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

Protein transport protein SEC24 (Abnormal nuclear morphology 1)

 SEC24_YEAST             Reviewed;         926 AA.
P40482; D6VVH8;
01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
01-FEB-1995, sequence version 1.
27-SEP-2017, entry version 162.
RecName: Full=Protein transport protein SEC24;
AltName: Full=Abnormal nuclear morphology 1;
Name=SEC24; Synonyms=ANU1; OrderedLocusNames=YIL109C;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169870;
Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D.,
Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N.,
Harris D.E., Horsnell T., Hunt S., Jagels K., Jones M., Lye G.,
Moule S., Odell C., Pearson D., Rajandream M.A., Rice P., Rowley N.,
Skelton J., Smith V., Walsh S.V., Whitehead S., Barrell B.G.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome IX.";
Nature 387:84-87(1997).
[2]
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).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=17322287; DOI=10.1101/gr.6037607;
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A.,
Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F.,
Williamson J., Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G.,
Kolodner R.D., LaBaer J.;
"Approaching a complete repository of sequence-verified protein-
encoding clones for Saccharomyces cerevisiae.";
Genome Res. 17:536-543(2007).
[4]
PROTEIN SEQUENCE OF 731-740 AND 774-793, INTERACTION WITH SED5, AND
MUTAGENESIS OF CYS-231.
PubMed=10097109; DOI=10.1073/pnas.96.7.3751;
Peng R., Grabowski R., De Antoni A., Gallwitz D.;
"Specific interaction of the yeast cis-Golgi syntaxin Sed5p and the
coat protein complex II component Sec24p of endoplasmic reticulum-
derived transport vesicles.";
Proc. Natl. Acad. Sci. U.S.A. 96:3751-3756(1999).
[5]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=8548805; DOI=10.1016/0092-8674(95)90144-2;
Bednarek S.Y., Ravazzola M., Hosobuchi M., Amherdt M., Perrelet A.,
Schekman R.W., Orci L.;
"COPI- and COPII-coated vesicles bud directly from the endoplasmic
reticulum in yeast.";
Cell 83:1183-1196(1995).
[6]
INTERACTION WITH SEC16.
PubMed=8930902; DOI=10.1091/mbc.7.11.1815;
Gimeno R.E., Espenshade P.J., Kaiser C.A.;
"COPII coat subunit interactions: Sec24p and Sec23p bind to adjacent
regions of Sec16p.";
Mol. Biol. Cell 7:1815-1823(1996).
[7]
IDENTIFICATION IN THE COPII COAT, AND INTERACTION WITH SEC16.
PubMed=9325247; DOI=10.1074/jbc.272.41.25413;
Shaywitz D.A., Espenshade P.J., Gimeno R.E., Kaiser C.A.;
"COPII subunit interactions in the assembly of the vesicle coat.";
J. Biol. Chem. 272:25413-25416(1997).
[8]
FUNCTION.
PubMed=9023343; DOI=10.1073/pnas.94.3.837;
Campbell J.L., Schekman R.W.;
"Selective packaging of cargo molecules into endoplasmic reticulum-
derived COPII vesicles.";
Proc. Natl. Acad. Sci. U.S.A. 94:837-842(1997).
[9]
SUBUNIT, AND SUBCELLULAR LOCATION.
PubMed=9568718; DOI=10.1016/S0092-8674(00)81577-9;
Matsuoka K., Orci L., Amherdt M., Bednarek S.Y., Hamamoto S.,
Schekman R.W., Yeung T.;
"COPII-coated vesicle formation reconstituted with purified coat
proteins and chemically defined liposomes.";
Cell 93:263-275(1998).
[10]
FUNCTION OF THE SEC23/24 COMPLEX.
PubMed=9428766; DOI=10.1038/34438;
Kuehn M.J., Herrmann J.M., Schekman R.W.;
"COPII-cargo interactions direct protein sorting into ER-derived
transport vesicles.";
Nature 391:187-190(1998).
[11]
INTERACTION WITH BET1; BOS1; SAR1 AND SEC23.
PubMed=9685263; DOI=10.1126/science.281.5377.698;
Springer S., Schekman R.W.;
"Nucleation of COPII vesicular coat complex by endoplasmic reticulum
to Golgi vesicle SNAREs.";
Science 281:698-700(1998).
[12]
FUNCTION OF THE SEC23/24 COMPLEX.
PubMed=10198022;
Penalver E., Lucero P., Moreno E., Lagunas R.;
"Clathrin and two components of the COPII complex, Sec23p and Sec24p,
could be involved in endocytosis of the Saccharomyces cerevisiae
maltose transporter.";
J. Bacteriol. 181:2555-2563(1999).
[13]
INTERACTION WITH SHR3.
PubMed=10564255; DOI=10.1091/mbc.10.11.3549;
Gilstring C.F., Melin-Larsson M., Ljungdahl P.O.;
"Shr3p mediates specific COPII coatomer-cargo interactions required
for the packaging of amino acid permeases into ER-derived transport
vesicles.";
Mol. Biol. Cell 10:3549-3565(1999).
[14]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=10753972; DOI=10.1074/jbc.275.15.11521;
Peng R., De Antoni A., Gallwitz D.;
"Evidence for overlapping and distinct functions in protein transport
of coat protein Sec24p family members.";
J. Biol. Chem. 275:11521-11528(2000).
[15]
FUNCTION.
PubMed=10749860; DOI=10.1074/jbc.M000751200;
Higashio H., Kimata Y., Kiriyama T., Hirata A., Kohno K.;
"Sfb2p, a yeast protein related to Sec24p, can function as a
constituent of COPII coats required for vesicle budding from the
endoplasmic reticulum.";
J. Biol. Chem. 275:17900-17908(2000).
[16]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH PMA1.
PubMed=11086000; DOI=10.1083/jcb.151.5.973;
Shimoni Y., Kurihara T., Ravazzola M., Amherdt M., Orci L.,
Schekman R.W.;
"Lst1p and Sec24p cooperate in sorting of the plasma membrane ATPase
into COPII vesicles in Saccharomyces cerevisiae.";
J. Cell Biol. 151:973-984(2000).
[17]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=10720463; DOI=10.1006/meth.2000.0955;
Matsuoka K., Schekman R.W.;
"The use of liposomes to study COPII- and COPI-coated vesicle
formation and membrane protein sorting.";
Methods 20:417-428(2000).
[18]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=10712514; DOI=10.1091/mbc.11.3.983;
Kurihara T., Hamamoto S., Gimeno R.E., Kaiser C.A., Schekman R.W.,
Yoshihisa T.;
"Sec24p and Iss1p function interchangeably in transport vesicle
formation from the endoplasmic reticulum in Saccharomyces
cerevisiae.";
Mol. Biol. Cell 11:983-998(2000).
[19]
INTERACTION WITH SYS1.
PubMed=11726510; DOI=10.1093/emboj/20.23.6742;
Votsmeier C., Gallwitz D.;
"An acidic sequence of a putative yeast Golgi membrane protein binds
COPII and facilitates ER export.";
EMBO J. 20:6742-6750(2001).
[20]
INTERACTION WITH EMP24 AND ERV25.
PubMed=11560939; DOI=10.1074/jbc.M108113200;
Belden W.J., Barlowe C.;
"Distinct roles for the cytoplasmic tail sequences of Emp24p and
Erv25p in transport between the endoplasmic reticulum and Golgi
complex.";
J. Biol. Chem. 276:43040-43048(2001).
[21]
IDENTIFICATION IN THE COPII COAT.
PubMed=11389436; DOI=10.1038/35078500;
Antonny B., Madden D.T., Hamamoto S., Orci L., Schekman R.W.;
"Dynamics of the COPII coat with GTP and stable analogues.";
Nat. Cell Biol. 3:531-537(2001).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-178, AND 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).
[23]
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).
[24]
ELECTRON MICROSCOPY OF THE SEC23/24 COMPLEX.
PubMed=11535824; DOI=10.1073/pnas.191359398;
Lederkremer G.Z., Cheng Y., Petre B.M., Vogan E., Springer S.,
Schekman R.W., Walz T., Kirchhausen T.;
"Structure of the Sec23p/24p and Sec13p/31p complexes of COPII.";
Proc. Natl. Acad. Sci. U.S.A. 98:10704-10709(2001).
[25]
ELECTRON MICROSCOPY OF THE SEC23/24 COMPLEX.
PubMed=11717432; DOI=10.1073/pnas.241522198;
Matsuoka K., Schekman R.W., Orci L., Heuser J.E.;
"Surface structure of the COPII-coated vesicle.";
Proc. Natl. Acad. Sci. U.S.A. 98:13705-13709(2001).
[26]
SUBCELLULAR LOCATION.
PubMed=12235121; DOI=10.1083/jcb.200207053;
Supek F., Madden D.T., Hamamoto S., Orci L., Schekman R.W.;
"Sec16p potentiates the action of COPII proteins to bud transport
vesicles.";
J. Cell Biol. 158:1029-1038(2002).
[27]
STRUCTURE OF THE COPII COMPLEX.
PubMed=12671686; DOI=10.1038/sj.embor.embor812;
Antonny B., Gounon P., Schekman R.W., Orci L.;
"Self-assembly of minimal COPII cages.";
EMBO Rep. 4:419-424(2003).
[28]
FUNCTION, INTERACTION WITH BET1 AND SYS1, AND MUTAGENESIS OF ARG-230;
ARG-235; ARG-559; ARG-561 AND LEU-616.
PubMed=12941277; DOI=10.1016/S0092-8674(03)00609-3;
Miller E.A., Beilharz T.H., Malkus P.N., Lee M.C.S., Hamamoto S.,
Orci L., Schekman R.W.;
"Multiple cargo binding sites on the COPII subunit Sec24p ensure
capture of diverse membrane proteins into transport vesicles.";
Cell 114:497-509(2003).
[29]
FUNCTION.
PubMed=12655150; DOI=10.1247/csf.28.49;
Hamasaki M., Noda T., Ohsumi Y.;
"The early secretory pathway contributes to autophagy in yeast.";
Cell Struct. Funct. 28:49-54(2003).
[30]
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).
[31]
INTERACTION WITH SEC23.
PubMed=12778054; DOI=10.1038/ncb1003;
Cohen M., Stutz F., Belgareh N., Haguenauer-Tsapis R., Dargemont C.;
"Ubp3 requires a cofactor, Bre5, to specifically de-ubiquitinate the
COPII protein, Sec23.";
Nat. Cell Biol. 5:661-667(2003).
[32]
COPII COMPLEX ASSEMBLY, AND FUNCTION OF THE COPII COMPLEX.
PubMed=14627716; DOI=10.1074/jbc.C300457200;
Sato K., Nakano A.;
"Reconstitution of coat protein complex II (COPII) vesicle formation
from cargo-reconstituted proteoliposomes reveals the potential role of
GTP hydrolysis by Sar1p in protein sorting.";
J. Biol. Chem. 279:1330-1335(2004).
[33]
FUNCTION, AND INTERACTION WITH GRH1.
PubMed=16269340; DOI=10.1016/j.cell.2005.08.031;
Schuldiner M., Collins S.R., Thompson N.J., Denic V., Bhamidipati A.,
Punna T., Ihmels J., Andrews B., Boone C., Greenblatt J.F.,
Weissman J.S., Krogan N.J.;
"Exploration of the function and organization of the yeast early
secretory pathway through an epistatic miniarray profile.";
Cell 123:507-519(2005).
[34]
INTERACTION WITH GHR1.
PubMed=17261844; DOI=10.1083/jcb.200607151;
Behnia R., Barr F.A., Flanagan J.J., Barlowe C., Munro S.;
"The yeast orthologue of GRASP65 forms a complex with a coiled-coil
protein that contributes to ER to Golgi traffic.";
J. Cell Biol. 176:255-261(2007).
[35]
X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) IN COMPLEX WITH SEC23 AND ZINC.
PubMed=12239560; DOI=10.1038/nature01040;
Bi X., Corpina R.A., Goldberg J.;
"Structure of the Sec23/24-Sar1 pre-budding complex of the COPII
vesicle coat.";
Nature 419:271-277(2002).
[36]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 117-926 IN COMPLEX WITH SED5;
SYS1; BET1 AND ZINC, AND INTERACTION WITH SEC22.
PubMed=12941276; DOI=10.1016/S0092-8674(03)00608-1;
Mossessova E., Bickford L.C., Goldberg J.;
"SNARE selectivity of the COPII coat.";
Cell 114:483-495(2003).
-!- FUNCTION: Component of the coat protein complex II (COPII) which
promotes the formation of transport vesicles from the endoplasmic
reticulum (ER). The coat has two main functions, the physical
deformation of the endoplasmic reticulum membrane into vesicles
and the selection of cargo molecules. SEC24 specifically recruits
cargo proteins like BET1 or SYS1 to the COPII vesicles. The
SEC23/24 complex is also involved in internalisation of plasma
membrane proteins like the maltose transporter.
{ECO:0000269|PubMed:10198022, ECO:0000269|PubMed:10712514,
ECO:0000269|PubMed:10720463, ECO:0000269|PubMed:10749860,
ECO:0000269|PubMed:10753972, ECO:0000269|PubMed:11086000,
ECO:0000269|PubMed:12655150, ECO:0000269|PubMed:12941277,
ECO:0000269|PubMed:14627716, ECO:0000269|PubMed:16269340,
ECO:0000269|PubMed:8548805, ECO:0000269|PubMed:9023343,
ECO:0000269|PubMed:9428766}.
-!- SUBUNIT: The COPII coat is composed of at least 7 proteins: the
SEC23/24 complex, the SEC13/31 complex, SFB2, SFB3 and the protein
SAR1. Interacts with BET1, EMP24, GRH1, SEC22, SED5 and SYS1.
{ECO:0000269|PubMed:10097109, ECO:0000269|PubMed:10564255,
ECO:0000269|PubMed:11086000, ECO:0000269|PubMed:11389436,
ECO:0000269|PubMed:11560939, ECO:0000269|PubMed:11726510,
ECO:0000269|PubMed:12239560, ECO:0000269|PubMed:12778054,
ECO:0000269|PubMed:12941276, ECO:0000269|PubMed:12941277,
ECO:0000269|PubMed:16269340, ECO:0000269|PubMed:17261844,
ECO:0000269|PubMed:8930902, ECO:0000269|PubMed:9325247,
ECO:0000269|PubMed:9568718, ECO:0000269|PubMed:9685263}.
-!- INTERACTION:
O43186:CRX (xeno); NbExp=3; IntAct=EBI-16592, EBI-748171;
Q5JST6:EFHC2 (xeno); NbExp=3; IntAct=EBI-16592, EBI-2349927;
Q9UPT5-1:EXOC7 (xeno); NbExp=3; IntAct=EBI-16592, EBI-6251402;
Q04410:GRH1; NbExp=5; IntAct=EBI-16592, EBI-32083;
O76081-6:RGS20 (xeno); NbExp=3; IntAct=EBI-16592, EBI-10178530;
P15303:SEC23; NbExp=5; IntAct=EBI-16592, EBI-16584;
P38968:SEC31; NbExp=4; IntAct=EBI-16592, EBI-20524;
P48775:TDO2 (xeno); NbExp=3; IntAct=EBI-16592, EBI-743494;
Q9BYV6-2:TRIM55 (xeno); NbExp=3; IntAct=EBI-16592, EBI-11522718;
Q5T124-6:UBXN11 (xeno); NbExp=3; IntAct=EBI-16592, EBI-11524408;
Q9Y2W2:WBP11 (xeno); NbExp=3; IntAct=EBI-16592, EBI-714455;
Q96BR9:ZBTB8A (xeno); NbExp=3; IntAct=EBI-16592, EBI-742740;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:8548805}.
Cytoplasmic vesicle, COPII-coated vesicle membrane
{ECO:0000269|PubMed:10720463, ECO:0000269|PubMed:10753972,
ECO:0000269|PubMed:11086000, ECO:0000269|PubMed:12235121,
ECO:0000269|PubMed:8548805, ECO:0000269|PubMed:9568718};
Peripheral membrane protein {ECO:0000269|PubMed:11086000,
ECO:0000269|PubMed:8548805}; Cytoplasmic side
{ECO:0000269|PubMed:8548805}. Endoplasmic reticulum membrane
{ECO:0000269|PubMed:10712514, ECO:0000269|PubMed:8548805};
Peripheral membrane protein; Cytoplasmic side. Golgi apparatus
membrane {ECO:0000305|PubMed:8548805}; Peripheral membrane protein
{ECO:0000305}; Cytoplasmic side {ECO:0000305}.
-!- SIMILARITY: Belongs to the SEC23/SEC24 family. SEC24 subfamily.
{ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; Z38125; CAA86271.1; -; Genomic_DNA.
EMBL; AY692888; AAT92907.1; -; Genomic_DNA.
EMBL; BK006942; DAA08444.1; -; Genomic_DNA.
PIR; S48463; S48463.
RefSeq; NP_012157.3; NM_001179457.3.
PDB; 1M2V; X-ray; 2.75 A; B=1-926.
PDB; 1PCX; X-ray; 2.50 A; A=117-926.
PDB; 1PD0; X-ray; 2.60 A; A=117-926.
PDB; 1PD1; X-ray; 2.60 A; A=117-926.
PDB; 4BZI; EM; 23.00 A; E/F/L/M/N/O=1-926.
PDBsum; 1M2V; -.
PDBsum; 1PCX; -.
PDBsum; 1PD0; -.
PDBsum; 1PD1; -.
PDBsum; 4BZI; -.
ProteinModelPortal; P40482; -.
SMR; P40482; -.
BioGrid; 34882; 236.
DIP; DIP-2233N; -.
IntAct; P40482; 34.
MINT; MINT-476513; -.
STRING; 4932.YIL109C; -.
iPTMnet; P40482; -.
MaxQB; P40482; -.
PRIDE; P40482; -.
EnsemblFungi; YIL109C; YIL109C; YIL109C.
GeneID; 854697; -.
KEGG; sce:YIL109C; -.
EuPathDB; FungiDB:YIL109C; -.
SGD; S000001371; SEC24.
GeneTree; ENSGT00590000082962; -.
HOGENOM; HOG000196365; -.
InParanoid; P40482; -.
KO; K14007; -.
OMA; QNFLSQV; -.
OrthoDB; EOG092C0DKG; -.
BioCyc; YEAST:G3O-31364-MONOMER; -.
Reactome; R-SCE-204005; COPII (Coat Protein 2) Mediated Vesicle Transport.
Reactome; R-SCE-5694530; Cargo concentration in the ER.
Reactome; R-SCE-983170; Antigen Presentation: Folding, assembly and peptide loading of class I MHC.
EvolutionaryTrace; P40482; -.
PRO; PR:P40482; -.
Proteomes; UP000002311; Chromosome IX.
GO; GO:0030127; C:COPII vesicle coat; IDA:SGD.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
GO; GO:0005048; F:signal sequence binding; IMP:SGD.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0090110; P:cargo loading into COPII-coated vesicle; IDA:SGD.
GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
GO; GO:0016236; P:macroautophagy; IMP:SGD.
Gene3D; 3.40.20.10; -; 1.
Gene3D; 3.40.50.410; -; 1.
InterPro; IPR029006; ADF-H/Gelsolin-like_dom.
InterPro; IPR007123; Gelsolin-like_dom.
InterPro; IPR006900; Sec23/24_helical_dom.
InterPro; IPR006896; Sec23/24_trunk_dom.
InterPro; IPR012990; Sec23_24_beta_S.
InterPro; IPR002035; VWF_A.
InterPro; IPR006895; Znf_Sec23_Sec24.
Pfam; PF00626; Gelsolin; 1.
Pfam; PF08033; Sec23_BS; 1.
Pfam; PF04815; Sec23_helical; 1.
Pfam; PF04811; Sec23_trunk; 1.
Pfam; PF04810; zf-Sec23_Sec24; 1.
SUPFAM; SSF53300; SSF53300; 1.
SUPFAM; SSF81811; SSF81811; 1.
SUPFAM; SSF82754; SSF82754; 1.
SUPFAM; SSF82919; SSF82919; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Cytoplasm; Cytoplasmic vesicle;
Direct protein sequencing; Endoplasmic reticulum; ER-Golgi transport;
Golgi apparatus; Membrane; Metal-binding; Phosphoprotein;
Protein transport; Reference proteome; Transport; Zinc.
CHAIN 1 926 Protein transport protein SEC24.
/FTId=PRO_0000205150.
REGION 231 256 Zinc finger-like.
COMPBIAS 110 114 Poly-Gln.
COMPBIAS 157 160 Poly-Pro.
METAL 231 231 Zinc. {ECO:0000269|PubMed:12239560,
ECO:0000269|PubMed:12941276}.
METAL 234 234 Zinc. {ECO:0000269|PubMed:12239560,
ECO:0000269|PubMed:12941276}.
METAL 253 253 Zinc. {ECO:0000269|PubMed:12239560,
ECO:0000269|PubMed:12941276}.
METAL 256 256 Zinc. {ECO:0000269|PubMed:12239560,
ECO:0000269|PubMed:12941276}.
MOD_RES 178 178 Phosphoserine.
{ECO:0000244|PubMed:17330950}.
MUTAGEN 230 230 R->A: Abolishes binding to and packaging
of cargo protein BET1.
{ECO:0000269|PubMed:12941277}.
MUTAGEN 231 231 C->S: Lethal.
{ECO:0000269|PubMed:10097109}.
MUTAGEN 235 235 R->A: Abolishes binding to and packaging
of cargo protein BET1.
{ECO:0000269|PubMed:12941277}.
MUTAGEN 559 559 R->M: Abolishes binding to and packaging
of cargo protein BET1.
{ECO:0000269|PubMed:12941277}.
MUTAGEN 561 561 R->M: Abolishes binding to and packaging
of cargo protein BET1.
{ECO:0000269|PubMed:12941277}.
MUTAGEN 616 616 L->W: Abolishes binding to and packaging
of cargo protein BET1.
{ECO:0000269|PubMed:12941277}.
HELIX 64 72 {ECO:0000244|PDB:1M2V}.
STRAND 140 142 {ECO:0000244|PDB:1PCX}.
HELIX 143 145 {ECO:0000244|PDB:1PCX}.
HELIX 151 155 {ECO:0000244|PDB:1PCX}.
HELIX 165 167 {ECO:0000244|PDB:1PCX}.
STRAND 168 170 {ECO:0000244|PDB:1PCX}.
HELIX 173 175 {ECO:0000244|PDB:1PCX}.
TURN 179 181 {ECO:0000244|PDB:1PCX}.
STRAND 182 192 {ECO:0000244|PDB:1PCX}.
HELIX 193 199 {ECO:0000244|PDB:1PCX}.
STRAND 204 207 {ECO:0000244|PDB:1PCX}.
STRAND 212 214 {ECO:0000244|PDB:1PCX}.
TURN 232 234 {ECO:0000244|PDB:1PCX}.
STRAND 243 245 {ECO:0000244|PDB:1PCX}.
TURN 246 249 {ECO:0000244|PDB:1PCX}.
STRAND 250 252 {ECO:0000244|PDB:1PCX}.
TURN 254 256 {ECO:0000244|PDB:1PCX}.
STRAND 259 261 {ECO:0000244|PDB:1PCX}.
HELIX 264 267 {ECO:0000244|PDB:1PCX}.
HELIX 277 279 {ECO:0000244|PDB:1PCX}.
HELIX 281 284 {ECO:0000244|PDB:1PCX}.
STRAND 286 291 {ECO:0000244|PDB:1PCX}.
HELIX 294 296 {ECO:0000244|PDB:1PCX}.
STRAND 305 311 {ECO:0000244|PDB:1PCX}.
HELIX 314 319 {ECO:0000244|PDB:1PCX}.
HELIX 321 332 {ECO:0000244|PDB:1PCX}.
TURN 333 335 {ECO:0000244|PDB:1PCX}.
STRAND 344 358 {ECO:0000244|PDB:1PCX}.
HELIX 362 364 {ECO:0000244|PDB:1PCX}.
STRAND 374 376 {ECO:0000244|PDB:1PCX}.
TURN 390 392 {ECO:0000244|PDB:1PCX}.
STRAND 393 395 {ECO:0000244|PDB:1PCX}.
TURN 396 399 {ECO:0000244|PDB:1PCX}.
HELIX 400 413 {ECO:0000244|PDB:1PCX}.
TURN 414 416 {ECO:0000244|PDB:1PCX}.
HELIX 424 435 {ECO:0000244|PDB:1PCX}.
TURN 436 438 {ECO:0000244|PDB:1PCX}.
STRAND 440 448 {ECO:0000244|PDB:1PCX}.
HELIX 471 475 {ECO:0000244|PDB:1M2V}.
HELIX 482 492 {ECO:0000244|PDB:1PCX}.
STRAND 495 505 {ECO:0000244|PDB:1PCX}.
HELIX 509 517 {ECO:0000244|PDB:1PCX}.
TURN 518 520 {ECO:0000244|PDB:1PCX}.
STRAND 523 527 {ECO:0000244|PDB:1PCX}.
HELIX 534 549 {ECO:0000244|PDB:1PCX}.
STRAND 554 562 {ECO:0000244|PDB:1PCX}.
STRAND 566 576 {ECO:0000244|PDB:1PCX}.
STRAND 578 587 {ECO:0000244|PDB:1PCX}.
STRAND 594 600 {ECO:0000244|PDB:1PCX}.
STRAND 606 618 {ECO:0000244|PDB:1PCX}.
TURN 620 622 {ECO:0000244|PDB:1M2V}.
STRAND 624 637 {ECO:0000244|PDB:1PCX}.
HELIX 639 644 {ECO:0000244|PDB:1PCX}.
HELIX 648 665 {ECO:0000244|PDB:1PCX}.
HELIX 668 689 {ECO:0000244|PDB:1PCX}.
STRAND 696 699 {ECO:0000244|PDB:1M2V}.
STRAND 702 704 {ECO:0000244|PDB:1PCX}.
HELIX 705 707 {ECO:0000244|PDB:1PCX}.
HELIX 710 718 {ECO:0000244|PDB:1PCX}.
TURN 721 723 {ECO:0000244|PDB:1PCX}.
HELIX 730 742 {ECO:0000244|PDB:1PCX}.
HELIX 745 752 {ECO:0000244|PDB:1PCX}.
STRAND 755 758 {ECO:0000244|PDB:1PCX}.
TURN 759 761 {ECO:0000244|PDB:1M2V}.
HELIX 791 793 {ECO:0000244|PDB:1PD0}.
STRAND 799 803 {ECO:0000244|PDB:1PCX}.
STRAND 805 812 {ECO:0000244|PDB:1PCX}.
HELIX 818 825 {ECO:0000244|PDB:1PCX}.
HELIX 830 832 {ECO:0000244|PDB:1PCX}.
HELIX 847 860 {ECO:0000244|PDB:1PCX}.
STRAND 870 875 {ECO:0000244|PDB:1PCX}.
HELIX 885 899 {ECO:0000244|PDB:1PCX}.
HELIX 913 923 {ECO:0000244|PDB:1PCX}.
SEQUENCE 926 AA; 103636 MW; 35E2BDD24CC75899 CRC64;
MSHHKKRVYP QAQLQYGQNA TPLQQPAQFM PPQDPAAAGM SYGQMGMPPQ GAVPSMGQQQ
FLTPAQEQLH QQIDQATTSM NDMHLHNVPL VDPNAYMQPQ VPVQMGTPLQ QQQQPMAAPA
YGQPSAAMGQ NMRPMNQLYP IDLLTELPPP ITDLTLPPPP LVIPPERMLV PSELSNASPD
YIRSTLNAVP KNSSLLKKSK LPFGLVIRPY QHLYDDIDPP PLNEDGLIVR CRRCRSYMNP
FVTFIEQGRR WRCNFCRLAN DVPMQMDQSD PNDPKSRYDR NEIKCAVMEY MAPKEYTLRQ
PPPATYCFLI DVSQSSIKSG LLATTINTLL QNLDSIPNHD ERTRISILCV DNAIHYFKIP
LDSENNEESA DQINMMDIAD LEEPFLPRPN SMVVSLKACR QNIETLLTKI PQIFQSNLIT
NFALGPALKS AYHLIGGVGG KIIVVSGTLP NLGIGKLQRR NESGVVNTSK ETAQLLSCQD
SFYKNFTIDC SKVQITVDLF LASEDYMDVA SLSNLSRFTA GQTHFYPGFS GKNPNDIVKF
STEFAKHISM DFCMETVMRA RGSTGLRMSR FYGHFFNRSS DLCAFSTMPR DQSYLFEVNV
DESIMADYCY VQVAVLLSLN NSQRRIRIIT LAMPTTESLA EVYASADQLA IASFYNSKAV
EKALNSSLDD ARVLINKSVQ DILATYKKEI VVSNTAGGAP LRLCANLRMF PLLMHSLTKH
MAFRSGIVPS DHRASALNNL ESLPLKYLIK NIYPDVYSLH DMADEAGLPV QTEDGEATGT
IVLPQPINAT SSLFERYGLY LIDNGNELFL WMGGDAVPAL VFDVFGTQDI FDIPIGKQEI
PVVENSEFNQ RVRNIINQLR NHDDVITYQS LYIVRGASLS EPVNHASARE VATLRLWASS
TLVEDKILNN ESYREFLQIM KARISK


Related products :

Catalog number Product name Quantity
EIAAB37411 Homo sapiens,Human,KIAA0755,Protein transport protein Sec24D,SEC24D,SEC24-related protein D
EIAAB37410 Homo sapiens,Human,KIAA0079,Protein transport protein Sec24C,SEC24C,SEC24-related protein C
EIAAB37409 Homo sapiens,Human,Protein transport protein Sec24B,SEC24B,SEC24-related protein B
EIAAB37406 Homo sapiens,Human,Protein transport protein Sec24A,SEC24A,SEC24-related protein A
EIAAB37407 Mouse,Mus musculus,Protein transport protein Sec24A,Sec24a,SEC24-related protein A
EIAAB37408 Bos taurus,Bovine,Protein transport protein Sec24A,SEC24A,SEC24-related protein A
29-311 XPO1 mediates leucine-rich nuclear export signal (NES)-dependent protein transport. Exportin 1 specifically inhibits the nuclear export of Rev and U snRNAs. It is involved in the control of several ce 0.05 mg
orb81243 Human Nuclear Transport Factor 2 protein Proteins 5
30-909 CCIN is a basic protein of the sperm head cytoskeleton. This protein contains kelch repeats and a BTB_POZ domain and is necessary for normal morphology during sperm differentiation.The protein encoded 0.05 mg
B364 *Yeast Morphology Agar USE For classification of yeasts on the basis of their colonial characteristics and cell morphology. Qty per Litre of Medium: 35
B364 Yeast Morphology Agar USE : For classification of yeasts on the basis of their colonial characteristics and cell morphology. 5x500gm
EIAAB05063 Antigen nuclear dot 52 kDa protein,Calcium-binding and coiled-coil domain-containing protein 2,CALCOCO2,Homo sapiens,Human,NDP52,Nuclear domain 10 protein 52,Nuclear domain 10 protein NDP52,Nuclear do
EIAAB44652 Citrate transport protein,CTP,Homo sapiens,Human,SLC20A3,SLC25A1,Solute carrier family 25 member 1,Tricarboxylate carrier protein,Tricarboxylate transport protein, mitochondrial
EIAAB44650 Bos taurus,Bovine,Citrate transport protein,CTP,SLC20A3,SLC25A1,Solute carrier family 25 member 1,Tricarboxylate carrier protein,Tricarboxylate transport protein, mitochondrial
EIAAB44651 Citrate transport protein,CTP,Rat,Rattus norvegicus,Slc20a3,Slc25a1,Solute carrier family 25 member 1,Tricarboxylate carrier protein,Tricarboxylate transport protein, mitochondrial
EIAAB28039 Homo sapiens,Human,NTF2,NTF-2,Nuclear transport factor 2,NUTF2,Placental protein 15,PP15
EIAAB33742 Androgen receptor-associated protein 24,ARA24,GTPase Ran,GTP-binding nuclear protein Ran,Homo sapiens,Human,OK_SW-cl.81,RAN,Ras-like protein TC4,Ras-related nuclear protein
EIAAB41165 Mouse,Mus musculus,p53-dependent damage-inducible nuclear protein 1,p53DINP1,Sip,Stress-induced protein,TEAP,Thymus-expressed acidic protein,Trp53inp1,Tumor protein p53-inducible nuclear protein 1
EIAAB41166 p53-dependent damage-inducible nuclear protein 1,p53DINP1,Rat,Rattus norvegicus,Sip,Stress-induced protein,TEAP,Thymus-expressed acidic protein,Trp53inp1,Tumor protein p53-inducible nuclear protein 1
EIAAB40793 C6orf98,Enaptin,Homo sapiens,Human,KIAA0796,KIAA1262,KIAA1756,MYNE1,Myne-1,Myocyte nuclear envelope protein 1,Nesprin-1,Nuclear envelope spectrin repeat protein 1,Synaptic nuclear envelope protein 1,S
EIAAB40794 Enaptin,Mouse,Mus musculus,Myne-1,Myocyte nuclear envelope protein 1,Nesprin-1,Nuclear envelope spectrin repeat protein 1,Synaptic nuclear envelope protein 1,Syne1,Syne-1
30-558 UNC84A is a a nuclear nuclear envelope protein with an Unc84 (SUN) domain. The protein is involved in nuclear anchorage and migration.This gene is a member of the unc-84 homolog family and encodes a n 0.05 mg
18-373-88001 Nesprin-1 - Nuclear envelope spectrin repeat protein 1; Synaptic nuclear envelope protein 1; Syne-1; Myocyte nuclear envelope protein 1; Myne-1; Enaptin Polyclonal 0.1 ml
EIAAB45295 E3 ubiquitin-protein ligase UHRF1,Homo sapiens,Human,HuNp95,ICBP90,Inverted CCAAT box-binding protein of 90 kDa,NP95,Nuclear protein 95,Nuclear zinc finger protein Np95,RING finger protein 106,RNF106,
EIAAB40795 Mouse,Mus musculus,Nesprin-2,Nuclear envelope spectrin repeat protein 2,Nucleus and actin connecting element protein,Protein NUANCE,Synaptic nuclear envelope protein 2,Syne2,Syne-2


 

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 Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | 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

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
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 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
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | 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
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

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