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P21242

- PSA7_YEAST

UniProt

P21242 - PSA7_YEAST

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Protein

Probable proteasome subunit alpha type-7

Gene
PRE10, PRC1, PRS1, YOR362C, O6650
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.

GO - Molecular functioni

  1. mRNA binding Source: SGD
  2. protein binding Source: IntAct
  3. 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-33832-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.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable proteasome subunit alpha type-7 (EC:3.4.25.1)
Alternative name(s):
Macropain subunit C1
Multicatalytic endopeptidase complex subunit C1
Proteasome component C1
Proteinase YSCE subunit 1
Gene namesi
Name:PRE10
Synonyms:PRC1, PRS1
Ordered Locus Names:YOR362C
ORF Names:O6650
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome XV

Organism-specific databases

SGDiS000005889. PRE10.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: SGD
  2. nuclear outer membrane-endoplasmic reticulum membrane network Source: SGD
  3. nucleus Source: SGD
  4. proteasome core complex, alpha-subunit complex Source: SGD
  5. proteasome storage granule Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Proteasome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 288287Probable proteasome subunit alpha type-7PRO_0000124102Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylthreonine1 Publication

Post-translational modificationi

The alpha and beta forms are probably products of the same gene with different post-translational modifications.

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP21242.
PaxDbiP21242.
PeptideAtlasiP21242.

Expressioni

Gene expression databases

GenevestigatoriP21242.

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.

Binary interactionsi

WithEntry#Exp.IntActNotes
PRE1P221413EBI-13963,EBI-13988
SCL1P212436EBI-13963,EBI-13975

Protein-protein interaction databases

BioGridi34747. 92 interactions.
DIPiDIP-1526N.
IntActiP21242. 29 interactions.
MINTiMINT-411846.
STRINGi4932.YOR362C.

Structurei

Secondary structure

1
288
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi8 – 114
Beta strandi17 – 193
Helixi22 – 3211
Beta strandi37 – 426
Beta strandi45 – 539
Turni61 – 633
Beta strandi68 – 703
Turni71 – 733
Beta strandi74 – 807
Helixi82 – 10322
Helixi109 – 12214
Turni123 – 1253
Beta strandi127 – 1293
Beta strandi134 – 1429
Beta strandi145 – 1517
Turni153 – 1553
Beta strandi157 – 16610
Helixi169 – 18214
Helixi189 – 20315
Helixi204 – 2074
Beta strandi212 – 2209
Turni221 – 2233
Beta strandi227 – 2304
Helixi234 – 24512

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FNTX-ray3.20G/U2-288[»]
1G0UX-ray2.40F/T1-248[»]
1G65X-ray2.25F/T5-248[»]
1JD2X-ray3.001/F5-248[»]
1RYPX-ray1.90G/U5-248[»]
1VSYX-ray3.00G/U5-248[»]
1Z7QX-ray3.22G/U1-288[»]
2F16X-ray2.80F/T5-248[»]
2FAKX-ray2.80F/T5-248[»]
2GPLX-ray2.81F/T5-248[»]
2ZCYX-ray2.90F/T2-288[»]
3BDMX-ray2.70F/T2-288[»]
3D29X-ray2.60F/T5-248[»]
3DY3X-ray2.81F/T5-248[»]
3DY4X-ray2.80F/T5-248[»]
3E47X-ray3.00F/T5-248[»]
3GPJX-ray2.70F/T5-248[»]
3GPTX-ray2.41F/T5-248[»]
3GPWX-ray2.50F/T5-248[»]
3HYEX-ray2.50F/T5-248[»]
3L5QX-ray3.00L/X5-248[»]
3MG0X-ray2.68F/T5-248[»]
3MG4X-ray3.11F/T5-248[»]
3MG6X-ray2.60F/T1-248[»]
3MG7X-ray2.78F/T1-248[»]
3MG8X-ray2.59F/T1-248[»]
3NZJX-ray2.40F/T1-288[»]
3NZWX-ray2.50F/T1-288[»]
3NZXX-ray2.70F/T1-288[»]
3OEUX-ray2.60F/T7-248[»]
3OEVX-ray2.85F/T7-248[»]
3OKJX-ray2.70F/T5-248[»]
3SDIX-ray2.65F/T7-248[»]
3SDKX-ray2.70F/T7-248[»]
3SHJX-ray2.80F/T5-248[»]
3TDDX-ray2.70F/T5-248[»]
3UN4X-ray3.40F/T1-288[»]
3UN8X-ray2.70F/T1-288[»]
4CR2electron microscopy7.70G1-288[»]
4CR3electron microscopy9.30G1-288[»]
4CR4electron microscopy8.80G1-288[»]
4EU2X-ray2.51G/U5-248[»]
4FZCX-ray2.80F/T5-248[»]
4FZGX-ray3.00F/T5-248[»]
4G4SX-ray2.49G1-288[»]
4GK7X-ray2.80F/T5-248[»]
4HNPX-ray2.80F/T5-248[»]
4HRCX-ray2.80F/T5-248[»]
4HRDX-ray2.80F/T5-248[»]
4INRX-ray2.70F/T1-288[»]
4INTX-ray2.90F/T1-288[»]
4INUX-ray3.10F/T1-288[»]
4J70X-ray2.80F/T1-288[»]
4JSQX-ray2.80F/T1-288[»]
4JSUX-ray2.90F/T1-288[»]
4JT0X-ray3.10F/T1-288[»]
4LQIX-ray2.70F/T5-248[»]
4NNNX-ray2.50F/T1-288[»]
4NNWX-ray2.60F/T1-288[»]
4NO1X-ray2.50F/T1-288[»]
4NO6X-ray3.00F/T1-288[»]
4NO8X-ray2.70F/T1-288[»]
4NO9X-ray2.90F/T1-288[»]
4QBYX-ray3.00F/T1-288[»]
ProteinModelPortaliP21242.
SMRiP21242. Positions 5-248.

Miscellaneous databases

EvolutionaryTraceiP21242.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1A family.

Phylogenomic databases

eggNOGiCOG0638.
GeneTreeiENSGT00550000074912.
HOGENOMiHOG000091086.
KOiK02727.
OMAiVPDGRHF.
OrthoDBiEOG7SBP0C.

Family and domain databases

Gene3Di3.60.20.10. 1 hit.
InterProiIPR029055. Ntn_hydrolases_N.
IPR000426. Proteasome_asu_N.
IPR023332. Proteasome_suA-type.
IPR001353. Proteasome_sua/b.
[Graphical view]
PfamiPF00227. Proteasome. 1 hit.
PF10584. Proteasome_A_N. 1 hit.
[Graphical view]
SMARTiSM00948. Proteasome_A_N. 1 hit.
[Graphical view]
SUPFAMiSSF56235. SSF56235. 1 hit.
PROSITEiPS00388. PROTEASOME_ALPHA_1. 1 hit.
PS51475. PROTEASOME_ALPHA_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P21242-1 [UniParc]FASTAAdd to Basket

« Hide

MTSIGTGYDL SNSVFSPDGR NFQVEYAVKA VENGTTSIGI KCNDGVVFAV    50
EKLITSKLLV PQKNVKIQVV DRHIGCVYSG LIPDGRHLVN RGREEAASFK 100
KLYKTPIPIP AFADRLGQYV QAHTLYNSVR PFGVSTIFGG VDKNGAHLYM 150
LEPSGSYWGY KGAATGKGRQ SAKAELEKLV DHHPEGLSAR EAVKQAAKII 200
YLAHEDNKEK DFELEISWCS LSETNGLHKF VKGDLLQEAI DFAQKEINGD 250
DDEDEDDSDN VMSSDDENAP VATNANATTD QEGDIHLE 288
Length:288
Mass (Da):31,536
Last modified:January 23, 2007 - v2
Checksum:i1E51D904CF336747
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M55436 mRNA. Translation: AAA35227.1.
Z75270 Genomic DNA. Translation: CAA99691.1.
BK006948 Genomic DNA. Translation: DAA11123.1.
PIRiS11182. SNBYC1.
RefSeqiNP_015007.1. NM_001183782.1.

Genome annotation databases

EnsemblFungiiYOR362C; YOR362C; YOR362C.
GeneIDi854544.
KEGGisce:YOR362C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M55436 mRNA. Translation: AAA35227.1 .
Z75270 Genomic DNA. Translation: CAA99691.1 .
BK006948 Genomic DNA. Translation: DAA11123.1 .
PIRi S11182. SNBYC1.
RefSeqi NP_015007.1. NM_001183782.1.

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 G/U 2-288 [» ]
1G0U X-ray 2.40 F/T 1-248 [» ]
1G65 X-ray 2.25 F/T 5-248 [» ]
1JD2 X-ray 3.00 1/F 5-248 [» ]
1RYP X-ray 1.90 G/U 5-248 [» ]
1VSY X-ray 3.00 G/U 5-248 [» ]
1Z7Q X-ray 3.22 G/U 1-288 [» ]
2F16 X-ray 2.80 F/T 5-248 [» ]
2FAK X-ray 2.80 F/T 5-248 [» ]
2GPL X-ray 2.81 F/T 5-248 [» ]
2ZCY X-ray 2.90 F/T 2-288 [» ]
3BDM X-ray 2.70 F/T 2-288 [» ]
3D29 X-ray 2.60 F/T 5-248 [» ]
3DY3 X-ray 2.81 F/T 5-248 [» ]
3DY4 X-ray 2.80 F/T 5-248 [» ]
3E47 X-ray 3.00 F/T 5-248 [» ]
3GPJ X-ray 2.70 F/T 5-248 [» ]
3GPT X-ray 2.41 F/T 5-248 [» ]
3GPW X-ray 2.50 F/T 5-248 [» ]
3HYE X-ray 2.50 F/T 5-248 [» ]
3L5Q X-ray 3.00 L/X 5-248 [» ]
3MG0 X-ray 2.68 F/T 5-248 [» ]
3MG4 X-ray 3.11 F/T 5-248 [» ]
3MG6 X-ray 2.60 F/T 1-248 [» ]
3MG7 X-ray 2.78 F/T 1-248 [» ]
3MG8 X-ray 2.59 F/T 1-248 [» ]
3NZJ X-ray 2.40 F/T 1-288 [» ]
3NZW X-ray 2.50 F/T 1-288 [» ]
3NZX X-ray 2.70 F/T 1-288 [» ]
3OEU X-ray 2.60 F/T 7-248 [» ]
3OEV X-ray 2.85 F/T 7-248 [» ]
3OKJ X-ray 2.70 F/T 5-248 [» ]
3SDI X-ray 2.65 F/T 7-248 [» ]
3SDK X-ray 2.70 F/T 7-248 [» ]
3SHJ X-ray 2.80 F/T 5-248 [» ]
3TDD X-ray 2.70 F/T 5-248 [» ]
3UN4 X-ray 3.40 F/T 1-288 [» ]
3UN8 X-ray 2.70 F/T 1-288 [» ]
4CR2 electron microscopy 7.70 G 1-288 [» ]
4CR3 electron microscopy 9.30 G 1-288 [» ]
4CR4 electron microscopy 8.80 G 1-288 [» ]
4EU2 X-ray 2.51 G/U 5-248 [» ]
4FZC X-ray 2.80 F/T 5-248 [» ]
4FZG X-ray 3.00 F/T 5-248 [» ]
4G4S X-ray 2.49 G 1-288 [» ]
4GK7 X-ray 2.80 F/T 5-248 [» ]
4HNP X-ray 2.80 F/T 5-248 [» ]
4HRC X-ray 2.80 F/T 5-248 [» ]
4HRD X-ray 2.80 F/T 5-248 [» ]
4INR X-ray 2.70 F/T 1-288 [» ]
4INT X-ray 2.90 F/T 1-288 [» ]
4INU X-ray 3.10 F/T 1-288 [» ]
4J70 X-ray 2.80 F/T 1-288 [» ]
4JSQ X-ray 2.80 F/T 1-288 [» ]
4JSU X-ray 2.90 F/T 1-288 [» ]
4JT0 X-ray 3.10 F/T 1-288 [» ]
4LQI X-ray 2.70 F/T 5-248 [» ]
4NNN X-ray 2.50 F/T 1-288 [» ]
4NNW X-ray 2.60 F/T 1-288 [» ]
4NO1 X-ray 2.50 F/T 1-288 [» ]
4NO6 X-ray 3.00 F/T 1-288 [» ]
4NO8 X-ray 2.70 F/T 1-288 [» ]
4NO9 X-ray 2.90 F/T 1-288 [» ]
4QBY X-ray 3.00 F/T 1-288 [» ]
ProteinModelPortali P21242.
SMRi P21242. Positions 5-248.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 34747. 92 interactions.
DIPi DIP-1526N.
IntActi P21242. 29 interactions.
MINTi MINT-411846.
STRINGi 4932.YOR362C.

Proteomic databases

MaxQBi P21242.
PaxDbi P21242.
PeptideAtlasi P21242.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YOR362C ; YOR362C ; YOR362C .
GeneIDi 854544.
KEGGi sce:YOR362C.

Organism-specific databases

SGDi S000005889. PRE10.

Phylogenomic databases

eggNOGi COG0638.
GeneTreei ENSGT00550000074912.
HOGENOMi HOG000091086.
KOi K02727.
OMAi VPDGRHF.
OrthoDBi EOG7SBP0C.

Enzyme and pathway databases

BioCyci YEAST:G3O-33832-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 P21242.
NextBioi 976955.
PROi P21242.

Gene expression databases

Genevestigatori P21242.

Family and domain databases

Gene3Di 3.60.20.10. 1 hit.
InterProi IPR029055. Ntn_hydrolases_N.
IPR000426. Proteasome_asu_N.
IPR023332. Proteasome_suA-type.
IPR001353. Proteasome_sua/b.
[Graphical view ]
Pfami PF00227. Proteasome. 1 hit.
PF10584. Proteasome_A_N. 1 hit.
[Graphical view ]
SMARTi SM00948. Proteasome_A_N. 1 hit.
[Graphical view ]
SUPFAMi SSF56235. SSF56235. 1 hit.
PROSITEi PS00388. PROTEASOME_ALPHA_1. 1 hit.
PS51475. PROTEASOME_ALPHA_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Proteasomes are essential for yeast proliferation. cDNA cloning and gene disruption of two major subunits."
    Fujiwara T., Tanaka K., Orino E., Yoshimura T., Kumatori A., Tamura T., Chung C.H., Nakai T., Yamaguchi K., Shin S., Kakizuka A., Nakanishi S., Ichihara A.
    J. Biol. Chem. 265:16604-16613(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 106-135; 180-195 AND 200-209, CLEAVAGE OF INITIATOR METHIONINE.
  2. "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.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  5. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  6. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [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 5-248 OF COMPLEX WITH THE 20S PROTEASOME.
  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 1-288 OF COMPLEX WITH THE 20S PROTEASOME AND A 11S REGULATORY COMPLEX.
  9. Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1-248 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 5-248 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 5-248 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 5-248 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 5-248 IN COMPLEX WITH THE PROTEASOME.
  14. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (7.4 ANGSTROMS) OF THE 26S PROTEASOME.

Entry informationi

Entry nameiPSA7_YEAST
AccessioniPrimary (citable) accession number: P21242
Secondary accession number(s): D6W357
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: January 23, 2007
Last modified: September 3, 2014
This is version 164 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 12000 molecules/cell in log phase SD medium.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, 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

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