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Entry version 175 (11 Dec 2019)
Sequence version 1 (01 Feb 1994)
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Protein

eIF-2-alpha kinase activator GCN1

Gene

GCN1

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

Acts as a positive activator of the GCN2 protein kinase activity in response to amino acid starvation (PubMed:8497269, PubMed:24333428). Component of the GCN1-GCN20 complex that forms a complex with GCN2 on translating ribosomes; during this process, GCN1 seems to act as a chaperone to facilitate delivery of uncharged tRNAs that enter the A site of ribosomes to the tRNA-binding domain of GCN2, and hence stimulating GCN2 kinase activity (PubMed:7621831, PubMed:9234705, PubMed:15722345). Participates in the repression of global protein synthesis and in gene-specific mRNA translation activation, such as the transcriptional activator GCN4, by promoting the GCN2-mediated phosphorylation of eukaryotic translation initiation factor 2 (eIF-2-alpha/SUI2) on 'Ser-52', and hence allowing GCN4-mediated reprogramming of amino acid biosynthetic gene expression to alleviate nutrient depletion (PubMed:8497269, PubMed:10801780, PubMed:11350982, PubMed:15722345).7 Publications

Miscellaneous

Present with 7330 molecules/cell in log phase SD medium.1 Publication

<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 functionActivator
Biological processStress response, Translation regulation

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
YEAST:G3O-30676-MONOMER

<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:
eIF-2-alpha kinase activator GCN1Curated
Alternative name(s):
General control non-derepressible protein 1Imported
Translational activator GCN1Curated
<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:GCN1Imported
Ordered Locus Names:YGL195W
ORF Names:G1318
<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

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EuPathDBi
FungiDB:YGL195W

Saccharomyces Genome Database

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SGDi
S000003163 GCN1

<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

<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>Mutagenesisi757 – 758KK → AA or DD: Does not inhibit interaction with GCN20, reduces ribosome binding, ribosome binding by GCN20, weakly impairs eIF-2-alpha phosphorylation but strongly impairs eIF-2-alpha phosphorylation in a YEF3-dependent manner; when associated with A-762; A-765; A-775; 777-A-A-778; 782-A-A-783; 786-A-A-787 and A-790. 2 Publications2
Mutagenesisi762K → A: Does not inhibit interaction with GCN20, reduces ribosome binding, ribosome binding by GCN20, weakly impairs eIF-2-alpha phosphorylation but strongly impairs eIF-2-alpha phosphorylation in a YEF3-dependent manner; when associated with A-757-758-A; A-765; A-775; 777-A-A-778; 782-A-A-783; 786-A-A-787 and A-790. 2 Publications1
Mutagenesisi765K → A: Does not inhibit interaction with GCN20, reduces ribosome binding, ribosome binding by GCN20, weakly impairs eIF-2-alpha phosphorylation but strongly impairs eIF-2-alpha phosphorylation in a YEF3-dependent manner; when associated with A-757-758-A; A-762; A-775; 777-A-A-778; 782-A-A-783; 786-A-A-787 and A-790. 2 Publications1
Mutagenesisi775K → A: Does not inhibit interaction with GCN20, reduces ribosome binding, ribosome binding by GCN20, weakly impairs eIF-2-alpha phosphorylation but strongly impairs eIF-2-alpha phosphorylation in a YEF3-dependent manner; when associated with A-757-758-A; A-762; A-765; 777-A-A-778; 782-A-A-783; 786-A-A-787 and A-790. 2 Publications1
Mutagenesisi777 – 778RK → AA: Does not inhibit interaction with GCN20, reduces ribosome binding, ribosome binding by GCN20, weakly impairs eIF-2-alpha phosphorylation but strongly impairs eIF-2-alpha phosphorylation in a YEF3-dependent manner; when associated with A-757-758-A; A-762; A-765; A-775; 782-A-A-783; 786-A-A-787 and A-790. 2 Publications2
Mutagenesisi782 – 783KK → AA: Does not inhibit interaction with GCN20, reduces ribosome binding, ribosome binding by GCN20, weakly impairs eIF-2-alpha phosphorylation but strongly impairs eIF-2-alpha phosphorylation in a YEF3-dependent manner; when associated with A-757-758-A; A-762; A-765; A-775; 777-A-A-778; 786-A-A-787 and A-790. 2 Publications2
Mutagenesisi786 – 787KK → AA: Does not inhibit interaction with GCN20, reduces ribosome binding, ribosome binding by GCN20, weakly impairs eIF-2-alpha phosphorylation but strongly impairs eIF-2-alpha phosphorylation in a YEF3-dependent manner; when associated with A-757-758-A; A-762; A-765; A-775; 777-A-A-778; 782-A-A-783 and A-790. 2 Publications2
Mutagenesisi790K → A: Does not inhibit interaction with GCN20, reduces ribosome binding, ribosome binding by GCN20, weakly impairs eIF-2-alpha phosphorylation but strongly impairs eIF-2-alpha phosphorylation in a YEF3-dependent manner; when associated with A-757-758-A; A-762; A-765; A-775; 777-A-A-778; 782-A-A-783 and 786-A-A-787. 2 Publications1
Mutagenesisi1444G → D: Decreases interaction with GCN20 and polysomal association. 1 Publication1
Mutagenesisi1458E → A: Does not inhibit interaction with GCN20, reduces ribosome binding, ribosome binding by GCN20 and strongly impairs eIF-2-alpha phosphorylation; when associated with 1461-A--A-1465. 1 Publication1
Mutagenesisi1461 – 1465WRTKR → AAAAA: Does not inhibit interaction with GCN20, reduces ribosome binding, ribosome binding by GCN20 and strongly impairs eIF-2-alpha phosphorylation; when associated with A-1458. 1 Publication5
Mutagenesisi2259R → A: Decreases interaction with GCN2 and YIH1 but not with GCN20 and ribosomes. 3 Publications1
Mutagenesisi2291F → L: Does not interact with GCN2, impairs eIF-2-alpha phosphorylation and fails to derepress GCN4 translation in amino acid-starved cells. 1 Publication1
Mutagenesisi2304S → P: Does not interact with GCN2. 1 Publication1
Mutagenesisi2353L → P: Does not interact with GCN2. 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_00000874441 – 2672eIF-2-alpha kinase activator GCN1Add BLAST2672

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P33892

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

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PaxDbi
P33892

PRoteomics IDEntifications database

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PRIDEi
P33892

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P33892

<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

Interacts (via N- and C-terminus) with GCN2 (via N-terminal RWD domain); this interaction stimulates GCN2 kinase activity in a GCN20-dependent manner in response to amino acid starvation (PubMed:10775272, PubMed:11101534, PubMed:10801780, PubMed:11350982, PubMed:15126500, PubMed:15722345, PubMed:21849502).

Interacts (via C-terminus) with GCN20 (via N-terminus); this interaction stimulates GCN2 kinase activity in response to amino acid starvation (PubMed:7621831, PubMed:9234705, PubMed:11101534). The GCN1-GCN20 complex interacts with GCN2 on translating ribosomes in amino acid-starved cells; GCN1 may bind near the ribosomal A-site and promotes the transfer of uncharged tRNAs from the A-site to the tRNA-binding domain in GCN2 for its subsequent kinase activation, and hence allowing GCN4 translational activation and derepression of amino acid biosynthetic genes (PubMed:7621831, PubMed:9234705, PubMed:10775272, PubMed:11101534).

Interacts (via C-terminus) with YIH1 (via N-terminus); this interaction reduces the GCN1-GCN20 complex formation and prevents the interaction of GCN1 with GCN2 and GCN2 kinase activation in amino acid-starved cells (PubMed:15126500, PubMed:21239490, PubMed:22404850).

Interacts with GIR2; this interaction prevents the interaction of GCN1 with GCN2 and GCN2 kinase activation in amino acid-starved cells (PubMed:19448108).

Interacts (via middle region) with RPS10A and RPS10B; these interactions are direct and promote GCN2 kinase activation (PubMed:25437641). Associates (via N-terminus) with ribosomes; this association is stimulated in a ATP- and GCN20-dependent manner and is necessary to activate GCN2 kinase activity (PubMed:7621831, PubMed:9234705, PubMed:11101534, PubMed:15722345, PubMed:19448108, PubMed:21849502, PubMed:22888004, PubMed:25437641).

14 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

WithEntry#Exp.IntActNotes
P435353EBI-7442,EBI-7423

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
33062, 468 interactors

ComplexPortal: manually curated resource of macromolecular complexes

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ComplexPortali
CPX-1808 GCN1-GCN20 complex

Database of interacting proteins

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DIPi
DIP-2344N

Protein interaction database and analysis system

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IntActi
P33892, 134 interactors

Molecular INTeraction database

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MINTi
P33892

STRING: functional protein association networks

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STRINGi
4932.YGL195W

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

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RNActi
P33892 protein

<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 ‘Family and Domains’ section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati5 – 42HEAT 1Sequence analysisAdd BLAST38
Repeati79 – 117HEAT 2Sequence analysisAdd BLAST39
Repeati174 – 211HEAT 3Sequence analysisAdd BLAST38
Repeati227 – 267HEAT 4Sequence analysisAdd BLAST41
Repeati329 – 366HEAT 5Sequence analysisAdd BLAST38
Repeati372 – 410HEAT 6Sequence analysisAdd BLAST39
Repeati509 – 549HEAT 7Sequence analysisAdd BLAST41
Repeati611 – 648HEAT 8Sequence analysisAdd BLAST38
Repeati706 – 745HEAT 9Sequence analysisAdd BLAST40
Repeati902 – 932HEAT 10Sequence analysisAdd BLAST31
Repeati933 – 970HEAT 11Sequence analysisAdd BLAST38
Repeati975 – 994HEAT 12; degenerateSequence analysisAdd BLAST20
Repeati995 – 1030HEAT 13; degenerateSequence analysisAdd BLAST36
Repeati1031 – 1067HEAT 14Sequence analysisAdd BLAST37
Repeati1099 – 1138HEAT 15Sequence analysisAdd BLAST40
Repeati1185 – 1224HEAT 16Sequence analysisAdd BLAST40
Repeati1243 – 1281HEAT 17Sequence analysisAdd BLAST39
Repeati1284 – 1321HEAT 18Sequence analysisAdd BLAST38
Repeati1363 – 1401HEAT 19Sequence analysisAdd BLAST39
Repeati1405 – 1442HEAT 20Sequence analysisAdd BLAST38
Repeati1444 – 1480HEAT 21Sequence analysisAdd BLAST37
Repeati1484 – 1521HEAT 22Sequence analysisAdd BLAST38
Repeati1523 – 1559HEAT 23Sequence analysisAdd BLAST37
Repeati1561 – 1598HEAT 24Sequence analysisAdd BLAST38
Repeati1603 – 1640HEAT 25Sequence analysisAdd BLAST38
Repeati1641 – 1679HEAT 26Sequence analysisAdd BLAST39
Repeati1681 – 1717HEAT 27Sequence analysisAdd BLAST37
Repeati1721 – 1758HEAT 28Sequence analysisAdd BLAST38
Repeati1760 – 1796HEAT 29Sequence analysisAdd BLAST37
Repeati1825 – 1862HEAT 30Sequence analysisAdd BLAST38
Repeati1863 – 1903HEAT 31Sequence analysisAdd BLAST41
Repeati1905 – 1942HEAT 32Sequence analysisAdd BLAST38
Repeati1947 – 1984HEAT 33Sequence analysisAdd BLAST38
Repeati1985 – 2024HEAT 34Sequence analysisAdd BLAST40
Repeati2026 – 2055HEAT 35Sequence analysisAdd BLAST30
Repeati2057 – 2095HEAT 36Sequence analysisAdd BLAST39
Repeati2097 – 2134HEAT 37Sequence analysisAdd BLAST38
Repeati2138 – 2175HEAT 38Sequence analysisAdd BLAST38
Repeati2206 – 2243HEAT 39Sequence analysisAdd BLAST38
Repeati2250 – 2286HEAT 40Sequence analysisAdd BLAST37
Repeati2290 – 2328HEAT 41Sequence analysisAdd BLAST39
Repeati2347 – 2384HEAT 42Sequence analysisAdd BLAST38
Repeati2392 – 2429HEAT 43Sequence analysisAdd BLAST38
Repeati2450 – 2487HEAT 44Sequence analysisAdd BLAST38
Repeati2506 – 2546HEAT 45Sequence analysisAdd BLAST41

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>Regioni1330 – 1641EF3-like region1 PublicationAdd BLAST312

<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 EF3-like region is necessary and sufficient for interaction with GCN20 (PubMed:9234705).1 Publication

<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 GCN1 family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000213714

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P33892

Identification of Orthologs from Complete Genome Data

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OMAi
QHRKRIR

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
1.25.10.10, 3 hits

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR011989 ARM-like
IPR016024 ARM-type_fold
IPR033173 Gcn1
IPR022716 Gcn1_N
IPR021133 HEAT_type_2
IPR034085 TOG

The PANTHER Classification System

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PANTHERi
PTHR23346:SF7 PTHR23346:SF7, 1 hit

Pfam protein domain database

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Pfami
View protein in Pfam
PF12074 Gcn1_N, 2 hits

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM01349 TOG, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF48371 SSF48371, 4 hits

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50077 HEAT_REPEAT, 4 hits

<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.

P33892-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MTAILNWEDI SPVLEKGTRE SHVSKRVPFL QDISQLVRQE TLEKPQLSEI
60 70 80 90 100
AFVLLNTFTI YEDNRSKSLV TSILLDILNL EPCLLENFIR FISDVVISNP
110 120 130 140 150
ATKAVADYLN LLDWINSFLI FVSHNSNLFE EYIPKLLVAH SYATFGVETI
160 170 180 190 200
LDNQEEGKKS QDKQNQHRKR IRYCIFQTTV KAFLKCLKDN DDSISFMKIS
210 220 230 240 250
IKTVLESYSK LKITSVGVVM IMGALTQAAL QLLSRQPALH SVLKENSAEK
260 270 280 290 300
YCEYLGKEVF LGKNPPSSFC LEIGLKPFLK EFVSQELFIK FFIPNIEKAV
310 320 330 340 350
LRSPEVGFSI LSELYAGVSP EKVNLLNAFA SSKLINQYFS SFKSSKEVVR
360 370 380 390 400
SVSLQSMIIL LRKISNTDTT LEDLTKLIDE IFKNIKSNLN ADYKSLISKI
410 420 430 440 450
LIEIPLTHYE VSEKICKGLS PYIGKEGNEA ALTLMLNAFF VHYFSLGKPI
460 470 480 490 500
EDLDKIISAG FADKKPALKK CWFAAFLNNS NAASEEVILN FIDGCLEFVK
510 520 530 540 550
DSIIHYQTHG HACILASIEF TNKILALDNT ELNDRVMQLI ETLPENSSIG
560 570 580 590 600
DAILTAALST ELSIENRIHA VNLLQELFYK KPEFIGFSVI DAIERRMRVQ
610 620 630 640 650
ELIPQQNTSF KYVTSVLLAI TSELPDKEAS IKVLINALVI AQWNIFNIKN
660 670 680 690 700
GWAGLVLRAR LDPAEVVKEH ASVIMEKILE ITGSCEWIDT IYGACGLQAA
710 720 730 740 750
AYAAFIQPNE FTPILCKTIE ADLTADDFSR LSEEDFEIFA GEEGVLVVDV
760 770 780 790 800
LEESMNKKLS NKNSKEYETL MWEQKIRKEQ AKKNVKKLSK EEQELVNEQL
810 820 830 840 850
AKESAVRSHV SEISTRLKRG IRLVSELSKA ACLVQNGIAT WFPLAVTKLL
860 870 880 890 900
YLCSEPNISK LTEDVNNVFL QLSQNVSERL GNIRLFLGLA TLRVHNANGI
910 920 930 940 950
SQDYLQEPLV ELLTRVLFRI KFVSNQAAID SISLTYILPL LINVLEKGKA
960 970 980 990 1000
IALKNADKPV VKAEFVEEDE EEEHLLLAME IISVHAEAFE DPSIPRISIV
1010 1020 1030 1040 1050
EVLLSLLSLP SKAKIAKDCF NALCQSISVA PNQEDLDMIL SNLLSPNQFV
1060 1070 1080 1090 1100
RSTILETLDN EFELEPFMKY SPEVFICRFD SDPSNREIAD FIWEFNKFVV
1110 1120 1130 1140 1150
NDELLKSLFP LFNQDDSGLR LFAANAYAFG AVSLFTSEEN SSKDYLNDLL
1160 1170 1180 1190 1200
NFYKEKAKPL EPILDQFGLV LVSASEQKDP WQGRSTVAIT LKIMAKAFSA
1210 1220 1230 1240 1250
EDDTVVNIIK FLVDDGGLVD REPIVRQEMK EAGVELITLH GSQNSKDLIP
1260 1270 1280 1290 1300
IFEEALSSST DSALKENVII LYGTLARHLQ QSDARIHTII ERLLSTLDTP
1310 1320 1330 1340 1350
SADIQQAVSA CIAPLVFQFK QKVGDYLGIL MEKLLNPTVA SSMRKGAAWG
1360 1370 1380 1390 1400
IAGLVKGYGI SALSEFDIIR NLIEAAEDKK EPKRRESVGF CFQYLSESLG
1410 1420 1430 1440 1450
KFFEPYVIEI LPNILKNLGD AVPEVRDATA RATKAIMAHT TGYGVKKLIP
1460 1470 1480 1490 1500
VAVSNLDEIA WRTKRGSVQL LGNMAYLDPT QLSASLSTIV PEIVGVLNDS
1510 1520 1530 1540 1550
HKEVRKAADE SLKRFGEVIR NPEIQKLVPV LLQAIGDPTK YTEEALDSLI
1560 1570 1580 1590 1600
QTQFVHYIDG PSLALIIHII HRGMHDRSAN IKRKACKIVG NMAILVDTKD
1610 1620 1630 1640 1650
LIPYLQQLID EVEIAMVDPV PNTRATAARA LGALVERLGE EQFPDLIPRL
1660 1670 1680 1690 1700
LDTLSDESKS GDRLGSAQAL AEVISGLGLT KLDEMLPTIL AGVTNFRAYI
1710 1720 1730 1740 1750
REGFMPLLLF LPVCFGSQFA PYINQIIQPI LSGLADNDEN IRDTALKAGK
1760 1770 1780 1790 1800
LIVKNYATKA VDLLLPELER GMFDENDRIR LSSVQLTGEL LFQVTGISSR
1810 1820 1830 1840 1850
NEFSEEDGDH NGEFSGKLVD VLGQDRRDRI LAALFVCRND TSGIVRATTV
1860 1870 1880 1890 1900
DIWKALVPNT PRAVKEILPT LTGMIVTHLA SSSNVLRNIA AQTLGDLVRR
1910 1920 1930 1940 1950
VGGNALSQLL PSLEESLIET SNSDSRQGVC IALYELIESA STETISQFQS
1960 1970 1980 1990 2000
TIVNIIRTAL IDESATVREA AALSFDVFQD VVGKTAVDEV LPYLLHMLES
2010 2020 2030 2040 2050
SDNSDFALLG LQEIMSKKSD VIFPILIPTL LAPPIDAFRA SALGSLAEVA
2060 2070 2080 2090 2100
GSALYKRLSI IINALVDAII GTSEDESTKG ALELALDRVF LSVNDDEGLH
2110 2120 2130 2140 2150
PLLQQIMSLL KSDNIEKRIA VLERLPNFFD KTVLDFDVYI PNFVSHAILS
2160 2170 2180 2190 2200
LDDEDQRVVN GNFNALSTLL KKVDKPTLEK LVKPAKQSLA LTGRQGQDVA
2210 2220 2230 2240 2250
AFKLPRGPNC VLPIFLHGLM YGSNDEREES ALAIADVVSK TPAANLKPFV
2260 2270 2280 2290 2300
SVITGPLIRV VGERFSSDIK AAILFALNVL FIKIPMFLRP FIPQLQRTFV
2310 2320 2330 2340 2350
KSLSDATNET LRLRAAKALG ALIEHQPRVD PLVIELVTGA KQATDEGVKT
2360 2370 2380 2390 2400
AMLKALLEVI MKAGSKLNEN SKTNIVNLVE EEMLGSNDKL AVAYAKLIGS
2410 2420 2430 2440 2450
LSEILSNDEA HKILQDKVLN ADLDGETGKF AILTLNSFLK DAPTHIFNTG
2460 2470 2480 2490 2500
LIDEFVSYIL NAIRSPDVYF GENGTIAAGK LLLLEGEKRS PFVKKDAAEP
2510 2520 2530 2540 2550
FKIGDENINL LINELSKAVL QPASNSTDVR RLALVVIRTL ARFKFDECIK
2560 2570 2580 2590 2600
QYFDVVGPSV FSCLRDPVIP IKLAAEKAYL ALFKLVEEDD MHTFNEWFAK
2610 2620 2630 2640 2650
ISDRGNSIET VTGTTIQLRS VGDYTKRVGK RLANVERERI AAGGDAETMF
2660 2670
SDRFEDEREI WAVGGVELTT DI
Length:2,672
Mass (Da):296,698
Last modified:February 1, 1994 - 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:i980FDD03753E9D1C
GO

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

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DDBJi
Links Updated
L12467 Genomic DNA Translation: AAA34635.1
X91837 Genomic DNA Translation: CAA62949.1
Z72717 Genomic DNA Translation: CAA96907.1
BK006941 Genomic DNA Translation: DAA07919.1

Protein sequence database of the Protein Information Resource

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PIRi
A48126

NCBI Reference Sequences

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RefSeqi
NP_011320.3, NM_001181060.3

Genome annotation databases

Ensembl fungal genome annotation project

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EnsemblFungii
YGL195W_mRNA; YGL195W; YGL195W

Database of genes from NCBI RefSeq genomes

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GeneIDi
852680

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
sce:YGL195W

<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
L12467 Genomic DNA Translation: AAA34635.1
X91837 Genomic DNA Translation: CAA62949.1
Z72717 Genomic DNA Translation: CAA96907.1
BK006941 Genomic DNA Translation: DAA07919.1
PIRiA48126
RefSeqiNP_011320.3, NM_001181060.3

3D structure databases

Database of comparative protein structure models

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ModBasei
Search...

SWISS-MODEL Interactive Workspace

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

Protein-protein interaction databases

BioGridi33062, 468 interactors
ComplexPortaliCPX-1808 GCN1-GCN20 complex
DIPiDIP-2344N
IntActiP33892, 134 interactors
MINTiP33892
STRINGi4932.YGL195W

PTM databases

iPTMnetiP33892

Proteomic databases

MaxQBiP33892
PaxDbiP33892
PRIDEiP33892

Genome annotation databases

EnsemblFungiiYGL195W_mRNA; YGL195W; YGL195W
GeneIDi852680
KEGGisce:YGL195W

Organism-specific databases

EuPathDBiFungiDB:YGL195W
SGDiS000003163 GCN1

Phylogenomic databases

HOGENOMiHOG000213714
InParanoidiP33892
OMAiQHRKRIR

Enzyme and pathway databases

BioCyciYEAST:G3O-30676-MONOMER

Miscellaneous databases

Protein Ontology

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PROi
PR:P33892
RNActiP33892 protein

Family and domain databases

Gene3Di1.25.10.10, 3 hits
InterProiView protein in InterPro
IPR011989 ARM-like
IPR016024 ARM-type_fold
IPR033173 Gcn1
IPR022716 Gcn1_N
IPR021133 HEAT_type_2
IPR034085 TOG
PANTHERiPTHR23346:SF7 PTHR23346:SF7, 1 hit
PfamiView protein in Pfam
PF12074 Gcn1_N, 2 hits
SMARTiView protein in SMART
SM01349 TOG, 1 hit
SUPFAMiSSF48371 SSF48371, 4 hits
PROSITEiView protein in PROSITE
PS50077 HEAT_REPEAT, 4 hits

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

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

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiGCN1_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: P33892
Secondary accession number(s): D6VTV8
<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: February 1, 1994
Last sequence update: February 1, 1994
Last modified: December 11, 2019
This is version 175 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

Reference proteome

Documents

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