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Entry version 187 (18 Sep 2019)
Sequence version 1 (01 Oct 1996)
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Protein

Serine/threonine-protein kinase ATG1

Gene

ATG1

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

Serine/threonine protein kinase involved in the cytoplasm to vacuole transport (Cvt) and found to be essential in autophagy, where it is required for the formation of autophagosomes. Involved in the clearance of protein aggregates which cannot be efficiently cleared by the proteasome. Required for selective autophagic degradation of the nucleus (nucleophagy) as well as for mitophagy which contributes to regulate mitochondrial quantity and quality by eliminating the mitochondria to a basal level to fulfill cellular energy requirements and preventing excess ROS production. Also involved in endoplasmic reticulum-specific autophagic process, in selective removal of ER-associated degradation (ERAD) substrates. Plays a key role in ATG9 and ATG23 cycling through the pre-autophagosomal structure and is necessary to promote ATG18 binding to ATG9 through phosphorylation of ATG9. Finally, ATG1 is also required for the maintenance of cell viability under starvation and for glycogen storage during stationary phase. Plays a role in genome stability through suppression of abnormal mitosis under starvation, and in regulation of filamentous growth.33 Publications

Miscellaneous

Present with 1070 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 <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

Activated by hypophosphorylated form of ATG13 (present in nitrogen starvation conditions). Also activated by autophopsphorylation of Thr-226 and inhibited by phosphorylation of Ser-34.2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 sitei54ATPPROSITE-ProRule annotation1
<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 sitei172Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi30 – 38ATPPROSITE-ProRule annotation9

<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 functionKinase, Serine/threonine-protein kinase, Transferase
Biological processAutophagy, Protein transport, Transport
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
YEAST:G3O-30667-MONOMER

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
2.7.11.1 984

Protein family/group databases

Transport Classification Database

More...
TCDBi
9.A.15.1.1 the autophagy-related phagophore-formation transporter (apt) family

<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:
Serine/threonine-protein kinase ATG1Curated (EC:2.7.11.11 Publication)
Alternative name(s):
Autophagy protein 31 Publication
Autophagy-related protein 11 Publication
Cytoplasm to vacuole targeting protein 101 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:ATG11 Publication
Synonyms:APG11 Publication, AUT31 Publication, CVT101 Publication
Ordered Locus Names:YGL180WImported
ORF Names:G1615
<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 VII

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
FungiDB:YGL180W

Saccharomyces Genome Database

More...
SGDi
S000003148 ATG1

<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

Cytoplasm, Membrane

<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>Mutagenesisi34S → D or E: Impairs kinase activity. 1 Publication1
Mutagenesisi54K → A: Defect in the Cvt pathway. 3 Publications1
Mutagenesisi102M → A: Enables the binding of the inhibitor of the kinase activity 1-NA-PP1. 1 Publication1
Mutagenesisi211D → A: Loss of cell viability under starvation. 2 Publications1
Mutagenesisi226T → E: Leads to constitutive autophosphorylation activity. 1 Publication1
Mutagenesisi237E → R: Loss of cell viability under starvation. 1 Publication1
Mutagenesisi429Y → A: Impairs interaction with ATG8 and decreases autophagy efficiency; when associated with A-432. 1 Publication1
Mutagenesisi432V → A: Impairs interaction with ATG8 and decreases autophagy efficiency; when associated with A-429. 1 Publication1
Mutagenesisi508S → A: Impairs autophagic activity; when associated with A-515. 1 Publication1
Mutagenesisi515S → A: Impairs autophagic activity; when associated with A-508. 1 Publication1
Mutagenesisi551S → A: Decreases autophagic activity. 1 Publication1
Mutagenesisi552S → A: Decreases autophagic activity. 1 Publication1
Mutagenesisi621S → A: Decreases autophagic activity. 1 Publication1
Mutagenesisi677S → A: Decreases autophagic activity. 1 Publication1
Mutagenesisi680S → A: Decreases autophagic activity. 1 Publication1
Mutagenesisi683S → A: Decreases autophagic activity. 1 Publication1
Mutagenesisi769S → A: Decreases autophagic activity. 1 Publication1
Mutagenesisi783S → A: Decreases autophagic activity. 1 Publication1
Mutagenesisi884N → A: No effect. 1 Publication1
Mutagenesisi886L → G: Cvt pathway specific block. 1 Publication1

<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_00000856551 – 897Serine/threonine-protein kinase ATG1Add BLAST897

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 residuei34Phosphoserine1 Publication1
Modified residuei129Phosphothreonine1 Publication1
Modified residuei226Phosphothreonine; by autocatalysis1 Publication1
Modified residuei304Phosphoserine1 Publication1
Modified residuei365Phosphoserine1 Publication1
Modified residuei390PhosphoserineCombined sources1 Publication1
Modified residuei508Phosphoserine; by PKA1 Publication1
Modified residuei515Phosphoserine; by PKA2 Publications1
Modified residuei533Phosphoserine1 Publication1
Modified residuei551Phosphoserine1 Publication1
Modified residuei552Phosphoserine1 Publication1
Modified residuei590Phosphothreonine1 Publication1
Modified residuei621Phosphoserine1 Publication1
Modified residuei635PhosphoserineCombined sources1
Modified residuei638PhosphoserineCombined sources1
Modified residuei647PhosphoserineCombined sources1
Modified residuei677PhosphoserineCombined sources1 Publication1
Modified residuei680Phosphoserine1 Publication1
Modified residuei683Phosphoserine1 Publication1
Modified residuei769Phosphoserine1 Publication1
Modified residuei783Phosphoserine1 Publication1

<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

Autophosphorylated at Thr-226 and Ser-390. The phosphorylation state may play a role in the induction of protein degradation upon starvation. Phosphorylation at Thr-226 within the activation loop is required for protein kinase activity whereas phosphorylation at Ser-34 leads to inhibition of kinase activity. Phosphorylation of Ser-508 and Ser-515 by PKA is required to induce autophagy but not for kinase activity.4 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P53104

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

More...
PaxDbi
P53104

PRoteomics IDEntifications database

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PRIDEi
P53104

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P53104

<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

Homodimer. Dimerization requires the presence of ATG13.

Forms a ternary complex with ATG13 and ATG17.

Interacts also with ATG11.

6 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

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
33074, 617 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...
ComplexPortali
CPX-1676 ATG1 kinase complex

Database of interacting proteins

More...
DIPi
DIP-1192N

Protein interaction database and analysis system

More...
IntActi
P53104, 24 interactors

Molecular INTeraction database

More...
MINTi
P53104

STRING: functional protein association networks

More...
STRINGi
4932.YGL180W

<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>Domaini24 – 325Protein kinasePROSITE-ProRule annotationAdd BLAST302

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni880 – 886Required for Cvt trafficking7

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>Motifi429 – 432LIR4

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 biasi542 – 548Poly-Gln7

<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 LIR motif is required for the interaction with ATG8 and for the association of ATG1 with autophagosomes.2 Publications

<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 protein kinase superfamily. Ser/Thr protein kinase family. APG1/unc-51/ULK1 subfamily.PROSITE-ProRule annotation

Phylogenomic databases

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000246715

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P53104

KEGG Orthology (KO)

More...
KOi
K08269

Identification of Orthologs from Complete Genome Data

More...
OMAi
CEIAYVT

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR011009 Kinase-like_dom_sf
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
IPR008271 Ser/Thr_kinase_AS
IPR022708 Ser/Thr_kinase_C

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF12063 DUF3543, 1 hit
PF00069 Pkinase, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00220 S_TKc, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF56112 SSF56112, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00107 PROTEIN_KINASE_ATP, 1 hit
PS50011 PROTEIN_KINASE_DOM, 1 hit
PS00108 PROTEIN_KINASE_ST, 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.

P53104-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MGDIKNKDHT TSVNHNLMAS AGNYTAEKEI GKGSFATVYR GHLTSDKSQH
60 70 80 90 100
VAIKEVSRAK LKNKKLLENL EIEIAILKKI KHPHIVGLID CERTSTDFYL
110 120 130 140 150
IMEYCALGDL TFLLKRRKEL MENHPLLRTV FEKYPPPSEN HNGLHRAFVL
160 170 180 190 200
SYLQQLASAL KFLRSKNLVH RDIKPQNLLL STPLIGYHDS KSFHELGFVG
210 220 230 240 250
IYNLPILKIA DFGFARFLPN TSLAETLCGS PLYMAPEILN YQKYNAKADL
260 270 280 290 300
WSVGTVVFEM CCGTPPFRAS NHLELFKKIK RANDVITFPS YCNIEPELKE
310 320 330 340 350
LICSLLTFDP AQRIGFEEFF ANKVVNEDLS SYELEDDLPE LESKSKGIVE
360 370 380 390 400
SNMFVSEYLS KQPKSPNSNL AGHQSMADNP AELSDALKNS NILTAPAVKT
410 420 430 440 450
DHTQAVDKKA SNNKYHNSLV SDRSFEREYV VVEKKSVEVN SLADEVAQAG
460 470 480 490 500
FNPNPIKHPT STQNQNVLLN EQFSPNNQQY FQNQGENPRL LRATSSSSGG
510 520 530 540 550
SDGSRRPSLV DRRLSISSLN PSNALSRALG IASTRLFGGA NQQQQQQQIT
560 570 580 590 600
SSPPYSQTLL NSQLFHELTE NIILRIDHLQ HPETLKLDNT NIVSILESLA
610 620 630 640 650
AKAFVVYSYA EVKFSQIVPL STTLKGMANF ENRRSMDSNA IAEEQDSDDA
660 670 680 690 700
EEEDETLKKY KEDCLSTKTF GKGRTLSATS QLSATFNKLP RSEMILLCNE
710 720 730 740 750
AIVLYMKALS ILSKSMQVTS NWWYESQEKS CSLRVNVLVQ WLREKFNECL
760 770 780 790 800
EKADFLRLKI NDLRFKHASE VAENQTLEEK GSSEEPVYLE KLLYDRALEI
810 820 830 840 850
SKMAAHMELK GENLYNCELA YATSLWMLET SLDDDDFTNA YGDYPFKTNI
860 870 880 890
HLKSNDVEDK EKYHSVLDEN DRIIIRKYID SIANRLKILR QKMNHQN
Length:897
Mass (Da):101,717
Last modified:October 1, 1996 - 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:i7F4C785AA3A7CC46
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
X91489 Genomic DNA Translation: CAA62794.1
D29991 Genomic DNA Translation: BAA21481.1
Z72702 Genomic DNA Translation: CAA96892.1
BK006941 Genomic DNA Translation: DAA07934.1

Protein sequence database of the Protein Information Resource

More...
PIRi
S61137

NCBI Reference Sequences

More...
RefSeqi
NP_011335.1, NM_001181045.1

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
YGL180W_mRNA; YGL180W; YGL180W

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
852695

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
sce:YGL180W

<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
X91489 Genomic DNA Translation: CAA62794.1
D29991 Genomic DNA Translation: BAA21481.1
Z72702 Genomic DNA Translation: CAA96892.1
BK006941 Genomic DNA Translation: DAA07934.1
PIRiS61137
RefSeqiNP_011335.1, NM_001181045.1

3D structure databases

Database of comparative protein structure models

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ModBasei
Search...

SWISS-MODEL Interactive Workspace

More...
SWISS-MODEL-Workspacei
Submit a new modelling project...

Protein-protein interaction databases

BioGridi33074, 617 interactors
ComplexPortaliCPX-1676 ATG1 kinase complex
DIPiDIP-1192N
IntActiP53104, 24 interactors
MINTiP53104
STRINGi4932.YGL180W

Protein family/group databases

TCDBi9.A.15.1.1 the autophagy-related phagophore-formation transporter (apt) family

PTM databases

iPTMnetiP53104

Proteomic databases

MaxQBiP53104
PaxDbiP53104
PRIDEiP53104

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYGL180W_mRNA; YGL180W; YGL180W
GeneIDi852695
KEGGisce:YGL180W

Organism-specific databases

EuPathDBiFungiDB:YGL180W
SGDiS000003148 ATG1

Phylogenomic databases

HOGENOMiHOG000246715
InParanoidiP53104
KOiK08269
OMAiCEIAYVT

Enzyme and pathway databases

BioCyciYEAST:G3O-30667-MONOMER
BRENDAi2.7.11.1 984

Miscellaneous databases

Protein Ontology

More...
PROi
PR:P53104

Family and domain databases

InterProiView protein in InterPro
IPR011009 Kinase-like_dom_sf
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
IPR008271 Ser/Thr_kinase_AS
IPR022708 Ser/Thr_kinase_C
PfamiView protein in Pfam
PF12063 DUF3543, 1 hit
PF00069 Pkinase, 1 hit
SMARTiView protein in SMART
SM00220 S_TKc, 1 hit
SUPFAMiSSF56112 SSF56112, 1 hit
PROSITEiView protein in PROSITE
PS00107 PROTEIN_KINASE_ATP, 1 hit
PS50011 PROTEIN_KINASE_DOM, 1 hit
PS00108 PROTEIN_KINASE_ST, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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MobiDB: a database of protein disorder and mobility annotations

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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 nameiATG1_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: P53104
Secondary accession number(s): D6VTX3
<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: October 1, 1996
Last sequence update: October 1, 1996
Last modified: September 18, 2019
This is version 187 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

Complete proteome, Reference proteome

Documents

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