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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 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

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)DescriptionActionsGraphical viewLength
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

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000874441 – 2672eIF-2-alpha kinase activator GCN1Add BLAST2672

Proteomic databases

MaxQBiP33892.
PRIDEiP33892.

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. 296 interactors.
DIPiDIP-2344N.
IntActiP33892. 128 interactors.
MINTiMINT-634438.

Structurei

3D structure databases

ProteinModelPortaliP33892.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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
Regioni1330 – 1641EF3-like region1 PublicationAdd BLAST312

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.
OrthoDBiEOG092C00Q9.

Family and domain databases

Gene3Di1.25.10.10. 10 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33062. 296 interactors.
DIPiDIP-2344N.
IntActiP33892. 128 interactors.
MINTiMINT-634438.

PTM databases

iPTMnetiP33892.

Proteomic databases

MaxQBiP33892.
PRIDEiP33892.

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.
OrthoDBiEOG092C00Q9.

Enzyme and pathway databases

BioCyciYEAST:G3O-30676-MONOMER.

Miscellaneous databases

PROiP33892.

Family and domain databases

Gene3Di1.25.10.10. 10 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...

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: November 30, 2016
This is version 146 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.