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P22141

- PSB4_YEAST

UniProt

P22141 - PSB4_YEAST

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Protein

Proteasome subunit beta type-4

Gene

PRE1

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. This subunit has a chymotrypsin-like activity.

Catalytic activityi

Cleavage of peptide bonds with very broad specificity.

GO - Molecular functioni

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

GO - Biological processi

  1. positive regulation of endopeptidase activity Source: GOC
  2. proteasomal ubiquitin-independent protein catabolic process Source: SGD
  3. 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-30199-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

MEROPSiT01.984.

Names & Taxonomyi

Protein namesi
Recommended name:
Proteasome subunit beta type-4 (EC:3.4.25.1)
Alternative name(s):
Macropain subunit C11
Multicatalytic endopeptidase complex subunit C11
Proteasome component C11
Proteinase YSCE subunit 11
Gene namesi
Name:PRE1
Ordered Locus Names:YER012W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome V

Organism-specific databases

CYGDiYER012w.
SGDiS000000814. PRE1.

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
Chaini1 – 198198Proteasome subunit beta type-4PRO_0000148055Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication
Modified residuei76 – 761Phosphoserine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP22141.
PaxDbiP22141.
PeptideAtlasiP22141.

Expressioni

Gene expression databases

GenevestigatoriP22141.

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
PRE10P212423EBI-13988,EBI-13963
PRE6P403033EBI-13988,EBI-13980
RPT1P332992EBI-13988,EBI-13910

Protein-protein interaction databases

BioGridi36744. 134 interactions.
DIPiDIP-2808N.
IntActiP22141. 26 interactions.
MINTiMINT-592869.
STRINGi4932.YER012W.

Structurei

Secondary structure

1
198
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 85
Beta strandi13 – 186
Beta strandi21 – 233
Beta strandi26 – 305
Beta strandi35 – 395
Beta strandi42 – 498
Helixi50 – 7122
Helixi77 – 9115
Beta strandi94 – 963
Beta strandi100 – 1089
Turni109 – 1124
Beta strandi113 – 1197
Turni121 – 1233
Beta strandi125 – 1273
Beta strandi129 – 1324
Helixi136 – 14712
Helixi154 – 17118
Beta strandi179 – 1857
Beta strandi188 – 1925
Turni194 – 1974

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FNTX-ray3.20K/Y1-198[»]
1G0UX-ray2.40J/X1-198[»]
1G65X-ray2.25J/X1-198[»]
1JD2X-ray3.00J/Q1-198[»]
1RYPX-ray1.90K/Y1-198[»]
1VSYX-ray3.00K/Y1-198[»]
1Z7QX-ray3.22K/Y1-198[»]
2F16X-ray2.80J/X1-198[»]
2FAKX-ray2.80J/X1-198[»]
2GPLX-ray2.81J/X1-198[»]
2ZCYX-ray2.90J/X1-198[»]
3BDMX-ray2.70J/X1-198[»]
3D29X-ray2.60J/X1-198[»]
3DY3X-ray2.81J/X1-198[»]
3DY4X-ray2.80J/X1-198[»]
3E47X-ray3.00J/X1-198[»]
3GPJX-ray2.70J/X1-198[»]
3GPTX-ray2.41J/X1-198[»]
3GPWX-ray2.50J/X1-198[»]
3HYEX-ray2.50J/X1-198[»]
3L5QX-ray3.001/O1-198[»]
3MG0X-ray2.68J/X1-198[»]
3MG4X-ray3.11J/X1-198[»]
3MG6X-ray2.60J/X1-198[»]
3MG7X-ray2.78J/X1-198[»]
3MG8X-ray2.59J/X1-198[»]
3NZJX-ray2.40J/X1-198[»]
3NZWX-ray2.50J/X1-198[»]
3NZXX-ray2.70J/X1-198[»]
3OEUX-ray2.60J/X1-198[»]
3OEVX-ray2.85J/X1-198[»]
3OKJX-ray2.70J/X1-198[»]
3SDIX-ray2.65J/X1-198[»]
3SDKX-ray2.70J/X1-198[»]
3SHJX-ray2.80J/X1-198[»]
3TDDX-ray2.70J/X1-198[»]
3UN4X-ray3.40J/X1-198[»]
3UN8X-ray2.70J/X1-198[»]
4CR2electron microscopy7.7041-198[»]
4CR3electron microscopy9.3041-198[»]
4CR4electron microscopy8.8041-198[»]
4EU2X-ray2.51K/Y1-198[»]
4FZCX-ray2.80J/X1-198[»]
4FZGX-ray3.00J/X1-198[»]
4G4SX-ray2.49K1-198[»]
4GK7X-ray2.80J/X1-198[»]
4HNPX-ray2.80J/X1-198[»]
4HRCX-ray2.80J/X1-198[»]
4HRDX-ray2.80J/X1-198[»]
4INRX-ray2.70J/X1-198[»]
4INTX-ray2.90J/X1-198[»]
4INUX-ray3.10J/X1-198[»]
4J70X-ray2.80J/X1-198[»]
4JSQX-ray2.80J/X1-198[»]
4JSUX-ray2.90J/X1-198[»]
4JT0X-ray3.10J/X1-198[»]
4LQIX-ray2.70J/X1-198[»]
4LTCX-ray2.50J/X1-198[»]
4NNNX-ray2.50J/X1-198[»]
4NNWX-ray2.60J/X1-198[»]
4NO1X-ray2.50J/X1-198[»]
4NO6X-ray3.00J/X1-198[»]
4NO8X-ray2.70J/X1-198[»]
4NO9X-ray2.90J/X1-198[»]
4Q1SX-ray2.60J/X1-198[»]
4QBYX-ray3.00J/X1-198[»]
4QLQX-ray2.40J/X1-198[»]
4QLSX-ray2.80J/X1-198[»]
4QLTX-ray2.80J/X1-198[»]
4QLUX-ray2.80J/X1-198[»]
4QLVX-ray2.90J/X1-198[»]
4R02X-ray2.50J/X1-198[»]
ProteinModelPortaliP22141.
SMRiP22141. Positions 1-198.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP22141.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1B family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0638.
GeneTreeiENSGT00640000091536.
HOGENOMiHOG000188743.
InParanoidiP22141.
KOiK02734.
OMAiHFVRGEL.
OrthoDBiEOG7SJDGT.

Family and domain databases

Gene3Di3.60.20.10. 1 hit.
InterProiIPR029055. Ntn_hydrolases_N.
IPR016050. Proteasome_bsu_CS.
IPR001353. Proteasome_sua/b.
IPR023333. Proteasome_suB-type.
[Graphical view]
PfamiPF00227. Proteasome. 1 hit.
[Graphical view]
SUPFAMiSSF56235. SSF56235. 1 hit.
PROSITEiPS00854. PROTEASOME_BETA_1. 1 hit.
PS51476. PROTEASOME_BETA_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P22141-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MDIILGIRVQ DSVILASSKA VTRGISVLKD SDDKTRQLSP HTLMSFAGEA
60 70 80 90 100
GDTVQFAEYI QANIQLYSIR EDYELSPQAV SSFVRQELAK SIRSRRPYQV
110 120 130 140 150
NVLIGGYDKK KNKPELYQID YLGTKVELPY GAHGYSGFYT FSLLDHHYRP
160 170 180 190
DMTTEEGLDL LKLCVQELEK RMPMDFKGVI VKIVDKDGIR QVDDFQAQ
Length:198
Mass (Da):22,517
Last modified:February 1, 1995 - v2
Checksum:iED43D319A5895B40
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti183 – 1831I → T(PubMed:2001673)Curated
Sequence conflicti188 – 1881G → R(PubMed:2001673)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X56812 Genomic DNA. Translation: CAA40149.1.
U18778 Genomic DNA. Translation: AAB64545.1.
AY557807 Genomic DNA. Translation: AAS56133.1.
BK006939 Genomic DNA. Translation: DAA07663.1.
PIRiS50470.
RefSeqiNP_010928.1. NM_001178903.1.

Genome annotation databases

EnsemblFungiiYER012W; YER012W; YER012W.
GeneIDi856731.
KEGGisce:YER012W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X56812 Genomic DNA. Translation: CAA40149.1 .
U18778 Genomic DNA. Translation: AAB64545.1 .
AY557807 Genomic DNA. Translation: AAS56133.1 .
BK006939 Genomic DNA. Translation: DAA07663.1 .
PIRi S50470.
RefSeqi NP_010928.1. NM_001178903.1.

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 K/Y 1-198 [» ]
1G0U X-ray 2.40 J/X 1-198 [» ]
1G65 X-ray 2.25 J/X 1-198 [» ]
1JD2 X-ray 3.00 J/Q 1-198 [» ]
1RYP X-ray 1.90 K/Y 1-198 [» ]
1VSY X-ray 3.00 K/Y 1-198 [» ]
1Z7Q X-ray 3.22 K/Y 1-198 [» ]
2F16 X-ray 2.80 J/X 1-198 [» ]
2FAK X-ray 2.80 J/X 1-198 [» ]
2GPL X-ray 2.81 J/X 1-198 [» ]
2ZCY X-ray 2.90 J/X 1-198 [» ]
3BDM X-ray 2.70 J/X 1-198 [» ]
3D29 X-ray 2.60 J/X 1-198 [» ]
3DY3 X-ray 2.81 J/X 1-198 [» ]
3DY4 X-ray 2.80 J/X 1-198 [» ]
3E47 X-ray 3.00 J/X 1-198 [» ]
3GPJ X-ray 2.70 J/X 1-198 [» ]
3GPT X-ray 2.41 J/X 1-198 [» ]
3GPW X-ray 2.50 J/X 1-198 [» ]
3HYE X-ray 2.50 J/X 1-198 [» ]
3L5Q X-ray 3.00 1/O 1-198 [» ]
3MG0 X-ray 2.68 J/X 1-198 [» ]
3MG4 X-ray 3.11 J/X 1-198 [» ]
3MG6 X-ray 2.60 J/X 1-198 [» ]
3MG7 X-ray 2.78 J/X 1-198 [» ]
3MG8 X-ray 2.59 J/X 1-198 [» ]
3NZJ X-ray 2.40 J/X 1-198 [» ]
3NZW X-ray 2.50 J/X 1-198 [» ]
3NZX X-ray 2.70 J/X 1-198 [» ]
3OEU X-ray 2.60 J/X 1-198 [» ]
3OEV X-ray 2.85 J/X 1-198 [» ]
3OKJ X-ray 2.70 J/X 1-198 [» ]
3SDI X-ray 2.65 J/X 1-198 [» ]
3SDK X-ray 2.70 J/X 1-198 [» ]
3SHJ X-ray 2.80 J/X 1-198 [» ]
3TDD X-ray 2.70 J/X 1-198 [» ]
3UN4 X-ray 3.40 J/X 1-198 [» ]
3UN8 X-ray 2.70 J/X 1-198 [» ]
4CR2 electron microscopy 7.70 4 1-198 [» ]
4CR3 electron microscopy 9.30 4 1-198 [» ]
4CR4 electron microscopy 8.80 4 1-198 [» ]
4EU2 X-ray 2.51 K/Y 1-198 [» ]
4FZC X-ray 2.80 J/X 1-198 [» ]
4FZG X-ray 3.00 J/X 1-198 [» ]
4G4S X-ray 2.49 K 1-198 [» ]
4GK7 X-ray 2.80 J/X 1-198 [» ]
4HNP X-ray 2.80 J/X 1-198 [» ]
4HRC X-ray 2.80 J/X 1-198 [» ]
4HRD X-ray 2.80 J/X 1-198 [» ]
4INR X-ray 2.70 J/X 1-198 [» ]
4INT X-ray 2.90 J/X 1-198 [» ]
4INU X-ray 3.10 J/X 1-198 [» ]
4J70 X-ray 2.80 J/X 1-198 [» ]
4JSQ X-ray 2.80 J/X 1-198 [» ]
4JSU X-ray 2.90 J/X 1-198 [» ]
4JT0 X-ray 3.10 J/X 1-198 [» ]
4LQI X-ray 2.70 J/X 1-198 [» ]
4LTC X-ray 2.50 J/X 1-198 [» ]
4NNN X-ray 2.50 J/X 1-198 [» ]
4NNW X-ray 2.60 J/X 1-198 [» ]
4NO1 X-ray 2.50 J/X 1-198 [» ]
4NO6 X-ray 3.00 J/X 1-198 [» ]
4NO8 X-ray 2.70 J/X 1-198 [» ]
4NO9 X-ray 2.90 J/X 1-198 [» ]
4Q1S X-ray 2.60 J/X 1-198 [» ]
4QBY X-ray 3.00 J/X 1-198 [» ]
4QLQ X-ray 2.40 J/X 1-198 [» ]
4QLS X-ray 2.80 J/X 1-198 [» ]
4QLT X-ray 2.80 J/X 1-198 [» ]
4QLU X-ray 2.80 J/X 1-198 [» ]
4QLV X-ray 2.90 J/X 1-198 [» ]
4R02 X-ray 2.50 J/X 1-198 [» ]
ProteinModelPortali P22141.
SMRi P22141. Positions 1-198.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 36744. 134 interactions.
DIPi DIP-2808N.
IntActi P22141. 26 interactions.
MINTi MINT-592869.
STRINGi 4932.YER012W.

Chemistry

BindingDBi P22141.
ChEMBLi CHEMBL4206.

Protein family/group databases

MEROPSi T01.984.

Proteomic databases

MaxQBi P22141.
PaxDbi P22141.
PeptideAtlasi P22141.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YER012W ; YER012W ; YER012W .
GeneIDi 856731.
KEGGi sce:YER012W.

Organism-specific databases

CYGDi YER012w.
SGDi S000000814. PRE1.

Phylogenomic databases

eggNOGi COG0638.
GeneTreei ENSGT00640000091536.
HOGENOMi HOG000188743.
InParanoidi P22141.
KOi K02734.
OMAi HFVRGEL.
OrthoDBi EOG7SJDGT.

Enzyme and pathway databases

BioCyci YEAST:G3O-30199-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 P22141.
NextBioi 982843.
PROi P22141.

Gene expression databases

Genevestigatori P22141.

Family and domain databases

Gene3Di 3.60.20.10. 1 hit.
InterProi IPR029055. Ntn_hydrolases_N.
IPR016050. Proteasome_bsu_CS.
IPR001353. Proteasome_sua/b.
IPR023333. Proteasome_suB-type.
[Graphical view ]
Pfami PF00227. Proteasome. 1 hit.
[Graphical view ]
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. "Proteinase yscE, the yeast proteasome/multicatalytic-multifunctional proteinase: mutants unravel its function in stress induced proteolysis and uncover its necessity for cell survival."
    Heinemeyer W., Kleinschmidt J.A., Saidowsky J., Escher C., Wolf D.H.
    EMBO J. 10:555-562(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  5. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  6. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-76, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "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 COMPLEX WITH THE 20S PROTEASOME.
  9. "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 COMPLEX WITH THE 20S PROTEASOME AND A 11S REGULATORY COMPLEX.
  10. Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF COMPLEX WITH THE 20S PROTEASOME.
  11. "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 COMPLEX WITH THE 20S PROTEASOME AND A TMC-95-BASED INHIBITOR.
  12. "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 COMPLEX WITH THE 20S PROTEASOME AND SALINOSPORAMIDE.
  13. "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 COMPLEX WITH THE 20S PROTEASOME AND BORTEZOMIB.
  14. "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) IN COMPLEX WITH THE PROTEASOME.
  15. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (7.4 ANGSTROMS) OF THE 26S PROTEASOME.

Entry informationi

Entry nameiPSB4_YEAST
AccessioniPrimary (citable) accession number: P22141
Secondary accession number(s): D3DLQ9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: February 1, 1995
Last modified: October 29, 2014
This is version 158 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 21800 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 V
    Yeast (Saccharomyces cerevisiae) chromosome V: entries and gene names

External Data

Dasty 3