Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(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)

Q01532

- BLH1_YEAST

UniProt

Q01532 - BLH1_YEAST

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
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 148 (01 Oct 2014)
      Sequence version 3 (26 Jun 2007)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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

    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-SubCell

    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.
    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. 16 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.
    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

    MLPTSVSRSL YLKTFRSHLL RAPQIVLKRM SSSIDISKIN SWNKEFQSDL    50
    THQLATTVLK NYNADDALLN KTRLQKQDNR VFNTVVSTDS TPVTNQKSSG 100
    RCWLFAATNQ LRLNVLSELN LKEFELSQAY LFFYDKLEKA NYFLDQIVSS 150
    ADQDIDSRLV QYLLAAPTED GGQYSMFLNL VKKYGLIPKD LYGDLPYSTT 200
    ASRKWNSLLT TKLREFAETL RTALKERSAD DSIIVTLREQ MQREIFRLMS 250
    LFMDIPPVQP NEQFTWEYVD KDKKIHTIKS TPLEFASKYA KLDPSTPVSL 300
    INDPRHPYGK LIKIDRLGNV LGGDAVIYLN VDNETLSKLV VKRLQNNKAV 350
    FFGSHTPKFM DKKTGVMDIE LWNYPAIGYN LPQQKASRIR YHESLMTHAM 400
    LITGCHVDET SKLPLRYRVE NSWGKDSGKD GLYVMTQKYF EEYCFQIVVD 450
    INELPKELAS KFTSGKEEPI VLPIWDPMGA LAK 483
    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. 16 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.
    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

    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 1, 2014
    This is version 148 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