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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.
13-FEB-2019, entry version 200.
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}.
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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.
PDB; 6H39; X-ray; 2.50 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; -.
PDBsum; 6H39; -.
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; -.
EuPathDB; FungiDB:YGR135W; -.
SGD; S000003367; PRE9.
GeneTree; ENSGT00550000074827; -.
HOGENOM; HOG000091085; -.
InParanoid; P23638; -.
KO; K02728; -.
OMA; MSKTMDS; -.
BioCyc; YEAST:G3O-30841-MONOMER; -.
Reactome; R-SCE-187577; SCF(Skp2)-mediated degradation of p27/p21.
Reactome; R-SCE-5689880; Ub-specific processing proteases.
Reactome; R-SCE-68949; Orc1 removal from chromatin.
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


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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

Kits Elisa; taq POLYMERASE

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Gentaur; yes we can

Pathways :
WP2272: Pathogenic Escherichia coli infection
WP1566: Citrate cycle (TCA cycle)
WP1614: 1- and 2-Methylnaphthalene degradation
WP1655: Geraniol degradation
WP1626: Benzoate degradation via CoA ligation
WP1634: Butanoate metabolism
WP1644: DNA replication
WP1663: Homologous recombination
WP1671: Methane metabolism
WP1672: Mismatch repair
WP1680: Oxidative phosphorylation
WP1693: Purine metabolism
WP1694: Pyrimidine metabolism
WP1711: Trinitrotoluene degradation
WP1718: Vitamin B6 metabolism
WP2292: Chemokine signaling pathway
WP470: Proteasome Degradation
WP1079: Proteasome Degradation
WP1196: Proteasome Degradation
WP1209: EBV LMP1 signaling
WP1224: EBV LMP1 signaling
WP1240: Proteasome Degradation
WP1571: EBV LMP1 signaling
WP158: Proteasome Degradation
WP1584: Type II diabetes mellitus

Related Genes :
[PRE9 PRS5 YGR135W] 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)
[P2RY13 GPR86 GPR94 FKSG77] P2Y purinoceptor 13 (P2Y13) (G-protein coupled receptor 86) (G-protein coupled receptor 94)
[SCL1 PRC2 PRS2 YGL011C] Proteasome subunit alpha type-1 (EC 3.4.25.1) (Macropain subunit C7-alpha) (Multicatalytic endopeptidase complex C7) (Proteasome component C7-alpha) (Proteasome component Y8) (Proteinase YSCE subunit 7) (SCL1 suppressor protein)
[PRE1 YER012W] Proteasome subunit beta type-4 (EC 3.4.25.1) (Macropain subunit C11) (Multicatalytic endopeptidase complex subunit C11) (Proteasome component C11) (Proteinase YSCE subunit 11)
[PRE8 PRS4 YML092C] Proteasome subunit alpha type-2 (EC 3.4.25.1) (Macropain subunit Y7) (Multicatalytic endopeptidase complex subunit Y7) (Proteasome component Y7) (Proteinase YSCE subunit 7)
[PRE10 PRC1 PRS1 YOR362C O6650] Probable proteasome subunit alpha type-7 (EC 3.4.25.1) (Macropain subunit C1) (Multicatalytic endopeptidase complex subunit C1) (Proteasome component C1) (Proteinase YSCE subunit 1)
[PRE6 YOL038W] Proteasome subunit alpha type-4 (EC 3.4.25.1) (Macropain subunit PRE6) (Multicatalytic endopeptidase complex subunit PRE6) (Proteasome component PRE6) (Proteinase YSCE subunit PRE6)
[PUP2 DOA5 YGR253C G9155] Proteasome subunit alpha type-5 (EC 3.4.25.1) (Macropain subunit PUP2) (Multicatalytic endopeptidase complex subunit PUP2) (Proteasome component PUP2) (Proteinase YSCE subunit PUP2)
[PRE3 YJL001W J1407] Proteasome subunit beta type-1 (EC 3.4.25.1) (Macropain subunit PRE3) (Multicatalytic endopeptidase complex subunit PRE3) (Proteasome component PRE3) (Proteinase YSCE subunit PRE3)
[PRE5 YMR314W YM9924.06] Proteasome subunit alpha type-6 (EC 3.4.25.1) (Macropain subunit PRE5) (Multicatalytic endopeptidase complex subunit PRE5) (Proteasome component PRE5) (Proteinase YSCE subunit PRE5)
[PRE4 YFR050C] Proteasome subunit beta type-7 (EC 3.4.25.1) (Macropain subunit PRE4) (Multicatalytic endopeptidase complex subunit PRE4) (Proteasome component PRE4) (Proteinase YSCE subunit PRE4)
[PRE2 DOA3 PRG1 YPR103W P8283.10] Proteasome subunit beta type-5 (EC 3.4.25.1) (Macropain subunit PRE2) (Multicatalytic endopeptidase complex subunit PRE2) (Proteasome component PRE2) (Proteinase YSCE subunit PRE2)
[PUP1 YOR157C] 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)
[Psmb8 Lmp7 Mc13] Proteasome subunit beta type-8 (EC 3.4.25.1) (Low molecular mass protein 7) (Macropain subunit C13) (Multicatalytic endopeptidase complex subunit C13) (Proteasome component C13) (Proteasome subunit beta-5i)
[PSMB8 LMP7 PSMB5i RING10 Y2] Proteasome subunit beta type-8 (EC 3.4.25.1) (Low molecular mass protein 7) (Macropain subunit C13) (Multicatalytic endopeptidase complex subunit C13) (Proteasome component C13) (Proteasome subunit beta-5i) (Really interesting new gene 10 protein)
[Psma1] Proteasome subunit alpha type-1 (EC 3.4.25.1) (Macropain subunit C2) (Multicatalytic endopeptidase complex subunit C2) (Proteasome component C2) (Proteasome nu chain)
[PSMA1 HC2 NU PROS30 PSC2] Proteasome subunit alpha type-1 (EC 3.4.25.1) (30 kDa prosomal protein) (PROS-30) (Macropain subunit C2) (Multicatalytic endopeptidase complex subunit C2) (Proteasome component C2) (Proteasome nu chain)
[PSMA4 HC9 PSC9] Proteasome subunit alpha type-4 (EC 3.4.25.1) (Macropain subunit C9) (Multicatalytic endopeptidase complex subunit C9) (Proteasome component C9) (Proteasome subunit L)
[PSMA3 HC8 PSC8] Proteasome subunit alpha type-3 (EC 3.4.25.1) (Macropain subunit C8) (Multicatalytic endopeptidase complex subunit C8) (Proteasome component C8)
[PSMA2 HC3 PSC3] Proteasome subunit alpha type-2 (EC 3.4.25.1) (Macropain subunit C3) (Multicatalytic endopeptidase complex subunit C3) (Proteasome component C3)
[PSMB10 LMP10 MECL1] Proteasome subunit beta type-10 (EC 3.4.25.1) (Low molecular mass protein 10) (Macropain subunit MECl-1) (Multicatalytic endopeptidase complex subunit MECl-1) (Proteasome MECl-1) (Proteasome subunit beta-2i)
[Psma3] Proteasome subunit alpha type-3 (EC 3.4.25.1) (Macropain subunit C8) (Multicatalytic endopeptidase complex subunit C8) (Proteasome component C8) (Proteasome subunit K)
[PSMB1 PSC5] Proteasome subunit beta type-1 (EC 3.4.25.1) (Macropain subunit C5) (Multicatalytic endopeptidase complex subunit C5) (Proteasome component C5) (Proteasome gamma chain)
[PUP3 YER094C] Proteasome subunit beta type-3 (EC 3.4.25.1) (Macropain subunit PUP3) (Multicatalytic endopeptidase complex subunit PUP3) (Proteasome component PUP3)
[Psma2 Lmpc3] Proteasome subunit alpha type-2 (EC 3.4.25.1) (Macropain subunit C3) (Multicatalytic endopeptidase complex subunit C3) (Proteasome component C3)
[PSMB5 LMPX MB1 X] Proteasome subunit beta type-5 (EC 3.4.25.1) (Macropain epsilon chain) (Multicatalytic endopeptidase complex epsilon chain) (Proteasome chain 6) (Proteasome epsilon chain) (Proteasome subunit MB1) (Proteasome subunit X)
[Psma4] Proteasome subunit alpha type-4 (EC 3.4.25.1) (Macropain subunit C9) (Multicatalytic endopeptidase complex subunit C9) (Proteasome component C9) (Proteasome subunit L)
[PSMB9 LMP2 PSMB6i RING12] Proteasome subunit beta type-9 (EC 3.4.25.1) (Low molecular mass protein 2) (Macropain chain 7) (Multicatalytic endopeptidase complex chain 7) (Proteasome chain 7) (Proteasome subunit beta-1i) (Really interesting new gene 12 protein)
[Psmb10 Lmp10 Mecl1] Proteasome subunit beta type-10 (EC 3.4.25.1) (Low molecular mass protein 10) (Macropain subunit MECl-1) (Multicatalytic endopeptidase complex subunit MECl-1) (Proteasome MECl-1) (Proteasome subunit beta-2i)
[Psmb1] Proteasome subunit beta type-1 (EC 3.4.25.1) (Macropain subunit C5) (Multicatalytic endopeptidase complex subunit C5) (Proteasome component C5) (Proteasome gamma chain)

Bibliography :
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