Basic Information

NameeIF-2-alpha kinase activator GCN1 (General control non-derepressible protein 1) (Translational activator GCN1)
Uniprot IDP33892
Systematic gene nameYGL195W
Standard gene nameGCN1
Gene namesGCN1 YGL195W G1318
Description from SGDYGL195W GCN1 SGDID:S000003163, Chr VII from 131525-139543, Genome Release 64-3-1, Verified ORF, "Positive regulator of the Gcn2p kinase activity; forms a complex with Gcn20p; proposed to stimulate Gcn2p activation by an uncharged tRNA"
Protein length2672
Downloadsequence (fasta, from Uniprot), modifications (csv format)
Database linksUniprot, SGD, TheCellVision.org, FungiDB

Sequence

MTAILNWEDI SPVLEKGTRE SHVSKRVPFL QDISQLVRQE TLEKPQLSEI
AFVLLNTFTI YEDNRSKSLV TSILLDILNL EPCLLENFIR FISDVVISNP
ATKAVADYLN LLDWINSFLI FVSHNSNLFE EYIPKLLVAH SYATFGVETI
LDNQEEGKKS QDKQNQHRKR IRYCIFQTTV KAFLKCLKDN DDSISFMKIS
IKTVLESYSK LKITSVGVVM IMGALTQAAL QLLSRQPALH SVLKENSAEK
YCEYLGKEVF LGKNPPSSFC LEIGLKPFLK EFVSQELFIK FFIPNIEKAV
LRSPEVGFSI LSELYAGVSP EKVNLLNAFA SSKLINQYFS SFKSSKEVVR
SVSLQSMIIL LRKISNTDTT LEDLTKLIDE IFKNIKSNLN ADYKSLISKI
LIEIPLTHYE VSEKICKGLS PYIGKEGNEA ALTLMLNAFF VHYFSLGKPI
EDLDKIISAG FADKKPALKK CWFAAFLNNS NAASEEVILN FIDGCLEFVK
DSIIHYQTHG HACILASIEF TNKILALDNT ELNDRVMQLI ETLPENSSIG
DAILTAALST ELSIENRIHA VNLLQELFYK KPEFIGFSVI DAIERRMRVQ
ELIPQQNTSF KYVTSVLLAI TSELPDKEAS IKVLINALVI AQWNIFNIKN
GWAGLVLRAR LDPAEVVKEH ASVIMEKILE ITGSCEWIDT IYGACGLQAA
AYAAFIQPNE FTPILCKTIE ADLTADDFSR LSEEDFEIFA GEEGVLVVDV
LEESMNKKLS NKNSKEYETL MWEQKIRKEQ AKKNVKKLSK EEQELVNEQL
AKESAVRSHV SEISTRLKRG IRLVSELSKA ACLVQNGIAT WFPLAVTKLL
YLCSEPNISK LTEDVNNVFL QLSQNVSERL GNIRLFLGLA TLRVHNANGI
SQDYLQEPLV ELLTRVLFRI KFVSNQAAID SISLTYILPL LINVLEKGKA
IALKNADKPV VKAEFVEEDE EEEHLLLAME IISVHAEAFE DPSIPRISIV
EVLLSLLSLP SKAKIAKDCF NALCQSISVA PNQEDLDMIL SNLLSPNQFV
RSTILETLDN EFELEPFMKY SPEVFICRFD SDPSNREIAD FIWEFNKFVV
NDELLKSLFP LFNQDDSGLR LFAANAYAFG AVSLFTSEEN SSKDYLNDLL
NFYKEKAKPL EPILDQFGLV LVSASEQKDP WQGRSTVAIT LKIMAKAFSA
EDDTVVNIIK FLVDDGGLVD REPIVRQEMK EAGVELITLH GSQNSKDLIP
IFEEALSSST DSALKENVII LYGTLARHLQ QSDARIHTII ERLLSTLDTP
SADIQQAVSA CIAPLVFQFK QKVGDYLGIL MEKLLNPTVA SSMRKGAAWG
IAGLVKGYGI SALSEFDIIR NLIEAAEDKK EPKRRESVGF CFQYLSESLG
KFFEPYVIEI LPNILKNLGD AVPEVRDATA RATKAIMAHT TGYGVKKLIP
VAVSNLDEIA WRTKRGSVQL LGNMAYLDPT QLSASLSTIV PEIVGVLNDS
HKEVRKAADE SLKRFGEVIR NPEIQKLVPV LLQAIGDPTK YTEEALDSLI
QTQFVHYIDG PSLALIIHII HRGMHDRSAN IKRKACKIVG NMAILVDTKD
LIPYLQQLID EVEIAMVDPV PNTRATAARA LGALVERLGE EQFPDLIPRL
LDTLSDESKS GDRLGSAQAL AEVISGLGLT KLDEMLPTIL AGVTNFRAYI
REGFMPLLLF LPVCFGSQFA PYINQIIQPI LSGLADNDEN IRDTALKAGK
LIVKNYATKA VDLLLPELER GMFDENDRIR LSSVQLTGEL LFQVTGISSR
NEFSEEDGDH NGEFSGKLVD VLGQDRRDRI LAALFVCRND TSGIVRATTV
DIWKALVPNT PRAVKEILPT LTGMIVTHLA SSSNVLRNIA AQTLGDLVRR
VGGNALSQLL PSLEESLIET SNSDSRQGVC IALYELIESA STETISQFQS
TIVNIIRTAL IDESATVREA AALSFDVFQD VVGKTAVDEV LPYLLHMLES
SDNSDFALLG LQEIMSKKSD VIFPILIPTL LAPPIDAFRA SALGSLAEVA
GSALYKRLSI IINALVDAII GTSEDESTKG ALELALDRVF LSVNDDEGLH
PLLQQIMSLL KSDNIEKRIA VLERLPNFFD KTVLDFDVYI PNFVSHAILS
LDDEDQRVVN GNFNALSTLL KKVDKPTLEK LVKPAKQSLA LTGRQGQDVA
AFKLPRGPNC VLPIFLHGLM YGSNDEREES ALAIADVVSK TPAANLKPFV
SVITGPLIRV VGERFSSDIK AAILFALNVL FIKIPMFLRP FIPQLQRTFV
KSLSDATNET LRLRAAKALG ALIEHQPRVD PLVIELVTGA KQATDEGVKT
AMLKALLEVI MKAGSKLNEN SKTNIVNLVE EEMLGSNDKL AVAYAKLIGS
LSEILSNDEA HKILQDKVLN ADLDGETGKF AILTLNSFLK DAPTHIFNTG
LIDEFVSYIL NAIRSPDVYF GENGTIAAGK LLLLEGEKRS PFVKKDAAEP
FKIGDENINL LINELSKAVL QPASNSTDVR RLALVVIRTL ARFKFDECIK
QYFDVVGPSV FSCLRDPVIP IKLAAEKAYL ALFKLVEEDD MHTFNEWFAK
ISDRGNSIET VTGTTIQLRS VGDYTKRVGK RLANVERERI AAGGDAETMF
SDRFEDEREI WAVGGVELTT DI

Legend

  • X Phoshorylation

Structure

Structure visualized by GLmol written by biochem_fan. The structure was downloaded from the AlphaFold Protein Structure Database.


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References

[241, Phos]Bai Y, Chen B, Li M, et al (2017) FPD: A comprehensive phosphorylation database in fungi. Fungal Biology 121:869–875. (Publication) (All modifications)
[241, Phos]Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)
[724, Phos]Lanz MC, Yugandhar K, Gupta S, Sanford EJ, Faça VM, Vega S, Joiner AMN, Fromme JC, Yu H, Smolka MB (2021). In-depth and 3-dimensional exploration of the budding yeast phosphoproteome. EMBO Reports, e51121. (Publication) (All modifications)
[724, Phos]Zhou, X., Li, W., Liu, Y., Amon, A. (2021. Cross-compartment signal propagation in the mitotic exit network. Elife 10:e63645. (Publication) (All modifications)
[729, Phos]Zhou, X., Li, W., Liu, Y., Amon, A. (2021. Cross-compartment signal propagation in the mitotic exit network. Elife 10:e63645. (Publication) (All modifications)
[732, Phos]Lanz MC, Yugandhar K, Gupta S, Sanford EJ, Faça VM, Vega S, Joiner AMN, Fromme JC, Yu H, Smolka MB (2021). In-depth and 3-dimensional exploration of the budding yeast phosphoproteome. EMBO Reports, e51121. (Publication) (All modifications)
[754, Phos]Lanz MC, Yugandhar K, Gupta S, Sanford EJ, Faça VM, Vega S, Joiner AMN, Fromme JC, Yu H, Smolka MB (2021). In-depth and 3-dimensional exploration of the budding yeast phosphoproteome. EMBO Reports, e51121. (Publication) (All modifications)
[764, Phos]Bai Y, Chen B, Li M, et al (2017) FPD: A comprehensive phosphorylation database in fungi. Fungal Biology 121:869–875. (Publication) (All modifications)
[764, Phos]Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)
[767, Phos]Bai Y, Chen B, Li M, et al (2017) FPD: A comprehensive phosphorylation database in fungi. Fungal Biology 121:869–875. (Publication) (All modifications)
[767, Phos]Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)
[1107, Phos]Zhou, X., Li, W., Liu, Y., Amon, A. (2021. Cross-compartment signal propagation in the mitotic exit network. Elife 10:e63645. (Publication) (All modifications)
[1326, Phos]Bai Y, Chen B, Li M, et al (2017) FPD: A comprehensive phosphorylation database in fungi. Fungal Biology 121:869–875. (Publication) (All modifications)
[1326, Phos]Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)
[1398, Phos]Lanz MC, Yugandhar K, Gupta S, Sanford EJ, Faça VM, Vega S, Joiner AMN, Fromme JC, Yu H, Smolka MB (2021). In-depth and 3-dimensional exploration of the budding yeast phosphoproteome. EMBO Reports, e51121. (Publication) (All modifications)
[1660, Phos]Lanz MC, Yugandhar K, Gupta S, Sanford EJ, Faça VM, Vega S, Joiner AMN, Fromme JC, Yu H, Smolka MB (2021). In-depth and 3-dimensional exploration of the budding yeast phosphoproteome. EMBO Reports, e51121. (Publication) (All modifications)
[1804, Phos]Lanz MC, Yugandhar K, Gupta S, Sanford EJ, Faça VM, Vega S, Joiner AMN, Fromme JC, Yu H, Smolka MB (2021). In-depth and 3-dimensional exploration of the budding yeast phosphoproteome. EMBO Reports, e51121. (Publication) (All modifications)
[2302, Phos]Zhou, X., Li, W., Liu, Y., Amon, A. (2021. Cross-compartment signal propagation in the mitotic exit network. Elife 10:e63645. (Publication) (All modifications)
[2304, Phos]Zhou, X., Li, W., Liu, Y., Amon, A. (2021. Cross-compartment signal propagation in the mitotic exit network. Elife 10:e63645. (Publication) (All modifications)
[2648, Phos]Zhou, X., Li, W., Liu, Y., Amon, A. (2021. Cross-compartment signal propagation in the mitotic exit network. Elife 10:e63645. (Publication) (All modifications)