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P25043

- PSB2_YEAST

UniProt

P25043 - PSB2_YEAST

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Protein

Proteasome subunit beta type-2

Gene

PUP1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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 activityi

Cleavage of peptide bonds with very broad specificity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei30 – 301Nucleophile1 Publication

GO - Molecular functioni

  1. endopeptidase activity Source: SGD
  2. threonine-type endopeptidase activity Source: UniProtKB-KW

GO - Biological processi

  1. proteasomal ubiquitin-independent protein catabolic process Source: SGD
  2. proteasome-mediated ubiquitin-dependent protein catabolic process Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Threonine protease

Enzyme and pathway databases

BioCyciYEAST:G3O-33674-MONOMER.
ReactomeiREACT_100522. Regulation of activated PAK-2p34 by proteasome mediated degradation.
REACT_189025. ER-Phagosome pathway.
REACT_189047. Cross-presentation of soluble exogenous antigens (endosomes).
REACT_189060. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_189250. AUF1 (hnRNP D0) destabilizes mRNA.
REACT_83036. Orc1 removal from chromatin.

Protein family/group databases

MEROPSiT01.011.

Names & Taxonomyi

Protein namesi
Recommended name:
Proteasome subunit beta type-2 (EC:3.4.25.1)
Alternative name(s):
Macropain subunit PUP1
Multicatalytic endopeptidase complex subunit PUP1
Proteasome component PUP1
Proteinase YSCE subunit PUP1
Gene namesi
Name:PUP1
Ordered Locus Names:YOR157C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome XV

Organism-specific databases

CYGDiYOR157c.
SGDiS000005683. PUP1.

Subcellular locationi

GO - Cellular componenti

  1. endoplasmic reticulum membrane Source: SGD
  2. nucleus Source: SGD
  3. proteasome core complex, beta-subunit complex Source: SGD
  4. proteasome storage granule Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Proteasome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Propeptidei1 – 2929Removed in mature formPRO_0000026657Add
BLAST
Chaini30 – 261232Proteasome subunit beta type-2PRO_0000026658Add
BLAST

Keywords - PTMi

Zymogen

Proteomic databases

MaxQBiP25043.
PaxDbiP25043.
PeptideAtlasiP25043.

Expressioni

Gene expression databases

GenevestigatoriP25043.

Interactioni

Subunit structurei

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.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
PUP3P254513EBI-14009,EBI-13993

Protein-protein interaction databases

BioGridi34553. 57 interactions.
DIPiDIP-2818N.
IntActiP25043. 9 interactions.
MINTiMINT-498378.
STRINGi4932.YOR157C.

Structurei

Secondary structure

1
261
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi32 – 376
Beta strandi40 – 456
Beta strandi49 – 513
Beta strandi54 – 596
Beta strandi63 – 675
Beta strandi70 – 767
Helixi78 – 9922
Helixi105 – 11814
Turni119 – 1213
Beta strandi125 – 1339
Beta strandi136 – 1427
Turni144 – 1463
Beta strandi148 – 1503
Beta strandi152 – 1576
Helixi160 – 17011
Helixi177 – 19418
Beta strandi202 – 2087
Beta strandi213 – 2208
Beta strandi241 – 2466

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FNTX-ray3.20I/W30-261[»]
1G0UX-ray2.40H/V30-251[»]
1G65X-ray2.25H/V30-251[»]
1JD2X-ray3.00H/O30-251[»]
1RYPX-ray1.90I/W30-251[»]
1VSYX-ray3.00I/W30-251[»]
1Z7QX-ray3.22I/W30-251[»]
2F16X-ray2.80H/V30-251[»]
2FAKX-ray2.80H/V30-251[»]
2GPLX-ray2.81H/V30-251[»]
2ZCYX-ray2.90H/V30-261[»]
3BDMX-ray2.70H/V30-261[»]
3D29X-ray2.60H/V30-251[»]
3DY3X-ray2.81H/V30-251[»]
3DY4X-ray2.80H/V30-251[»]
3E47X-ray3.00H/V30-251[»]
3GPJX-ray2.70H/V30-251[»]
3GPTX-ray2.41H/V30-251[»]
3GPWX-ray2.50H/V30-251[»]
3HYEX-ray2.50H/V30-251[»]
3L5QX-ray3.00M/Y30-251[»]
3MG0X-ray2.68H/V30-251[»]
3MG4X-ray3.11H/V30-251[»]
3MG6X-ray2.60H/V30-251[»]
3MG7X-ray2.78H/V30-251[»]
3MG8X-ray2.59H/V30-251[»]
3NZJX-ray2.40H/V1-261[»]
3NZWX-ray2.50H/V1-261[»]
3NZXX-ray2.70H/V1-261[»]
3OEUX-ray2.60H/V30-251[»]
3OEVX-ray2.85H/V30-251[»]
3OKJX-ray2.70H/V30-251[»]
3SDIX-ray2.65H/V30-251[»]
3SDKX-ray2.70H/V30-251[»]
3SHJX-ray2.80H/V30-251[»]
3TDDX-ray2.70H/V30-251[»]
3UN4X-ray3.40H/V30-261[»]
3UN8X-ray2.70H/V30-261[»]
4CR2electron microscopy7.7021-261[»]
4CR3electron microscopy9.3021-261[»]
4CR4electron microscopy8.8021-261[»]
4EU2X-ray2.51I/W30-251[»]
4FZCX-ray2.80H/V30-251[»]
4FZGX-ray3.00H/V30-251[»]
4G4SX-ray2.49I30-261[»]
4GK7X-ray2.80H/V30-251[»]
4HNPX-ray2.80H/V30-251[»]
4HRCX-ray2.80H/V30-251[»]
4HRDX-ray2.80H/V30-251[»]
4INRX-ray2.70H/V30-261[»]
4INTX-ray2.90H/V30-261[»]
4INUX-ray3.10H/V30-261[»]
4J70X-ray2.80H/V30-261[»]
4JSQX-ray2.80H/V30-261[»]
4JSUX-ray2.90H/V30-261[»]
4JT0X-ray3.10H/V30-261[»]
4LQIX-ray2.70H/V30-251[»]
4LTCX-ray2.50H/V30-261[»]
4NNNX-ray2.50H/V30-261[»]
4NNWX-ray2.60H/V30-261[»]
4NO1X-ray2.50H/V30-261[»]
4NO6X-ray3.00H/V30-261[»]
4NO8X-ray2.70H/V30-261[»]
4NO9X-ray2.90H/V30-261[»]
4Q1SX-ray2.60H/V30-261[»]
4QBYX-ray3.00H/V30-261[»]
4QLQX-ray2.40H/V30-261[»]
4QLSX-ray2.80H/V30-261[»]
4QLTX-ray2.80H/V30-261[»]
4QLUX-ray2.80H/V30-261[»]
4QLVX-ray2.90H/V30-261[»]
4R02X-ray2.50H/V30-261[»]
ProteinModelPortaliP25043.
SMRiP25043. Positions 30-251.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP25043.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1B family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0638.
GeneTreeiENSGT00510000046533.
HOGENOMiHOG000182856.
InParanoidiP25043.
KOiK02739.
OMAiQIWCAGA.
OrthoDBiEOG7TJ3V6.

Family and domain databases

Gene3Di3.60.20.10. 1 hit.
InterProiIPR029055. Ntn_hydrolases_N.
IPR000243. Pept_T1A_subB.
IPR024689. Proteasome_bsu_C.
IPR016050. Proteasome_bsu_CS.
IPR001353. Proteasome_sua/b.
IPR023333. Proteasome_suB-type.
[Graphical view]
PfamiPF12465. Pr_beta_C. 1 hit.
PF00227. Proteasome. 1 hit.
[Graphical view]
PRINTSiPR00141. PROTEASOME.
SUPFAMiSSF56235. SSF56235. 1 hit.
PROSITEiPS00854. PROTEASOME_BETA_1. 1 hit.
PS51476. PROTEASOME_BETA_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P25043-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAGLSFDNYQ RNNFLAENSH TQPKATSTGT TIVGVKFNNG VVIAADTRST
60 70 80 90 100
QGPIVADKNC AKLHRISPKI WCAGAGTAAD TEAVTQLIGS NIELHSLYTS
110 120 130 140 150
REPRVVSALQ MLKQHLFKYQ GHIGAYLIVA GVDPTGSHLF SIHAHGSTDV
160 170 180 190 200
GYYLSLGSGS LAAMAVLESH WKQDLTKEEA IKLASDAIQA GIWNDLGSGS
210 220 230 240 250
NVDVCVMEIG KDAEYLRNYL TPNVREEKQK SYKFPRGTTA VLKESIVNIC
260
DIQEEQVDIT A
Length:261
Mass (Da):28,268
Last modified:May 1, 1992 - v1
Checksum:i13A8F2B75584539A
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X61189 Genomic DNA. Translation: CAA43492.1.
U55020 Genomic DNA. Translation: AAC49643.1.
Z75065 Genomic DNA. Translation: CAA99363.1.
BK006948 Genomic DNA. Translation: DAA10930.1.
PIRiS26996.
RefSeqiNP_014800.3. NM_001183576.3.

Genome annotation databases

EnsemblFungiiYOR157C; YOR157C; YOR157C.
GeneIDi854328.
KEGGisce:YOR157C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X61189 Genomic DNA. Translation: CAA43492.1 .
U55020 Genomic DNA. Translation: AAC49643.1 .
Z75065 Genomic DNA. Translation: CAA99363.1 .
BK006948 Genomic DNA. Translation: DAA10930.1 .
PIRi S26996.
RefSeqi NP_014800.3. NM_001183576.3.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1FNT X-ray 3.20 I/W 30-261 [» ]
1G0U X-ray 2.40 H/V 30-251 [» ]
1G65 X-ray 2.25 H/V 30-251 [» ]
1JD2 X-ray 3.00 H/O 30-251 [» ]
1RYP X-ray 1.90 I/W 30-251 [» ]
1VSY X-ray 3.00 I/W 30-251 [» ]
1Z7Q X-ray 3.22 I/W 30-251 [» ]
2F16 X-ray 2.80 H/V 30-251 [» ]
2FAK X-ray 2.80 H/V 30-251 [» ]
2GPL X-ray 2.81 H/V 30-251 [» ]
2ZCY X-ray 2.90 H/V 30-261 [» ]
3BDM X-ray 2.70 H/V 30-261 [» ]
3D29 X-ray 2.60 H/V 30-251 [» ]
3DY3 X-ray 2.81 H/V 30-251 [» ]
3DY4 X-ray 2.80 H/V 30-251 [» ]
3E47 X-ray 3.00 H/V 30-251 [» ]
3GPJ X-ray 2.70 H/V 30-251 [» ]
3GPT X-ray 2.41 H/V 30-251 [» ]
3GPW X-ray 2.50 H/V 30-251 [» ]
3HYE X-ray 2.50 H/V 30-251 [» ]
3L5Q X-ray 3.00 M/Y 30-251 [» ]
3MG0 X-ray 2.68 H/V 30-251 [» ]
3MG4 X-ray 3.11 H/V 30-251 [» ]
3MG6 X-ray 2.60 H/V 30-251 [» ]
3MG7 X-ray 2.78 H/V 30-251 [» ]
3MG8 X-ray 2.59 H/V 30-251 [» ]
3NZJ X-ray 2.40 H/V 1-261 [» ]
3NZW X-ray 2.50 H/V 1-261 [» ]
3NZX X-ray 2.70 H/V 1-261 [» ]
3OEU X-ray 2.60 H/V 30-251 [» ]
3OEV X-ray 2.85 H/V 30-251 [» ]
3OKJ X-ray 2.70 H/V 30-251 [» ]
3SDI X-ray 2.65 H/V 30-251 [» ]
3SDK X-ray 2.70 H/V 30-251 [» ]
3SHJ X-ray 2.80 H/V 30-251 [» ]
3TDD X-ray 2.70 H/V 30-251 [» ]
3UN4 X-ray 3.40 H/V 30-261 [» ]
3UN8 X-ray 2.70 H/V 30-261 [» ]
4CR2 electron microscopy 7.70 2 1-261 [» ]
4CR3 electron microscopy 9.30 2 1-261 [» ]
4CR4 electron microscopy 8.80 2 1-261 [» ]
4EU2 X-ray 2.51 I/W 30-251 [» ]
4FZC X-ray 2.80 H/V 30-251 [» ]
4FZG X-ray 3.00 H/V 30-251 [» ]
4G4S X-ray 2.49 I 30-261 [» ]
4GK7 X-ray 2.80 H/V 30-251 [» ]
4HNP X-ray 2.80 H/V 30-251 [» ]
4HRC X-ray 2.80 H/V 30-251 [» ]
4HRD X-ray 2.80 H/V 30-251 [» ]
4INR X-ray 2.70 H/V 30-261 [» ]
4INT X-ray 2.90 H/V 30-261 [» ]
4INU X-ray 3.10 H/V 30-261 [» ]
4J70 X-ray 2.80 H/V 30-261 [» ]
4JSQ X-ray 2.80 H/V 30-261 [» ]
4JSU X-ray 2.90 H/V 30-261 [» ]
4JT0 X-ray 3.10 H/V 30-261 [» ]
4LQI X-ray 2.70 H/V 30-251 [» ]
4LTC X-ray 2.50 H/V 30-261 [» ]
4NNN X-ray 2.50 H/V 30-261 [» ]
4NNW X-ray 2.60 H/V 30-261 [» ]
4NO1 X-ray 2.50 H/V 30-261 [» ]
4NO6 X-ray 3.00 H/V 30-261 [» ]
4NO8 X-ray 2.70 H/V 30-261 [» ]
4NO9 X-ray 2.90 H/V 30-261 [» ]
4Q1S X-ray 2.60 H/V 30-261 [» ]
4QBY X-ray 3.00 H/V 30-261 [» ]
4QLQ X-ray 2.40 H/V 30-261 [» ]
4QLS X-ray 2.80 H/V 30-261 [» ]
4QLT X-ray 2.80 H/V 30-261 [» ]
4QLU X-ray 2.80 H/V 30-261 [» ]
4QLV X-ray 2.90 H/V 30-261 [» ]
4R02 X-ray 2.50 H/V 30-261 [» ]
ProteinModelPortali P25043.
SMRi P25043. Positions 30-251.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 34553. 57 interactions.
DIPi DIP-2818N.
IntActi P25043. 9 interactions.
MINTi MINT-498378.
STRINGi 4932.YOR157C.

Protein family/group databases

MEROPSi T01.011.

Proteomic databases

MaxQBi P25043.
PaxDbi P25043.
PeptideAtlasi P25043.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YOR157C ; YOR157C ; YOR157C .
GeneIDi 854328.
KEGGi sce:YOR157C.

Organism-specific databases

CYGDi YOR157c.
SGDi S000005683. PUP1.

Phylogenomic databases

eggNOGi COG0638.
GeneTreei ENSGT00510000046533.
HOGENOMi HOG000182856.
InParanoidi P25043.
KOi K02739.
OMAi QIWCAGA.
OrthoDBi EOG7TJ3V6.

Enzyme and pathway databases

BioCyci YEAST:G3O-33674-MONOMER.
Reactomei REACT_100522. Regulation of activated PAK-2p34 by proteasome mediated degradation.
REACT_189025. ER-Phagosome pathway.
REACT_189047. Cross-presentation of soluble exogenous antigens (endosomes).
REACT_189060. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_189250. AUF1 (hnRNP D0) destabilizes mRNA.
REACT_83036. Orc1 removal from chromatin.

Miscellaneous databases

EvolutionaryTracei P25043.
NextBioi 976378.
PROi P25043.

Gene expression databases

Genevestigatori P25043.

Family and domain databases

Gene3Di 3.60.20.10. 1 hit.
InterProi IPR029055. Ntn_hydrolases_N.
IPR000243. Pept_T1A_subB.
IPR024689. Proteasome_bsu_C.
IPR016050. Proteasome_bsu_CS.
IPR001353. Proteasome_sua/b.
IPR023333. Proteasome_suB-type.
[Graphical view ]
Pfami PF12465. Pr_beta_C. 1 hit.
PF00227. Proteasome. 1 hit.
[Graphical view ]
PRINTSi PR00141. PROTEASOME.
SUPFAMi SSF56235. SSF56235. 1 hit.
PROSITEi PS00854. PROTEASOME_BETA_1. 1 hit.
PS51476. PROTEASOME_BETA_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Nucleotide sequence of PUP1 encoding a putative proteasome subunit in Saccharomyces cerevisiae."
    Haffter P., Fox T.D.
    Nucleic Acids Res. 19:5075-5075(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Analysis of a 35.6 kb region on the right arm of Saccharomyces cerevisiae chromosome XV."
    Bordonne R., Camasses A., Madania A., Poch O., Tarassov I.A., Winsor B., Martin R.P.
    Yeast 13:73-83(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: S288c / FY1678.
  3. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV."
    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.
    Nature 387:98-102(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. "Structure of 20S proteasome from yeast at 2.4-A resolution."
    Groll M., Ditzel L., Loewe J., Stock D., Bochtler M., Bartunik H.D., Huber R.
    Nature 386:463-471(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 30-251 OF COMPLEX WITH THE 20S PROTEASOME, PROTEOLYTIC PROCESSING, ACTIVE SITE.
  8. "Structural basis for the activation of 20S proteasomes by 11S regulators."
    Whitby F.G., Masters E.I., Kramer L., Knowlton J.R., Yao Y., Wang C.C., Hill C.P.
    Nature 408:115-120(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 30-261 OF COMPLEX WITH THE 20S PROTEASOME AND A 11S REGULATORY COMPLEX.
  9. Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF COMPLEX WITH THE 20S PROTEASOME.
  10. "TMC-95-based inhibitor design provides evidence for the catalytic versatility of the proteasome."
    Groll M., Goetz M., Kaiser M., Weyher E., Moroder L.
    Chem. Biol. 13:607-614(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.81 ANGSTROMS) OF 30-251 OF COMPLEX WITH THE 20S PROTEASOME AND A TMC-95-BASED INHIBITOR.
  11. "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."
    Groll M., Huber R., Potts B.C.M.
    J. Am. Chem. Soc. 128:5136-5141(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 30-251 OF COMPLEX WITH THE 20S PROTEASOME AND SALINOSPORAMIDE.
  12. "Crystal structure of the boronic acid-based proteasome inhibitor bortezomib in complex with the yeast 20S proteasome."
    Groll M., Berkers C.R., Ploegh H.L., Ovaa H.
    Structure 14:451-456(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 30-251 OF COMPLEX WITH THE 20S PROTEASOME AND BORTEZOMIB.
  13. "Structure of a Blm10 complex reveals common mechanisms for proteasome binding and gate opening."
    Sadre-Bazzaz K., Whitby F.G., Robinson H., Formosa T., Hill C.P.
    Mol. Cell 37:728-735(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 30-251 IN COMPLEX WITH THE PROTEASOME.
  14. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (7.4 ANGSTROMS) OF THE 26S PROTEASOME.

Entry informationi

Entry nameiPSB2_YEAST
AccessioniPrimary (citable) accession number: P25043
Secondary accession number(s): D6W2L4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: May 1, 1992
Last modified: October 29, 2014
This is version 150 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

The side chain of Thr-30 acts as nucleophile, and the N-terminal amino group acts as proton acceptor.
Present with 11400 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families
  4. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  5. Yeast chromosome XV
    Yeast (Saccharomyces cerevisiae) chromosome XV: entries and gene names

External Data

Dasty 3