Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q01532

- BLH1_YEAST

UniProt

Q01532 - BLH1_YEAST

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Cysteine proteinase 1, mitochondrial

Gene

LAP3

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 normal physiological role of the enzyme is unknown, but it is not essential for the viability of yeast cells. Has aminopeptidase activity, shortening substrate peptides sequentially by 1 amino acid. Has bleomycin hydrolase activity, which can protect the cell from the toxic effects of bleomycin. Has homocysteine-thiolactonase activity, protecting the cell against homocysteine toxicity. Acts as a repressor in the GAL4 regulatory system, but this does not require either the peptidase or nucleic acid-binding activities.2 Publications

Catalytic activityi

Inactivates bleomycin B2 (a cytotoxic glycometallopeptide) by hydrolysis of a carboxyamide bond of beta-aminoalanine, but also shows general aminopeptidase activity. The specificity varies somewhat with source, but amino acid arylamides of Met, Leu and Ala are preferred.

Enzyme regulationi

Inhibited by E64, a specific inhibitor of cysteine proteases, N-ethylmaleimide, iodacetamide, and mercury and zinc ions.2 Publications

Kineticsi

N-terminal acetylation of lysine-4-methyl-7-coumarylamide (Ac-Lys-AMC) reduces the catalytic efficiency 50-fold towards this substrate.

  1. KM=12.8 µM for arginine-4-methyl-7-coumarylamide3 Publications
  2. KM=0.33 mM for glutamine-beta-naphthylamide3 Publications
  3. KM=228 µM for lysine-4-methyl-7-coumarylamide3 Publications

Vmax=2.56 µmol/h/mg enzyme for arginine-4-methyl-7-coumarylamide3 Publications

Vmax=370 nmol/min/mg enzyme for glutamine-beta-naphthylamide3 Publications

pH dependencei

Optimum pH is 7.5.3 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei102 – 1021
Active sitei398 – 3981
Active sitei421 – 4211

GO - Molecular functioni

  1. cysteine-type endopeptidase activity Source: InterPro
  2. cysteine-type peptidase activity Source: SGD
  3. double-stranded DNA binding Source: SGD
  4. mRNA binding Source: SGD
  5. RNA polymerase II core promoter proximal region sequence-specific DNA binding Source: SGD
  6. single-stranded DNA binding Source: SGD

GO - Biological processi

  1. homocysteine catabolic process Source: SGD
  2. negative regulation of transcription from RNA polymerase II promoter Source: SGD
  3. response to antibiotic Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-33237-MONOMER.
BRENDAi3.4.22.40. 984.
ReactomeiREACT_189060. Antigen processing: Ubiquitination & Proteasome degradation.
SABIO-RKQ01532.

Protein family/group databases

MEROPSiC01.085.

Names & Taxonomyi

Protein namesi
Recommended name:
Cysteine proteinase 1, mitochondrial (EC:3.4.22.40)
Alternative name(s):
Bleomycin hydrolase
Short name:
BLM hydrolase
Homocysteine-thiolactonase
Short name:
HTLase
Short name:
Hcy-thiolactonase
Leucine aminopeptidase 3
Y3
Gene namesi
Name:LAP3
Synonyms:BLH1, GAL6, YCP1
Ordered Locus Names:YNL239W
ORF Names:N1118
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome XIV

Organism-specific databases

CYGDiYNL239w.
SGDiS000005183. LAP3.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: SGD
  2. mitochondrion Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Mitochondrion

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi102 – 1021C → A: Abolishes peptidase activity, which also hinders autocatalytic processing of the enzyme to the mature form. 1 Publication
Mutagenesisi271 – 2744KDKK → ADAA in GAL6DB; disrupts nucleic acid-binding activity, but retains normal peptidase activity. 1 Publication
Mutagenesisi398 – 3981H → A: Abolishes Hcy-thiolactonase activity. 1 Publication
Mutagenesisi479 – 4791G → A: Results in the abnormal cleavage of 3 C-terminal residues instead of only 1 during autocatalytic processing. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3030MitochondrionSequence AnalysisAdd
BLAST
Chaini31 – 482452Cysteine proteinase 1, mitochondrialPRO_0000050554Add
BLAST
Propeptidei483 – 4831Removed in mature form; by autocatalysis1 PublicationPRO_0000292865

Post-translational modificationi

The N-terminus of isoform Cytoplasmic is blocked.

Proteomic databases

MaxQBiQ01532.
PaxDbiQ01532.
PeptideAtlasiQ01532.

Expressioni

Gene expression databases

GenevestigatoriQ01532.

Interactioni

Subunit structurei

Homohexamer. Binds to nucleic acids. Binds single-stranded DNA and RNA with higher affinity than double-stranded DNA.1 Publication

Protein-protein interaction databases

BioGridi35600. 17 interactions.
DIPiDIP-2941N.
IntActiQ01532. 11 interactions.
MINTiMINT-513897.
STRINGi4932.YNL239W.

Structurei

Secondary structure

1
483
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi36 – 4712
Helixi50 – 5910
Helixi64 – 685
Helixi71 – 777
Beta strandi83 – 853
Beta strandi98 – 1003
Helixi102 – 11817
Helixi128 – 14922
Turni150 – 1523
Helixi158 – 1658
Helixi174 – 18411
Helixi189 – 1913
Helixi197 – 2004
Helixi203 – 22624
Beta strandi229 – 2313
Helixi232 – 25221
Beta strandi264 – 2696
Beta strandi275 – 2806
Helixi282 – 2887
Beta strandi296 – 3016
Beta strandi311 – 3144
Beta strandi326 – 3305
Helixi333 – 34513
Beta strandi350 – 3545
Turni356 – 3594
Turni362 – 3654
Helixi374 – 3774
Helixi385 – 3906
Beta strandi398 – 40710
Turni409 – 4113
Beta strandi414 – 4207
Turni425 – 4284
Beta strandi432 – 4365
Helixi437 – 4437
Beta strandi444 – 4507
Helixi451 – 4533
Helixi456 – 4638
Beta strandi470 – 4723
Helixi477 – 4793

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1A6RX-ray2.05A32-483[»]
1GCBX-ray2.20A30-483[»]
2DZYX-ray2.57A30-482[»]
2DZZX-ray2.15A30-482[»]
2E00X-ray2.00A30-482[»]
2E01X-ray1.73A30-482[»]
2E02X-ray2.20A30-482[»]
2E03X-ray2.13A30-482[»]
3GCBX-ray1.87A30-482[»]
ProteinModelPortaliQ01532.
SMRiQ01532. Positions 30-482.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ01532.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase C1 family.PROSITE-ProRule annotation

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG3579.
HOGENOMiHOG000064089.
InParanoidiQ01532.
KOiK01372.
OMAiNIFFNHI.
OrthoDBiEOG7X0VS5.

Family and domain databases

InterProiIPR000169. Pept_cys_AS.
IPR025660. Pept_his_AS.
IPR004134. Peptidase_C1B.
[Graphical view]
PANTHERiPTHR10363. PTHR10363. 1 hit.
PfamiPF03051. Peptidase_C1_2. 1 hit.
[Graphical view]
PIRSFiPIRSF005700. PepC. 1 hit.
PROSITEiPS00139. THIOL_PROTEASE_CYS. 1 hit.
PS00639. THIOL_PROTEASE_HIS. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative initiation. Align

Isoform Mitochondrial (identifier: Q01532-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MLPTSVSRSL YLKTFRSHLL RAPQIVLKRM SSSIDISKIN SWNKEFQSDL
60 70 80 90 100
THQLATTVLK NYNADDALLN KTRLQKQDNR VFNTVVSTDS TPVTNQKSSG
110 120 130 140 150
RCWLFAATNQ LRLNVLSELN LKEFELSQAY LFFYDKLEKA NYFLDQIVSS
160 170 180 190 200
ADQDIDSRLV QYLLAAPTED GGQYSMFLNL VKKYGLIPKD LYGDLPYSTT
210 220 230 240 250
ASRKWNSLLT TKLREFAETL RTALKERSAD DSIIVTLREQ MQREIFRLMS
260 270 280 290 300
LFMDIPPVQP NEQFTWEYVD KDKKIHTIKS TPLEFASKYA KLDPSTPVSL
310 320 330 340 350
INDPRHPYGK LIKIDRLGNV LGGDAVIYLN VDNETLSKLV VKRLQNNKAV
360 370 380 390 400
FFGSHTPKFM DKKTGVMDIE LWNYPAIGYN LPQQKASRIR YHESLMTHAM
410 420 430 440 450
LITGCHVDET SKLPLRYRVE NSWGKDSGKD GLYVMTQKYF EEYCFQIVVD
460 470 480
INELPKELAS KFTSGKEEPI VLPIWDPMGA LAK
Length:483
Mass (Da):55,483
Last modified:June 26, 2007 - v3
Checksum:iBF92A6049F98DD3D
GO
Isoform Cytoplasmic (identifier: Q01532-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-29: Missing.

Note: Produced by alternative initiation at Met-30 of isoform Mitochondrial.

Show »
Length:454
Mass (Da):52,089
Checksum:i2F4B6236AEE3BABF
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti187 – 1871I → M in CAA48878. (PubMed:8424954)Curated

Mass spectrometryi

Molecular mass is 51830 Da from positions 31 - 482. Determined by ESI. 1 Publication

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 2929Missing in isoform Cytoplasmic. CuratedVSP_026453Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M97910 Genomic DNA. Translation: AAA35231.1.
X69124 Genomic DNA. Translation: CAA48878.1.
X68228 Genomic DNA. Translation: CAA48309.1.
Z71515 Genomic DNA. Translation: CAA96144.1.
Z69381 Genomic DNA. Translation: CAA93359.1.
U74299 Genomic DNA. Translation: AAB18260.1.
BK006947 Genomic DNA. Translation: DAA10320.1.
PIRiA46093. S25606.
RefSeqiNP_014160.2. NM_001183077.1. [Q01532-2]

Genome annotation databases

GeneIDi855482.
KEGGisce:YNL239W.

Keywords - Coding sequence diversityi

Alternative initiation

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M97910 Genomic DNA. Translation: AAA35231.1 .
X69124 Genomic DNA. Translation: CAA48878.1 .
X68228 Genomic DNA. Translation: CAA48309.1 .
Z71515 Genomic DNA. Translation: CAA96144.1 .
Z69381 Genomic DNA. Translation: CAA93359.1 .
U74299 Genomic DNA. Translation: AAB18260.1 .
BK006947 Genomic DNA. Translation: DAA10320.1 .
PIRi A46093. S25606.
RefSeqi NP_014160.2. NM_001183077.1. [Q01532-2 ]

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1A6R X-ray 2.05 A 32-483 [» ]
1GCB X-ray 2.20 A 30-483 [» ]
2DZY X-ray 2.57 A 30-482 [» ]
2DZZ X-ray 2.15 A 30-482 [» ]
2E00 X-ray 2.00 A 30-482 [» ]
2E01 X-ray 1.73 A 30-482 [» ]
2E02 X-ray 2.20 A 30-482 [» ]
2E03 X-ray 2.13 A 30-482 [» ]
3GCB X-ray 1.87 A 30-482 [» ]
ProteinModelPortali Q01532.
SMRi Q01532. Positions 30-482.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 35600. 17 interactions.
DIPi DIP-2941N.
IntActi Q01532. 11 interactions.
MINTi MINT-513897.
STRINGi 4932.YNL239W.

Protein family/group databases

MEROPSi C01.085.

Proteomic databases

MaxQBi Q01532.
PaxDbi Q01532.
PeptideAtlasi Q01532.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 855482.
KEGGi sce:YNL239W.

Organism-specific databases

CYGDi YNL239w.
SGDi S000005183. LAP3.

Phylogenomic databases

eggNOGi COG3579.
HOGENOMi HOG000064089.
InParanoidi Q01532.
KOi K01372.
OMAi NIFFNHI.
OrthoDBi EOG7X0VS5.

Enzyme and pathway databases

BioCyci YEAST:G3O-33237-MONOMER.
BRENDAi 3.4.22.40. 984.
Reactomei REACT_189060. Antigen processing: Ubiquitination & Proteasome degradation.
SABIO-RK Q01532.

Miscellaneous databases

EvolutionaryTracei Q01532.
NextBioi 979451.
PROi Q01532.

Gene expression databases

Genevestigatori Q01532.

Family and domain databases

InterProi IPR000169. Pept_cys_AS.
IPR025660. Pept_his_AS.
IPR004134. Peptidase_C1B.
[Graphical view ]
PANTHERi PTHR10363. PTHR10363. 1 hit.
Pfami PF03051. Peptidase_C1_2. 1 hit.
[Graphical view ]
PIRSFi PIRSF005700. PepC. 1 hit.
PROSITEi PS00139. THIOL_PROTEASE_CYS. 1 hit.
PS00639. THIOL_PROTEASE_HIS. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and characterization of a cysteine proteinase from Saccharomyces cerevisiae."
    Kambouris N.G., Burke D.J., Creutz C.E.
    J. Biol. Chem. 267:21570-21576(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION.
  2. "A yeast gene (BLH1) encodes a polypeptide with high homology to vertebrate bleomycin hydrolase, a family member of thiol proteinases."
    Magdolen U., Mueller G., Magdolen V., Bandlow W.
    Biochim. Biophys. Acta 1171:299-303(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 228-250 AND 367-387.
  3. "BLH1 codes for a yeast thiol aminopeptidase, the equivalent of mammalian bleomycin hydrolase."
    Enenkel C., Wolf D.H.
    J. Biol. Chem. 268:7036-7043(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION.
  4. "The DNA sequence of cosmid 14-5 from chromosome XIV reveals 21 open reading frames including a novel gene encoding a globin-like domain."
    Pandolfo D., de Antoni A., Lanfranchi G., Valle G.
    Yeast 12:1071-1076(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  5. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its evolutionary implications."
    Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K., Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K., Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M., Beinhauer J.D., Boskovic J., Buitrago M.J.
    , Bussereau F., Coster F., Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F., Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C., Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A., Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H., Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L., Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R., Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D., Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A., Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C., Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F., Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G., Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M., Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.
    Nature 387:93-98(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  6. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  7. "The cysteine-peptidase bleomycin hydrolase is a member of the galactose regulon in yeast."
    Zheng W., Xu H.E., Johnston S.A.
    J. Biol. Chem. 272:30350-30355(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-58, MASS SPECTROMETRY, MUTAGENESIS OF CYS-102 AND 271-LYS--LYS-274.
  8. "Calcium-dependent secretory vesicle-binding and lipid-binding proteins of Saccharomyces cerevisiae."
    Creutz C.E., Snyder S.L., Kambouris N.G.
    Yeast 7:229-244(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 228-251 AND 367-387.
  9. "Crystal structure of a conserved protease that binds DNA: the bleomycin hydrolase, Gal6."
    Joshua-Tor L., Xu H.E., Johnston S.A., Rees D.C.
    Science 269:945-950(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF C-TERMINUS, X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 30-483, SUBUNIT.
  10. "Yeast bleomycin hydrolase is a DNA-binding cysteine protease. Identification, purification, biochemical characterization."
    Xu H.E., Johnston S.A.
    J. Biol. Chem. 269:21177-21183(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: DNA-BINDING, BIOPHYSICOCHEMICAL PROPERTIES.
  11. "The nucleic acid binding activity of bleomycin hydrolase is involved in bleomycin detoxification."
    Zheng W., Johnston S.A.
    Mol. Cell. Biol. 18:3580-3585(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: DNA-BINDING, SUBCELLULAR LOCATION.
  12. "Cellular resistance to bleomycin in Saccharomyces cerevisiae is not affected by changes in bleomycin hydrolase levels."
    Wang H., Ramotar D.
    Biochem. Cell Biol. 80:789-796(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  13. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  14. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  15. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    Strain: ATCC 76625 / YPH499.
  16. "Protective mechanisms against homocysteine toxicity: the role of bleomycin hydrolase."
    Zimny J., Sikora M., Guranowski A., Jakubowski H.
    J. Biol. Chem. 281:22485-22492(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF HIS-398.
  17. "A large-scale full-length cDNA analysis to explore the budding yeast transcriptome."
    Miura F., Kawaguchi N., Sese J., Toyoda A., Hattori M., Morishita S., Ito T.
    Proc. Natl. Acad. Sci. U.S.A. 103:17846-17851(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: ALTERNATIVE INITIATION.
  18. "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].
  19. "The unusual active site of Gal6/bleomycin hydrolase can act as a carboxypeptidase, aminopeptidase, and peptide ligase."
    Zheng W., Johnston S.A., Joshua-Tor L.
    Cell 93:103-109(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.87 ANGSTROMS) OF 30-483 OF MUTANT ALA-102, MUTAGENESIS OF GLY-479.

Entry informationi

Entry nameiBLH1_YEAST
AccessioniPrimary (citable) accession number: Q01532
Secondary accession number(s): D6W0V4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: June 26, 2007
Last modified: October 29, 2014
This is version 149 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 521 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 XIV
    Yeast (Saccharomyces cerevisiae) chromosome XIV: entries and gene names

External Data

Dasty 3