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P30657

- PSB7_YEAST

UniProt

P30657 - PSB7_YEAST

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Protein
Proteasome subunit beta type-7
Gene
PRE4, YFR050C
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. PRE3 and PRE4 are necessary for the peptidyl-glutamyl-peptide-hydrolyzing activity.1 Publication

Catalytic activityi

Cleavage of peptide bonds with very broad specificity.1 Publication

GO - Molecular functioni

  1. threonine-type endopeptidase activity Source: UniProtKB-KW
Complete GO annotation...

GO - Biological processi

  1. proteasomal ubiquitin-independent protein catabolic process Source: SGD
  2. proteasome assembly 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-30496-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

MEROPSiT01.987.

Names & Taxonomyi

Protein namesi
Recommended name:
Proteasome subunit beta type-7 (EC:3.4.25.1)
Alternative name(s):
Macropain subunit PRE4
Multicatalytic endopeptidase complex subunit PRE4
Proteasome component PRE4
Proteinase YSCE subunit PRE4
Gene namesi
Name:PRE4
Ordered Locus Names:YFR050C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome VI

Organism-specific databases

CYGDiYFR050c.
SGDiS000001946. PRE4.

Subcellular locationi

Cytoplasm. Nucleus 1 Publication

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 – 3333
PRO_0000331490Add
BLAST
Chaini34 – 266233Proteasome subunit beta type-7
PRO_0000148073Add
BLAST

Proteomic databases

MaxQBiP30657.
PaxDbiP30657.
PeptideAtlasiP30657.

Expressioni

Gene expression databases

GenevestigatoriP30657.

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. Interacts with CIC1.2 Publications

Protein-protein interaction databases

BioGridi31208. 74 interactions.
DIPiDIP-2807N.
IntActiP30657. 20 interactions.
MINTiMINT-592513.
STRINGi4932.YFR050C.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi39 – 413
Beta strandi44 – 496
Beta strandi52 – 587
Beta strandi61 – 633
Beta strandi66 – 705
Beta strandi75 – 784
Turni79 – 813
Beta strandi82 – 898
Helixi90 – 10819
Turni112 – 1187
Helixi122 – 13817
Beta strandi145 – 1528
Beta strandi158 – 1647
Beta strandi169 – 1713
Beta strandi173 – 1764
Helixi179 – 18810
Turni189 – 1913
Beta strandi192 – 1943
Helixi195 – 2006
Helixi203 – 22018
Beta strandi226 – 2349
Turni235 – 2373
Beta strandi238 – 2469
Helixi253 – 2575
Beta strandi260 – 2634

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FNTX-ray3.20N/b34-265[»]
1G0UX-ray2.401/M1-266[»]
1G65X-ray2.251/M34-266[»]
1JD2X-ray3.00M/T34-266[»]
1RYPX-ray1.902/N34-266[»]
1VSYX-ray3.002/N34-266[»]
1Z7QX-ray3.22N/b34-266[»]
2F16X-ray2.801/M34-266[»]
2FAKX-ray2.801/M34-266[»]
2GPLX-ray2.811/M34-266[»]
2ZCYX-ray2.900/M1-266[»]
3BDMX-ray2.700/M1-266[»]
3D29X-ray2.601/M34-266[»]
3DY3X-ray2.811/M34-266[»]
3DY4X-ray2.801/M34-266[»]
3E47X-ray3.001/M34-266[»]
3GPJX-ray2.701/M34-266[»]
3GPTX-ray2.411/M34-266[»]
3GPWX-ray2.501/M34-266[»]
3HYEX-ray2.501/M34-266[»]
3L5QX-ray3.004/R34-266[»]
3MG0X-ray2.681/M34-266[»]
3MG4X-ray3.111/M34-266[»]
3MG6X-ray2.601/M1-266[»]
3MG7X-ray2.781/M1-266[»]
3MG8X-ray2.591/M1-266[»]
3NZJX-ray2.401/M1-266[»]
3NZWX-ray2.501/M1-266[»]
3NZXX-ray2.701/M1-266[»]
3OEUX-ray2.601/M34-266[»]
3OEVX-ray2.851/M34-266[»]
3OKJX-ray2.701/M34-266[»]
3SDIX-ray2.651/M34-253[»]
3SDKX-ray2.701/M34-266[»]
3SHJX-ray2.801/M34-266[»]
3TDDX-ray2.701/M34-266[»]
3UN4X-ray3.40M/a34-266[»]
3UN8X-ray2.70M/a34-266[»]
4CR2electron microscopy7.7071-266[»]
4CR3electron microscopy9.3071-266[»]
4CR4electron microscopy8.8071-266[»]
4EU2X-ray2.512/N34-266[»]
4FZCX-ray2.80M/a34-266[»]
4FZGX-ray3.00M/a34-266[»]
4G4SX-ray2.49N34-266[»]
4GK7X-ray2.80M/a34-266[»]
4HNPX-ray2.80M/a34-266[»]
4HRCX-ray2.80M/a34-266[»]
4HRDX-ray2.80M/a34-266[»]
4INRX-ray2.70M/a34-266[»]
4INTX-ray2.90M/a34-266[»]
4INUX-ray3.10M/a34-266[»]
4J70X-ray2.80M/a34-266[»]
4JSQX-ray2.80M/a34-266[»]
4JSUX-ray2.90M/a34-266[»]
4JT0X-ray3.10M/a34-266[»]
4LQIX-ray2.70M/a34-266[»]
4NNNX-ray2.50M/a21-266[»]
4NNWX-ray2.60M/a21-266[»]
4NO1X-ray2.50M/a21-266[»]
4NO6X-ray3.00M/a21-266[»]
4NO8X-ray2.70M/a21-266[»]
4NO9X-ray2.90M/a21-266[»]
4QBYX-ray3.00M/a21-266[»]
ProteinModelPortaliP30657.
SMRiP30657. Positions 34-266.

Miscellaneous databases

EvolutionaryTraceiP30657.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1B family.

Phylogenomic databases

eggNOGiCOG0638.
GeneTreeiENSGT00390000000698.
HOGENOMiHOG000181719.
KOiK02736.
OMAiYHASTIA.
OrthoDBiEOG73BVQ8.

Family and domain databases

Gene3Di3.60.20.10. 1 hit.
InterProiIPR029055. Ntn_hydrolases_N.
IPR016050. Proteasome_bsu_CS.
IPR016295. Proteasome_endopept_cplx_B.
IPR001353. Proteasome_sua/b.
IPR023333. Proteasome_suB-type.
[Graphical view]
PfamiPF00227. Proteasome. 1 hit.
[Graphical view]
PIRSFiPIRSF001213. Psome_endopept_beta. 1 hit.
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.

P30657-1 [UniParc]FASTAAdd to Basket

« Hide

MNHDPFSWGR PADSTYGAYN TQIANAGASP MVNTQQPIVT GTSVISMKYD    50
NGVIIAADNL GSYGSLLRFN GVERLIPVGD NTVVGISGDI SDMQHIERLL 100
KDLVTENAYD NPLADAEEAL EPSYIFEYLA TVMYQRRSKM NPLWNAIIVA 150
GVQSNGDQFL RYVNLLGVTY SSPTLATGFG AHMANPLLRK VVDRESDIPK 200
TTVQVAEEAI VNAMRVLYYR DARSSRNFSL AIIDKNTGLT FKKNLQVENM 250
KWDFAKDIKG YGTQKI 266
Length:266
Mass (Da):29,443
Last modified:April 1, 1993 - v1
Checksum:iE585BB3B5D0C8E2C
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti188 – 1881L → V in AAT92966. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X68663 Genomic DNA. Translation: CAA48629.1.
D50617 Genomic DNA. Translation: BAA09289.1.
AY692947 Genomic DNA. Translation: AAT92966.1.
BK006940 Genomic DNA. Translation: DAA12493.1.
PIRiA46610.
RefSeqiNP_116708.1. NM_001180015.1.

Genome annotation databases

EnsemblFungiiYFR050C; YFR050C; YFR050C.
GeneIDi850611.
KEGGisce:YFR050C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X68663 Genomic DNA. Translation: CAA48629.1 .
D50617 Genomic DNA. Translation: BAA09289.1 .
AY692947 Genomic DNA. Translation: AAT92966.1 .
BK006940 Genomic DNA. Translation: DAA12493.1 .
PIRi A46610.
RefSeqi NP_116708.1. NM_001180015.1.

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 N/b 34-265 [» ]
1G0U X-ray 2.40 1/M 1-266 [» ]
1G65 X-ray 2.25 1/M 34-266 [» ]
1JD2 X-ray 3.00 M/T 34-266 [» ]
1RYP X-ray 1.90 2/N 34-266 [» ]
1VSY X-ray 3.00 2/N 34-266 [» ]
1Z7Q X-ray 3.22 N/b 34-266 [» ]
2F16 X-ray 2.80 1/M 34-266 [» ]
2FAK X-ray 2.80 1/M 34-266 [» ]
2GPL X-ray 2.81 1/M 34-266 [» ]
2ZCY X-ray 2.90 0/M 1-266 [» ]
3BDM X-ray 2.70 0/M 1-266 [» ]
3D29 X-ray 2.60 1/M 34-266 [» ]
3DY3 X-ray 2.81 1/M 34-266 [» ]
3DY4 X-ray 2.80 1/M 34-266 [» ]
3E47 X-ray 3.00 1/M 34-266 [» ]
3GPJ X-ray 2.70 1/M 34-266 [» ]
3GPT X-ray 2.41 1/M 34-266 [» ]
3GPW X-ray 2.50 1/M 34-266 [» ]
3HYE X-ray 2.50 1/M 34-266 [» ]
3L5Q X-ray 3.00 4/R 34-266 [» ]
3MG0 X-ray 2.68 1/M 34-266 [» ]
3MG4 X-ray 3.11 1/M 34-266 [» ]
3MG6 X-ray 2.60 1/M 1-266 [» ]
3MG7 X-ray 2.78 1/M 1-266 [» ]
3MG8 X-ray 2.59 1/M 1-266 [» ]
3NZJ X-ray 2.40 1/M 1-266 [» ]
3NZW X-ray 2.50 1/M 1-266 [» ]
3NZX X-ray 2.70 1/M 1-266 [» ]
3OEU X-ray 2.60 1/M 34-266 [» ]
3OEV X-ray 2.85 1/M 34-266 [» ]
3OKJ X-ray 2.70 1/M 34-266 [» ]
3SDI X-ray 2.65 1/M 34-253 [» ]
3SDK X-ray 2.70 1/M 34-266 [» ]
3SHJ X-ray 2.80 1/M 34-266 [» ]
3TDD X-ray 2.70 1/M 34-266 [» ]
3UN4 X-ray 3.40 M/a 34-266 [» ]
3UN8 X-ray 2.70 M/a 34-266 [» ]
4CR2 electron microscopy 7.70 7 1-266 [» ]
4CR3 electron microscopy 9.30 7 1-266 [» ]
4CR4 electron microscopy 8.80 7 1-266 [» ]
4EU2 X-ray 2.51 2/N 34-266 [» ]
4FZC X-ray 2.80 M/a 34-266 [» ]
4FZG X-ray 3.00 M/a 34-266 [» ]
4G4S X-ray 2.49 N 34-266 [» ]
4GK7 X-ray 2.80 M/a 34-266 [» ]
4HNP X-ray 2.80 M/a 34-266 [» ]
4HRC X-ray 2.80 M/a 34-266 [» ]
4HRD X-ray 2.80 M/a 34-266 [» ]
4INR X-ray 2.70 M/a 34-266 [» ]
4INT X-ray 2.90 M/a 34-266 [» ]
4INU X-ray 3.10 M/a 34-266 [» ]
4J70 X-ray 2.80 M/a 34-266 [» ]
4JSQ X-ray 2.80 M/a 34-266 [» ]
4JSU X-ray 2.90 M/a 34-266 [» ]
4JT0 X-ray 3.10 M/a 34-266 [» ]
4LQI X-ray 2.70 M/a 34-266 [» ]
4NNN X-ray 2.50 M/a 21-266 [» ]
4NNW X-ray 2.60 M/a 21-266 [» ]
4NO1 X-ray 2.50 M/a 21-266 [» ]
4NO6 X-ray 3.00 M/a 21-266 [» ]
4NO8 X-ray 2.70 M/a 21-266 [» ]
4NO9 X-ray 2.90 M/a 21-266 [» ]
4QBY X-ray 3.00 M/a 21-266 [» ]
ProteinModelPortali P30657.
SMRi P30657. Positions 34-266.
ModBasei Search...

Protein-protein interaction databases

BioGridi 31208. 74 interactions.
DIPi DIP-2807N.
IntActi P30657. 20 interactions.
MINTi MINT-592513.
STRINGi 4932.YFR050C.

Protein family/group databases

MEROPSi T01.987.

Proteomic databases

MaxQBi P30657.
PaxDbi P30657.
PeptideAtlasi P30657.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YFR050C ; YFR050C ; YFR050C .
GeneIDi 850611.
KEGGi sce:YFR050C.

Organism-specific databases

CYGDi YFR050c.
SGDi S000001946. PRE4.

Phylogenomic databases

eggNOGi COG0638.
GeneTreei ENSGT00390000000698.
HOGENOMi HOG000181719.
KOi K02736.
OMAi YHASTIA.
OrthoDBi EOG73BVQ8.

Enzyme and pathway databases

BioCyci YEAST:G3O-30496-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 P30657.
NextBioi 966499.
PROi P30657.

Gene expression databases

Genevestigatori P30657.

Family and domain databases

Gene3Di 3.60.20.10. 1 hit.
InterProi IPR029055. Ntn_hydrolases_N.
IPR016050. Proteasome_bsu_CS.
IPR016295. Proteasome_endopept_cplx_B.
IPR001353. Proteasome_sua/b.
IPR023333. Proteasome_suB-type.
[Graphical view ]
Pfami PF00227. Proteasome. 1 hit.
[Graphical view ]
PIRSFi PIRSF001213. Psome_endopept_beta. 1 hit.
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. "The PRE4 gene codes for a subunit of the yeast proteasome necessary for peptidylglutamyl-peptide-hydrolyzing activity. Mutations link the proteasome to stress- and ubiquitin-dependent proteolysis."
    Hilt W., Enenkel C., Gruhler A., Singer T., Wolf D.H.
    J. Biol. Chem. 268:3479-3486(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, SUBUNIT.
  2. "Analysis of a 36.2 kb DNA sequence including the right telomere of chromosome VI from Saccharomyces cerevisiae."
    Eki T., Naitou M., Hagiwara H., Ozawa M., Sasanuma S., Sasanuma M., Tsuchiya Y., Shibata T., Hanaoka F., Murakami Y.
    Yeast 12:149-167(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204511 / S288c / AB972.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  6. "Cic1, an adaptor protein specifically linking the 26S proteasome to its substrate, the SCF component Cdc4."
    Jaeger S., Strayle J., Heinemeyer W., Wolf D.H.
    EMBO J. 20:4423-4431(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CIC1.
  7. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  8. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  9. "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 34-266 OF COMPLEX WITH THE 20S PROTEASOME, PROTEOLYTIC PROCESSING.
  10. "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 34-266 OF COMPLEX WITH THE 20S PROTEASOME AND A 11S REGULATORY COMPLEX.
  11. Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF COMPLEX WITH THE 20S PROTEASOME.
  12. "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 34-266 OF COMPLEX WITH THE 20S PROTEASOME AND A TMC-95-BASED INHIBITOR.
  13. "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 34-266 OF COMPLEX WITH THE 20S PROTEASOME AND SALINOSPORAMIDE.
  14. "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 34-266 OF COMPLEX WITH THE 20S PROTEASOME AND BORTEZOMIB.
  15. "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 34-266 IN COMPLEX WITH THE PROTEASOME.
  16. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (7.4 ANGSTROMS) OF THE 26S PROTEASOME.

Entry informationi

Entry nameiPSB7_YEAST
AccessioniPrimary (citable) accession number: P30657
Secondary accession number(s): D6VTT3, E9P8Z8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: April 1, 1993
Last modified: September 3, 2014
This is version 152 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 16900 molecules/cell in log phase SD medium.

Caution

It is uncertain whether Met-1 or Met-31 is the initiator.

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 VI
    Yeast (Saccharomyces cerevisiae) chromosome VI: entries and gene names

External Data

Dasty 3

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