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Entry version 194 (11 Dec 2019)
Sequence version 1 (01 Jul 1989)
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Protein

Cerevisin

Gene

PRB1

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

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Vacuolar proteinase B involved in protein degradation in the vacuole. Among other substrates, acts on carboxypeptidase Y (cpY/PRC1) to activate it by processing its Pro-peptide. Required for meiosis and spore formation, and for optimal survival in stationary phase.2 Publications

Miscellaneous

[beta] is the prion form of PrB. In contrast to other prions, [beta] is not the result of a conformational change of the cellular PrB, but distinguishes itself by autoactivation in trans. Usually, PrB is already involved in its own maturatiuon, but PrA plays a critical role. PrpA mutants lack PrB. However, in growth conditions that favor PRB1 expression, PrB activity persists in PrA mutants due to autocleavage of PrB in trans. This condition is stably transmitted to daughter cells in mitosis. [beta] can be cured by growing in PRB1-repressing conditions. Once a cell has lost PrB activity, it remains stably inactive. Thus, there are 2 alternative states, that are chromosomally identical, but phenotypically distinct. Since PrA is able to activate PrB, normal cells always carry the [beta] prion. Its absence and transmission are only observable in the absence of PrA.1 Publication
Present with 1600 molecules/cell in log phase SD medium.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

  • Hydrolysis of proteins with broad specificity, and of Bz-Arg-OEt > Ac-Tyr-OEt. Does not hydrolyze peptide amides. EC:3.4.21.48

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei325Charge relay systemPROSITE-ProRule annotation1
Active sitei357Charge relay systemPROSITE-ProRule annotation1
Active sitei519Charge relay systemPROSITE-ProRule annotation1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionHydrolase, Prion, Protease, Serine protease

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
YEAST:YEL060C-MONOMER

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
3.4.21.48 984

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-SCE-8866427 VLDLR internalisation and degradation
R-SCE-8964038 LDL clearance

Protein family/group databases

MEROPS protease database

More...
MEROPSi
S08.052

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Cerevisin (EC:3.4.21.48)
Alternative name(s):
Proteinase YSCB
Vacuolar protease B
Short name:
PrB
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:PRB1
Ordered Locus Names:YEL060C
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri559292 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000002311 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome V

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
FungiDB:YEL060C

Saccharomyces Genome Database

More...
SGDi
S000000786 PRB1

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Amyloid, Vacuole

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 19Sequence analysisAdd BLAST19
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes a propeptide, which is a part of a protein that is cleaved during maturation or activation. Once cleaved, a propeptide generally has no independent biological function.<p><a href='/help/propep' target='_top'>More...</a></p>PropeptideiPRO_000002713620 – 2801 PublicationAdd BLAST261
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_0000027137281 – ?574CerevisinAdd BLAST294
PropeptideiPRO_0000417567?575 – 635Add BLAST61

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi460 ↔ 491Sequence analysis
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi594N-linked (GlcNAc...) asparagineCurated1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Activated by N- and C-terminal proteolytic cleavage. Protease B (PrB/PRB1) processing requires at least 4 cleavages. First, the signal peptide is removed from the 76 kDa preproprotease B by signal peptidase in the ER. Then, PrB removes its own Pro-region (in trans) at the N-terminus, producing a 39 kDa form before exiting the ER. In the Golgi complex, the C-terminal Post-region of the 40 kDa proprotease B undergoes protease A (PrA/PEP4)-mediated processing to a 37 kDa intermediate, which in turn is quickly processed again by PrB in trans to yield the 31 kDa mature PrB.
Glycosylated. Preproprotease B is a 76 kDa unglycosylated precursor that enters the endoplasmic reticulum (ER), where it receives one Asn-linked and an undetermined number of non-Asn-linked carbohydrate side chains. In the Golgi complex, the 39 kDa form becomes 40 kDa, due to elaboration of the Asn-linked side chain. The ultimate processing step removes a peptide containing the Asn-linked chain. Mature PrB has only non-Asn-linked carbohydrates.

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P09232

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P09232

PRoteomics IDEntifications database

More...
PRIDEi
P09232

Consortium for Top Down Proteomics

More...
TopDownProteomicsi
P09232

2D gel databases

University College Dublin 2-DE Proteome Database

More...
UCD-2DPAGEi
P09232

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P09232

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Repressed by glucose.1 Publication

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
36669, 132 interactors

Database of interacting proteins

More...
DIPi
DIP-2544N

Protein interaction database and analysis system

More...
IntActi
P09232, 23 interactors

Molecular INTeraction database

More...
MINTi
P09232

STRING: functional protein association networks

More...
STRINGi
4932.YEL060C

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...
RNActi
P09232 protein

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
P09232

Database of comparative protein structure models

More...
ModBasei
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini182 – 278Inhibitor I9Sequence analysisAdd BLAST97
Domaini289 – 614Peptidase S8PROSITE-ProRule annotationAdd BLAST326

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi63 – 154Lys-richAdd BLAST92

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the peptidase S8 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000199176

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P09232

KEGG Orthology (KO)

More...
KOi
K01336

Identification of Orthologs from Complete Genome Data

More...
OMAi
WIGSKHA

Family and domain databases

Conserved Domains Database

More...
CDDi
cd04077 Peptidases_S8_PCSK9_ProteinaseK_like, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.30.70.80, 1 hit
3.40.50.200, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR034193 PCSK9_ProteinaseK-like
IPR000209 Peptidase_S8/S53_dom
IPR036852 Peptidase_S8/S53_dom_sf
IPR023827 Peptidase_S8_Asp-AS
IPR022398 Peptidase_S8_His-AS
IPR023828 Peptidase_S8_Ser-AS
IPR015500 Peptidase_S8_subtilisin-rel
IPR010259 S8pro/Inhibitor_I9
IPR037045 S8pro/Inhibitor_I9_sf

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF05922 Inhibitor_I9, 1 hit
PF00082 Peptidase_S8, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00723 SUBTILISIN

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF52743 SSF52743, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS51892 SUBTILASE, 1 hit
PS00136 SUBTILASE_ASP, 1 hit
PS00137 SUBTILASE_HIS, 1 hit
PS00138 SUBTILASE_SER, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

P09232-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MKLENTLFTL GALGSISAAL VIPNLENAAD HHELINKEDH HERPRKVEFT
60 70 80 90 100
KDDDEEPSDS EDKEHGKFHK KGRKGQDKES PEFNGKRASG SHGSAHEGGK
110 120 130 140 150
GMKPKHESSN DDDNDDKKKK PHHKGGCHEN KVEEKKMKGK KVKGKKHHEK
160 170 180 190 200
TLEKGRHHNR LAPLVSTAQF NPDAISKIIP NRYIIVFKRG APQEEIDFHK
210 220 230 240 250
ENVQQAQLQS VENLSAEDAF FISTKDTSLS TSEAGGIQDS FNIDNLFSGY
260 270 280 290 300
IGYFTQEIVD LIRQNPLVDF VERDSIVEAT EFDTQNSAPW GLARISHRER
310 320 330 340 350
LNLGSFNKYL YDDDAGRGVT SYVIDTGVNI NHKDFEKRAI WGKTIPLNDE
360 370 380 390 400
DLDGNGHGTH CAGTIASKHY GVAKNANVVA VKVLRSNGSG TMSDVVKGVE
410 420 430 440 450
YAAKAHQKEA QEKKKGFKGS TANMSLGGGK SPALDLAVNA AVEVGIHFAV
460 470 480 490 500
AAGNENQDAC NTSPASADKA ITVGASTLSD DRAYFSNWGK CVDVFAPGLN
510 520 530 540 550
ILSTYIGSDD ATATLSGTSM ASPHVAGLLT YFLSLQPGSD SEFFELGQDS
560 570 580 590 600
LTPQQLKKKL IHYSTKDILF DIPEDTPNVL IYNGGGQDLS AFWNDTKKSH
610 620 630
SSGFKQELNM DEFIGSKTDL IFDQVRDILD KLNII
Length:635
Mass (Da):69,621
Last modified:July 1, 1989 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iC346C2B1C7DDDC48
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti622F → K in CAA77886 (Ref. 4) Curated1
Sequence conflicti622F → K in AAA34495 (Ref. 4) Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
M18097 Genomic DNA Translation: AAA34901.1
U18795 Genomic DNA Translation: AAB65027.1
Z11859 Genomic DNA Translation: CAA77886.1
M90522 Genomic DNA Translation: AAA34495.1
BK006939 Genomic DNA Translation: DAA07594.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A29358

NCBI Reference Sequences

More...
RefSeqi
NP_010854.1, NM_001178875.1

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
YEL060C_mRNA; YEL060C; YEL060C

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
856649

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
sce:YEL060C

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M18097 Genomic DNA Translation: AAA34901.1
U18795 Genomic DNA Translation: AAB65027.1
Z11859 Genomic DNA Translation: CAA77886.1
M90522 Genomic DNA Translation: AAA34495.1
BK006939 Genomic DNA Translation: DAA07594.1
PIRiA29358
RefSeqiNP_010854.1, NM_001178875.1

3D structure databases

SMRiP09232
ModBaseiSearch...

Protein-protein interaction databases

BioGridi36669, 132 interactors
DIPiDIP-2544N
IntActiP09232, 23 interactors
MINTiP09232
STRINGi4932.YEL060C

Protein family/group databases

MEROPSiS08.052

PTM databases

iPTMnetiP09232

2D gel databases

UCD-2DPAGEiP09232

Proteomic databases

MaxQBiP09232
PaxDbiP09232
PRIDEiP09232
TopDownProteomicsiP09232

Genome annotation databases

EnsemblFungiiYEL060C_mRNA; YEL060C; YEL060C
GeneIDi856649
KEGGisce:YEL060C

Organism-specific databases

EuPathDBiFungiDB:YEL060C
SGDiS000000786 PRB1

Phylogenomic databases

HOGENOMiHOG000199176
InParanoidiP09232
KOiK01336
OMAiWIGSKHA

Enzyme and pathway databases

BioCyciYEAST:YEL060C-MONOMER
BRENDAi3.4.21.48 984
ReactomeiR-SCE-8866427 VLDLR internalisation and degradation
R-SCE-8964038 LDL clearance

Miscellaneous databases

Protein Ontology

More...
PROi
PR:P09232
RNActiP09232 protein

Family and domain databases

CDDicd04077 Peptidases_S8_PCSK9_ProteinaseK_like, 1 hit
Gene3Di3.30.70.80, 1 hit
3.40.50.200, 1 hit
InterProiView protein in InterPro
IPR034193 PCSK9_ProteinaseK-like
IPR000209 Peptidase_S8/S53_dom
IPR036852 Peptidase_S8/S53_dom_sf
IPR023827 Peptidase_S8_Asp-AS
IPR022398 Peptidase_S8_His-AS
IPR023828 Peptidase_S8_Ser-AS
IPR015500 Peptidase_S8_subtilisin-rel
IPR010259 S8pro/Inhibitor_I9
IPR037045 S8pro/Inhibitor_I9_sf
PfamiView protein in Pfam
PF05922 Inhibitor_I9, 1 hit
PF00082 Peptidase_S8, 1 hit
PRINTSiPR00723 SUBTILISIN
SUPFAMiSSF52743 SSF52743, 1 hit
PROSITEiView protein in PROSITE
PS51892 SUBTILASE, 1 hit
PS00136 SUBTILASE_ASP, 1 hit
PS00137 SUBTILASE_HIS, 1 hit
PS00138 SUBTILASE_SER, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiPRTB_YEAST
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P09232
Secondary accession number(s): D3DLJ0
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: December 11, 2019
This is version 194 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome V
    Yeast (Saccharomyces cerevisiae) chromosome V: entries and gene names
  4. Peptidase families
    Classification of peptidase families and list of entries
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