686}.
-!- INTERACTION:
P32521:PAN1; NbExp=9; IntAct=EBI-6460, EBI-12875;
P32790:SLA1; NbExp=4; IntAct=EBI-6460, EBI-17313;
-!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein;
Cytoplasmic side. Endosome membrane; Peripheral membrane protein;
Cytoplasmic side. Cytoplasm, cytoskeleton, actin patch.
Note=Cytoplasmic and cortical actin patches.
-!- MISCELLANEOUS: Present with 2610 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the END3 family. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; X79473; CAA55981.1; -; Genomic_DNA.
EMBL; AF458969; AAM00520.1; -; Genomic_DNA.
EMBL; AF458970; AAM00526.1; -; Genomic_DNA.
EMBL; AF458971; AAM00532.1; -; Genomic_DNA.
EMBL; AF458972; AAM00538.1; -; Genomic_DNA.
EMBL; AF458973; AAM00544.1; -; Genomic_DNA.
EMBL; AF458974; AAM00550.1; -; Genomic_DNA.
EMBL; AF458975; AAM00556.1; -; Genomic_DNA.
EMBL; AF458976; AAM00562.1; -; Genomic_DNA.
EMBL; AF458977; AAM00568.1; -; Genomic_DNA.
EMBL; AF458978; AAM00574.1; -; Genomic_DNA.
EMBL; AF458979; AAM00580.1; -; Genomic_DNA.
EMBL; AF458980; AAM00586.1; -; Genomic_DNA.
EMBL; AF458981; AAM00592.1; -; Genomic_DNA.
EMBL; DQ115393; AAZ22524.1; -; Genomic_DNA.
EMBL; X89016; CAA61426.1; -; Genomic_DNA.
EMBL; Z71360; CAA95959.1; -; Genomic_DNA.
EMBL; BK006947; DAA10461.1; -; Genomic_DNA.
PIR; S57538; S57538.
RefSeq; NP_014315.1; NM_001182922.1.
ProteinModelPortal; P39013; -.
BioGrid; 35739; 339.
ComplexPortal; CPX-426; PAN1 actin cytoskeleton-regulatory complex.
DIP; DIP-2220N; -.
IntAct; P39013; 18.
MINT; P39013; -.
STRING; 4932.YNL084C; -.
iPTMnet; P39013; -.
MaxQB; P39013; -.
PaxDb; P39013; -.
PRIDE; P39013; -.
EnsemblFungi; YNL084C_mRNA; YNL084C_mRNA; YNL084C.
GeneID; 855640; -.
KEGG; sce:YNL084C; -.
SGD; S000005028; END3.
HOGENOM; HOG000076607; -.
InParanoid; P39013; -.
KO; K20048; -.
OMA; DWYISPT; -.
OrthoDB; EOG092C4EUW; -.
BioCyc; YEAST:G3O-33113-MONOMER; -.
PRO; PR:P39013; -.
Proteomes; UP000002311; Chromosome XIV.
GO; GO:0030479; C:actin cortical patch; TAS:SGD.
GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0030674; F:protein binding, bridging; IPI:SGD.
GO; GO:0000147; P:actin cortical patch assembly; TAS:SGD.
GO; GO:0007015; P:actin filament organization; TAS:SGD.
GO; GO:0030476; P:ascospore wall assembly; IMP:SGD.
GO; GO:0007121; P:bipolar cellular bud site selection; TAS:SGD.
GO; GO:0006897; P:endocytosis; IMP:SGD.
CDD; cd00052; EH; 1.
InterPro; IPR011992; EF-hand-dom_pair.
InterPro; IPR018247; EF_Hand_1_Ca_BS.
InterPro; IPR002048; EF_hand_dom.
InterPro; IPR000261; EH_dom.
InterPro; IPR025604; End3.
Pfam; PF12763; EF-hand_4; 1.
Pfam; PF12761; End3; 2.
SMART; SM00027; EH; 2.
SUPFAM; SSF47473; SSF47473; 2.
PROSITE; PS00018; EF_HAND_1; 1.
PROSITE; PS50222; EF_HAND_2; 2.
PROSITE; PS50031; EH; 2.
1: Evidence at protein level;
Actin-binding; Cell membrane; Coiled coil; Complete proteome;
Cytoplasm; Cytoskeleton; Endocytosis; Endosome; Membrane;
Phosphoprotein; Reference proteome; Repeat.
CHAIN 1 349 Actin cytoskeleton-regulatory complex
protein END3.
/FTId=PRO_0000073648.
DOMAIN 8 98 EH 1. {ECO:0000255|PROSITE-
ProRule:PRU00077}.
DOMAIN 130 222 EH 2. {ECO:0000255|PROSITE-
ProRule:PRU00077}.
REPEAT 276 295 1.
REPEAT 315 334 2.
REGION 96 105 Polyphosphoinositide (PIP2)-binding.
{ECO:0000255}.
REGION 276 334 2 X 20 AA approximate repeats.
COILED 307 349 {ECO:0000255}.
COMPBIAS 53 64 Asp/Glu-rich (acidic).
MOD_RES 276 276 Phosphoserine.
{ECO:0000244|PubMed:18407956}.
VARIANT 245 245 D -> E (in strain: YJM 421).
{ECO:0000269|PubMed:11907579}.
VARIANT 258 258 S -> N (in strain: YJM 280, YJM 320, YJM
326, YJM 627, YJM 789 and YJM 1129).
{ECO:0000269|PubMed:11907579}.
VARIANT 268 268 D -> N (in strain: SK1, YJM 269, YJM 270,
YJM 280, YJM 320, YJM 326, YJM 339, YJM
421, YJM 627, YJM 789 and YJM 1129).
{ECO:0000269|PubMed:11907579,
ECO:0000269|PubMed:16273108}.
SEQUENCE 349 AA; 40297 MW; 0F6709AFF15B84EF CRC64;
MPKLEQFEIK KYWQIFSGLK PIENKVNHDQ VLPILYNSKL DSSVLNKIWF LADIDDDDNL
DFEEFVICMR LIFDMVNKNI SSVPDELPDW LIPGSKVNLI KERKKRKQIE NADLPPKKEI
KVDWYMSPDD LNQYEKIYNS CAKLTDGTIT FNELSTKLST KFFNISKTDL NKVWSLINPQ
NLPSIDRDPT FYFIHCLRQR NDLGAEIPAS LPNSLAEVCN KKQLSYDLRS SQPPTKRKEE
ANEVDNLRDN GQNSSSDSSG SNVLSNEDSI KQKYASLTDD QVANMREQLE GLLNYKKSEK
TQGGSKLSKR INIRSITDDL DNIEQQVEVL ENYLNNKRHE LQALQAEIN


Related products :

Catalog number Product name Quantity
28-124 EPLIN is a cytoskeleton-associated protein that inhibits actin filament depolymerization and cross-links filaments in bundles. EPLIN is a cytoskeleton-associated protein that inhibits actin filament d 0.05 mg
EIAAB05289 Actin regulatory protein CAP-G,Actin-capping protein GCAP39,Capg,Macrophage-capping protein,Mbh1,Mouse,Mus musculus,Myc basic motif homolog 1
27-647 HS1 which is hematopoietic lineage cell-specific protein 1, is a substrate of protein tyrosine kinases in lymphocytes, it binds to F-actin, and promotes Arp2_3 complex-mediated actin polymerization. H 0.1 mg
30-801 WASF3 is a member of the Wiskott-Aldrich syndrome protein family. It is a protein that forms a multiprotein complex that links receptor kinases and actin. Binding to actin occurs through a C-terminal 0.05 mg
30-802 WASF3 is a member of the Wiskott-Aldrich syndrome protein family. It is a protein that forms a multiprotein complex that links receptor kinases and actin. Binding to actin occurs through a C-terminal 0.05 mg
30-793 ARPC3 is one of seven subunits of the human Arp2_3 protein complex. The Arp2_3 protein complex has been implicated in the control of actin polymerization in cells and has been conserved through evolut 0.05 mg
27-191 ARPC2 is one of seven subunits of the human Arp2_3 protein complex. The Arp2_3 protein complex has been implicated in the control of actin polymerization in cells and has been conserved through evolut 0.05 mg
26-557 ANKRA2 contains 3 ANK repeats. It may facilitate endocytosis by linking megalin to components of the cytoskeleton or endocytic machinery. 0.05 mg
26-936 CDC42EP4 is a member of the CDC42-binding protein family. Members of this family interact with Rho family GTPases and regulate the organization of the actin cytoskeleton. The protein has been shown to 0.05 mg
25-094 AVIL is a member of the gelsolin_villin family of actin regulatory proteins. This protein has structural similarity to villin. It binds actin and may play a role in the development of neuronal cells t 0.05 mg
25-452 AVIL is a member of the gelsolin_villin family of actin regulatory proteins. This protein has structural similarity to villin. It binds actin and may play a role in the development of neuronal cells t 0.05 mg
15-288-22527F Macrophage capping protein - Actin-regulatory protein CAP-G Polyclonal 0.1 mg
15-288-22527F Macrophage capping protein - Actin-regulatory protein CAP-G Polyclonal 0.05 mg
EIAAB05288 Actin regulatory protein CAP-G,Capg,Macrophage-capping protein,Rat,Rattus norvegicus
EIAAB05290 Actin regulatory protein CAP-G,Bos taurus,Bovine,CAPG,Macrophage-capping protein
10-288-22527F Macrophage capping protein - Actin-regulatory protein CAP-G 0.1 mg
10-288-22527F Macrophage capping protein - Actin-regulatory protein CAP-G 0.05 mg
EIAAB41519 Ckap1,Cytoskeleton-associated protein 1,Cytoskeleton-associated protein CKAPI,Mouse,Mus musculus,Tbcb,Tubulin-folding cofactor B,Tubulin-specific chaperone B
EIAAB41520 Bos taurus,Bovine,CKAP1,Cytoskeleton-associated protein 1,Cytoskeleton-associated protein CKAPI,TBCB,Tubulin-folding cofactor B,Tubulin-specific chaperone B
EIAAB41521 CG22,CKAP1,Cytoskeleton-associated protein 1,Cytoskeleton-associated protein CKAPI,Homo sapiens,Human,TBCB,Tubulin-folding cofactor B,Tubulin-specific chaperone B
EIAAB05287 Actin regulatory protein CAP-G,AFCP,CAPG,Homo sapiens,Human,Macrophage-capping protein,MCP
EIAAB30958 HKMT1098,Homo sapiens,Human,KIAA1949,Phostensin,Protein phosphatase 1 F-actin cytoskeleton-targeting subunit
AP1G1 AP1AR Gene adaptor-related protein complex 1 associated regulatory protein
30-178 NCAPH is a member of the barr family and a regulatory subunit of the condensin complex. This complex is required for the conversion of interphase chromatin into condensed chromosomes. The protein is a 0.05 mg
26-111 NCAPH is a member of the barr family and a regulatory subunit of the condensin complex. This complex is required for the conversion of interphase chromatin into condensed chromosomes. The protein is a 0.05 mg


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur | Gentaur





GENTAUR Ltd.
Unicorn House, Station Cl
Hertfordshire, Potters Bar EN6 1TL
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017
RIB 30004 00187 00010092253 10
BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG
IBAN FR76 3000 4001 8700 0100 9225 310
france@gentaur.com | Gentaur | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: +49 0241 40 08 90 86, +49 0241 95 78 94 78, +49 0241 40 08 90 86
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur | Gentaur