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Protein

Probable proteasome subunit alpha type-7

Gene

PRE10

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: 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.PROSITE-ProRule annotation

GO - Molecular functioni

  • mRNA binding Source: SGD
  • threonine-type endopeptidase activity Source: UniProtKB-KW

GO - Biological processi

  • proteasomal ubiquitin-independent protein catabolic process Source: SGD
  • 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.
ReactomeiR-SCE-1236978. Cross-presentation of soluble exogenous antigens (endosomes).
R-SCE-174113. SCF-beta-TrCP mediated degradation of Emi1.
R-SCE-349425. Autodegradation of the E3 ubiquitin ligase COP1.
R-SCE-382556. ABC-family proteins mediated transport.
R-SCE-450408. AUF1 (hnRNP D0) binds and destabilizes mRNA.
R-SCE-5668541. TNFR2 non-canonical NF-kB pathway.
R-SCE-5687128. MAPK6/MAPK4 signaling.
R-SCE-5689880. Ub-specific processing proteases.
R-SCE-68949. Orc1 removal from chromatin.
R-SCE-69017. CDK-mediated phosphorylation and removal of Cdc6.
R-SCE-69229. Ubiquitin-dependent degradation of Cyclin D1.
R-SCE-69601. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
R-SCE-8854050. FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
R-SCE-983168. Antigen processing: Ubiquitination & Proteasome degradation.

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
Proteomesi
  • UP000002311 Componenti: Chromosome XV

Organism-specific databases

EuPathDBiFungiDB:YOR362C.
SGDiS000005889. PRE10.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm, Nucleus, Proteasome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources1 Publication
ChainiPRO_00001241022 – 288Probable proteasome subunit alpha type-7Add BLAST287

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylthreonineCombined sources1

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.
PRIDEiP21242.

PTM databases

iPTMnetiP21242.

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
PRE1P221413EBI-13963,EBI-13988
SCL1P212436EBI-13963,EBI-13975

Protein-protein interaction databases

BioGridi34747. 95 interactors.
DIPiDIP-1526N.
IntActiP21242. 29 interactors.
MINTiMINT-411846.

Structurei

Secondary structure

1288
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi8 – 10Combined sources3
Beta strandi11 – 13Combined sources3
Beta strandi17 – 19Combined sources3
Helixi22 – 32Combined sources11
Beta strandi37 – 42Combined sources6
Beta strandi45 – 53Combined sources9
Turni61 – 63Combined sources3
Beta strandi68 – 70Combined sources3
Turni71 – 73Combined sources3
Beta strandi74 – 80Combined sources7
Helixi82 – 103Combined sources22
Helixi109 – 122Combined sources14
Turni123 – 125Combined sources3
Beta strandi127 – 129Combined sources3
Beta strandi134 – 142Combined sources9
Beta strandi145 – 151Combined sources7
Turni153 – 155Combined sources3
Beta strandi157 – 166Combined sources10
Helixi169 – 182Combined sources14
Helixi189 – 203Combined sources15
Helixi204 – 207Combined sources4
Beta strandi212 – 220Combined sources9
Turni221 – 223Combined sources3
Beta strandi227 – 230Combined sources4
Helixi234 – 245Combined sources12

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
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[»]
3JCOelectron microscopy4.80G/g1-288[»]
3JCPelectron microscopy4.60G/g1-288[»]
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[»]
3WXRX-ray3.15G/U13-288[»]
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[»]
4LTCX-ray2.50F/T2-288[»]
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[»]
4Q1SX-ray2.60F/T1-288[»]
4QBYX-ray3.00F/T1-288[»]
4QLQX-ray2.40F/T1-288[»]
4QLSX-ray2.80F/T1-288[»]
4QLTX-ray2.80F/T1-288[»]
4QLUX-ray2.80F/T1-288[»]
4QLVX-ray2.90F/T1-288[»]
4QUXX-ray3.00F/T1-288[»]
4QUYX-ray2.80F/T1-288[»]
4QV0X-ray3.10F/T1-288[»]
4QV1X-ray2.50F/T1-288[»]
4QV3X-ray3.00F/T1-288[»]
4QV4X-ray2.70F/T1-288[»]
4QV5X-ray2.70F/T1-288[»]
4QV6X-ray2.80F/T1-288[»]
4QV7X-ray2.60F/T1-288[»]
4QV8X-ray2.90F/T1-288[»]
4QV9X-ray2.60F/T1-288[»]
4QVLX-ray2.80F/T1-288[»]
4QVMX-ray2.80F/T1-288[»]
4QVNX-ray2.90F/T1-288[»]
4QVPX-ray2.30F/T1-288[»]
4QVQX-ray2.60F/T1-288[»]
4QVVX-ray2.80F/T1-288[»]
4QVWX-ray3.00F/T1-288[»]
4QVYX-ray2.51F/T1-288[»]
4QW0X-ray2.90F/T1-288[»]
4QW1X-ray2.90F/T1-288[»]
4QW3X-ray2.90F/T1-288[»]
4QW4X-ray2.80F/T1-288[»]
4QW5X-ray3.00F/T1-288[»]
4QW6X-ray2.90F/T1-288[»]
4QW7X-ray2.70F/T1-288[»]
4QWFX-ray3.00F/T1-288[»]
4QWGX-ray2.60F/T1-288[»]
4QWIX-ray2.60F/T1-288[»]
4QWJX-ray2.90F/T1-288[»]
4QWKX-ray2.80F/T1-288[»]
4QWLX-ray2.60F/T1-288[»]
4QWRX-ray2.90F/T1-288[»]
4QWSX-ray3.00F/T1-288[»]
4QWUX-ray3.00F/T1-288[»]
4QWXX-ray2.90F/T1-288[»]
4QXJX-ray2.80F/T1-288[»]
4QZ0X-ray3.00F/T1-288[»]
4QZ1X-ray3.00F/T1-288[»]
4QZ2X-ray2.70F/T1-288[»]
4QZ3X-ray2.80F/T1-288[»]
4QZ4X-ray3.00F/T1-288[»]
4QZ5X-ray2.80F/T1-288[»]
4QZ6X-ray2.90F/T1-288[»]
4QZ7X-ray2.80F/T1-288[»]
4QZWX-ray3.00F/T1-288[»]
4QZXX-ray2.60F/T1-288[»]
4QZZX-ray2.90F/T1-288[»]
4R00X-ray2.80F/T1-288[»]
4R02X-ray2.50F/T1-288[»]
4R17X-ray2.10F/T1-288[»]
4R18X-ray2.40F/T1-288[»]
4RURX-ray2.50F/T1-288[»]
4V7OX-ray3.00AL/AX/BG/BU5-248[»]
4X6ZX-ray2.70G/U1-288[»]
4Y69X-ray2.90F/T1-288[»]
4Y6AX-ray2.60F/T1-288[»]
4Y6VX-ray2.80F/T1-288[»]
4Y6ZX-ray2.70F/T1-288[»]
4Y70X-ray2.40F/T1-288[»]
4Y74X-ray2.70F/T1-288[»]
4Y75X-ray2.80F/T1-288[»]
4Y77X-ray2.50F/T1-288[»]
4Y78X-ray2.80F/T1-288[»]
4Y7WX-ray2.50F/T1-288[»]
4Y7XX-ray2.60F/T1-288[»]
4Y7YX-ray2.40F/T1-288[»]
4Y80X-ray2.50F/T1-288[»]
4Y81X-ray2.80F/T1-288[»]
4Y82X-ray2.80F/T1-288[»]
4Y84X-ray2.70F/T1-288[»]
4Y8GX-ray2.60F/T1-288[»]
4Y8HX-ray2.50F/T1-288[»]
4Y8IX-ray2.60F/T1-288[»]
4Y8JX-ray2.70F/T1-288[»]
4Y8KX-ray2.60F/T1-288[»]
4Y8LX-ray2.40F/T1-288[»]
4Y8MX-ray2.80F/T1-288[»]
4Y8NX-ray2.60F/T1-288[»]
4Y8OX-ray2.70F/T1-288[»]
4Y8PX-ray2.80F/T1-288[»]
4Y8QX-ray2.60F/T1-288[»]
4Y8RX-ray2.70F/T1-288[»]
4Y8SX-ray2.70F/T1-288[»]
4Y8TX-ray2.70F/T1-288[»]
4Y8UX-ray2.90F/T1-288[»]
4Y9YX-ray2.80F/T1-288[»]
4Y9ZX-ray2.80F/T1-288[»]
4YA0X-ray2.80F/T1-288[»]
4YA1X-ray2.90F/T1-288[»]
4YA2X-ray2.70F/T1-288[»]
4YA3X-ray2.70F/T1-288[»]
4YA4X-ray2.90F/T1-288[»]
4YA5X-ray2.50F/T1-288[»]
4YA7X-ray2.70F/T1-288[»]
4YA9X-ray2.70F/T1-288[»]
4Z1LX-ray3.00F/T1-288[»]
4ZZGX-ray3.00G/U1-288[»]
5A5Belectron microscopy9.50G1-288[»]
5AHJX-ray2.80F/T1-288[»]
5BOUX-ray2.60F/T1-288[»]
5BXLX-ray2.80F/T1-288[»]
5BXNX-ray2.80F/T1-288[»]
5CGFX-ray2.80F/T1-288[»]
5CGGX-ray2.90F/T1-288[»]
5CGHX-ray2.50F/T1-288[»]
5CGIX-ray2.80F/T1-288[»]
5CZ4X-ray2.30F/T1-288[»]
5CZ5X-ray2.80F/T1-288[»]
5CZ6X-ray2.70F/T1-288[»]
5CZ7X-ray2.50F/T1-288[»]
5CZ8X-ray2.80F/T1-288[»]
5CZ9X-ray2.90F/T1-288[»]
5CZAX-ray2.50F/T1-288[»]
5D0SX-ray2.50F/T1-288[»]
5D0TX-ray2.60F/T1-288[»]
5D0VX-ray2.90F/T1-288[»]
5D0WX-ray2.80F/T1-288[»]
5D0XX-ray2.60F/T1-288[»]
5D0ZX-ray2.90F/T1-288[»]
5DKIX-ray2.80F/T1-288[»]
5DKJX-ray2.80F/T1-288[»]
5FG7X-ray2.70F/T1-288[»]
5FG9X-ray2.60F/T1-288[»]
5FGAX-ray2.70F/T1-288[»]
5FGDX-ray2.80F/T1-288[»]
5FGEX-ray2.60F/T1-288[»]
5FGFX-ray2.60F/T1-288[»]
5FGGX-ray2.70F/T1-288[»]
5FGHX-ray2.80F/T1-288[»]
5FGIX-ray2.90F/T1-288[»]
5FHSX-ray2.70F/T1-288[»]
5JHRX-ray2.90F/T1-288[»]
5JHSX-ray3.00F/T1-288[»]
ProteinModelPortaliP21242.
SMRiP21242.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP21242.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1A family.PROSITE-ProRule annotation

Phylogenomic databases

GeneTreeiENSGT00550000074912.
HOGENOMiHOG000091086.
InParanoidiP21242.
KOiK02727.
OMAiVPDGRHF.
OrthoDBiEOG092C47D8.

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

        10         20         30         40         50
MTSIGTGYDL SNSVFSPDGR NFQVEYAVKA VENGTTSIGI KCNDGVVFAV
60 70 80 90 100
EKLITSKLLV PQKNVKIQVV DRHIGCVYSG LIPDGRHLVN RGREEAASFK
110 120 130 140 150
KLYKTPIPIP AFADRLGQYV QAHTLYNSVR PFGVSTIFGG VDKNGAHLYM
160 170 180 190 200
LEPSGSYWGY KGAATGKGRQ SAKAELEKLV DHHPEGLSAR EAVKQAAKII
210 220 230 240 250
YLAHEDNKEK DFELEISWCS LSETNGLHKF VKGDLLQEAI DFAQKEINGD
260 270 280
DDEDEDDSDN VMSSDDENAP VATNANATTD QEGDIHLE
Length:288
Mass (Da):31,536
Last modified:January 23, 2007 - v2
Checksum:i1E51D904CF336747
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
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[»]
3JCOelectron microscopy4.80G/g1-288[»]
3JCPelectron microscopy4.60G/g1-288[»]
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[»]
3WXRX-ray3.15G/U13-288[»]
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[»]
4LTCX-ray2.50F/T2-288[»]
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[»]
4Q1SX-ray2.60F/T1-288[»]
4QBYX-ray3.00F/T1-288[»]
4QLQX-ray2.40F/T1-288[»]
4QLSX-ray2.80F/T1-288[»]
4QLTX-ray2.80F/T1-288[»]
4QLUX-ray2.80F/T1-288[»]
4QLVX-ray2.90F/T1-288[»]
4QUXX-ray3.00F/T1-288[»]
4QUYX-ray2.80F/T1-288[»]
4QV0X-ray3.10F/T1-288[»]
4QV1X-ray2.50F/T1-288[»]
4QV3X-ray3.00F/T1-288[»]
4QV4X-ray2.70F/T1-288[»]
4QV5X-ray2.70F/T1-288[»]
4QV6X-ray2.80F/T1-288[»]
4QV7X-ray2.60F/T1-288[»]
4QV8X-ray2.90F/T1-288[»]
4QV9X-ray2.60F/T1-288[»]
4QVLX-ray2.80F/T1-288[»]
4QVMX-ray2.80F/T1-288[»]
4QVNX-ray2.90F/T1-288[»]
4QVPX-ray2.30F/T1-288[»]
4QVQX-ray2.60F/T1-288[»]
4QVVX-ray2.80F/T1-288[»]
4QVWX-ray3.00F/T1-288[»]
4QVYX-ray2.51F/T1-288[»]
4QW0X-ray2.90F/T1-288[»]
4QW1X-ray2.90F/T1-288[»]
4QW3X-ray2.90F/T1-288[»]
4QW4X-ray2.80F/T1-288[»]
4QW5X-ray3.00F/T1-288[»]
4QW6X-ray2.90F/T1-288[»]
4QW7X-ray2.70F/T1-288[»]
4QWFX-ray3.00F/T1-288[»]
4QWGX-ray2.60F/T1-288[»]
4QWIX-ray2.60F/T1-288[»]
4QWJX-ray2.90F/T1-288[»]
4QWKX-ray2.80F/T1-288[»]
4QWLX-ray2.60F/T1-288[»]
4QWRX-ray2.90F/T1-288[»]
4QWSX-ray3.00F/T1-288[»]
4QWUX-ray3.00F/T1-288[»]
4QWXX-ray2.90F/T1-288[»]
4QXJX-ray2.80F/T1-288[»]
4QZ0X-ray3.00F/T1-288[»]
4QZ1X-ray3.00F/T1-288[»]
4QZ2X-ray2.70F/T1-288[»]
4QZ3X-ray2.80F/T1-288[»]
4QZ4X-ray3.00F/T1-288[»]
4QZ5X-ray2.80F/T1-288[»]
4QZ6X-ray2.90F/T1-288[»]
4QZ7X-ray2.80F/T1-288[»]
4QZWX-ray3.00F/T1-288[»]
4QZXX-ray2.60F/T1-288[»]
4QZZX-ray2.90F/T1-288[»]
4R00X-ray2.80F/T1-288[»]
4R02X-ray2.50F/T1-288[»]
4R17X-ray2.10F/T1-288[»]
4R18X-ray2.40F/T1-288[»]
4RURX-ray2.50F/T1-288[»]
4V7OX-ray3.00AL/AX/BG/BU5-248[»]
4X6ZX-ray2.70G/U1-288[»]
4Y69X-ray2.90F/T1-288[»]
4Y6AX-ray2.60F/T1-288[»]
4Y6VX-ray2.80F/T1-288[»]
4Y6ZX-ray2.70F/T1-288[»]
4Y70X-ray2.40F/T1-288[»]
4Y74X-ray2.70F/T1-288[»]
4Y75X-ray2.80F/T1-288[»]
4Y77X-ray2.50F/T1-288[»]
4Y78X-ray2.80F/T1-288[»]
4Y7WX-ray2.50F/T1-288[»]
4Y7XX-ray2.60F/T1-288[»]
4Y7YX-ray2.40F/T1-288[»]
4Y80X-ray2.50F/T1-288[»]
4Y81X-ray2.80F/T1-288[»]
4Y82X-ray2.80F/T1-288[»]
4Y84X-ray2.70F/T1-288[»]
4Y8GX-ray2.60F/T1-288[»]
4Y8HX-ray2.50F/T1-288[»]
4Y8IX-ray2.60F/T1-288[»]
4Y8JX-ray2.70F/T1-288[»]
4Y8KX-ray2.60F/T1-288[»]
4Y8LX-ray2.40F/T1-288[»]
4Y8MX-ray2.80F/T1-288[»]
4Y8NX-ray2.60F/T1-288[»]
4Y8OX-ray2.70F/T1-288[»]
4Y8PX-ray2.80F/T1-288[»]
4Y8QX-ray2.60F/T1-288[»]
4Y8RX-ray2.70F/T1-288[»]
4Y8SX-ray2.70F/T1-288[»]
4Y8TX-ray2.70F/T1-288[»]
4Y8UX-ray2.90F/T1-288[»]
4Y9YX-ray2.80F/T1-288[»]
4Y9ZX-ray2.80F/T1-288[»]
4YA0X-ray2.80F/T1-288[»]
4YA1X-ray2.90F/T1-288[»]
4YA2X-ray2.70F/T1-288[»]
4YA3X-ray2.70F/T1-288[»]
4YA4X-ray2.90F/T1-288[»]
4YA5X-ray2.50F/T1-288[»]
4YA7X-ray2.70F/T1-288[»]
4YA9X-ray2.70F/T1-288[»]
4Z1LX-ray3.00F/T1-288[»]
4ZZGX-ray3.00G/U1-288[»]
5A5Belectron microscopy9.50G1-288[»]
5AHJX-ray2.80F/T1-288[»]
5BOUX-ray2.60F/T1-288[»]
5BXLX-ray2.80F/T1-288[»]
5BXNX-ray2.80F/T1-288[»]
5CGFX-ray2.80F/T1-288[»]
5CGGX-ray2.90F/T1-288[»]
5CGHX-ray2.50F/T1-288[»]
5CGIX-ray2.80F/T1-288[»]
5CZ4X-ray2.30F/T1-288[»]
5CZ5X-ray2.80F/T1-288[»]
5CZ6X-ray2.70F/T1-288[»]
5CZ7X-ray2.50F/T1-288[»]
5CZ8X-ray2.80F/T1-288[»]
5CZ9X-ray2.90F/T1-288[»]
5CZAX-ray2.50F/T1-288[»]
5D0SX-ray2.50F/T1-288[»]
5D0TX-ray2.60F/T1-288[»]
5D0VX-ray2.90F/T1-288[»]
5D0WX-ray2.80F/T1-288[»]
5D0XX-ray2.60F/T1-288[»]
5D0ZX-ray2.90F/T1-288[»]
5DKIX-ray2.80F/T1-288[»]
5DKJX-ray2.80F/T1-288[»]
5FG7X-ray2.70F/T1-288[»]
5FG9X-ray2.60F/T1-288[»]
5FGAX-ray2.70F/T1-288[»]
5FGDX-ray2.80F/T1-288[»]
5FGEX-ray2.60F/T1-288[»]
5FGFX-ray2.60F/T1-288[»]
5FGGX-ray2.70F/T1-288[»]
5FGHX-ray2.80F/T1-288[»]
5FGIX-ray2.90F/T1-288[»]
5FHSX-ray2.70F/T1-288[»]
5JHRX-ray2.90F/T1-288[»]
5JHSX-ray3.00F/T1-288[»]
ProteinModelPortaliP21242.
SMRiP21242.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34747. 95 interactors.
DIPiDIP-1526N.
IntActiP21242. 29 interactors.
MINTiMINT-411846.

PTM databases

iPTMnetiP21242.

Proteomic databases

MaxQBiP21242.
PRIDEiP21242.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

EuPathDBiFungiDB:YOR362C.
SGDiS000005889. PRE10.

Phylogenomic databases

GeneTreeiENSGT00550000074912.
HOGENOMiHOG000091086.
InParanoidiP21242.
KOiK02727.
OMAiVPDGRHF.
OrthoDBiEOG092C47D8.

Enzyme and pathway databases

BioCyciYEAST:G3O-33832-MONOMER.
ReactomeiR-SCE-1236978. Cross-presentation of soluble exogenous antigens (endosomes).
R-SCE-174113. SCF-beta-TrCP mediated degradation of Emi1.
R-SCE-349425. Autodegradation of the E3 ubiquitin ligase COP1.
R-SCE-382556. ABC-family proteins mediated transport.
R-SCE-450408. AUF1 (hnRNP D0) binds and destabilizes mRNA.
R-SCE-5668541. TNFR2 non-canonical NF-kB pathway.
R-SCE-5687128. MAPK6/MAPK4 signaling.
R-SCE-5689880. Ub-specific processing proteases.
R-SCE-68949. Orc1 removal from chromatin.
R-SCE-69017. CDK-mediated phosphorylation and removal of Cdc6.
R-SCE-69229. Ubiquitin-dependent degradation of Cyclin D1.
R-SCE-69601. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
R-SCE-8854050. FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
R-SCE-983168. Antigen processing: Ubiquitination & Proteasome degradation.

Miscellaneous databases

EvolutionaryTraceiP21242.
PROiP21242.

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]
ProtoNetiSearch...

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: November 30, 2016
This is version 189 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.1 Publication

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.