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Proteasome subunit beta type-2 (EC 3.4.25.1) (Macropain subunit PUP1) (Multicatalytic endopeptidase complex subunit PUP1) (Proteasome component PUP1) (Proteinase YSCE subunit PUP1)

 PSB2_YEAST              Reviewed;         261 AA.
P25043; D6W2L4;
01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
01-MAY-1992, sequence version 1.
23-MAY-2018, entry version 186.
RecName: Full=Proteasome subunit beta type-2;
EC=3.4.25.1;
AltName: Full=Macropain subunit PUP1;
AltName: Full=Multicatalytic endopeptidase complex subunit PUP1;
AltName: Full=Proteasome component PUP1;
AltName: Full=Proteinase YSCE subunit PUP1;
Flags: Precursor;
Name=PUP1; OrderedLocusNames=YOR157C;
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].
PubMed=1923775; DOI=10.1093/nar/19.18.5075;
Haffter P., Fox T.D.;
"Nucleotide sequence of PUP1 encoding a putative proteasome subunit in
Saccharomyces cerevisiae.";
Nucleic Acids Res. 19:5075-5075(1991).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=S288c / FY1678;
PubMed=9046089;
DOI=10.1002/(SICI)1097-0061(199701)13:1<73::AID-YEA52>3.0.CO;2-M;
Bordonne R., Camasses A., Madania A., Poch O., Tarassov I.A.,
Winsor B., Martin R.P.;
"Analysis of a 35.6 kb region on the right arm of Saccharomyces
cerevisiae chromosome XV.";
Yeast 13:73-83(1997).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169874;
Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W.,
Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R.,
Boyer J., Camasses A., Casamayor A., Casas C., Cheret G.,
Cziepluch C., Daignan-Fornier B., Dang V.-D., de Haan M., Delius H.,
Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F.,
Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A.,
Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J.,
Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P.,
Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M.,
Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R.,
Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S.,
Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A.,
Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M.,
Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C.,
Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S.,
Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
Nature 387:98-102(1997).
[4]
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).
[5]
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).
[6]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[7]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 30-251 OF COMPLEX WITH THE
20S PROTEASOME, PROTEOLYTIC PROCESSING, AND ACTIVE SITE.
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 30-261 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 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 30-251 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 30-251 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 30-251 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 30-251 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: Cleavage of peptide bonds with very broad
specificity.
-!- 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:
P25451:PUP3; NbExp=3; IntAct=EBI-14009, EBI-13993;
-!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
-!- MISCELLANEOUS: The side chain of Thr-30 acts as nucleophile, and
the N-terminal amino group acts as proton acceptor.
-!- MISCELLANEOUS: Present with 11400 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the peptidase T1B family.
{ECO:0000255|PROSITE-ProRule:PRU00809}.
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EMBL; X61189; CAA43492.1; -; Genomic_DNA.
EMBL; U55020; AAC49643.1; -; Genomic_DNA.
EMBL; Z75065; CAA99363.1; -; Genomic_DNA.
EMBL; BK006948; DAA10930.1; -; Genomic_DNA.
PIR; S26996; S26996.
RefSeq; NP_014800.3; NM_001183576.3.
PDB; 1FNT; X-ray; 3.20 A; I/W=30-261.
PDB; 1G0U; X-ray; 2.40 A; H/V=30-251.
PDB; 1G65; X-ray; 2.25 A; H/V=30-251.
PDB; 1JD2; X-ray; 3.00 A; H/O=30-251.
PDB; 1RYP; X-ray; 1.90 A; I/W=30-251.
PDB; 1Z7Q; X-ray; 3.22 A; I/W=30-251.
PDB; 2F16; X-ray; 2.80 A; H/V=30-251.
PDB; 2FAK; X-ray; 2.80 A; H/V=30-251.
PDB; 2GPL; X-ray; 2.81 A; H/V=30-251.
PDB; 2ZCY; X-ray; 2.90 A; H/V=30-261.
PDB; 3BDM; X-ray; 2.70 A; H/V=30-261.
PDB; 3D29; X-ray; 2.60 A; H/V=30-251.
PDB; 3DY3; X-ray; 2.81 A; H/V=30-251.
PDB; 3DY4; X-ray; 2.80 A; H/V=30-251.
PDB; 3E47; X-ray; 3.00 A; H/V=30-251.
PDB; 3GPJ; X-ray; 2.70 A; H/V=30-251.
PDB; 3GPT; X-ray; 2.41 A; H/V=30-251.
PDB; 3GPW; X-ray; 2.50 A; H/V=30-251.
PDB; 3HYE; X-ray; 2.50 A; H/V=30-251.
PDB; 3JCO; EM; 4.80 A; 4/i=1-261.
PDB; 3JCP; EM; 4.60 A; 4/i=1-261.
PDB; 3MG0; X-ray; 2.68 A; H/V=30-251.
PDB; 3MG4; X-ray; 3.11 A; H/V=30-251.
PDB; 3MG6; X-ray; 2.60 A; H/V=30-251.
PDB; 3MG7; X-ray; 2.78 A; H/V=30-251.
PDB; 3MG8; X-ray; 2.59 A; H/V=30-251.
PDB; 3NZJ; X-ray; 2.40 A; H/V=1-261.
PDB; 3NZW; X-ray; 2.50 A; H/V=1-261.
PDB; 3NZX; X-ray; 2.70 A; H/V=1-261.
PDB; 3OEU; X-ray; 2.60 A; H/V=30-251.
PDB; 3OEV; X-ray; 2.85 A; H/V=30-251.
PDB; 3OKJ; X-ray; 2.70 A; H/V=30-251.
PDB; 3SDI; X-ray; 2.65 A; H/V=30-251.
PDB; 3SDK; X-ray; 2.70 A; H/V=30-251.
PDB; 3SHJ; X-ray; 2.80 A; H/V=30-251.
PDB; 3TDD; X-ray; 2.70 A; H/V=30-251.
PDB; 3UN4; X-ray; 3.40 A; H/V=30-261.
PDB; 3UN8; X-ray; 2.70 A; H/V=30-261.
PDB; 3WXR; X-ray; 3.15 A; I/W=1-261.
PDB; 4CR2; EM; 7.70 A; 2=1-261.
PDB; 4CR3; EM; 9.30 A; 2=1-261.
PDB; 4CR4; EM; 8.80 A; 2=1-261.
PDB; 4EU2; X-ray; 2.51 A; I/W=30-251.
PDB; 4FZC; X-ray; 2.80 A; H/V=30-251.
PDB; 4FZG; X-ray; 3.00 A; H/V=30-251.
PDB; 4G4S; X-ray; 2.49 A; I=30-261.
PDB; 4GK7; X-ray; 2.80 A; H/V=30-251.
PDB; 4HNP; X-ray; 2.80 A; H/V=30-251.
PDB; 4HRC; X-ray; 2.80 A; H/V=30-251.
PDB; 4HRD; X-ray; 2.80 A; H/V=30-251.
PDB; 4INR; X-ray; 2.70 A; H/V=30-261.
PDB; 4INT; X-ray; 2.90 A; H/V=30-261.
PDB; 4INU; X-ray; 3.10 A; H/V=30-261.
PDB; 4J70; X-ray; 2.80 A; H/V=30-261.
PDB; 4JSQ; X-ray; 2.80 A; H/V=30-261.
PDB; 4JSU; X-ray; 2.90 A; H/V=30-261.
PDB; 4JT0; X-ray; 3.10 A; H/V=30-261.
PDB; 4LQI; X-ray; 2.70 A; H/V=30-251.
PDB; 4LTC; X-ray; 2.50 A; H/V=30-261.
PDB; 4NNN; X-ray; 2.50 A; H/V=30-261.
PDB; 4NNW; X-ray; 2.60 A; H/V=30-261.
PDB; 4NO1; X-ray; 2.50 A; H/V=30-261.
PDB; 4NO6; X-ray; 3.00 A; H/V=30-261.
PDB; 4NO8; X-ray; 2.70 A; H/V=30-261.
PDB; 4NO9; X-ray; 2.90 A; H/V=30-261.
PDB; 4Q1S; X-ray; 2.60 A; H/V=30-261.
PDB; 4QBY; X-ray; 3.00 A; H/V=30-261.
PDB; 4QLQ; X-ray; 2.40 A; H/V=30-261.
PDB; 4QLS; X-ray; 2.80 A; H/V=30-261.
PDB; 4QLT; X-ray; 2.80 A; H/V=30-261.
PDB; 4QLU; X-ray; 2.80 A; H/V=30-261.
PDB; 4QLV; X-ray; 2.90 A; H/V=30-261.
PDB; 4QUX; X-ray; 3.00 A; H/V=30-261.
PDB; 4QUY; X-ray; 2.80 A; H/V=30-261.
PDB; 4QV0; X-ray; 3.10 A; H/V=30-261.
PDB; 4QV1; X-ray; 2.50 A; H/V=30-261.
PDB; 4QV3; X-ray; 3.00 A; H/V=30-261.
PDB; 4QV4; X-ray; 2.70 A; H/V=30-261.
PDB; 4QV5; X-ray; 2.70 A; H/V=30-261.
PDB; 4QV6; X-ray; 2.80 A; H/V=30-261.
PDB; 4QV7; X-ray; 2.60 A; H/V=30-261.
PDB; 4QV8; X-ray; 2.90 A; H/V=30-261.
PDB; 4QV9; X-ray; 2.60 A; H/V=30-261.
PDB; 4QVL; X-ray; 2.80 A; H/V=30-261.
PDB; 4QVM; X-ray; 2.80 A; H/V=30-261.
PDB; 4QVN; X-ray; 2.90 A; H/V=30-261.
PDB; 4QVP; X-ray; 2.30 A; H/V=30-261.
PDB; 4QVQ; X-ray; 2.60 A; H/V=30-261.
PDB; 4QVV; X-ray; 2.80 A; H/V=30-261.
PDB; 4QVW; X-ray; 3.00 A; H/V=30-261.
PDB; 4QVY; X-ray; 2.51 A; H/V=30-261.
PDB; 4QW0; X-ray; 2.90 A; H/V=30-261.
PDB; 4QW1; X-ray; 2.90 A; H/V=30-261.
PDB; 4QW3; X-ray; 2.90 A; H/V=30-261.
PDB; 4QW4; X-ray; 2.80 A; H/V=30-261.
PDB; 4QW5; X-ray; 3.00 A; H/V=30-261.
PDB; 4QW6; X-ray; 2.90 A; H/V=30-261.
PDB; 4QW7; X-ray; 2.70 A; H/V=30-261.
PDB; 4QWF; X-ray; 3.00 A; H/V=30-261.
PDB; 4QWG; X-ray; 2.60 A; H/V=30-261.
PDB; 4QWI; X-ray; 2.60 A; H/V=30-261.
PDB; 4QWJ; X-ray; 2.90 A; H/V=30-261.
PDB; 4QWK; X-ray; 2.80 A; H/V=30-261.
PDB; 4QWL; X-ray; 2.60 A; H/V=30-261.
PDB; 4QWR; X-ray; 2.90 A; H/V=30-261.
PDB; 4QWS; X-ray; 3.00 A; H/V=30-261.
PDB; 4QWU; X-ray; 3.00 A; H/V=30-261.
PDB; 4QWX; X-ray; 2.90 A; H/V=30-261.
PDB; 4QXJ; X-ray; 2.80 A; H/V=30-261.
PDB; 4QZ0; X-ray; 3.00 A; H/V=30-261.
PDB; 4QZ1; X-ray; 3.00 A; H/V=30-261.
PDB; 4QZ2; X-ray; 2.70 A; H/V=30-261.
PDB; 4QZ3; X-ray; 2.80 A; H/V=30-261.
PDB; 4QZ4; X-ray; 3.00 A; H/V=30-261.
PDB; 4QZ5; X-ray; 2.80 A; H/V=30-261.
PDB; 4QZ6; X-ray; 2.90 A; H/V=30-261.
PDB; 4QZ7; X-ray; 2.80 A; H/V=30-261.
PDB; 4QZW; X-ray; 3.00 A; H/V=30-261.
PDB; 4QZX; X-ray; 2.60 A; H/V=30-261.
PDB; 4QZZ; X-ray; 2.90 A; H/V=30-261.
PDB; 4R00; X-ray; 2.80 A; H/V=30-261.
PDB; 4R02; X-ray; 2.50 A; H/V=30-261.
PDB; 4R17; X-ray; 2.10 A; H/V=30-261.
PDB; 4R18; X-ray; 2.40 A; H/V=30-261.
PDB; 4RUR; X-ray; 2.50 A; H/V=30-261.
PDB; 4V7O; X-ray; 3.00 A; AM/AY/BI/BW=30-251.
PDB; 4X6Z; X-ray; 2.70 A; I/W=1-261.
PDB; 4Y69; X-ray; 2.90 A; H/V=30-261.
PDB; 4Y6A; X-ray; 2.60 A; H/V=30-261.
PDB; 4Y6V; X-ray; 2.80 A; H/V=30-261.
PDB; 4Y6Z; X-ray; 2.70 A; H/V=30-261.
PDB; 4Y70; X-ray; 2.40 A; H/V=30-261.
PDB; 4Y74; X-ray; 2.70 A; H/V=30-261.
PDB; 4Y75; X-ray; 2.80 A; H/V=30-261.
PDB; 4Y77; X-ray; 2.50 A; H/V=30-261.
PDB; 4Y78; X-ray; 2.80 A; H/V=30-261.
PDB; 4Y7W; X-ray; 2.50 A; H/V=30-261.
PDB; 4Y7X; X-ray; 2.60 A; H/V=30-261.
PDB; 4Y7Y; X-ray; 2.40 A; H/V=30-261.
PDB; 4Y80; X-ray; 2.50 A; H/V=30-261.
PDB; 4Y81; X-ray; 2.80 A; H/V=30-261.
PDB; 4Y82; X-ray; 2.80 A; H/V=30-261.
PDB; 4Y84; X-ray; 2.70 A; H/V=30-261.
PDB; 4Y8G; X-ray; 2.60 A; H/V=30-261.
PDB; 4Y8H; X-ray; 2.50 A; H/V=30-261.
PDB; 4Y8I; X-ray; 2.60 A; H/V=30-261.
PDB; 4Y8J; X-ray; 2.70 A; H/V=30-261.
PDB; 4Y8K; X-ray; 2.60 A; H/V=30-261.
PDB; 4Y8L; X-ray; 2.40 A; H/V=30-261.
PDB; 4Y8M; X-ray; 2.80 A; H/V=30-261.
PDB; 4Y8N; X-ray; 2.60 A; H/V=30-261.
PDB; 4Y8O; X-ray; 2.70 A; H/V=30-261.
PDB; 4Y8P; X-ray; 2.80 A; H/V=30-261.
PDB; 4Y8Q; X-ray; 2.60 A; H/V=30-261.
PDB; 4Y8R; X-ray; 2.70 A; H/V=30-261.
PDB; 4Y8S; X-ray; 2.70 A; H/V=30-261.
PDB; 4Y8T; X-ray; 2.70 A; H/V=30-261.
PDB; 4Y8U; X-ray; 2.90 A; H/V=30-261.
PDB; 4Y9Y; X-ray; 2.80 A; H/V=30-261.
PDB; 4Y9Z; X-ray; 2.80 A; H/V=30-261.
PDB; 4YA0; X-ray; 2.80 A; H/V=30-261.
PDB; 4YA1; X-ray; 2.90 A; H/V=30-261.
PDB; 4YA2; X-ray; 2.70 A; H/V=30-261.
PDB; 4YA3; X-ray; 2.70 A; H/V=30-261.
PDB; 4YA4; X-ray; 2.90 A; H/V=30-261.
PDB; 4YA5; X-ray; 2.50 A; H/V=30-261.
PDB; 4YA7; X-ray; 2.70 A; H/V=30-261.
PDB; 4YA9; X-ray; 2.70 A; H/V=30-261.
PDB; 4Z1L; X-ray; 3.00 A; H/V=30-261.
PDB; 5A5B; EM; 9.50 A; 2=1-261.
PDB; 5AHJ; X-ray; 2.80 A; H/V=30-261.
PDB; 5BOU; X-ray; 2.60 A; H/V=30-261.
PDB; 5BXL; X-ray; 2.80 A; H/V=30-261.
PDB; 5BXN; X-ray; 2.80 A; H/V=30-261.
PDB; 5CGF; X-ray; 2.80 A; H/V=30-261.
PDB; 5CGG; X-ray; 2.90 A; H/V=30-261.
PDB; 5CGH; X-ray; 2.50 A; H/V=30-261.
PDB; 5CGI; X-ray; 2.80 A; H/V=30-261.
PDB; 5CZ4; X-ray; 2.30 A; H/V=30-261.
PDB; 5CZ5; X-ray; 2.80 A; H/V=30-261.
PDB; 5CZ6; X-ray; 2.70 A; H/V=30-261.
PDB; 5CZ7; X-ray; 2.50 A; H/V=30-261.
PDB; 5CZ8; X-ray; 2.80 A; H/V=30-261.
PDB; 5CZ9; X-ray; 2.90 A; H/V=30-261.
PDB; 5CZA; X-ray; 2.50 A; H/V=30-261.
PDB; 5D0S; X-ray; 2.50 A; H/V=30-261.
PDB; 5D0T; X-ray; 2.60 A; H/V=30-261.
PDB; 5D0V; X-ray; 2.90 A; H/V=30-261.
PDB; 5D0W; X-ray; 2.80 A; H/V=30-261.
PDB; 5D0X; X-ray; 2.60 A; H/V=30-261.
PDB; 5D0Z; X-ray; 2.90 A; H/V=30-261.
PDB; 5DKI; X-ray; 2.80 A; H/V=30-261.
PDB; 5DKJ; X-ray; 2.80 A; H/V=30-261.
PDB; 5FG7; X-ray; 2.70 A; H/V=24-261.
PDB; 5FG9; X-ray; 2.60 A; H/V=26-261.
PDB; 5FGA; X-ray; 2.70 A; H/V=30-261.
PDB; 5FGD; X-ray; 2.80 A; H/V=30-261.
PDB; 5FGE; X-ray; 2.60 A; H/V=30-261.
PDB; 5FGF; X-ray; 2.60 A; H/V=30-261.
PDB; 5FGG; X-ray; 2.70 A; H/V=30-261.
PDB; 5FGH; X-ray; 2.80 A; H/V=30-261.
PDB; 5FGI; X-ray; 2.90 A; H/V=18-261.
PDB; 5FHS; X-ray; 2.70 A; H/V=30-261.
PDB; 5JHR; X-ray; 2.90 A; H/V=30-261.
PDB; 5JHS; X-ray; 3.00 A; H/V=30-261.
PDB; 5L52; X-ray; 2.70 A; H/V=30-261.
PDB; 5L54; X-ray; 2.80 A; H/V=30-261.
PDB; 5L55; X-ray; 2.90 A; H/V=30-261.
PDB; 5L5A; X-ray; 2.40 A; H/V=30-261.
PDB; 5L5B; X-ray; 2.80 A; H/V=30-261.
PDB; 5L5D; X-ray; 2.80 A; H/V=30-261.
PDB; 5L5E; X-ray; 2.90 A; H/V=30-261.
PDB; 5L5F; X-ray; 2.50 A; H/V=30-261.
PDB; 5L5H; X-ray; 2.60 A; H/V=30-261.
PDB; 5L5I; X-ray; 2.90 A; H/V=30-261.
PDB; 5L5J; X-ray; 2.90 A; H/V=30-261.
PDB; 5L5O; X-ray; 2.60 A; H/V=30-261.
PDB; 5L5P; X-ray; 2.80 A; H/V=30-261.
PDB; 5L5Q; X-ray; 2.80 A; H/V=30-261.
PDB; 5L5R; X-ray; 2.90 A; H/V=30-261.
PDB; 5L5S; X-ray; 2.60 A; H/V=30-261.
PDB; 5L5T; X-ray; 2.90 A; H/V=30-261.
PDB; 5L5U; X-ray; 2.60 A; H/V=30-261.
PDB; 5L5V; X-ray; 2.70 A; H/V=30-261.
PDB; 5L5W; X-ray; 2.80 A; H/V=30-261.
PDB; 5L5X; X-ray; 2.90 A; H/V=30-261.
PDB; 5L5Y; X-ray; 2.70 A; H/V=30-261.
PDB; 5L5Z; X-ray; 2.70 A; H/V=30-261.
PDB; 5L60; X-ray; 2.70 A; H/V=30-261.
PDB; 5L61; X-ray; 2.80 A; H/V=30-261.
PDB; 5L62; X-ray; 2.80 A; H/V=30-261.
PDB; 5L63; X-ray; 2.70 A; H/V=30-261.
PDB; 5L64; X-ray; 2.70 A; H/V=30-261.
PDB; 5L65; X-ray; 2.90 A; H/V=30-261.
PDB; 5L66; X-ray; 2.80 A; H/V=30-261.
PDB; 5L67; X-ray; 2.60 A; H/V=30-261.
PDB; 5L68; X-ray; 2.80 A; H/V=30-261.
PDB; 5L69; X-ray; 2.70 A; H/V=30-261.
PDB; 5L6A; X-ray; 2.80 A; H/V=30-261.
PDB; 5L6B; X-ray; 2.60 A; H/V=30-261.
PDB; 5L6C; X-ray; 2.60 A; H/V=30-261.
PDB; 5LAI; X-ray; 2.50 A; H/V=30-261.
PDB; 5LAJ; X-ray; 2.90 A; H/V=30-261.
PDB; 5LTT; X-ray; 2.70 A; H/V=30-261.
PDB; 5M2B; X-ray; 2.70 A; H/V=30-261.
PDB; 5MP9; EM; 4.10 A; 2/i=1-261.
PDB; 5MPA; EM; 4.50 A; 2/i=1-261.
PDB; 5MPB; EM; 7.80 A; 2/i=1-261.
PDB; 5MPC; EM; 7.70 A; 2/i=1-261.
PDB; 5NIF; X-ray; 3.00 A; I/W=1-261.
PDB; 5WVI; EM; 6.30 A; 2/i=1-261.
PDB; 5WVK; EM; 4.20 A; 2/i=1-261.
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; -.
ProteinModelPortal; P25043; -.
SMR; P25043; -.
BioGrid; 34553; 270.
DIP; DIP-2818N; -.
IntAct; P25043; 12.
MINT; P25043; -.
STRING; 4932.YOR157C; -.
MEROPS; T01.011; -.
MaxQB; P25043; -.
PaxDb; P25043; -.
PRIDE; P25043; -.
EnsemblFungi; YOR157C; YOR157C; YOR157C.
GeneID; 854328; -.
KEGG; sce:YOR157C; -.
EuPathDB; FungiDB:YOR157C; -.
SGD; S000005683; PUP1.
GeneTree; ENSGT00510000046533; -.
HOGENOM; HOG000182856; -.
InParanoid; P25043; -.
KO; K02739; -.
OMA; DLCVIRK; -.
OrthoDB; EOG092C44RU; -.
BioCyc; YEAST:G3O-33674-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-349425; Autodegradation of the E3 ubiquitin ligase COP1.
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-6798695; Neutrophil degranulation.
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; P25043; -.
PRO; PR:P25043; -.
Proteomes; UP000002311; Chromosome XV.
GO; GO:0005789; C:endoplasmic reticulum membrane; IC:SGD.
GO; GO:0005634; C:nucleus; IDA:SGD.
GO; GO:0019774; C:proteasome core complex, beta-subunit complex; IDA:SGD.
GO; GO:0034515; C:proteasome storage granule; IDA:SGD.
GO; GO:0004175; F:endopeptidase activity; IMP:SGD.
GO; GO:0004298; F:threonine-type endopeptidase activity; IEA:UniProtKB-KW.
GO; GO:0010499; P:proteasomal ubiquitin-independent protein catabolic process; IDA: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; IPR000243; Pept_T1A_subB.
InterPro; IPR035216; Proteasome_beta7.
InterPro; IPR024689; Proteasome_bsu_C.
InterPro; IPR016050; Proteasome_bsu_CS.
InterPro; IPR001353; Proteasome_sua/b.
InterPro; IPR023333; Proteasome_suB-type.
PANTHER; PTHR11599:SF44; PTHR11599:SF44; 1.
Pfam; PF12465; Pr_beta_C; 1.
Pfam; PF00227; Proteasome; 1.
PRINTS; PR00141; PROTEASOME.
SUPFAM; SSF56235; SSF56235; 1.
PROSITE; PS00854; PROTEASOME_BETA_1; 1.
PROSITE; PS51476; PROTEASOME_BETA_2; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Cytoplasm; Hydrolase; Nucleus;
Protease; Proteasome; Reference proteome; Threonine protease; Zymogen.
PROPEP 1 29 Removed in mature form.
/FTId=PRO_0000026657.
CHAIN 30 261 Proteasome subunit beta type-2.
/FTId=PRO_0000026658.
ACT_SITE 30 30 Nucleophile.
{ECO:0000269|PubMed:9087403}.
STRAND 23 25 {ECO:0000244|PDB:5FGI}.
STRAND 32 37 {ECO:0000244|PDB:1RYP}.
STRAND 40 45 {ECO:0000244|PDB:1RYP}.
STRAND 49 51 {ECO:0000244|PDB:1RYP}.
STRAND 54 59 {ECO:0000244|PDB:1RYP}.
STRAND 63 67 {ECO:0000244|PDB:1RYP}.
STRAND 70 76 {ECO:0000244|PDB:1RYP}.
HELIX 78 99 {ECO:0000244|PDB:1RYP}.
HELIX 105 118 {ECO:0000244|PDB:1RYP}.
TURN 119 121 {ECO:0000244|PDB:1RYP}.
STRAND 125 133 {ECO:0000244|PDB:1RYP}.
STRAND 136 142 {ECO:0000244|PDB:1RYP}.
TURN 144 146 {ECO:0000244|PDB:1G0U}.
STRAND 148 150 {ECO:0000244|PDB:1RYP}.
STRAND 152 157 {ECO:0000244|PDB:1RYP}.
HELIX 160 170 {ECO:0000244|PDB:1RYP}.
HELIX 177 194 {ECO:0000244|PDB:1RYP}.
STRAND 202 208 {ECO:0000244|PDB:1RYP}.
STRAND 213 220 {ECO:0000244|PDB:1RYP}.
STRAND 241 246 {ECO:0000244|PDB:1RYP}.
SEQUENCE 261 AA; 28268 MW; 13A8F2B75584539A CRC64;
MAGLSFDNYQ RNNFLAENSH TQPKATSTGT TIVGVKFNNG VVIAADTRST QGPIVADKNC
AKLHRISPKI WCAGAGTAAD TEAVTQLIGS NIELHSLYTS REPRVVSALQ MLKQHLFKYQ
GHIGAYLIVA GVDPTGSHLF SIHAHGSTDV GYYLSLGSGS LAAMAVLESH WKQDLTKEEA
IKLASDAIQA GIWNDLGSGS NVDVCVMEIG KDAEYLRNYL TPNVREEKQK SYKFPRGTTA
VLKESIVNIC DIQEEQVDIT A


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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
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
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
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
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


 

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