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Protein

Carboxypeptidase Y

Gene

PRC1

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

Involved in degradation of small peptides. Digests preferentially peptides containing an aliphatic or hydrophobic residue in P1' position, as well as methionine, leucine or phenylalanine in P1 position of ester substrate.1 Publication

Miscellaneous

Present with 44000 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

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Inhibited by ZPCK.

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

kcat is 4900 min(-1) with furylacryloyl-Phe-Leu-OH as substrate.1 Publication
  1. KM=0.021 mM for furylacryloyl-Phe-Leu-OH1 Publication

    pH dependencei

    Optimum pH is 6.5. Active from pH 4.5 to pH 8.5.1 Publication

    Temperature dependencei

    Optimum temperature is 30 degrees Celsius.1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Function’ 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 sitei2572 Publications1
    Active sitei4491 Publication1
    <p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei452Substrate1 Publication1
    Active sitei5081 Publication1 Publication1
    Binding sitei509Substrate1 Publication1

    <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

    • serine-type carboxypeptidase activity Source: SGD

    GO - Biological processi

    • macroautophagy Source: SGD
    • phytochelatin biosynthetic process Source: SGD
    • protein catabolic process in the vacuole Source: SGD
    • proteolysis involved in cellular protein catabolic process Source: GO_Central
    • zymogen activation Source: SGD

    <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 functionCarboxypeptidase, Hydrolase, Protease

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    MetaCyc:YMR297W-MONOMER
    YEAST:YMR297W-MONOMER

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    3.4.16.5 984

    Reactome - a knowledgebase of biological pathways and processes

    More...
    Reactomei
    R-SCE-2132295 MHC class II antigen presentation
    R-SCE-6798695 Neutrophil degranulation

    Protein family/group databases

    ESTHER database of the Alpha/Beta-hydrolase fold superfamily of proteins

    More...
    ESTHERi
    yeast-cbpy1 Carboxypeptidase_S10

    MEROPS protease database

    More...
    MEROPSi
    S10.001

    <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:
    Carboxypeptidase Y1 Publication (EC:3.4.16.51 Publication)
    Short name:
    CPD-Y1 Publication
    Short name:
    cpY
    Alternative name(s):
    Carboxypeptidase YSCY
    <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:PRC11 Publication
    Ordered Locus Names:YMR297WImported
    <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 XIII

    Organism-specific databases

    Saccharomyces Genome Database

    More...
    SGDi
    S000004912 PRC1

    <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; Source: COMPARTMENTS

    Keywords - Cellular componenti

    Vacuole

    <p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi508H → A or R: Inactivates enzyme. 1 Publication1

    Protein family/group databases

    Allergome; a platform for allergen knowledge

    More...
    Allergomei
    8267 Sac c Carboxypeptidase Y

    <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 – 20Sequence analysisAdd BLAST20
    <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_000000429321 – 111Mediates translocation across the endoplasmic reticulum, renders the enzyme inactive during transit, and targets the molecule to the vacuole1 Publication1 PublicationAdd BLAST91
    <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_0000004294112 – 532Carboxypeptidase YAdd BLAST421

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <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>Glycosylationi124N-linked (GlcNAc...) (high mannose) asparagine1 Publication1
    <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 bondi167 ↔ 4092 Publications
    Glycosylationi198N-linked (GlcNAc...) (high mannose) asparagine3 Publications1
    Glycosylationi279N-linked (GlcNAc...) (high mannose) asparagine3 Publications1
    Disulfide bondi304 ↔ 3182 Publications
    Disulfide bondi328 ↔ 3512 Publications
    Disulfide bondi335 ↔ 3442 Publications
    Disulfide bondi373 ↔ 3792 Publications
    Glycosylationi479N-linked (GlcNAc...) (high mannose) asparagine3 Publications1

    <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

    Enters the endoplasmic reticulum as an inactive zymogen and is modified by four N-linked core oligosaccharides, giving rise to a precursor known as P1 (67 kDa). As P1 transits through the Golgi, extension of its core oligosaccharides leads to the Golgi-modified P2 precursor (69 kDa). P2 is sorted away from secretory proteins at or beyond a late Golgi compartment and is subsequently delivered to the vacuole via a prevacuolar endosome-like compartment. Upon arrival in the vacuole, the N-terminal prosegment of P2 is cleaved by vacuolar proteases to yield the enzymatically active mature vacuolar form of CPY (61 kDa).1 Publication
    The four high mannose core N-glycans found in mature CPY are Man(11-15)GlcNAc2 at Asn-124, Man(8-12)GlcNAc2 at Asn-198, Man(9-14)GlcNAc2 at Asn-279 and phosphorylated Man(12-17)GlcNAc2 as well as Man(11-16)GlcNAc2 at Asn-479.1 Publication

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Zymogen

    Proteomic databases

    MaxQB - The MaxQuant DataBase

    More...
    MaxQBi
    P00729

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

    More...
    PaxDbi
    P00729

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P00729

    PTM databases

    iPTMnet integrated resource for PTMs in systems biology context

    More...
    iPTMneti
    P00729

    <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

    <p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGrid)

    More...
    BioGridi
    35477, 77 interactors

    Database of interacting proteins

    More...
    DIPi
    DIP-2394N

    Protein interaction database and analysis system

    More...
    IntActi
    P00729, 18 interactors

    Molecular INTeraction database

    More...
    MINTi
    P00729

    STRING: functional protein association networks

    More...
    STRINGi
    4932.YMR297W

    <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

    Secondary structure

    1532
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

    Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

    More...
    ProteinModelPortali
    P00729

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

    More...
    SMRi
    P00729

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    MobiDB: a database of protein disorder and mobility annotations

    More...
    MobiDBi
    Search...

    Miscellaneous databases

    Relative evolutionary importance of amino acids within a protein sequence

    More...
    EvolutionaryTracei
    P00729

    <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

    Motif

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi24 – 27Vacuolar targeting signal1 Publication4

    <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 S10 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    HOG000198296

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    P00729

    KEGG Orthology (KO)

    More...
    KOi
    K13289

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    TWSKTHN

    Database of Orthologous Groups

    More...
    OrthoDBi
    EOG092C1EU7

    Family and domain databases

    Gene3D Structural and Functional Annotation of Protein Families

    More...
    Gene3Di
    3.40.50.1820, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR029058 AB_hydrolase
    IPR001563 Peptidase_S10
    IPR008442 Propeptide_carboxypepY
    IPR033124 Ser_caboxypep_his_AS
    IPR018202 Ser_caboxypep_ser_AS

    The PANTHER Classification System

    More...
    PANTHERi
    PTHR11802 PTHR11802, 1 hit

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF05388 Carbpep_Y_N, 1 hit
    PF00450 Peptidase_S10, 1 hit

    Protein Motif fingerprint database; a protein domain database

    More...
    PRINTSi
    PR00724 CRBOXYPTASEC

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF53474 SSF53474, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS00560 CARBOXYPEPT_SER_HIS, 1 hit
    PS00131 CARBOXYPEPT_SER_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>.<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.

    P00729-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MKAFTSLLCG LGLSTTLAKA ISLQRPLGLD KDVLLQAAEK FGLDLDLDHL
    60 70 80 90 100
    LKELDSNVLD AWAQIEHLYP NQVMSLETST KPKFPEAIKT KKDWDFVVKN
    110 120 130 140 150
    DAIENYQLRV NKIKDPKILG IDPNVTQYTG YLDVEDEDKH FFFWTFESRN
    160 170 180 190 200
    DPAKDPVILW LNGGPGCSSL TGLFFELGPS SIGPDLKPIG NPYSWNSNAT
    210 220 230 240 250
    VIFLDQPVNV GFSYSGSSGV SNTVAAGKDV YNFLELFFDQ FPEYVNKGQD
    260 270 280 290 300
    FHIAGESYAG HYIPVFASEI LSHKDRNFNL TSVLIGNGLT DPLTQYNYYE
    310 320 330 340 350
    PMACGEGGEP SVLPSEECSA MEDSLERCLG LIESCYDSQS VWSCVPATIY
    360 370 380 390 400
    CNNAQLAPYQ RTGRNVYDIR KDCEGGNLCY PTLQDIDDYL NQDYVKEAVG
    410 420 430 440 450
    AEVDHYESCN FDINRNFLFA GDWMKPYHTA VTDLLNQDLP ILVYAGDKDF
    460 470 480 490 500
    ICNWLGNKAW TDVLPWKYDE EFASQKVRNW TASITDEVAG EVKSYKHFTY
    510 520 530
    LRVFNGGHMV PFDVPENALS MVNEWIHGGF SL
    Length:532
    Mass (Da):59,802
    Last modified:November 1, 1988 - 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:i7227F3489CBDD952
    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 conflicti260 – 261GH → HG AA sequence (Ref. 4) Curated2
    Sequence conflicti389Y → E AA sequence (Ref. 4) Curated1
    Sequence conflicti529G → D AA sequence (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
    M15482 Genomic DNA Translation: AAA34902.1
    X80836 Genomic DNA Translation: CAA56806.1
    BK006946 Genomic DNA Translation: DAA10198.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    A26597 CPBYY

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_014026.1, NM_001182806.1

    Genome annotation databases

    Ensembl fungal genome annotation project

    More...
    EnsemblFungii
    YMR297W_mRNA; YMR297W_mRNA; YMR297W

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    855343

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    sce:YMR297W

    <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

    <p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

    Worthington enzyme manual

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M15482 Genomic DNA Translation: AAA34902.1
    X80836 Genomic DNA Translation: CAA56806.1
    BK006946 Genomic DNA Translation: DAA10198.1
    PIRiA26597 CPBYY
    RefSeqiNP_014026.1, NM_001182806.1

    3D structure databases

    Select the link destinations:

    Protein Data Bank Europe

    More...
    PDBei

    Protein Data Bank RCSB

    More...
    RCSB PDBi

    Protein Data Bank Japan

    More...
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1CPYX-ray2.60A112-532[»]
    1WPXX-ray2.70A112-532[»]
    1YSCX-ray2.80A112-532[»]
    ProteinModelPortaliP00729
    SMRiP00729
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi35477, 77 interactors
    DIPiDIP-2394N
    IntActiP00729, 18 interactors
    MINTiP00729
    STRINGi4932.YMR297W

    Protein family/group databases

    Allergomei8267 Sac c Carboxypeptidase Y
    ESTHERiyeast-cbpy1 Carboxypeptidase_S10
    MEROPSiS10.001

    PTM databases

    iPTMnetiP00729

    Proteomic databases

    MaxQBiP00729
    PaxDbiP00729
    PRIDEiP00729

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblFungiiYMR297W_mRNA; YMR297W_mRNA; YMR297W
    GeneIDi855343
    KEGGisce:YMR297W

    Organism-specific databases

    SGDiS000004912 PRC1

    Phylogenomic databases

    HOGENOMiHOG000198296
    InParanoidiP00729
    KOiK13289
    OMAiTWSKTHN
    OrthoDBiEOG092C1EU7

    Enzyme and pathway databases

    BioCyciMetaCyc:YMR297W-MONOMER
    YEAST:YMR297W-MONOMER
    BRENDAi3.4.16.5 984
    ReactomeiR-SCE-2132295 MHC class II antigen presentation
    R-SCE-6798695 Neutrophil degranulation

    Miscellaneous databases

    EvolutionaryTraceiP00729

    Protein Ontology

    More...
    PROi
    PR:P00729

    Family and domain databases

    Gene3Di3.40.50.1820, 1 hit
    InterProiView protein in InterPro
    IPR029058 AB_hydrolase
    IPR001563 Peptidase_S10
    IPR008442 Propeptide_carboxypepY
    IPR033124 Ser_caboxypep_his_AS
    IPR018202 Ser_caboxypep_ser_AS
    PANTHERiPTHR11802 PTHR11802, 1 hit
    PfamiView protein in Pfam
    PF05388 Carbpep_Y_N, 1 hit
    PF00450 Peptidase_S10, 1 hit
    PRINTSiPR00724 CRBOXYPTASEC
    SUPFAMiSSF53474 SSF53474, 1 hit
    PROSITEiView protein in PROSITE
    PS00560 CARBOXYPEPT_SER_HIS, 1 hit
    PS00131 CARBOXYPEPT_SER_SER, 1 hit

    ProtoNet; Automatic hierarchical classification of proteins

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    ProtoNeti
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    <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 nameiCBPY_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: P00729
    Secondary accession number(s): D6W0C4
    <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 21, 1986
    Last sequence update: November 1, 1988
    Last modified: December 5, 2018
    This is version 202 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

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

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