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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)

 PSA2_YEAST              Reviewed;         250 AA.
P23639; D6W0J3;
01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
01-NOV-1991, sequence version 1.
23-MAY-2018, entry version 196.
RecName: Full=Proteasome subunit alpha type-2;
EC=3.4.25.1;
AltName: Full=Macropain subunit Y7;
AltName: Full=Multicatalytic endopeptidase complex subunit Y7;
AltName: Full=Proteasome component Y7;
AltName: Full=Proteinase YSCE subunit 7;
Name=PRE8; Synonyms=PRS4; OrderedLocusNames=YML092C;
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 PARTIAL PROTEIN SEQUENCE.
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=9169872;
Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S.,
Jagels K., Lye G., Moule S., Odell C., Pearson D., Rajandream M.A.,
Rice P., Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome
XIII.";
Nature 387:90-93(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]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=17322287; DOI=10.1101/gr.6037607;
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A.,
Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F.,
Williamson J., Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G.,
Kolodner R.D., LaBaer J.;
"Approaching a complete repository of sequence-verified protein-
encoding clones for Saccharomyces cerevisiae.";
Genome Res. 17:536-543(2007).
[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=18407956; DOI=10.1074/mcp.M700468-MCP200;
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth
phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
[7]
UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-108, 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).
[8]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) 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).
[9]
X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) 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).
[10]
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).
[11]
X-RAY CRYSTALLOGRAPHY (2.81 ANGSTROMS) 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).
[12]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) 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).
[13]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) 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).
[14]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 20-250 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).
[15]
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. {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:
P23638:PRE9; NbExp=3; IntAct=EBI-13959, EBI-13967;
P21243:SCL1; NbExp=7; IntAct=EBI-13959, EBI-13975;
-!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
-!- MISCELLANEOUS: Present with 7060 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; X56731; CAA40055.1; -; Genomic_DNA.
EMBL; Z46660; CAA86646.1; -; Genomic_DNA.
EMBL; AY557762; AAS56088.1; -; Genomic_DNA.
EMBL; BK006946; DAA09807.1; -; Genomic_DNA.
PIR; S12938; SNBYY7.
RefSeq; NP_013618.1; NM_001182451.1.
PDB; 1FNT; X-ray; 3.20 A; B/P=1-250.
PDB; 1G0U; X-ray; 2.40 A; A/O=1-250.
PDB; 1G65; X-ray; 2.25 A; A/O=1-250.
PDB; 1JD2; X-ray; 3.00 A; A/V=1-250.
PDB; 1RYP; X-ray; 1.90 A; B/P=1-250.
PDB; 1Z7Q; X-ray; 3.22 A; B/P=1-250.
PDB; 2F16; X-ray; 2.80 A; A/O=1-250.
PDB; 2FAK; X-ray; 2.80 A; A/O=1-250.
PDB; 2GPL; X-ray; 2.81 A; A/O=1-250.
PDB; 2ZCY; X-ray; 2.90 A; A/O=1-250.
PDB; 3BDM; X-ray; 2.70 A; A/O=1-250.
PDB; 3D29; X-ray; 2.60 A; A/O=1-250.
PDB; 3DY3; X-ray; 2.81 A; A/O=1-250.
PDB; 3DY4; X-ray; 2.80 A; A/O=1-250.
PDB; 3E47; X-ray; 3.00 A; A/O=1-250.
PDB; 3GPJ; X-ray; 2.70 A; A/O=1-250.
PDB; 3GPT; X-ray; 2.41 A; A/O=1-250.
PDB; 3GPW; X-ray; 2.50 A; A/O=1-250.
PDB; 3HYE; X-ray; 2.50 A; A/O=1-250.
PDB; 3JCO; EM; 4.80 A; B/b=1-250.
PDB; 3JCP; EM; 4.60 A; B/b=1-250.
PDB; 3MG0; X-ray; 2.68 A; A/O=1-250.
PDB; 3MG4; X-ray; 3.11 A; A/O=1-250.
PDB; 3MG6; X-ray; 2.60 A; A/O=1-250.
PDB; 3MG7; X-ray; 2.78 A; A/O=1-250.
PDB; 3MG8; X-ray; 2.59 A; A/O=1-250.
PDB; 3NZJ; X-ray; 2.40 A; A/O=1-250.
PDB; 3NZW; X-ray; 2.50 A; A/O=1-250.
PDB; 3NZX; X-ray; 2.70 A; A/O=1-250.
PDB; 3OEU; X-ray; 2.60 A; A/O=1-250.
PDB; 3OEV; X-ray; 2.85 A; A/O=1-250.
PDB; 3OKJ; X-ray; 2.70 A; A/O=1-250.
PDB; 3SDI; X-ray; 2.65 A; A/O=1-250.
PDB; 3SDK; X-ray; 2.70 A; A/O=1-250.
PDB; 3SHJ; X-ray; 2.80 A; A/O=1-250.
PDB; 3TDD; X-ray; 2.70 A; A/O=1-250.
PDB; 3UN4; X-ray; 3.40 A; A/O=1-250.
PDB; 3UN8; X-ray; 2.70 A; A/O=1-250.
PDB; 3WXR; X-ray; 3.15 A; B/P=1-250.
PDB; 4CR2; EM; 7.70 A; B=1-250.
PDB; 4CR3; EM; 9.30 A; B=1-250.
PDB; 4CR4; EM; 8.80 A; B=1-250.
PDB; 4EU2; X-ray; 2.51 A; B/P=1-250.
PDB; 4FZC; X-ray; 2.80 A; A/O=1-250.
PDB; 4FZG; X-ray; 3.00 A; A/O=1-250.
PDB; 4G4S; X-ray; 2.49 A; B=1-250.
PDB; 4GK7; X-ray; 2.80 A; A/O=1-250.
PDB; 4HNP; X-ray; 2.80 A; A/O=1-250.
PDB; 4HRC; X-ray; 2.80 A; A/O=2-250.
PDB; 4HRD; X-ray; 2.80 A; A/O=1-250.
PDB; 4INR; X-ray; 2.70 A; A/O=1-250.
PDB; 4INT; X-ray; 2.90 A; A/O=1-250.
PDB; 4INU; X-ray; 3.10 A; A/O=1-250.
PDB; 4J70; X-ray; 2.80 A; A/O=1-250.
PDB; 4JSQ; X-ray; 2.80 A; A/O=1-250.
PDB; 4JSU; X-ray; 2.90 A; A/O=1-250.
PDB; 4JT0; X-ray; 3.10 A; A/O=1-250.
PDB; 4LQI; X-ray; 2.70 A; A/O=1-250.
PDB; 4LTC; X-ray; 2.50 A; A/O=1-250.
PDB; 4NNN; X-ray; 2.50 A; A/O=1-250.
PDB; 4NNW; X-ray; 2.60 A; A/O=1-250.
PDB; 4NO1; X-ray; 2.50 A; A/O=1-250.
PDB; 4NO6; X-ray; 3.00 A; A/O=1-250.
PDB; 4NO8; X-ray; 2.70 A; A/O=1-250.
PDB; 4NO9; X-ray; 2.90 A; A/O=1-250.
PDB; 4Q1S; X-ray; 2.60 A; A/O=1-250.
PDB; 4QBY; X-ray; 3.00 A; A/O=1-250.
PDB; 4QLQ; X-ray; 2.40 A; A/O=1-250.
PDB; 4QLS; X-ray; 2.80 A; A/O=1-250.
PDB; 4QLT; X-ray; 2.80 A; A/O=1-250.
PDB; 4QLU; X-ray; 2.80 A; A/O=1-250.
PDB; 4QLV; X-ray; 2.90 A; A/O=1-250.
PDB; 4QUX; X-ray; 3.00 A; A/O=1-250.
PDB; 4QUY; X-ray; 2.80 A; A/O=1-250.
PDB; 4QV0; X-ray; 3.10 A; A/O=1-250.
PDB; 4QV1; X-ray; 2.50 A; A/O=1-250.
PDB; 4QV3; X-ray; 3.00 A; A/O=1-250.
PDB; 4QV4; X-ray; 2.70 A; A/O=1-250.
PDB; 4QV5; X-ray; 2.70 A; A/O=1-250.
PDB; 4QV6; X-ray; 2.80 A; A/O=1-250.
PDB; 4QV7; X-ray; 2.60 A; A/O=1-250.
PDB; 4QV8; X-ray; 2.90 A; A/O=1-250.
PDB; 4QV9; X-ray; 2.60 A; A/O=1-250.
PDB; 4QVL; X-ray; 2.80 A; A/O=1-250.
PDB; 4QVM; X-ray; 2.80 A; A/O=1-250.
PDB; 4QVN; X-ray; 2.90 A; A/O=1-250.
PDB; 4QVP; X-ray; 2.30 A; A/O=1-250.
PDB; 4QVQ; X-ray; 2.60 A; A/O=1-250.
PDB; 4QVV; X-ray; 2.80 A; A/O=1-250.
PDB; 4QVW; X-ray; 3.00 A; A/O=1-250.
PDB; 4QVY; X-ray; 2.51 A; A/O=1-250.
PDB; 4QW0; X-ray; 2.90 A; A/O=1-250.
PDB; 4QW1; X-ray; 2.90 A; A/O=1-250.
PDB; 4QW3; X-ray; 2.90 A; A/O=1-250.
PDB; 4QW4; X-ray; 2.80 A; A/O=1-250.
PDB; 4QW5; X-ray; 3.00 A; A/O=1-250.
PDB; 4QW6; X-ray; 2.90 A; A/O=1-250.
PDB; 4QW7; X-ray; 2.70 A; A/O=1-250.
PDB; 4QWF; X-ray; 3.00 A; A/O=1-250.
PDB; 4QWG; X-ray; 2.60 A; A/O=1-250.
PDB; 4QWI; X-ray; 2.60 A; A/O=1-250.
PDB; 4QWJ; X-ray; 2.90 A; A/O=1-250.
PDB; 4QWK; X-ray; 2.80 A; A/O=1-250.
PDB; 4QWL; X-ray; 2.60 A; A/O=1-250.
PDB; 4QWR; X-ray; 2.90 A; A/O=1-250.
PDB; 4QWS; X-ray; 3.00 A; A/O=1-250.
PDB; 4QWU; X-ray; 3.00 A; A/O=1-250.
PDB; 4QWX; X-ray; 2.90 A; A/O=1-250.
PDB; 4QXJ; X-ray; 2.80 A; A/O=1-250.
PDB; 4QZ0; X-ray; 3.00 A; A/O=1-250.
PDB; 4QZ1; X-ray; 3.00 A; A/O=1-250.
PDB; 4QZ2; X-ray; 2.70 A; A/O=1-250.
PDB; 4QZ3; X-ray; 2.80 A; A/O=1-250.
PDB; 4QZ4; X-ray; 3.00 A; A/O=1-250.
PDB; 4QZ5; X-ray; 2.80 A; A/O=1-250.
PDB; 4QZ6; X-ray; 2.90 A; A/O=1-250.
PDB; 4QZ7; X-ray; 2.80 A; A/O=1-250.
PDB; 4QZW; X-ray; 3.00 A; A/O=1-250.
PDB; 4QZX; X-ray; 2.60 A; A/O=1-250.
PDB; 4QZZ; X-ray; 2.90 A; A/O=1-250.
PDB; 4R00; X-ray; 2.80 A; A/O=1-250.
PDB; 4R02; X-ray; 2.50 A; A/O=1-250.
PDB; 4R17; X-ray; 2.10 A; A/O=1-250.
PDB; 4R18; X-ray; 2.40 A; A/O=1-250.
PDB; 4RUR; X-ray; 2.50 A; A/O=1-250.
PDB; 4V7O; X-ray; 3.00 A; AG/AS/BB/BP=20-250.
PDB; 4X6Z; X-ray; 2.70 A; B/P=1-250.
PDB; 4Y69; X-ray; 2.90 A; A/O=1-250.
PDB; 4Y6A; X-ray; 2.60 A; A/O=1-250.
PDB; 4Y6V; X-ray; 2.80 A; A/O=1-250.
PDB; 4Y6Z; X-ray; 2.70 A; A/O=1-250.
PDB; 4Y70; X-ray; 2.40 A; A/O=1-250.
PDB; 4Y74; X-ray; 2.70 A; A/O=1-250.
PDB; 4Y75; X-ray; 2.80 A; A/O=1-250.
PDB; 4Y77; X-ray; 2.50 A; A/O=1-250.
PDB; 4Y78; X-ray; 2.80 A; A/O=1-250.
PDB; 4Y7W; X-ray; 2.50 A; A/O=1-250.
PDB; 4Y7X; X-ray; 2.60 A; A/O=1-250.
PDB; 4Y7Y; X-ray; 2.40 A; A/O=1-250.
PDB; 4Y80; X-ray; 2.50 A; A/O=1-250.
PDB; 4Y81; X-ray; 2.80 A; A/O=1-250.
PDB; 4Y82; X-ray; 2.80 A; A/O=1-250.
PDB; 4Y84; X-ray; 2.70 A; A/O=1-250.
PDB; 4Y8G; X-ray; 2.60 A; A/O=1-250.
PDB; 4Y8H; X-ray; 2.50 A; A/O=1-250.
PDB; 4Y8I; X-ray; 2.60 A; A/O=1-250.
PDB; 4Y8J; X-ray; 2.70 A; A/O=1-250.
PDB; 4Y8K; X-ray; 2.60 A; A/O=1-250.
PDB; 4Y8L; X-ray; 2.40 A; A/O=1-250.
PDB; 4Y8M; X-ray; 2.80 A; A/O=1-250.
PDB; 4Y8N; X-ray; 2.60 A; A/O=1-250.
PDB; 4Y8O; X-ray; 2.70 A; A/O=1-250.
PDB; 4Y8P; X-ray; 2.80 A; A/O=1-250.
PDB; 4Y8Q; X-ray; 2.60 A; A/O=1-250.
PDB; 4Y8R; X-ray; 2.70 A; A/O=1-250.
PDB; 4Y8S; X-ray; 2.70 A; A/O=1-250.
PDB; 4Y8T; X-ray; 2.70 A; A/O=1-250.
PDB; 4Y8U; X-ray; 2.90 A; A/O=1-250.
PDB; 4Y9Y; X-ray; 2.80 A; A/O=1-250.
PDB; 4Y9Z; X-ray; 2.80 A; A/O=1-250.
PDB; 4YA0; X-ray; 2.80 A; A/O=1-250.
PDB; 4YA1; X-ray; 2.90 A; A/O=1-250.
PDB; 4YA2; X-ray; 2.70 A; A/O=1-250.
PDB; 4YA3; X-ray; 2.70 A; A/O=1-250.
PDB; 4YA4; X-ray; 2.90 A; A/O=1-250.
PDB; 4YA5; X-ray; 2.50 A; A/O=1-250.
PDB; 4YA7; X-ray; 2.70 A; A/O=1-250.
PDB; 4YA9; X-ray; 2.70 A; A/O=1-250.
PDB; 4Z1L; X-ray; 3.00 A; A/O=1-250.
PDB; 5A5B; EM; 9.50 A; B=1-250.
PDB; 5AHJ; X-ray; 2.80 A; A/O=1-250.
PDB; 5BOU; X-ray; 2.60 A; A/O=1-250.
PDB; 5BXL; X-ray; 2.80 A; A/O=1-250.
PDB; 5BXN; X-ray; 2.80 A; A/O=1-250.
PDB; 5CGF; X-ray; 2.80 A; A/O=1-250.
PDB; 5CGG; X-ray; 2.90 A; A/O=1-250.
PDB; 5CGH; X-ray; 2.50 A; A/O=1-250.
PDB; 5CGI; X-ray; 2.80 A; A/O=1-250.
PDB; 5CZ4; X-ray; 2.30 A; A/O=1-250.
PDB; 5CZ5; X-ray; 2.80 A; A/O=1-250.
PDB; 5CZ6; X-ray; 2.70 A; A/O=1-250.
PDB; 5CZ7; X-ray; 2.50 A; A/O=1-250.
PDB; 5CZ8; X-ray; 2.80 A; A/O=1-250.
PDB; 5CZ9; X-ray; 2.90 A; A/O=1-250.
PDB; 5CZA; X-ray; 2.50 A; A/O=1-250.
PDB; 5D0S; X-ray; 2.50 A; A/O=1-250.
PDB; 5D0T; X-ray; 2.60 A; A/O=1-250.
PDB; 5D0V; X-ray; 2.90 A; A/O=1-250.
PDB; 5D0W; X-ray; 2.80 A; A/O=1-250.
PDB; 5D0X; X-ray; 2.60 A; A/O=1-250.
PDB; 5D0Z; X-ray; 2.90 A; A/O=1-250.
PDB; 5DKI; X-ray; 2.80 A; A/O=1-250.
PDB; 5DKJ; X-ray; 2.80 A; A/O=1-250.
PDB; 5FG7; X-ray; 2.70 A; A/O=1-250.
PDB; 5FG9; X-ray; 2.60 A; A/O=1-250.
PDB; 5FGA; X-ray; 2.70 A; A/O=1-250.
PDB; 5FGD; X-ray; 2.80 A; A/O=1-250.
PDB; 5FGE; X-ray; 2.60 A; A/O=1-250.
PDB; 5FGF; X-ray; 2.60 A; A/O=1-250.
PDB; 5FGG; X-ray; 2.70 A; A/O=1-250.
PDB; 5FGH; X-ray; 2.80 A; A/O=1-250.
PDB; 5FGI; X-ray; 2.90 A; A/O=1-250.
PDB; 5FHS; X-ray; 2.70 A; A/O=1-250.
PDB; 5JHR; X-ray; 2.90 A; A/O=1-250.
PDB; 5JHS; X-ray; 3.00 A; A/O=1-250.
PDB; 5L52; X-ray; 2.70 A; A/O=1-250.
PDB; 5L54; X-ray; 2.80 A; A/O=1-250.
PDB; 5L55; X-ray; 2.90 A; A/O=1-250.
PDB; 5L5A; X-ray; 2.40 A; A/O=1-250.
PDB; 5L5B; X-ray; 2.80 A; A/O=1-250.
PDB; 5L5D; X-ray; 2.80 A; A/O=1-250.
PDB; 5L5E; X-ray; 2.90 A; A/O=1-250.
PDB; 5L5F; X-ray; 2.50 A; A/O=1-250.
PDB; 5L5H; X-ray; 2.60 A; A/O=1-250.
PDB; 5L5I; X-ray; 2.90 A; A/O=1-250.
PDB; 5L5J; X-ray; 2.90 A; A/O=1-250.
PDB; 5L5O; X-ray; 2.60 A; A/O=1-250.
PDB; 5L5P; X-ray; 2.80 A; A/O=1-250.
PDB; 5L5Q; X-ray; 2.80 A; A/O=1-250.
PDB; 5L5R; X-ray; 2.90 A; A/O=1-250.
PDB; 5L5S; X-ray; 2.60 A; A/O=1-250.
PDB; 5L5T; X-ray; 2.90 A; A/O=1-250.
PDB; 5L5U; X-ray; 2.60 A; A/O=1-250.
PDB; 5L5V; X-ray; 2.70 A; A/O=1-250.
PDB; 5L5W; X-ray; 2.80 A; A/O=1-250.
PDB; 5L5X; X-ray; 2.90 A; A/O=1-250.
PDB; 5L5Y; X-ray; 2.70 A; A/O=1-250.
PDB; 5L5Z; X-ray; 2.70 A; A/O=1-250.
PDB; 5L60; X-ray; 2.70 A; A/O=1-250.
PDB; 5L61; X-ray; 2.80 A; A/O=1-250.
PDB; 5L62; X-ray; 2.80 A; A/O=1-250.
PDB; 5L63; X-ray; 2.70 A; A/O=1-250.
PDB; 5L64; X-ray; 2.70 A; A/O=1-250.
PDB; 5L65; X-ray; 2.90 A; A/O=1-250.
PDB; 5L66; X-ray; 2.80 A; A/O=1-250.
PDB; 5L67; X-ray; 2.60 A; A/O=1-250.
PDB; 5L68; X-ray; 2.80 A; A/O=1-250.
PDB; 5L69; X-ray; 2.70 A; A/O=1-250.
PDB; 5L6A; X-ray; 2.80 A; A/O=1-250.
PDB; 5L6B; X-ray; 2.60 A; A/O=1-250.
PDB; 5L6C; X-ray; 2.60 A; A/O=1-250.
PDB; 5LAI; X-ray; 2.50 A; A/O=1-250.
PDB; 5LAJ; X-ray; 2.90 A; A/O=1-250.
PDB; 5LTT; X-ray; 2.70 A; A/O=1-250.
PDB; 5M2B; X-ray; 2.70 A; A/O=1-250.
PDB; 5MP9; EM; 4.10 A; B/b=1-250.
PDB; 5MPA; EM; 4.50 A; B/b=1-250.
PDB; 5MPB; EM; 7.80 A; B/b=1-250.
PDB; 5MPC; EM; 7.70 A; B/b=1-250.
PDB; 5NIF; X-ray; 3.00 A; B/P=1-250.
PDB; 5WVI; EM; 6.30 A; B/j=1-250.
PDB; 5WVK; EM; 4.20 A; B/j=1-250.
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; P23639; -.
SMR; P23639; -.
BioGrid; 35051; 150.
DIP; DIP-2822N; -.
IntAct; P23639; 23.
MINT; P23639; -.
STRING; 4932.YML092C; -.
BindingDB; P23639; -.
iPTMnet; P23639; -.
MaxQB; P23639; -.
PaxDb; P23639; -.
PRIDE; P23639; -.
EnsemblFungi; YML092C; YML092C; YML092C.
GeneID; 854882; -.
KEGG; sce:YML092C; -.
EuPathDB; FungiDB:YML092C; -.
SGD; S000004557; PRE8.
GeneTree; ENSGT00550000074870; -.
HOGENOM; HOG000091085; -.
InParanoid; P23639; -.
KO; K02726; -.
OMA; FAWKASA; -.
OrthoDB; EOG092C47D8; -.
BioCyc; YEAST:G3O-32677-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; P23639; -.
PRO; PR:P23639; -.
Proteomes; UP000002311; Chromosome XIII.
GO; GO:0005737; C:cytoplasm; IC:SGD.
GO; GO:0042175; C:nuclear outer membrane-endoplasmic reticulum membrane network; IC:SGD.
GO; GO:0005634; C:nucleus; IC:SGD.
GO; GO:0019773; C:proteasome core complex, alpha-subunit complex; IDA:SGD.
GO; GO:0034515; C:proteasome storage granule; IDA: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; IPR023332; Proteasome_alpha-type.
InterPro; IPR000426; Proteasome_asu_N.
InterPro; IPR001353; Proteasome_sua/b.
InterPro; IPR034644; Proteasome_subunit_alpha2.
PANTHER; PTHR11599:SF16; PTHR11599:SF16; 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 1 250 Proteasome subunit alpha type-2.
/FTId=PRO_0000124090.
CROSSLNK 108 108 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000244|PubMed:22106047}.
STRAND 7 10 {ECO:0000244|PDB:1G65}.
TURN 14 16 {ECO:0000244|PDB:1G0U}.
HELIX 19 29 {ECO:0000244|PDB:1RYP}.
STRAND 34 39 {ECO:0000244|PDB:1RYP}.
STRAND 42 48 {ECO:0000244|PDB:1RYP}.
STRAND 54 56 {ECO:0000244|PDB:1RYP}.
HELIX 58 60 {ECO:0000244|PDB:1RYP}.
STRAND 63 68 {ECO:0000244|PDB:1RYP}.
STRAND 71 77 {ECO:0000244|PDB:1RYP}.
HELIX 79 95 {ECO:0000244|PDB:1RYP}.
HELIX 98 101 {ECO:0000244|PDB:1RYP}.
HELIX 107 120 {ECO:0000244|PDB:1RYP}.
TURN 121 123 {ECO:0000244|PDB:1RYP}.
STRAND 132 140 {ECO:0000244|PDB:1RYP}.
TURN 141 143 {ECO:0000244|PDB:1RYP}.
STRAND 144 150 {ECO:0000244|PDB:1RYP}.
STRAND 156 165 {ECO:0000244|PDB:1RYP}.
HELIX 168 178 {ECO:0000244|PDB:1RYP}.
HELIX 185 199 {ECO:0000244|PDB:1RYP}.
TURN 206 208 {ECO:0000244|PDB:1RYP}.
STRAND 209 214 {ECO:0000244|PDB:1RYP}.
HELIX 219 221 {ECO:0000244|PDB:1RYP}.
STRAND 223 226 {ECO:0000244|PDB:1RYP}.
STRAND 234 237 {ECO:0000244|PDB:1RYP}.
HELIX 240 247 {ECO:0000244|PDB:1RYP}.
SEQUENCE 250 AA; 27162 MW; 12D7DFB1AA10E9FE CRC64;
MTDRYSFSLT TFSPSGKLGQ IDYALTAVKQ GVTSLGIKAT NGVVIATEKK SSSPLAMSET
LSKVSLLTPD IGAVYSGMGP DYRVLVDKSR KVAHTSYKRI YGEYPPTKLL VSEVAKIMQE
ATQSGGVRPF GVSLLIAGHD EFNGFSLYQV DPSGSYFPWK ATAIGKGSVA AKTFLEKRWN
DELELEDAIH IALLTLKESV EGEFNGDTIE LAIIGDENPD LLGYTGIPTD KGPRFRKLTS
QEINDRLEAL


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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


 

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