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Entry version 187 (11 Dec 2019)
Sequence version 2 (01 Feb 1994)
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Protein

Vacuolar aminopeptidase 1

Gene

APE1

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

Resident vacuolar enzyme that catalyzes the removal of amino acids from the N-terminus of peptides and proteins. Also acts as the major cargo protein of the cytoplasm-to-vacuole targeting (Cvt) pathway. The precursor form of aminopeptidase 1 (prApe1) assembles into dodecamers and the propeptide mediates the aggregation of dodecamers into higher multimers. The multimers are then recognized via the propeptide by their receptor ATG19, and ATG19 further interacts with ATG11, which tethers the APE1-ATG19 complex to the pre-autophagosomal structure (PAS). The cargo-receptor complex (also Cvt complex) is selectively enwrapped by a double-membrane structure termed the Cvt vesicle under vegetative growth conditions and by a similar but larger double-membrane structure termed the autophagosome under nitrogen starvation conditions. The Cvt vesicle or the autophagosome fuses with the vacuolar membrane and release its content in the vacuolar lumen. In the vacuole, prApe1 is processed into mature aminopeptidase 1 (mApe1).8 Publications

Miscellaneous

Present with 5730 molecules/cell in log phase SD medium.1 Publication

Caution

It is unsure whether this protein is glycosylated or not. PubMed:5147 has shown that a preparation of aminopeptidase 1 contains about 12% of conjugated carbohydrate, while PubMed:1400574 could not identify any glycosylation, which is in agreement with the fact that aminopeptidase 1 does not transit through the secretory pathway.2 Publications

<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 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 similarity5 PublicationsNote: Binds 2 Zn2+ ions per subunit. The average amount of Zn2+ bound at physiological metal concentrations will be lower than stoichiometric.By similarity5 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> 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

Strongly and specifically activated by Cl- and Br-, which act as positive allosteric effectors. Inactivated by metal-chelating agents.3 Publications

<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>pH dependencei

Optimum pH is 7-8.5.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> 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 bindingi132Zinc 1By similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> 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 sitei210SubstrateBy similarity1
Metal bindingi303Zinc 1By similarity1
Metal bindingi303Zinc 2By similarity1
Binding sitei339SubstrateBy similarity1
Metal bindingi340Zinc 2By similarity1
Metal bindingi385Zinc 1By similarity1
Binding sitei385SubstrateBy similarity1
Binding sitei388SubstrateBy similarity1
Metal bindingi479Zinc 2By 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

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 functionAminopeptidase, Hydrolase, Metalloprotease, Protease
Biological processProtein transport, Transport
LigandMetal-binding, Zinc

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
YEAST:YKL103C-MONOMER

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
3.4.11.22 984

Protein family/group databases

MEROPS protease database

More...
MEROPSi
M18.001

<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:
Vacuolar aminopeptidase 11 Publication (EC:3.4.11.225 Publications)
Alternative name(s):
Aminopeptidase yscI1 Publication
Leucine aminopeptidase IV1 Publication
Short name:
LAPIV1 Publication
Lysosomal aminopeptidase III1 Publication
Polypeptidase1 Publication
Vacuolar aminopeptidase I1 Publication
<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:APE11 Publication
Synonyms:API1 Publication, LAP41 Publication, YSC11 Publication
Ordered Locus Names:YKL103CImported
ORF Names:YKL455
<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 XI

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
FungiDB:YKL103C

Saccharomyces Genome Database

More...
SGDi
S000001586 APE1

<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

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

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL1741175

<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 <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_00000268061 – 45Required for vacuolar localization. Mediates aggregation and vesicle formation in Cvt pathway3 PublicationsAdd BLAST45
<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_000002680746 – 514Vacuolar aminopeptidase 1Add BLAST469

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>Glycosylationi107N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Glycosylationi110N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei356PhosphoserineCombined sources1
Glycosylationi448N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1

<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

Synthesized in a precursor form (prApe1) that has an amino-terminal propeptide. The N-terminal extension of the 61 kDa precursor is proteolytically processed in two sequential steps. The first step involves proteinase A (PrA/PEP4) and produces a 55 kDa unstable intermediate (iAPI). The second step involves proteinase B (PrB/PRB1) and converts iAPI into the 50 kDa stable, mature enzyme (mApe1).1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei45 – 46Cleavage; by protease B (PrB/PRB1)1 Publication2

Keywords - PTMi

Glycoprotein, Phosphoprotein, Zymogen

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P14904

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

More...
PaxDbi
P14904

PRoteomics IDEntifications database

More...
PRIDEi
P14904

PTM databases

CarbonylDB database of protein carbonylation sites

More...
CarbonylDBi
P14904

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P14904

<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

Homododecamer. The precursor form of aminopeptidase 1 (prApe1) assembles into dodecamers and further aggregates into higher multimers (the Ape1 complex) in the cytoplasm. The Ape1 complex is disaggregated in the vacuolar lumen, but mature aminopeptidase 1 (mApe1) retains its dodecameric form. Dodecamer assembly in the cytoplasm is essential for formation of an enzymatically active complex. If cytoplasmic homododecamerization of prApe1 is disturbed in mutants, homododecamers of mApe1 will form in the vacuole, but they are enzymatically inactive.

Interacts with ATG19.

5 Publications

<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

Show more details

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
34031, 69 interactors

Database of interacting proteins

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DIPi
DIP-1409N

Protein interaction database and analysis system

More...
IntActi
P14904, 56 interactors

Molecular INTeraction database

More...
MINTi
P14904

STRING: functional protein association networks

More...
STRINGi
4932.YKL103C

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
P14904

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...
RNActi
P14904 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

Secondary structure

1514
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

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SMRi
P14904

Database of comparative protein structure models

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ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
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 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 M18 family.Curated

Phylogenomic databases

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000253244

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P14904

KEGG Orthology (KO)

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KOi
K01268

Identification of Orthologs from Complete Genome Data

More...
OMAi
WPIAKIP

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.30.250.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR001948 Peptidase_M18
IPR023358 Peptidase_M18_dom2

The PANTHER Classification System

More...
PANTHERi
PTHR28570 PTHR28570, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF02127 Peptidase_M18, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00932 AMINO1PTASE

<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.

P14904-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MEEQREILEQ LKKTLQMLTV EPSKNNQIAN EEKEKKENEN SWCILEHNYE
60 70 80 90 100
DIAQEFIDFI YKNPTTYHVV SFFAELLDKH NFKYLSEKSN WQDSIGEDGG
110 120 130 140 150
KFYTIRNGTN LSAFILGKNW RAEKGVGVIG SHVDALTVKL KPVSFKDTAE
160 170 180 190 200
GYGRIAVAPY GGTLNELWLD RDLGIGGRLL YKKKGTNEIK SALVDSTPLP
210 220 230 240 250
VCRIPSLAPH FGKPAEGPFD KEDQTIPVIG FPTPDEEGNE PPTDDEKKSP
260 270 280 290 300
LFGKHCIHLL RYVAKLAGVE VSELIQMDLD LFDVQKGTIG GIGKHFLFAP
310 320 330 340 350
RLDDRLCSFA AMIALICYAK DVNTEESDLF STVTLYDNEE IGSLTRQGAK
360 370 380 390 400
GGLLESVVER SSSAFTKKPV DLHTVWANSI ILSADVNHLY NPNFPEVYLK
410 420 430 440 450
NHFPVPNVGI TLSLDPNGHM ATDVVGTALV EELARRNGDK VQYFQIKNNS
460 470 480 490 500
RSGGTIGPSL ASQTGARTID LGIAQLSMHS IRAATGSKDV GLGVKFFNGF
510
FKHWRSVYDE FGEL
Length:514
Mass (Da):57,093
Last modified:February 1, 1994 - 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:i702A8C88A2124C24
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 conflicti233T → S in CAA68815 (PubMed:2689224).Curated1
Sequence conflicti323N → D in CAA68815 (PubMed:2689224).Curated1
Sequence conflicti328D → E in CAA68815 (PubMed:2689224).Curated1
Sequence conflicti369P → A in CAA68815 (PubMed:2689224).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
Y07522 Genomic DNA Translation: CAA68815.1
M25548 Genomic DNA Translation: AAA34738.1
X71133 Genomic DNA Translation: CAA50454.1
Z28103 Genomic DNA Translation: CAA81943.1
BK006944 Genomic DNA Translation: DAA09055.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A33879

NCBI Reference Sequences

More...
RefSeqi
NP_012819.1, NM_001179669.1

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
YKL103C_mRNA; YKL103C; YKL103C

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
853758

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
sce:YKL103C

<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
Y07522 Genomic DNA Translation: CAA68815.1
M25548 Genomic DNA Translation: AAA34738.1
X71133 Genomic DNA Translation: CAA50454.1
Z28103 Genomic DNA Translation: CAA81943.1
BK006944 Genomic DNA Translation: DAA09055.1
PIRiA33879
RefSeqiNP_012819.1, NM_001179669.1

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
4R8FX-ray2.50A/B/C/D46-514[»]
5JGEX-ray1.91C/F1-20[»]
5JGFX-ray1.83A/B/C/D46-514[»]
5JH9X-ray2.10A/B/C/D1-514[»]
5JHCX-ray3.40A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X/Y/Z/a/b/c/d1-22[»]
5JM9electron microscopy24.00A1-514[»]
SMRiP14904
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi34031, 69 interactors
DIPiDIP-1409N
IntActiP14904, 56 interactors
MINTiP14904
STRINGi4932.YKL103C

Chemistry databases

BindingDBiP14904
ChEMBLiCHEMBL1741175

Protein family/group databases

MEROPSiM18.001

PTM databases

CarbonylDBiP14904
iPTMnetiP14904

Proteomic databases

MaxQBiP14904
PaxDbiP14904
PRIDEiP14904

Genome annotation databases

EnsemblFungiiYKL103C_mRNA; YKL103C; YKL103C
GeneIDi853758
KEGGisce:YKL103C

Organism-specific databases

EuPathDBiFungiDB:YKL103C
SGDiS000001586 APE1

Phylogenomic databases

HOGENOMiHOG000253244
InParanoidiP14904
KOiK01268
OMAiWPIAKIP

Enzyme and pathway databases

BioCyciYEAST:YKL103C-MONOMER
BRENDAi3.4.11.22 984

Miscellaneous databases

Protein Ontology

More...
PROi
PR:P14904
RNActiP14904 protein

Family and domain databases

Gene3Di2.30.250.10, 1 hit
InterProiView protein in InterPro
IPR001948 Peptidase_M18
IPR023358 Peptidase_M18_dom2
PANTHERiPTHR28570 PTHR28570, 1 hit
PfamiView protein in Pfam
PF02127 Peptidase_M18, 1 hit
PRINTSiPR00932 AMINO1PTASE

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
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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 nameiAMPL_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: P14904
Secondary accession number(s): D6VXI5, P22060
<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: April 1, 1990
Last sequence update: February 1, 1994
Last modified: December 11, 2019
This is version 187 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

3D-structure, Direct protein sequencing, Reference proteome

Documents

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