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Protein

Carboxypeptidase S

Gene

CPS1

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

Necessary for use of certain peptides as sole nitrogen source. May also cleave intracellularly generated peptides to recycle amino acids for protein synthesis.

Miscellaneous

Present with 721 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

  • Release of a C-terminal amino acid from a peptide in which glycine is the penultimate amino acid, e.g. Z-Gly-|-Leu. EC:3.4.17.4

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Zn2+By similarityNote: Binds 2 Zn2+ ions per subunit.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi168Zinc 2By similarity1
<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 sitei170By similarity1
Metal bindingi205Zinc 1By similarity1
Metal bindingi205Zinc 2By similarity1
Active sitei239Proton acceptorBy similarity1
Metal bindingi240Zinc 1By similarity1
Metal bindingi268Zinc 2By similarity1
Metal bindingi547Zinc 1By similarity1

<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

  • carboxypeptidase activity Source: SGD
  • metal ion binding Source: UniProtKB-KW
  • metallocarboxypeptidase activity Source: InterPro

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 functionCarboxypeptidase, Hydrolase, Protease
LigandMetal-binding, Zinc

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
MetaCyc:YJL172W-MONOMER
YEAST:YJL172W-MONOMER

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-SCE-5423646 Aflatoxin activation and detoxification

Protein family/group databases

MEROPS protease database

More...
MEROPSi
M20.002

<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 S (EC:3.4.17.4)
Alternative name(s):
GLY-X carboxypeptidase
YSCS
<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:CPS1
Synonyms:CPS
Ordered Locus Names:YJL172W
ORF Names:J0510
<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 X

Organism-specific databases

Saccharomyces Genome Database

More...
SGDi
S000003708 CPS1

<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

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini1 – 19CytoplasmicSequence analysisAdd BLAST19
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei20 – 40HelicalSequence analysisAdd BLAST21
Topological domaini41 – 576LumenalSequence analysisAdd BLAST536

Keywords - Cellular componenti

Membrane, 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 describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001852711 – 576Carboxypeptidase SAdd BLAST576

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 describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki8Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
<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>Glycosylationi88N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi176N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi228N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi381N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi525N-linked (GlcNAc...) asparagineSequence analysis1

<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

Glycosylated.
Ubiquitinated. Ubiquitination mediates sorting into internal vesicles in late endosomes. TUL1 is required for ubiquitination.1 Publication

Keywords - PTMi

Glycoprotein, Isopeptide bond, Ubl conjugation

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P27614

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

More...
PaxDbi
P27614

PRoteomics IDEntifications database

More...
PRIDEi
P27614

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P27614

<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">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

yscS is synthesized as one polypeptide chain precursor which after carbohydrate modification in the secretory pathway yields two active precursor molecules. The proteolytically unprocessed forms are associated with the membrane, whereas the mature forms of the enzyme are soluble.

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
33588, 64 interactors

Database of interacting proteins

More...
DIPi
DIP-5566N

Protein interaction database and analysis system

More...
IntActi
P27614, 4 interactors

Molecular INTeraction database

More...
MINTi
P27614

STRING: functional protein association networks

More...
STRINGi
4932.YJL172W

<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

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
P27614

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

More...
SMRi
P27614

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
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

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The transmembrane domain contains polar residues that mediate the recognition by TUL1.

<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 M20A family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000194592

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P27614

KEGG Orthology (KO)

More...
KOi
K01293

Identification of Orthologs from Complete Genome Data

More...
OMAi
PGICIGN

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR001261 ArgE/DapE_CS
IPR036264 Bact_exopeptidase_dim_dom
IPR017141 Pept_M20_carboxypep
IPR002933 Peptidase_M20
IPR011650 Peptidase_M20_dimer

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF07687 M20_dimer, 1 hit
PF01546 Peptidase_M20, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF037217 Carboxypeptidase_S, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF55031 SSF55031, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00758 ARGE_DAPE_CPG2_1, 1 hit
PS00759 ARGE_DAPE_CPG2_2, 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.

P27614-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MIALPVEKAP RKSLWQRHRA FISGIVALII IGTFFLTSGL HPAPPHEAKR
60 70 80 90 100
PHHGKGPMHS PKCEKIEPLS PSFKHSVDTI LHDPAFRNSS IEKLSNAVRI
110 120 130 140 150
PTVVQDKNPN PADDPDFYKH FYELHDYFEK TFPNIHKHLK LEKVNELGLL
160 170 180 190 200
YTWEGSDPDL KPLLLMAHQD VVPVNNETLS SWKFPPFSGH YDPETDFVWG
210 220 230 240 250
RGSNDCKNLL IAEFEAIEQL LIDGFKPNRT IVMSLGFDEE ASGTLGAASL
260 270 280 290 300
ASFLHERYGD DGIYSIIDEG EGIMEVDKDV FVATPINAEK GYVDFEVSIL
310 320 330 340 350
GHGGHSSVPP DHTTIGIASE LITEFEANPF DYEFEFDNPI YGLLTCAAEH
360 370 380 390 400
SKSLSKDVKK TILGAPFCPR RKDKLVEYIS NQSHLRSLIR TTQAVDIING
410 420 430 440 450
GVKANALPET TRFLINHRIN LHSSVAEVFE RNIEYAKKIA EKYGYGLSKN
460 470 480 490 500
GDDYIIPETE LGHIDITLLR ELEPAPLSPS SGPVWDILAG TIQDVFENGV
510 520 530 540 550
LQNNEEFYVT TGLFSGNTDT KYYWNLSKNI YRFVGSIIDI DLLKTLHSVN
560 570
EHVDVPGHLS AIAFVYEYIV NVNEYA
Length:576
Mass (Da):64,597
Last modified:November 1, 1995 - v2
<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:i5CBB536D421B5F70
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 conflicti387S → T in CAA40571 (PubMed:1709881).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
X57316 Genomic DNA Translation: CAA40571.1
X63068 Genomic DNA Translation: CAA44790.1
Z49447 Genomic DNA Translation: CAA89467.1
BK006943 Genomic DNA Translation: DAA08632.1

Protein sequence database of the Protein Information Resource

More...
PIRi
S16693

NCBI Reference Sequences

More...
RefSeqi
NP_012363.1, NM_001181605.1

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
YJL172W_mRNA; YJL172W_mRNA; YJL172W

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
853267

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
sce:YJL172W

<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
X57316 Genomic DNA Translation: CAA40571.1
X63068 Genomic DNA Translation: CAA44790.1
Z49447 Genomic DNA Translation: CAA89467.1
BK006943 Genomic DNA Translation: DAA08632.1
PIRiS16693
RefSeqiNP_012363.1, NM_001181605.1

3D structure databases

ProteinModelPortaliP27614
SMRiP27614
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33588, 64 interactors
DIPiDIP-5566N
IntActiP27614, 4 interactors
MINTiP27614
STRINGi4932.YJL172W

Protein family/group databases

MEROPSiM20.002

PTM databases

iPTMnetiP27614

Proteomic databases

MaxQBiP27614
PaxDbiP27614
PRIDEiP27614

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYJL172W_mRNA; YJL172W_mRNA; YJL172W
GeneIDi853267
KEGGisce:YJL172W

Organism-specific databases

SGDiS000003708 CPS1

Phylogenomic databases

HOGENOMiHOG000194592
InParanoidiP27614
KOiK01293
OMAiPGICIGN

Enzyme and pathway databases

BioCyciMetaCyc:YJL172W-MONOMER
YEAST:YJL172W-MONOMER
ReactomeiR-SCE-5423646 Aflatoxin activation and detoxification

Miscellaneous databases

Protein Ontology

More...
PROi
PR:P27614

Family and domain databases

InterProiView protein in InterPro
IPR001261 ArgE/DapE_CS
IPR036264 Bact_exopeptidase_dim_dom
IPR017141 Pept_M20_carboxypep
IPR002933 Peptidase_M20
IPR011650 Peptidase_M20_dimer
PfamiView protein in Pfam
PF07687 M20_dimer, 1 hit
PF01546 Peptidase_M20, 1 hit
PIRSFiPIRSF037217 Carboxypeptidase_S, 1 hit
SUPFAMiSSF55031 SSF55031, 1 hit
PROSITEiView protein in PROSITE
PS00758 ARGE_DAPE_CPG2_1, 1 hit
PS00759 ARGE_DAPE_CPG2_2, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
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 nameiCBPS_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: P27614
Secondary accession number(s): D6VW16
<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: August 1, 1992
Last sequence update: November 1, 1995
Last modified: January 16, 2019
This is version 166 of the entry and version 2 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

Complete proteome, Reference proteome

Documents

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