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

Proteasome subunit alpha type-3 (EC 3.4.25.1) (Macropain subunit Y13) (Multicatalytic endopeptidase complex subunit Y13) (Proteasome component Y13) (Proteinase YSCE subunit 13)

 PSA3_YEAST              Reviewed;         258 AA.
P23638; D6VUR7;
01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
01-NOV-1991, sequence version 1.
05-DEC-2018, entry version 198.
RecName: Full=Proteasome subunit alpha type-3;
EC=3.4.25.1;
AltName: Full=Macropain subunit Y13;
AltName: Full=Multicatalytic endopeptidase complex subunit Y13;
AltName: Full=Proteasome component Y13;
AltName: Full=Proteinase YSCE subunit 13;
Name=PRE9; Synonyms=PRS5; OrderedLocusNames=YGR135W;
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], AND PROTEIN SEQUENCE OF 73-92;
120-139 AND 200-236.
STRAIN=ATCC 26786 / X2180-1A;
PubMed=1898763; DOI=10.1128/MCB.11.1.344;
Emori Y., Tsukahara T., Kawasaki H., Ishiura S., Sugita H., Suzuki K.;
"Molecular cloning and functional analysis of three subunits of yeast
proteasome.";
Mol. Cell. Biol. 11:344-353(1991).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169869;
Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M.,
Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J.,
Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E.,
Clemente M.L., Coblenz A., Coglievina M., Coissac E., Defoor E.,
Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B.,
Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L.,
Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M.,
Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M.,
Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B.,
Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W.,
Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A.,
Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S.,
Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L.,
Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S.,
Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J.,
Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M.,
Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B.,
Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J.,
Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M.,
van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M.,
Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H.,
Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M.,
Zollner A., Kleine K.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
Nature 387:81-84(1997).
[3]
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).
[4]
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).
[5]
UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-199, AND IDENTIFICATION
BY MASS SPECTROMETRY.
PubMed=14557538; DOI=10.1073/pnas.2135500100;
Hitchcock A.L., Auld K., Gygi S.P., Silver P.A.;
"A subset of membrane-associated proteins is ubiquitinated in response
to mutations in the endoplasmic reticulum degradation machinery.";
Proc. Natl. Acad. Sci. U.S.A. 100:12735-12740(2003).
[6]
UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-100; LYS-199 AND LYS-231,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22106047; DOI=10.1002/pmic.201100166;
Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
"Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
Proteomics 12:236-240(2012).
[7]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 2-245 OF COMPLEX WITH THE 20S
PROTEASOME.
PubMed=9087403; DOI=10.1038/386463a0;
Groll M., Ditzel L., Loewe J., Stock D., Bochtler M., Bartunik H.D.,
Huber R.;
"Structure of 20S proteasome from yeast at 2.4-A resolution.";
Nature 386:463-471(1997).
[8]
X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 1-245 OF COMPLEX WITH THE 20S
PROTEASOME AND A 11S REGULATORY COMPLEX.
PubMed=11081519; DOI=10.1038/35040607;
Whitby F.G., Masters E.I., Kramer L., Knowlton J.R., Yao Y.,
Wang C.C., Hill C.P.;
"Structural basis for the activation of 20S proteasomes by 11S
regulators.";
Nature 408:115-120(2000).
[9]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1-245 OF COMPLEX WITH THE 20S
PROTEASOME.
PubMed=11062564; DOI=10.1038/80992;
Groll M., Bajorek M., Koehler A., Moroder L., Rubin D.M., Huber R.,
Glickman M.H., Finley D.;
"A gated channel into the proteasome core particle.";
Nat. Struct. Biol. 7:1062-1067(2000).
[10]
X-RAY CRYSTALLOGRAPHY (2.81 ANGSTROMS) OF 2-245 OF COMPLEX WITH THE
20S PROTEASOME AND A TMC-95-BASED INHIBITOR.
PubMed=16793518; DOI=10.1016/j.chembiol.2006.04.005;
Groll M., Goetz M., Kaiser M., Weyher E., Moroder L.;
"TMC-95-based inhibitor design provides evidence for the catalytic
versatility of the proteasome.";
Chem. Biol. 13:607-614(2006).
[11]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 2-245 OF COMPLEX WITH THE 20S
PROTEASOME AND SALINOSPORAMIDE.
PubMed=16608349; DOI=10.1021/ja058320b;
Groll M., Huber R., Potts B.C.M.;
"Crystal structures of salinosporamide A (NPI-0052) and B (NPI-0047)
in complex with the 20S proteasome reveal important consequences of
beta-lactone ring opening and a mechanism for irreversible binding.";
J. Am. Chem. Soc. 128:5136-5141(2006).
[12]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 2-245 OF COMPLEX WITH THE 20S
PROTEASOME AND BORTEZOMIB.
PubMed=16531229; DOI=10.1016/j.str.2005.11.019;
Groll M., Berkers C.R., Ploegh H.L., Ovaa H.;
"Crystal structure of the boronic acid-based proteasome inhibitor
bortezomib in complex with the yeast 20S proteasome.";
Structure 14:451-456(2006).
[13]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 14-245 IN COMPLEX WITH THE
PROTEASOME.
PubMed=20227375; DOI=10.1016/j.molcel.2010.02.002;
Sadre-Bazzaz K., Whitby F.G., Robinson H., Formosa T., Hill C.P.;
"Structure of a Blm10 complex reveals common mechanisms for proteasome
binding and gate opening.";
Mol. Cell 37:728-735(2010).
[14]
STRUCTURE BY ELECTRON MICROSCOPY (7.4 ANGSTROMS) OF THE 26S
PROTEASOME.
PubMed=22927375; DOI=10.1073/pnas.1213333109;
Beck F., Unverdorben P., Bohn S., Schweitzer A., Pfeifer G.,
Sakata E., Nickell S., Plitzko J.M., Villa E., Baumeister W.,
Forster F.;
"Near-atomic resolution structural model of the yeast 26S
proteasome.";
Proc. Natl. Acad. Sci. U.S.A. 109:14870-14875(2012).
-!- FUNCTION: The proteasome degrades poly-ubiquitinated proteins in
the cytoplasm and in the nucleus. It is essential for the
regulated turnover of proteins and for the removal of misfolded
proteins. The proteasome is a multicatalytic proteinase complex
that is characterized by its ability to cleave peptides with Arg,
Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or
slightly basic pH. It has an ATP-dependent proteolytic activity.
-!- CATALYTIC ACTIVITY:
Reaction=Cleavage of peptide bonds with very broad specificity.;
EC=3.4.25.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU00808};
-!- SUBUNIT: The 26S proteasome consists of a 20S proteasome core and
two 19S regulatory subunits. The 20S proteasome core is composed
of 28 subunits that are arranged in four stacked rings, resulting
in a barrel-shaped structure. The two end rings are each formed by
seven alpha subunits, and the two central rings are each formed by
seven beta subunits. The catalytic chamber with the active sites
is on the inside of the barrel. {ECO:0000269|PubMed:20227375}.
-!- INTERACTION:
P30656:PRE2; NbExp=2; IntAct=EBI-13967, EBI-14001;
P23639:PRE8; NbExp=3; IntAct=EBI-13967, EBI-13959;
-!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
-!- MISCELLANEOUS: Present with 17100 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the peptidase T1A family.
{ECO:0000255|PROSITE-ProRule:PRU00808}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; M63851; AAA34907.1; -; Genomic_DNA.
EMBL; X56730; CAA40054.1; -; Genomic_DNA.
EMBL; Z72920; CAA97148.1; -; Genomic_DNA.
EMBL; BK006941; DAA08228.1; -; Genomic_DNA.
PIR; S12940; SNBYY3.
RefSeq; NP_011651.3; NM_001181264.3.
PDB; 1FNT; X-ray; 3.20 A; C/Q=1-245.
PDB; 1G0U; X-ray; 2.40 A; B/P=1-245.
PDB; 1G65; X-ray; 2.25 A; B/P=2-245.
PDB; 1JD2; X-ray; 3.00 A; B/W=2-245.
PDB; 1RYP; X-ray; 1.90 A; C/Q=2-245.
PDB; 1Z7Q; X-ray; 3.22 A; C/Q=1-258.
PDB; 2F16; X-ray; 2.80 A; B/P=2-245.
PDB; 2FAK; X-ray; 2.80 A; B/P=2-245.
PDB; 2GPL; X-ray; 2.81 A; B/P=2-245.
PDB; 2ZCY; X-ray; 2.90 A; B/P=1-258.
PDB; 3BDM; X-ray; 2.70 A; B/P=1-258.
PDB; 3D29; X-ray; 2.60 A; B/P=2-245.
PDB; 3DY3; X-ray; 2.81 A; B/P=2-245.
PDB; 3DY4; X-ray; 2.80 A; B/P=2-245.
PDB; 3E47; X-ray; 3.00 A; B/P=2-245.
PDB; 3GPJ; X-ray; 2.70 A; B/P=2-245.
PDB; 3GPT; X-ray; 2.41 A; B/P=2-245.
PDB; 3GPW; X-ray; 2.50 A; B/P=2-245.
PDB; 3HYE; X-ray; 2.50 A; B/P=2-245.
PDB; 3JCO; EM; 4.80 A; C/c=1-258.
PDB; 3JCP; EM; 4.60 A; C/c=1-258.
PDB; 3MG0; X-ray; 2.68 A; B/P=2-245.
PDB; 3MG4; X-ray; 3.11 A; B/P=2-245.
PDB; 3MG6; X-ray; 2.60 A; B/P=1-245.
PDB; 3MG7; X-ray; 2.78 A; B/P=1-245.
PDB; 3MG8; X-ray; 2.59 A; B/P=1-245.
PDB; 3NZJ; X-ray; 2.40 A; B/P=1-258.
PDB; 3NZW; X-ray; 2.50 A; B/P=1-258.
PDB; 3NZX; X-ray; 2.70 A; B/P=1-258.
PDB; 3OEU; X-ray; 2.60 A; B/P=11-245.
PDB; 3OEV; X-ray; 2.85 A; B/P=11-245.
PDB; 3OKJ; X-ray; 2.70 A; B/P=2-245.
PDB; 3SDI; X-ray; 2.65 A; B/P=11-245.
PDB; 3SDK; X-ray; 2.70 A; B/P=11-245.
PDB; 3SHJ; X-ray; 2.80 A; B/P=2-245.
PDB; 3TDD; X-ray; 2.70 A; B/P=2-245.
PDB; 3UN4; X-ray; 3.40 A; B/P=1-258.
PDB; 3UN8; X-ray; 2.70 A; B/P=1-258.
PDB; 3WXR; X-ray; 3.15 A; C/Q=1-258.
PDB; 4CR2; EM; 7.70 A; C=1-258.
PDB; 4CR3; EM; 9.30 A; C=1-258.
PDB; 4CR4; EM; 8.80 A; C=1-258.
PDB; 4EU2; X-ray; 2.51 A; C/Q=2-245.
PDB; 4FZC; X-ray; 2.80 A; B/P=2-245.
PDB; 4FZG; X-ray; 3.00 A; B/P=2-245.
PDB; 4G4S; X-ray; 2.49 A; C=1-258.
PDB; 4GK7; X-ray; 2.80 A; B/P=2-245.
PDB; 4HNP; X-ray; 2.80 A; B/P=2-245.
PDB; 4HRC; X-ray; 2.80 A; B/P=2-245.
PDB; 4HRD; X-ray; 2.80 A; B/P=2-245.
PDB; 4INR; X-ray; 2.70 A; B/P=1-258.
PDB; 4INT; X-ray; 2.90 A; B/P=1-258.
PDB; 4INU; X-ray; 3.10 A; B/P=1-258.
PDB; 4J70; X-ray; 2.80 A; B/P=1-258.
PDB; 4JSQ; X-ray; 2.80 A; B/P=1-258.
PDB; 4JSU; X-ray; 2.90 A; B/P=1-258.
PDB; 4JT0; X-ray; 3.10 A; B/P=1-258.
PDB; 4LQI; X-ray; 2.70 A; B/P=2-245.
PDB; 4LTC; X-ray; 2.50 A; B/P=1-258.
PDB; 4NNN; X-ray; 2.50 A; B/P=1-258.
PDB; 4NNW; X-ray; 2.60 A; B/P=1-258.
PDB; 4NO1; X-ray; 2.50 A; B/P=1-258.
PDB; 4NO6; X-ray; 3.00 A; B/P=1-258.
PDB; 4NO8; X-ray; 2.70 A; B/P=1-258.
PDB; 4NO9; X-ray; 2.90 A; B/P=1-258.
PDB; 4Q1S; X-ray; 2.60 A; B/P=1-258.
PDB; 4QBY; X-ray; 3.00 A; B/P=1-258.
PDB; 4QLQ; X-ray; 2.40 A; B/P=1-258.
PDB; 4QLS; X-ray; 2.80 A; B/P=1-258.
PDB; 4QLT; X-ray; 2.80 A; B/P=1-258.
PDB; 4QLU; X-ray; 2.80 A; B/P=1-258.
PDB; 4QLV; X-ray; 2.90 A; B/P=1-258.
PDB; 4QUX; X-ray; 3.00 A; B/P=1-258.
PDB; 4QUY; X-ray; 2.80 A; B/P=1-258.
PDB; 4QV0; X-ray; 3.10 A; B/P=1-258.
PDB; 4QV1; X-ray; 2.50 A; B/P=1-258.
PDB; 4QV3; X-ray; 3.00 A; B/P=1-258.
PDB; 4QV4; X-ray; 2.70 A; B/P=1-258.
PDB; 4QV5; X-ray; 2.70 A; B/P=1-258.
PDB; 4QV6; X-ray; 2.80 A; B/P=1-258.
PDB; 4QV7; X-ray; 2.60 A; B/P=1-258.
PDB; 4QV8; X-ray; 2.90 A; B/P=1-258.
PDB; 4QV9; X-ray; 2.60 A; B/P=1-258.
PDB; 4QVL; X-ray; 2.80 A; B/P=1-258.
PDB; 4QVM; X-ray; 2.80 A; B/P=1-258.
PDB; 4QVN; X-ray; 2.90 A; B/P=1-258.
PDB; 4QVP; X-ray; 2.30 A; B/P=1-258.
PDB; 4QVQ; X-ray; 2.60 A; B/P=1-258.
PDB; 4QVV; X-ray; 2.80 A; B/P=1-258.
PDB; 4QVW; X-ray; 3.00 A; B/P=1-258.
PDB; 4QVY; X-ray; 2.51 A; B/P=1-258.
PDB; 4QW0; X-ray; 2.90 A; B/P=1-258.
PDB; 4QW1; X-ray; 2.90 A; B/P=1-258.
PDB; 4QW3; X-ray; 2.90 A; B/P=1-258.
PDB; 4QW4; X-ray; 2.80 A; B/P=1-258.
PDB; 4QW5; X-ray; 3.00 A; B/P=1-258.
PDB; 4QW6; X-ray; 2.90 A; B/P=1-258.
PDB; 4QW7; X-ray; 2.70 A; B/P=1-258.
PDB; 4QWF; X-ray; 3.00 A; B/P=1-258.
PDB; 4QWG; X-ray; 2.60 A; B/P=1-258.
PDB; 4QWI; X-ray; 2.60 A; B/P=1-258.
PDB; 4QWJ; X-ray; 2.90 A; B/P=1-258.
PDB; 4QWK; X-ray; 2.80 A; B/P=1-258.
PDB; 4QWL; X-ray; 2.60 A; B/P=1-258.
PDB; 4QWR; X-ray; 2.90 A; B/P=1-258.
PDB; 4QWS; X-ray; 3.00 A; B/P=1-258.
PDB; 4QWU; X-ray; 3.00 A; B/P=1-258.
PDB; 4QWX; X-ray; 2.90 A; B/P=1-258.
PDB; 4QXJ; X-ray; 2.80 A; B/P=1-258.
PDB; 4QZ0; X-ray; 3.00 A; B/P=1-258.
PDB; 4QZ1; X-ray; 3.00 A; B/P=1-258.
PDB; 4QZ2; X-ray; 2.70 A; B/P=1-258.
PDB; 4QZ3; X-ray; 2.80 A; B/P=1-258.
PDB; 4QZ4; X-ray; 3.00 A; B/P=1-258.
PDB; 4QZ5; X-ray; 2.80 A; B/P=1-258.
PDB; 4QZ6; X-ray; 2.90 A; B/P=1-258.
PDB; 4QZ7; X-ray; 2.80 A; B/P=1-258.
PDB; 4QZW; X-ray; 3.00 A; B/P=1-258.
PDB; 4QZX; X-ray; 2.60 A; B/P=1-258.
PDB; 4QZZ; X-ray; 2.90 A; B/P=1-258.
PDB; 4R00; X-ray; 2.80 A; B/P=1-258.
PDB; 4R02; X-ray; 2.50 A; B/P=1-258.
PDB; 4R17; X-ray; 2.10 A; B/P=1-258.
PDB; 4R18; X-ray; 2.40 A; B/P=1-258.
PDB; 4RUR; X-ray; 2.50 A; B/P=1-258.
PDB; 4V7O; X-ray; 3.00 A; AH/AT/BC/BQ=14-245.
PDB; 4X6Z; X-ray; 2.70 A; C/Q=1-258.
PDB; 4Y69; X-ray; 2.90 A; B/P=1-258.
PDB; 4Y6A; X-ray; 2.60 A; B/P=1-258.
PDB; 4Y6V; X-ray; 2.80 A; B/P=1-258.
PDB; 4Y6Z; X-ray; 2.70 A; B/P=1-258.
PDB; 4Y70; X-ray; 2.40 A; B/P=1-258.
PDB; 4Y74; X-ray; 2.70 A; B/P=1-258.
PDB; 4Y75; X-ray; 2.80 A; B/P=1-258.
PDB; 4Y77; X-ray; 2.50 A; B/P=1-258.
PDB; 4Y78; X-ray; 2.80 A; B/P=1-258.
PDB; 4Y7W; X-ray; 2.50 A; B/P=1-258.
PDB; 4Y7X; X-ray; 2.60 A; B/P=1-258.
PDB; 4Y7Y; X-ray; 2.40 A; B/P=1-258.
PDB; 4Y80; X-ray; 2.50 A; B/P=1-258.
PDB; 4Y81; X-ray; 2.80 A; B/P=1-258.
PDB; 4Y82; X-ray; 2.80 A; B/P=1-258.
PDB; 4Y84; X-ray; 2.70 A; B/P=1-258.
PDB; 4Y8G; X-ray; 2.60 A; B/P=1-258.
PDB; 4Y8H; X-ray; 2.50 A; B/P=1-258.
PDB; 4Y8I; X-ray; 2.60 A; B/P=1-258.
PDB; 4Y8J; X-ray; 2.70 A; B/P=1-258.
PDB; 4Y8K; X-ray; 2.60 A; B/P=1-258.
PDB; 4Y8L; X-ray; 2.40 A; B/P=1-258.
PDB; 4Y8M; X-ray; 2.80 A; B/P=1-258.
PDB; 4Y8N; X-ray; 2.60 A; B/P=1-258.
PDB; 4Y8O; X-ray; 2.70 A; B/P=1-258.
PDB; 4Y8P; X-ray; 2.80 A; B/P=1-258.
PDB; 4Y8Q; X-ray; 2.60 A; B/P=1-258.
PDB; 4Y8R; X-ray; 2.70 A; B/P=1-258.
PDB; 4Y8S; X-ray; 2.70 A; B/P=1-258.
PDB; 4Y8T; X-ray; 2.70 A; B/P=1-258.
PDB; 4Y8U; X-ray; 2.90 A; B/P=1-258.
PDB; 4Y9Y; X-ray; 2.80 A; B/P=1-258.
PDB; 4Y9Z; X-ray; 2.80 A; B/P=1-258.
PDB; 4YA0; X-ray; 2.80 A; B/P=1-258.
PDB; 4YA1; X-ray; 2.90 A; B/P=1-258.
PDB; 4YA2; X-ray; 2.70 A; B/P=1-258.
PDB; 4YA3; X-ray; 2.70 A; B/P=1-258.
PDB; 4YA4; X-ray; 2.90 A; B/P=1-258.
PDB; 4YA5; X-ray; 2.50 A; B/P=1-258.
PDB; 4YA7; X-ray; 2.70 A; B/P=1-258.
PDB; 4YA9; X-ray; 2.70 A; B/P=1-258.
PDB; 4Z1L; X-ray; 3.00 A; B/P=1-258.
PDB; 5A5B; EM; 9.50 A; C=1-258.
PDB; 5AHJ; X-ray; 2.80 A; B/P=1-258.
PDB; 5BOU; X-ray; 2.60 A; B/P=1-258.
PDB; 5BXL; X-ray; 2.80 A; B/P=1-258.
PDB; 5BXN; X-ray; 2.80 A; B/P=1-258.
PDB; 5CGF; X-ray; 2.80 A; B/P=1-258.
PDB; 5CGG; X-ray; 2.90 A; B/P=1-258.
PDB; 5CGH; X-ray; 2.50 A; B/P=1-258.
PDB; 5CGI; X-ray; 2.80 A; B/P=1-258.
PDB; 5CZ4; X-ray; 2.30 A; B/P=1-258.
PDB; 5CZ5; X-ray; 2.80 A; B/P=1-258.
PDB; 5CZ6; X-ray; 2.70 A; B/P=1-258.
PDB; 5CZ7; X-ray; 2.50 A; B/P=1-258.
PDB; 5CZ8; X-ray; 2.80 A; B/P=1-258.
PDB; 5CZ9; X-ray; 2.90 A; B/P=1-258.
PDB; 5CZA; X-ray; 2.50 A; B/P=1-258.
PDB; 5D0S; X-ray; 2.50 A; B/P=1-258.
PDB; 5D0T; X-ray; 2.60 A; B/P=1-258.
PDB; 5D0V; X-ray; 2.90 A; B/P=1-258.
PDB; 5D0W; X-ray; 2.80 A; B/P=1-258.
PDB; 5D0X; X-ray; 2.60 A; B/P=1-258.
PDB; 5D0Z; X-ray; 2.90 A; B/P=1-258.
PDB; 5DKI; X-ray; 2.80 A; B/P=1-258.
PDB; 5DKJ; X-ray; 2.80 A; B/P=1-258.
PDB; 5FG7; X-ray; 2.70 A; B/P=1-258.
PDB; 5FG9; X-ray; 2.60 A; B/P=1-258.
PDB; 5FGA; X-ray; 2.70 A; B/P=1-258.
PDB; 5FGD; X-ray; 2.80 A; B/P=1-258.
PDB; 5FGE; X-ray; 2.60 A; B/P=1-258.
PDB; 5FGF; X-ray; 2.60 A; B/P=1-258.
PDB; 5FGG; X-ray; 2.70 A; B/P=1-258.
PDB; 5FGH; X-ray; 2.80 A; B/P=1-258.
PDB; 5FGI; X-ray; 2.90 A; B/P=1-258.
PDB; 5FHS; X-ray; 2.70 A; B/P=1-258.
PDB; 5JHR; X-ray; 2.90 A; B/P=1-258.
PDB; 5JHS; X-ray; 3.00 A; B/P=1-258.
PDB; 5L52; X-ray; 2.70 A; B/P=1-258.
PDB; 5L54; X-ray; 2.80 A; B/P=1-258.
PDB; 5L55; X-ray; 2.90 A; B/P=1-258.
PDB; 5L5A; X-ray; 2.40 A; B/P=1-258.
PDB; 5L5B; X-ray; 2.80 A; B/P=1-258.
PDB; 5L5D; X-ray; 2.80 A; B/P=1-258.
PDB; 5L5E; X-ray; 2.90 A; B/P=1-258.
PDB; 5L5F; X-ray; 2.50 A; B/P=1-258.
PDB; 5L5H; X-ray; 2.60 A; B/P=1-258.
PDB; 5L5I; X-ray; 2.90 A; B/P=1-258.
PDB; 5L5J; X-ray; 2.90 A; B/P=1-258.
PDB; 5L5O; X-ray; 2.60 A; B/P=1-258.
PDB; 5L5P; X-ray; 2.80 A; B/P=1-258.
PDB; 5L5Q; X-ray; 2.80 A; B/P=1-258.
PDB; 5L5R; X-ray; 2.90 A; B/P=1-258.
PDB; 5L5S; X-ray; 2.60 A; B/P=1-258.
PDB; 5L5T; X-ray; 2.90 A; B/P=1-258.
PDB; 5L5U; X-ray; 2.60 A; B/P=1-258.
PDB; 5L5V; X-ray; 2.70 A; B/P=1-258.
PDB; 5L5W; X-ray; 2.80 A; B/P=1-258.
PDB; 5L5X; X-ray; 2.90 A; B/P=1-258.
PDB; 5L5Y; X-ray; 2.70 A; B/P=1-258.
PDB; 5L5Z; X-ray; 2.70 A; B/P=1-258.
PDB; 5L60; X-ray; 2.70 A; B/P=1-258.
PDB; 5L61; X-ray; 2.80 A; B/P=1-258.
PDB; 5L62; X-ray; 2.80 A; B/P=1-258.
PDB; 5L63; X-ray; 2.70 A; B/P=1-258.
PDB; 5L64; X-ray; 2.70 A; B/P=1-258.
PDB; 5L65; X-ray; 2.90 A; B/P=1-258.
PDB; 5L66; X-ray; 2.80 A; B/P=1-258.
PDB; 5L67; X-ray; 2.60 A; B/P=1-258.
PDB; 5L68; X-ray; 2.80 A; B/P=1-258.
PDB; 5L69; X-ray; 2.70 A; B/P=1-258.
PDB; 5L6A; X-ray; 2.80 A; B/P=1-258.
PDB; 5L6B; X-ray; 2.60 A; B/P=1-258.
PDB; 5L6C; X-ray; 2.60 A; B/P=1-258.
PDB; 5LAI; X-ray; 2.50 A; B/P=1-258.
PDB; 5LAJ; X-ray; 2.90 A; B/P=1-258.
PDB; 5LTT; X-ray; 2.70 A; B/P=1-258.
PDB; 5M2B; X-ray; 2.70 A; B/P=1-258.
PDB; 5MP9; EM; 4.10 A; C/c=1-258.
PDB; 5MPA; EM; 4.50 A; C/c=1-258.
PDB; 5MPB; EM; 7.80 A; C/c=1-258.
PDB; 5MPC; EM; 7.70 A; C/c=1-258.
PDB; 5NIF; X-ray; 3.00 A; C/Q=1-258.
PDB; 5WVI; EM; 6.30 A; C/d=1-258.
PDB; 5WVK; EM; 4.20 A; C/d=1-258.
PDB; 6EF0; EM; 4.43 A; C=1-244.
PDB; 6EF1; EM; 4.73 A; C=8-245.
PDB; 6EF2; EM; 4.27 A; C=4-244.
PDB; 6EF3; EM; 4.17 A; C=1-258.
PDB; 6FVT; EM; 4.10 A; C/c=2-245.
PDB; 6FVU; EM; 4.50 A; C/c=2-245.
PDB; 6FVV; EM; 5.40 A; C/c=2-245.
PDB; 6FVW; EM; 4.50 A; C/c=5-245.
PDB; 6FVX; EM; 4.90 A; C/c=5-245.
PDB; 6FVY; EM; 6.10 A; C/c=5-245.
PDB; 6G7F; X-ray; 2.70 A; B/P=1-258.
PDB; 6G8M; X-ray; 2.70 A; B/P=1-258.
PDB; 6G8N; X-ray; 3.00 A; B/P=1-258.
PDB; 6GOP; X-ray; 2.90 A; B/P=1-258.
PDBsum; 1FNT; -.
PDBsum; 1G0U; -.
PDBsum; 1G65; -.
PDBsum; 1JD2; -.
PDBsum; 1RYP; -.
PDBsum; 1Z7Q; -.
PDBsum; 2F16; -.
PDBsum; 2FAK; -.
PDBsum; 2GPL; -.
PDBsum; 2ZCY; -.
PDBsum; 3BDM; -.
PDBsum; 3D29; -.
PDBsum; 3DY3; -.
PDBsum; 3DY4; -.
PDBsum; 3E47; -.
PDBsum; 3GPJ; -.
PDBsum; 3GPT; -.
PDBsum; 3GPW; -.
PDBsum; 3HYE; -.
PDBsum; 3JCO; -.
PDBsum; 3JCP; -.
PDBsum; 3MG0; -.
PDBsum; 3MG4; -.
PDBsum; 3MG6; -.
PDBsum; 3MG7; -.
PDBsum; 3MG8; -.
PDBsum; 3NZJ; -.
PDBsum; 3NZW; -.
PDBsum; 3NZX; -.
PDBsum; 3OEU; -.
PDBsum; 3OEV; -.
PDBsum; 3OKJ; -.
PDBsum; 3SDI; -.
PDBsum; 3SDK; -.
PDBsum; 3SHJ; -.
PDBsum; 3TDD; -.
PDBsum; 3UN4; -.
PDBsum; 3UN8; -.
PDBsum; 3WXR; -.
PDBsum; 4CR2; -.
PDBsum; 4CR3; -.
PDBsum; 4CR4; -.
PDBsum; 4EU2; -.
PDBsum; 4FZC; -.
PDBsum; 4FZG; -.
PDBsum; 4G4S; -.
PDBsum; 4GK7; -.
PDBsum; 4HNP; -.
PDBsum; 4HRC; -.
PDBsum; 4HRD; -.
PDBsum; 4INR; -.
PDBsum; 4INT; -.
PDBsum; 4INU; -.
PDBsum; 4J70; -.
PDBsum; 4JSQ; -.
PDBsum; 4JSU; -.
PDBsum; 4JT0; -.
PDBsum; 4LQI; -.
PDBsum; 4LTC; -.
PDBsum; 4NNN; -.
PDBsum; 4NNW; -.
PDBsum; 4NO1; -.
PDBsum; 4NO6; -.
PDBsum; 4NO8; -.
PDBsum; 4NO9; -.
PDBsum; 4Q1S; -.
PDBsum; 4QBY; -.
PDBsum; 4QLQ; -.
PDBsum; 4QLS; -.
PDBsum; 4QLT; -.
PDBsum; 4QLU; -.
PDBsum; 4QLV; -.
PDBsum; 4QUX; -.
PDBsum; 4QUY; -.
PDBsum; 4QV0; -.
PDBsum; 4QV1; -.
PDBsum; 4QV3; -.
PDBsum; 4QV4; -.
PDBsum; 4QV5; -.
PDBsum; 4QV6; -.
PDBsum; 4QV7; -.
PDBsum; 4QV8; -.
PDBsum; 4QV9; -.
PDBsum; 4QVL; -.
PDBsum; 4QVM; -.
PDBsum; 4QVN; -.
PDBsum; 4QVP; -.
PDBsum; 4QVQ; -.
PDBsum; 4QVV; -.
PDBsum; 4QVW; -.
PDBsum; 4QVY; -.
PDBsum; 4QW0; -.
PDBsum; 4QW1; -.
PDBsum; 4QW3; -.
PDBsum; 4QW4; -.
PDBsum; 4QW5; -.
PDBsum; 4QW6; -.
PDBsum; 4QW7; -.
PDBsum; 4QWF; -.
PDBsum; 4QWG; -.
PDBsum; 4QWI; -.
PDBsum; 4QWJ; -.
PDBsum; 4QWK; -.
PDBsum; 4QWL; -.
PDBsum; 4QWR; -.
PDBsum; 4QWS; -.
PDBsum; 4QWU; -.
PDBsum; 4QWX; -.
PDBsum; 4QXJ; -.
PDBsum; 4QZ0; -.
PDBsum; 4QZ1; -.
PDBsum; 4QZ2; -.
PDBsum; 4QZ3; -.
PDBsum; 4QZ4; -.
PDBsum; 4QZ5; -.
PDBsum; 4QZ6; -.
PDBsum; 4QZ7; -.
PDBsum; 4QZW; -.
PDBsum; 4QZX; -.
PDBsum; 4QZZ; -.
PDBsum; 4R00; -.
PDBsum; 4R02; -.
PDBsum; 4R17; -.
PDBsum; 4R18; -.
PDBsum; 4RUR; -.
PDBsum; 4V7O; -.
PDBsum; 4X6Z; -.
PDBsum; 4Y69; -.
PDBsum; 4Y6A; -.
PDBsum; 4Y6V; -.
PDBsum; 4Y6Z; -.
PDBsum; 4Y70; -.
PDBsum; 4Y74; -.
PDBsum; 4Y75; -.
PDBsum; 4Y77; -.
PDBsum; 4Y78; -.
PDBsum; 4Y7W; -.
PDBsum; 4Y7X; -.
PDBsum; 4Y7Y; -.
PDBsum; 4Y80; -.
PDBsum; 4Y81; -.
PDBsum; 4Y82; -.
PDBsum; 4Y84; -.
PDBsum; 4Y8G; -.
PDBsum; 4Y8H; -.
PDBsum; 4Y8I; -.
PDBsum; 4Y8J; -.
PDBsum; 4Y8K; -.
PDBsum; 4Y8L; -.
PDBsum; 4Y8M; -.
PDBsum; 4Y8N; -.
PDBsum; 4Y8O; -.
PDBsum; 4Y8P; -.
PDBsum; 4Y8Q; -.
PDBsum; 4Y8R; -.
PDBsum; 4Y8S; -.
PDBsum; 4Y8T; -.
PDBsum; 4Y8U; -.
PDBsum; 4Y9Y; -.
PDBsum; 4Y9Z; -.
PDBsum; 4YA0; -.
PDBsum; 4YA1; -.
PDBsum; 4YA2; -.
PDBsum; 4YA3; -.
PDBsum; 4YA4; -.
PDBsum; 4YA5; -.
PDBsum; 4YA7; -.
PDBsum; 4YA9; -.
PDBsum; 4Z1L; -.
PDBsum; 5A5B; -.
PDBsum; 5AHJ; -.
PDBsum; 5BOU; -.
PDBsum; 5BXL; -.
PDBsum; 5BXN; -.
PDBsum; 5CGF; -.
PDBsum; 5CGG; -.
PDBsum; 5CGH; -.
PDBsum; 5CGI; -.
PDBsum; 5CZ4; -.
PDBsum; 5CZ5; -.
PDBsum; 5CZ6; -.
PDBsum; 5CZ7; -.
PDBsum; 5CZ8; -.
PDBsum; 5CZ9; -.
PDBsum; 5CZA; -.
PDBsum; 5D0S; -.
PDBsum; 5D0T; -.
PDBsum; 5D0V; -.
PDBsum; 5D0W; -.
PDBsum; 5D0X; -.
PDBsum; 5D0Z; -.
PDBsum; 5DKI; -.
PDBsum; 5DKJ; -.
PDBsum; 5FG7; -.
PDBsum; 5FG9; -.
PDBsum; 5FGA; -.
PDBsum; 5FGD; -.
PDBsum; 5FGE; -.
PDBsum; 5FGF; -.
PDBsum; 5FGG; -.
PDBsum; 5FGH; -.
PDBsum; 5FGI; -.
PDBsum; 5FHS; -.
PDBsum; 5JHR; -.
PDBsum; 5JHS; -.
PDBsum; 5L52; -.
PDBsum; 5L54; -.
PDBsum; 5L55; -.
PDBsum; 5L5A; -.
PDBsum; 5L5B; -.
PDBsum; 5L5D; -.
PDBsum; 5L5E; -.
PDBsum; 5L5F; -.
PDBsum; 5L5H; -.
PDBsum; 5L5I; -.
PDBsum; 5L5J; -.
PDBsum; 5L5O; -.
PDBsum; 5L5P; -.
PDBsum; 5L5Q; -.
PDBsum; 5L5R; -.
PDBsum; 5L5S; -.
PDBsum; 5L5T; -.
PDBsum; 5L5U; -.
PDBsum; 5L5V; -.
PDBsum; 5L5W; -.
PDBsum; 5L5X; -.
PDBsum; 5L5Y; -.
PDBsum; 5L5Z; -.
PDBsum; 5L60; -.
PDBsum; 5L61; -.
PDBsum; 5L62; -.
PDBsum; 5L63; -.
PDBsum; 5L64; -.
PDBsum; 5L65; -.
PDBsum; 5L66; -.
PDBsum; 5L67; -.
PDBsum; 5L68; -.
PDBsum; 5L69; -.
PDBsum; 5L6A; -.
PDBsum; 5L6B; -.
PDBsum; 5L6C; -.
PDBsum; 5LAI; -.
PDBsum; 5LAJ; -.
PDBsum; 5LTT; -.
PDBsum; 5M2B; -.
PDBsum; 5MP9; -.
PDBsum; 5MPA; -.
PDBsum; 5MPB; -.
PDBsum; 5MPC; -.
PDBsum; 5NIF; -.
PDBsum; 5WVI; -.
PDBsum; 5WVK; -.
PDBsum; 6EF0; -.
PDBsum; 6EF1; -.
PDBsum; 6EF2; -.
PDBsum; 6EF3; -.
PDBsum; 6FVT; -.
PDBsum; 6FVU; -.
PDBsum; 6FVV; -.
PDBsum; 6FVW; -.
PDBsum; 6FVX; -.
PDBsum; 6FVY; -.
PDBsum; 6G7F; -.
PDBsum; 6G8M; -.
PDBsum; 6G8N; -.
PDBsum; 6GOP; -.
ProteinModelPortal; P23638; -.
SMR; P23638; -.
BioGrid; 33383; 519.
ComplexPortal; CPX-2262; 26S Proteasome complex.
DIP; DIP-2823N; -.
IntAct; P23638; 20.
MINT; P23638; -.
STRING; 4932.YGR135W; -.
MEROPS; T01.973; -.
iPTMnet; P23638; -.
MaxQB; P23638; -.
PaxDb; P23638; -.
PRIDE; P23638; -.
EnsemblFungi; YGR135W_mRNA; YGR135W_mRNA; YGR135W.
GeneID; 853036; -.
KEGG; sce:YGR135W; -.
SGD; S000003367; PRE9.
GeneTree; ENSGT00550000074827; -.
HOGENOM; HOG000091085; -.
InParanoid; P23638; -.
KO; K02728; -.
OMA; MSKTMDS; -.
OrthoDB; EOG092C47D8; -.
BioCyc; YEAST:G3O-30841-MONOMER; -.
Reactome; R-SCE-1236978; Cross-presentation of soluble exogenous antigens (endosomes).
Reactome; R-SCE-174113; SCF-beta-TrCP mediated degradation of Emi1.
Reactome; R-SCE-187577; SCF(Skp2)-mediated degradation of p27/p21.
Reactome; R-SCE-382556; ABC-family proteins mediated transport.
Reactome; R-SCE-450408; AUF1 (hnRNP D0) binds and destabilizes mRNA.
Reactome; R-SCE-5668541; TNFR2 non-canonical NF-kB pathway.
Reactome; R-SCE-5687128; MAPK6/MAPK4 signaling.
Reactome; R-SCE-5689880; Ub-specific processing proteases.
Reactome; R-SCE-68949; Orc1 removal from chromatin.
Reactome; R-SCE-69017; CDK-mediated phosphorylation and removal of Cdc6.
Reactome; R-SCE-69601; Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
Reactome; R-SCE-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
Reactome; R-SCE-983168; Antigen processing: Ubiquitination & Proteasome degradation.
EvolutionaryTrace; P23638; -.
PRO; PR:P23638; -.
Proteomes; UP000002311; Chromosome VII.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0042175; C:nuclear outer membrane-endoplasmic reticulum membrane network; IC:SGD.
GO; GO:0005634; C:nucleus; IBA:GO_Central.
GO; GO:0005839; C:proteasome core complex; IBA:GO_Central.
GO; GO:0019773; C:proteasome core complex, alpha-subunit complex; IDA:SGD.
GO; GO:0034515; C:proteasome storage granule; IDA:SGD.
GO; GO:0004175; F:endopeptidase activity; IBA:GO_Central.
GO; GO:0004298; F:threonine-type endopeptidase activity; IEA:UniProtKB-KW.
GO; GO:0010498; P:proteasomal protein catabolic process; IBA:GO_Central.
GO; GO:0010499; P:proteasomal ubiquitin-independent protein catabolic process; IDA:SGD.
GO; GO:0080129; P:proteasome core complex assembly; IMP:SGD.
GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IDA:SGD.
Gene3D; 3.60.20.10; -; 1.
InterPro; IPR029055; Ntn_hydrolases_N.
InterPro; IPR023332; Proteasome_alpha-type.
InterPro; IPR000426; Proteasome_asu_N.
InterPro; IPR016050; Proteasome_bsu_CS.
InterPro; IPR001353; Proteasome_sua/b.
InterPro; IPR034647; Proteasome_subunit_alpha4.
PANTHER; PTHR11599:SF13; PTHR11599:SF13; 1.
Pfam; PF00227; Proteasome; 1.
Pfam; PF10584; Proteasome_A_N; 1.
SMART; SM00948; Proteasome_A_N; 1.
SUPFAM; SSF56235; SSF56235; 1.
PROSITE; PS00388; PROTEASOME_ALPHA_1; 1.
PROSITE; PS51475; PROTEASOME_ALPHA_2; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Cytoplasm; Direct protein sequencing;
Hydrolase; Isopeptide bond; Nucleus; Protease; Proteasome;
Reference proteome; Threonine protease; Ubl conjugation.
CHAIN 1 258 Proteasome subunit alpha type-3.
/FTId=PRO_0000124116.
CROSSLNK 100 100 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000244|PubMed:22106047}.
CROSSLNK 199 199 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000244|PubMed:22106047}.
CROSSLNK 231 231 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000244|PubMed:22106047}.
HELIX 4 6 {ECO:0000244|PDB:1RYP}.
HELIX 20 29 {ECO:0000244|PDB:1RYP}.
STRAND 35 40 {ECO:0000244|PDB:1RYP}.
STRAND 43 49 {ECO:0000244|PDB:1RYP}.
STRAND 55 57 {ECO:0000244|PDB:1RYP}.
HELIX 59 61 {ECO:0000244|PDB:5CZ4}.
STRAND 64 79 {ECO:0000244|PDB:1RYP}.
HELIX 81 102 {ECO:0000244|PDB:1RYP}.
HELIX 108 124 {ECO:0000244|PDB:1RYP}.
STRAND 125 127 {ECO:0000244|PDB:1RYP}.
STRAND 133 141 {ECO:0000244|PDB:1RYP}.
TURN 142 144 {ECO:0000244|PDB:1RYP}.
STRAND 145 151 {ECO:0000244|PDB:1RYP}.
STRAND 157 166 {ECO:0000244|PDB:1RYP}.
HELIX 169 179 {ECO:0000244|PDB:1RYP}.
HELIX 186 200 {ECO:0000244|PDB:1RYP}.
STRAND 202 205 {ECO:0000244|PDB:1RYP}.
HELIX 208 210 {ECO:0000244|PDB:1RYP}.
STRAND 211 217 {ECO:0000244|PDB:1RYP}.
STRAND 220 224 {ECO:0000244|PDB:1RYP}.
STRAND 226 229 {ECO:0000244|PDB:1RYP}.
HELIX 232 241 {ECO:0000244|PDB:1RYP}.
TURN 242 244 {ECO:0000244|PDB:3BDM}.
SEQUENCE 258 AA; 28714 MW; B43BB05233A01A9E CRC64;
MGSRRYDSRT TIFSPEGRLY QVEYALESIS HAGTAIGIMA SDGIVLAAER KVTSTLLEQD
TSTEKLYKLN DKIAVAVAGL TADAEILINT ARIHAQNYLK TYNEDIPVEI LVRRLSDIKQ
GYTQHGGLRP FGVSFIYAGY DDRYGYQLYT SNPSGNYTGW KAISVGANTS AAQTLLQMDY
KDDMKVDDAI ELALKTLSKT TDSSALTYDR LEFATIRKGA NDGEVYQKIF KPQEIKDILV
KTGITKKDED EEADEDMK


Related products :

Catalog number Product name Quantity
EIAAB32718 HC9,Homo sapiens,Human,Macropain subunit C9,Multicatalytic endopeptidase complex subunit C9,Proteasome component C9,Proteasome subunit alpha type-4,Proteasome subunit L,PSC9,PSMA4
EIAAB32711 Macropain subunit C8,Multicatalytic endopeptidase complex subunit C8,Proteasome component C8,Proteasome subunit alpha type-3,Proteasome subunit K,Psma3,Rat,Rattus norvegicus
EIAAB32714 Macropain subunit C8,Mouse,Multicatalytic endopeptidase complex subunit C8,Mus musculus,Proteasome component C8,Proteasome subunit alpha type-3,Proteasome subunit K,Psma3
EIAAB32716 Macropain subunit C9,Multicatalytic endopeptidase complex subunit C9,Proteasome component C9,Proteasome subunit alpha type-4,Proteasome subunit L,Psma4,Rat,Rattus norvegicus
EIAAB32715 Macropain subunit C9,Mouse,Multicatalytic endopeptidase complex subunit C9,Mus musculus,Proteasome component C9,Proteasome subunit alpha type-4,Proteasome subunit L,Psma4
EIAAB32704 Macropain subunit C2,Mouse,Multicatalytic endopeptidase complex subunit C2,Mus musculus,Proteasome component C2,Proteasome nu chain,Proteasome subunit alpha type-1,Psma1
EIAAB32706 Macropain subunit C2,Multicatalytic endopeptidase complex subunit C2,Proteasome component C2,Proteasome nu chain,Proteasome subunit alpha type-1,Psma1,Rat,Rattus norvegicus
15-288-22044A Proteasome subunit alpha type 1 - EC 3.4.25.1; Proteasome component C2; Macropain subunit C2; Multicatalytic endopeptidase complex subunit C2; Proteasome nu chain; 30 kDa prosomal protein; PROS-30 Pol 0.1 mg
15-288-22044A Proteasome subunit alpha type 1 - EC 3.4.25.1; Proteasome component C2; Macropain subunit C2; Multicatalytic endopeptidase complex subunit C2; Proteasome nu chain; 30 kDa prosomal protein; PROS-30 Pol 0.05 mg
10-288-22044F Proteasome subunit alpha type 1 - EC 3.4.25.1; Proteasome component C2; Macropain subunit C2; Multicatalytic endopeptidase complex subunit C2; Proteasome nu chain; 30 kDa prosomal protein; PROS-30 0.05 mg
10-288-22044F Proteasome subunit alpha type 1 - EC 3.4.25.1; Proteasome component C2; Macropain subunit C2; Multicatalytic endopeptidase complex subunit C2; Proteasome nu chain; 30 kDa prosomal protein; PROS-30 0.1 mg
18-003-44182 Proteasome subunit alpha type-1 - EC 3.4.25.1; Proteasome component C2; Macropain subunit C2; Multicatalytic endopeptidase complex subunit C2; Proteasome nu chain; 30 kDa prosomal protein; PROS-30 Pol 0.1 mg Protein A
18-003-44181 Proteasome subunit alpha type-1 - EC 3.4.25.1; Proteasome component C2; Macropain subunit C2; Multicatalytic endopeptidase complex subunit C2; Proteasome nu chain; 30 kDa prosomal protein; PROS-30 Pol 0.05 mg Aff Pur
EIAAB32776 Homo sapiens,Human,LMP7,Low molecular mass protein 7,Macropain subunit C13,Multicatalytic endopeptidase complex subunit C13,Proteasome component C13,Proteasome subunit beta type-8,Proteasome subunit b
EIAAB32710 Macropain subunit C3,Multicatalytic endopeptidase complex subunit C3,Proteasome component C3,Proteasome subunit alpha type-2,Psma2,Rat,Rattus norvegicus
EIAAB32707 Lmpc3,Macropain subunit C3,Mouse,Multicatalytic endopeptidase complex subunit C3,Mus musculus,Proteasome component C3,Proteasome subunit alpha type-2,Psma2
EIAAB32712 HC8,Homo sapiens,Human,Macropain subunit C8,Multicatalytic endopeptidase complex subunit C8,Proteasome component C8,Proteasome subunit alpha type-3,PSC8,PSMA3
EIAAB32708 HC3,Homo sapiens,Human,Macropain subunit C3,Multicatalytic endopeptidase complex subunit C3,Proteasome component C3,Proteasome subunit alpha type-2,PSC3,PSMA2
EIAAB32735 Macropain subunit C5,Multicatalytic endopeptidase complex subunit C5,Proteasome component C5,Proteasome gamma chain,Proteasome subunit beta type-1,Psmb1,Rat,Rattus norvegicus
EIAAB32737 Macropain subunit C5,Mouse,Multicatalytic endopeptidase complex subunit C5,Mus musculus,Proteasome component C5,Proteasome gamma chain,Proteasome subunit beta type-1,Psmb1
EIAAB32738 Homo sapiens,Human,Macropain subunit C5,Multicatalytic endopeptidase complex subunit C5,Proteasome component C5,Proteasome gamma chain,Proteasome subunit beta type-1,PSC5,PSMB1
EIAAB32772 Lmp7,Low molecular mass protein 7,Macropain subunit C13,Mc13,Mouse,Multicatalytic endopeptidase complex subunit C13,Mus musculus,Proteasome component C13,Proteasome subunit beta type-8,Proteasome subu
EIAAB32777 Macropain subunit C13,Multicatalytic endopeptidase complex subunit C13,Proteasome component C13,Proteasome subunit beta type-8,Proteasome subunit beta-5i,Psmb8,Rat,Rattus norvegicus
EIAAB32773 Macropain subunit C13,Multicatalytic endopeptidase complex subunit C13,Pig,Proteasome component C13,Proteasome subunit beta type-8,Proteasome subunit beta-5i,PSMB8,Sus scrofa
EIAAB32748 Macropain subunit C7-I,Multicatalytic endopeptidase complex subunit C7-I,Proteasome component C7-I,Proteasome subunit beta type-2,Psmb2,Rat,Rattus norvegicus


 

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