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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-Experimental evidence at protein leveli

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

GO - Molecular functioni

  • ATP-dependent protein binding Source: UniProtKB
  • protein kinase binding Source: UniProtKB
  • protein kinase regulator activity Source: SGD
  • ribosome binding Source: UniProtKB
  • translation initiation factor binding Source: UniProtKB

GO - Biological processi

  • cellular response to amino acid starvation Source: UniProtKB
  • cellular response to benomyl Source: UniProtKB
  • cellular response to hydrogen peroxide Source: UniProtKB
  • cellular stress response to acidic pH Source: UniProtKB
  • positive regulation of cell death Source: UniProtKB
  • positive regulation of kinase activity Source: UniProtKB
  • positive regulation of protein phosphorylation Source: UniProtKB
  • positive regulation of translational initiation in response to starvation Source: UniProtKB
  • regulation of eIF2 alpha phosphorylation by amino acid starvation Source: UniProtKB
  • regulation of translational elongation Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Stress response, Translation regulation

Enzyme and pathway databases

BioCyciYEAST:G3O-30676-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
eIF-2-alpha kinase activator GCN1Curated
Alternative name(s):
General control non-derepressible protein 1Imported
Translational activator GCN1Curated
Gene namesi
Name:GCN1Imported
Ordered Locus Names:YGL195W
ORF Names:G1318
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome VII

Organism-specific databases

EuPathDBiFungiDB:YGL195W.
SGDiS000003163. GCN1.

Subcellular locationi

  • Cytoplasm 1 Publication

GO - Cellular componenti

  • cytosol Source: SGD
  • cytosolic ribosome Source: SGD
  • polysomal ribosome Source: UniProtKB
  • polysome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi757 – 7582KK → 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 Publications
Mutagenesisi762 – 7621K → 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 Publications
Mutagenesisi765 – 7651K → 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 Publications
Mutagenesisi775 – 7751K → 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 Publications
Mutagenesisi777 – 7782RK → 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 Publications
Mutagenesisi782 – 7832KK → 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 Publications
Mutagenesisi786 – 7872KK → 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 Publications
Mutagenesisi790 – 7901K → 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 Publications
Mutagenesisi1444 – 14441G → D: Decreases interaction with GCN20 and polysomal association. 1 Publication
Mutagenesisi1458 – 14581E → 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 Publication
Mutagenesisi1461 – 14655WRTKR → 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 Publication
Mutagenesisi2259 – 22591R → A: Decreases interaction with GCN2 and YIH1 but not with GCN20 and ribosomes. 3 Publications
Mutagenesisi2291 – 22911F → L: Does not interact with GCN2, impairs eIF-2-alpha phosphorylation and fails to derepress GCN4 translation in amino acid-starved cells. 1 Publication
Mutagenesisi2304 – 23041S → P: Does not interact with GCN2. 1 Publication
Mutagenesisi2353 – 23531L → P: Does not interact with GCN2. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 26722672eIF-2-alpha kinase activator GCN1PRO_0000087444Add
BLAST

Proteomic databases

MaxQBiP33892.

PTM databases

iPTMnetiP33892.

Interactioni

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

Binary interactionsi

WithEntry#Exp.IntActNotes
GCN20P435354EBI-7442,EBI-7423

GO - Molecular functioni

  • ATP-dependent protein binding Source: UniProtKB
  • protein kinase binding Source: UniProtKB
  • translation initiation factor binding Source: UniProtKB

Protein-protein interaction databases

BioGridi33062. 295 interactions.
DIPiDIP-2344N.
IntActiP33892. 128 interactions.
MINTiMINT-634438.

Structurei

3D structure databases

ProteinModelPortaliP33892.
SMRiP33892. Positions 1404-1674, 1726-1789, 1874-1974, 2104-2167, 2453-2482.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati5 – 4238HEAT 1Sequence analysisAdd
BLAST
Repeati79 – 11739HEAT 2Sequence analysisAdd
BLAST
Repeati174 – 21138HEAT 3Sequence analysisAdd
BLAST
Repeati227 – 26741HEAT 4Sequence analysisAdd
BLAST
Repeati329 – 36638HEAT 5Sequence analysisAdd
BLAST
Repeati372 – 41039HEAT 6Sequence analysisAdd
BLAST
Repeati509 – 54941HEAT 7Sequence analysisAdd
BLAST
Repeati611 – 64838HEAT 8Sequence analysisAdd
BLAST
Repeati706 – 74540HEAT 9Sequence analysisAdd
BLAST
Repeati902 – 93231HEAT 10Sequence analysisAdd
BLAST
Repeati933 – 97038HEAT 11Sequence analysisAdd
BLAST
Repeati975 – 99420HEAT 12; degenerateSequence analysisAdd
BLAST
Repeati995 – 103036HEAT 13; degenerateSequence analysisAdd
BLAST
Repeati1031 – 106737HEAT 14Sequence analysisAdd
BLAST
Repeati1099 – 113840HEAT 15Sequence analysisAdd
BLAST
Repeati1185 – 122440HEAT 16Sequence analysisAdd
BLAST
Repeati1243 – 128139HEAT 17Sequence analysisAdd
BLAST
Repeati1284 – 132138HEAT 18Sequence analysisAdd
BLAST
Repeati1363 – 140139HEAT 19Sequence analysisAdd
BLAST
Repeati1405 – 144238HEAT 20Sequence analysisAdd
BLAST
Repeati1444 – 148037HEAT 21Sequence analysisAdd
BLAST
Repeati1484 – 152138HEAT 22Sequence analysisAdd
BLAST
Repeati1523 – 155937HEAT 23Sequence analysisAdd
BLAST
Repeati1561 – 159838HEAT 24Sequence analysisAdd
BLAST
Repeati1603 – 164038HEAT 25Sequence analysisAdd
BLAST
Repeati1641 – 167939HEAT 26Sequence analysisAdd
BLAST
Repeati1681 – 171737HEAT 27Sequence analysisAdd
BLAST
Repeati1721 – 175838HEAT 28Sequence analysisAdd
BLAST
Repeati1760 – 179637HEAT 29Sequence analysisAdd
BLAST
Repeati1825 – 186238HEAT 30Sequence analysisAdd
BLAST
Repeati1863 – 190341HEAT 31Sequence analysisAdd
BLAST
Repeati1905 – 194238HEAT 32Sequence analysisAdd
BLAST
Repeati1947 – 198438HEAT 33Sequence analysisAdd
BLAST
Repeati1985 – 202440HEAT 34Sequence analysisAdd
BLAST
Repeati2026 – 205530HEAT 35Sequence analysisAdd
BLAST
Repeati2057 – 209539HEAT 36Sequence analysisAdd
BLAST
Repeati2097 – 213438HEAT 37Sequence analysisAdd
BLAST
Repeati2138 – 217538HEAT 38Sequence analysisAdd
BLAST
Repeati2206 – 224338HEAT 39Sequence analysisAdd
BLAST
Repeati2250 – 228637HEAT 40Sequence analysisAdd
BLAST
Repeati2290 – 232839HEAT 41Sequence analysisAdd
BLAST
Repeati2347 – 238438HEAT 42Sequence analysisAdd
BLAST
Repeati2392 – 242938HEAT 43Sequence analysisAdd
BLAST
Repeati2450 – 248738HEAT 44Sequence analysisAdd
BLAST
Repeati2506 – 254641HEAT 45Sequence analysisAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1330 – 1641312EF3-like region1 PublicationAdd
BLAST

Domaini

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

Sequence similaritiesi

Belongs to the GCN1 family.Curated
Contains 45 HEAT repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

GeneTreeiENSGT00390000011675.
HOGENOMiHOG000213714.
InParanoidiP33892.
OMAiEIAWRTK.
OrthoDBiEOG7FJH7S.

Family and domain databases

Gene3Di1.25.10.10. 8 hits.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR026827. Ecm29/Gcn1.
IPR033173. Gcn1.
IPR022716. Gcn1_N.
IPR021133. HEAT_type_2.
[Graphical view]
PANTHERiPTHR23346. PTHR23346. 2 hits.
PTHR23346:SF7. PTHR23346:SF7. 2 hits.
PfamiPF12074. DUF3554. 2 hits.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 8 hits.
PROSITEiPS50077. HEAT_REPEAT. 4 hits.
[Graphical view]

Sequencei

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
Checksum:i980FDD03753E9D1C
GO

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.

Genome annotation databases

EnsemblFungiiYGL195W; YGL195W; YGL195W.
GeneIDi852680.
KEGGisce:YGL195W.

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

ProteinModelPortaliP33892.
SMRiP33892. Positions 1404-1674, 1726-1789, 1874-1974, 2104-2167, 2453-2482.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33062. 295 interactions.
DIPiDIP-2344N.
IntActiP33892. 128 interactions.
MINTiMINT-634438.

PTM databases

iPTMnetiP33892.

Proteomic databases

MaxQBiP33892.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYGL195W; YGL195W; YGL195W.
GeneIDi852680.
KEGGisce:YGL195W.

Organism-specific databases

EuPathDBiFungiDB:YGL195W.
SGDiS000003163. GCN1.

Phylogenomic databases

GeneTreeiENSGT00390000011675.
HOGENOMiHOG000213714.
InParanoidiP33892.
OMAiEIAWRTK.
OrthoDBiEOG7FJH7S.

Enzyme and pathway databases

BioCyciYEAST:G3O-30676-MONOMER.

Miscellaneous databases

PROiP33892.

Family and domain databases

Gene3Di1.25.10.10. 8 hits.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR026827. Ecm29/Gcn1.
IPR033173. Gcn1.
IPR022716. Gcn1_N.
IPR021133. HEAT_type_2.
[Graphical view]
PANTHERiPTHR23346. PTHR23346. 2 hits.
PTHR23346:SF7. PTHR23346:SF7. 2 hits.
PfamiPF12074. DUF3554. 2 hits.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 8 hits.
PROSITEiPS50077. HEAT_REPEAT. 4 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "GCN1, a translational activator of GCN4 in Saccharomyces cerevisiae, is required for phosphorylation of eukaryotic translation initiation factor 2 by protein kinase GCN2."
    Marton M.J., Crouch D., Hinnebusch A.G.
    Mol. Cell. Biol. 13:3541-3556(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
  2. "Sequencing of a 40.5 kb fragment located on the left arm of chromosome VII from Saccharomyces cerevisiae."
    Coglievina M., Klima R., Bertani I., Delneri D., Zaccaria P., Bruschi C.V.
    Yeast 13:55-64(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 96604 / S288c / FY1679.
  3. "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII."
    Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E.
    , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K.
    Nature 387:81-84(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. "GCN20, a novel ATP binding cassette protein, and GCN1 reside in a complex that mediates activation of the eIF-2 alpha kinase GCN2 in amino acid-starved cells."
    Vazquez de Aldana C.R., Marton M.J., Hinnebusch A.G.
    EMBO J. 14:3184-3199(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH GCN20, ASSOCIATION WITH RIBOSOMES.
  6. "Evidence that GCN1 and GCN20, translational regulators of GCN4, function on elongating ribosomes in activation of eIF2alpha kinase GCN2."
    Marton M.J., Vazquez de Aldana C.R., Qiu H., Chakraburtty K., Hinnebusch A.G.
    Mol. Cell. Biol. 17:4474-4489(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH GCN20, ASSOCIATION WITH RIBOSOMES, SUBCELLULAR LOCATION, DOMAIN, MUTAGENESIS OF GLY-1444.
  7. "Association of GCN1-GCN20 regulatory complex with the N-terminus of eIF2alpha kinase GCN2 is required for GCN2 activation."
    Garcia-Barrio M., Dong J., Ufano S., Hinnebusch A.G.
    EMBO J. 19:1887-1899(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH GCN2, IDENTIFICATION IN A COMPLEX WITH GCN2 AND GCN20.
  8. "Separate domains in GCN1 for binding protein kinase GCN2 and ribosomes are required for GCN2 activation in amino acid-starved cells."
    Sattlegger E., Hinnebusch A.G.
    EMBO J. 19:6622-6633(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH GCN2 AND GCN20, IDENTIFICATION IN A COMPLEX WITH GCN2 AND GCN20, ASSOCIATION WITH RIBOSOMES, MUTAGENESIS OF ARG-2259.
  9. "GI domain-mediated association of the eukaryotic initiation factor 2alpha kinase GCN2 with its activator GCN1 is required for general amino acid control in budding yeast."
    Kubota H., Sakaki Y., Ito T.
    J. Biol. Chem. 275:20243-20246(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH GCN2.
  10. "Budding yeast GCN1 binds the GI domain to activate the eIF2alpha kinase GCN2."
    Kubota H., Ota K., Sakaki Y., Ito T.
    J. Biol. Chem. 276:17591-17596(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH GCN2, MUTAGENESIS OF PHE-2291; SER-2304 AND LEU-2353.
  11. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  12. "YIH1 is an actin-binding protein that inhibits protein kinase GCN2 and impairs general amino acid control when overexpressed."
    Sattlegger E., Swanson M.J., Ashcraft E.A., Jennings J.L., Fekete R.A., Link A.J., Hinnebusch A.G.
    J. Biol. Chem. 279:29952-29962(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH YIH1, MUTAGENESIS OF ARG-2259.
  13. "Polyribosome binding by GCN1 is required for full activation of eukaryotic translation initiation factor 2{alpha} kinase GCN2 during amino acid starvation."
    Sattlegger E., Hinnebusch A.G.
    J. Biol. Chem. 280:16514-16521(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH GCN20, ASSOCIATION WITH RIBOSOMES, MUTAGENESIS OF 757-LYS-LYS-758; LYS-762; LYS-765; LYS-775; 777-ARG-LYS-778; 782-LYS-LYS-783; 786-LYS-LYS-787; LYS-790; GLU-1458 AND 1461-TRP--ARG-1465.
  14. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
    Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
    J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  15. "Saccharomyces cerevisiae Rbg1 protein and its binding partner Gir2 interact on polyribosomes with Gcn1."
    Wout P.K., Sattlegger E., Sullivan S.M., Maddock J.R.
    Eukaryot. Cell 8:1061-1071(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH GIR2, ASSOCIATION WITH RIBOSOMES.
  16. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "Gcn1 and actin binding to Yih1: implications for activation of the eIF2 kinase GCN2."
    Sattlegger E., Barbosa J.A., Moraes M.C., Martins R.M., Hinnebusch A.G., Castilho B.A.
    J. Biol. Chem. 286:10341-10355(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH YIH1, MUTAGENESIS OF ARG-2259.
  18. "Evidence that Yih1 resides in a complex with ribosomes."
    Waller T., Lee S.J., Sattlegger E.
    FEBS J. 279:1761-1776(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH YIH1.
  19. "Evolutionarily conserved IMPACT impairs various stress responses that require GCN1 for activating the eIF2 kinase GCN2."
    Cambiaghi T.D., Pereira C.M., Shanmugam R., Bolech M., Wek R.C., Sattlegger E., Castilho B.A.
    Biochem. Biophys. Res. Commun. 443:592-597(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  20. "Evidence that eukaryotic translation elongation factor 1A (eEF1A) binds the Gcn2 protein C terminus and inhibits Gcn2 activity."
    Visweswaraiah J., Lageix S., Castilho B.A., Izotova L., Kinzy T.G., Hinnebusch A.G., Sattlegger E.
    J. Biol. Chem. 286:36568-36579(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH GCN2, ASSOCIATION WITH RIBOSOMES.
  21. "Overexpression of eukaryotic translation elongation factor 3 impairs Gcn2 protein activation."
    Visweswaraiah J., Lee S.J., Hinnebusch A.G., Sattlegger E.
    J. Biol. Chem. 287:37757-37768(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ASSOCIATION WITH RIBOSOMES, MUTAGENESIS OF 757-LYS-LYS-758; LYS-762; LYS-765; LYS-775; 777-ARG-LYS-778; 782-LYS-LYS-783; 786-LYS-LYS-787 AND LYS-790.
  22. "Gcn1 contacts the small ribosomal protein Rps10, which is required for full activation of the protein kinase Gcn2."
    Lee S.J., Swanson M.J., Sattlegger E.
    Biochem. J. 466:547-559(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RPS10A AND RPS10B, ASSOCIATION WITH RIBOSOMES.

Entry informationi

Entry nameiGCN1_YEAST
AccessioniPrimary (citable) accession number: P33892
Secondary accession number(s): D6VTV8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: July 6, 2016
This is version 142 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

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

Keywords - Technical termi

Complete proteome, 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.