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Protein

eIF-2-alpha kinase GCN2

Gene

GCN2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Metabolic-stress sensing protein kinase that phosphorylates the alpha subunit of eukaryotic translation initiation factor 2 (eIF-2-alpha/SUI2) on 'Ser-52' in response to low amino acid availability (PubMed:1739968, PubMed:7623840, PubMed:8798780, PubMed:9528799, PubMed:10983975, PubMed:17202131). Plays a role as an activator of the general amino acid control (GAAC) pathway required for adapatation to amino acid starvation. Converts phosphorylated eIF-2-alpha/SUI2 either to a competitive inhibitor of translation initiation factor eIF-2B, leading to a global protein synthesis repression, and thus to a reduced overall utilization of amino acids, or to a translational initiation activation of specific mRNAs, such as the transcriptional activator GCN4, and hence allowing GCN4-mediated reprogramming of amino acid biosynthetic gene expression to alleviate nutrient depletion (PubMed:2660141, PubMed:2188100, PubMed:1739968, PubMed:7621831, PubMed:7623840, PubMed:8798780, PubMed:10801780, PubMed:11350982, PubMed:24333428). Binds uncharged tRNAs (PubMed:7623840, PubMed:10983975).13 Publications
(orthologuous-specific) Binds to aminoacylated tRNA(Phe) less tightly than to deacylated tRNA(Phe) (PubMed:10983975). Binds to double-stranded RNA (PubMed:9430731).2 Publications

Miscellaneous

Present with 279 molecules/cell in log phase SD medium.1 Publication

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.5 Publications

Enzyme regulationi

The kinase activity is stimulated upon binding to uncharged tRNAs (PubMed:7623840).1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei628ATPPROSITE-ProRule annotation1
Active sitei835Proton acceptor1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi605 – 613ATPPROSITE-ProRule annotation9

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • double-stranded RNA binding Source: UniProtKB
  • eukaryotic translation initiation factor 2alpha kinase activity Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB
  • protein kinase activity Source: UniProtKB
  • protein self-association Source: UniProtKB
  • ribosomal large subunit binding Source: UniProtKB
  • ribosome binding Source: UniProtKB
  • translation initiation factor binding Source: UniProtKB
  • tRNA binding Source: UniProtKB

GO - Biological processi

  • cellular response to amino acid starvation Source: UniProtKB
  • cellular response to benomyl Source: UniProtKB
  • cellular response to histidine Source: UniProtKB
  • cellular response to hydrogen peroxide Source: UniProtKB
  • cellular stress response to acidic pH Source: UniProtKB
  • chronological cell aging Source: SGD
  • DNA damage checkpoint Source: SGD
  • negative regulation of protein kinase activity by protein phosphorylation Source: SGD
  • negative regulation of TORC1 signaling Source: SGD
  • positive regulation of cellular response to amino acid starvation Source: UniProtKB
  • positive regulation of macroautophagy Source: SGD
  • positive regulation of translational initiation in response to starvation Source: UniProtKB
  • protein autophosphorylation Source: UniProtKB
  • protein phosphorylation Source: UniProtKB
  • regulation of eIF2 alpha phosphorylation by amino acid starvation Source: UniProtKB
  • regulation of translational initiation Source: UniProtKB
  • translation Source: UniProtKB-KW

Keywordsi

Molecular functionActivator, Kinase, RNA-binding, Serine/threonine-protein kinase, Transferase, tRNA-binding
Biological processProtein biosynthesis, Stress response, Translation regulation
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-29848-MONOMER
ReactomeiR-SCE-1169408 ISG15 antiviral mechanism
R-SCE-381042 PERK regulates gene expression

Names & Taxonomyi

Protein namesi
Recommended name:
eIF-2-alpha kinase GCN2By similarity (EC:2.7.11.15 Publications)
Alternative name(s):
General control non-derepressible protein 2Imported
Serine/threonine-protein kinase GCN2Curated
Gene namesi
Name:GCN2Imported
Synonyms:AAS1
Ordered Locus Names:YDR283C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome IV

Organism-specific databases

EuPathDBiFungiDB:YDR283C
SGDiS000002691 GCN2

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; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi74Y → A: Inhibits interaction with GCN1, eIF-2-alpha phosphorylation and fails to derepress GCN4 translation in amino acid-starved cells. 2 Publications1
Mutagenesisi582S → F: Increases the constitutive kinase activity and induces derepression of GCN4 translation and amino acid biosynthetic genes in absence of amino acid starvation. 1 Publication1
Mutagenesisi594R → D: Inhibits autophosphorylation, eIF-2-alpha kinase activity and derepression of GCN4 translation. Restores eIF-2-alpha kinase activity and derepression of GCN4, but not autophosphorylation; when associated with R-598. 1 Publication1
Mutagenesisi598D → R: Inhibits autophosphorylation, eIF-2-alpha kinase activity and derepression of GCN4 translation. Restores eIF-2-alpha kinase activity and derepression of GCN4, but not autophosphorylation; when associated with D-594. 1 Publication1
Mutagenesisi601E → K: Increases the constitutive kinase activity in absence of amino acid starvation. 1 Publication1
Mutagenesisi628K → V or R: Inhibits autophosphorylation, eIF-2-alpha kinase activity and derepression of GCN4 translation in amino acid-starved cells. 6 Publications1
Mutagenesisi629K → A: Does not abolish derepression of GCN4 translation and amino acid biosynthetic genes in amino acid-starved cells. 1 Publication1
Mutagenesisi716F → S: Increases the constitutive kinase activity and induces derepression of GCN4 translation and amino acid biosynthetic genes in absence of amino acid starvation. 1 Publication1
Mutagenesisi788M → V: Increases the constitutive kinase activity and induces derepression of GCN4 translation and amino acid biosynthetic genes in absence of amino acid starvation. 1 Publication1
Mutagenesisi794R → G: Constitutively active allele, bypass the tRNA binding-requirement for kinase activity. 1 Publication1
Mutagenesisi803E → V: Increases tRNA binding and the constitutive kinase activity and induces derepression of GCN4 translation and amino acid biosynthetic genes in absence of amino acid starvation. 2 Publications1
Mutagenesisi821E → K: Increases the constitutive kinase activity and induces derepression of GCN4 translation and amino acid biosynthetic genes in absence of amino acid starvation. 2 Publications1
Mutagenesisi835D → N: Loss of function. 1 Publication1
Mutagenesisi861H → Y: Increases the constitutive kinase activity and induces derepression of GCN4 translation and amino acid biosynthetic genes in absence of amino acid starvation. 1 Publication1
Mutagenesisi882T → A, E or D: Partially impairs kinase activity. 1 Publication1
Mutagenesisi882T → S: No effect. 1 Publication1
Mutagenesisi887T → A, E or D: Completely abolishes kinase activity. 1 Publication1
Mutagenesisi887T → S: Partially impairs kinase activity. 1 Publication1
Mutagenesisi1080V → A: Inhibits dimerization; when associated with A-1088 and A-1090. 1 Publication1
Mutagenesisi1088L → A: Inhibits dimerization; when associated with A-1080 and A-1090. 1 Publication1
Mutagenesisi1090L → A: Inhibits dimerization; when associated with A-1080 and A-1088. 1 Publication1
Mutagenesisi1119Y → L: Inhibits binding to uncharged tRNAs, decreases eIF-2-alpha kinase activity and derepression of GCN4 translation and amino acid biosynthetic genes in amino acid-starved cells; when associated with L-1120. 3 Publications1
Mutagenesisi1120R → L: Inhibits binding to uncharged tRNAs, decreases eIF-2-alpha kinase activity and derepression of GCN4 translation and amino acid biosynthetic genes in amino acid-starved cells; when associated with L-1119. 3 Publications1
Mutagenesisi1134F → L: Increases the constitutive kinase activity and induces derepression of GCN4 translation and amino acid biosynthetic genes in absence of amino acid starvation. 1 Publication1
Mutagenesisi1138D → N: Increases the constitutive kinase activity and induces derepression of GCN4 translation and amino acid biosynthetic genes in absence of amino acid starvation. 1 Publication1
Mutagenesisi1197A → G: Increases the constitutive kinase activity and induces derepression of GCN4 translation and amino acid biosynthetic genes in absence of amino acid starvation. 1 Publication1
Mutagenesisi1308H → Y: Increases the constitutive kinase activity and induces derepression of GCN4 translation and amino acid biosynthetic genes in absence of amino acid starvation. 1 Publication1
Mutagenesisi1338G → D: Increases the constitutive kinase activity and induces derepression of GCN4 translation and amino acid biosynthetic genes in absence of amino acid starvation. 1 Publication1
Mutagenesisi1552 – 1556KKANK → LLANI: Fails to derepress of GCN4 translation and amino acid biosynthetic genes in amino acid-starved cells and does not inhibit autophosphorylation. 1 Publication5
Mutagenesisi1552K → L: Reduces interaction with TIF11, Inhibits binding to uncharged tRNAs, reduces autophosphorylation, eIF-2-alpha kinase activity and ribosome association, but not dimerization; when associated with I-1553 and I-1556. 2 Publications1
Mutagenesisi1553K → I: Reduces interaction with TIF11, Inhibits binding to uncharged tRNAs, reduces autophosphorylation, eIF-2-alpha kinase activity and ribosome association, but not dimerization; when associated with L-1552 and I-1556. 2 Publications1
Mutagenesisi1556K → I: Reduces interaction with TIF11, Inhibits binding to uncharged tRNAs, reduces autophosphorylation, eIF-2-alpha kinase activity and ribosome association, but not dimerization; when associated with L-1552 and I-1553. 2 Publications1
Mutagenesisi1557R → K: Increases the constitutive kinase activity and induces derepression of GCN4 translation and amino acid biosynthetic genes in absence of amino acid starvation. 1 Publication1
Mutagenesisi1591E → K: Increases the constitutive kinase activity and induces derepression of GCN4 translation and amino acid biosynthetic genes in absence of amino acid starvation. 1 Publication1
Mutagenesisi1606E → K: Increases the constitutive kinase activity and induces derepression of GCN4 translation and amino acid biosynthetic genes in absence of amino acid starvation. 2 Publications1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000859631 – 1659eIF-2-alpha kinase GCN2Add BLAST1659

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei761PhosphoserineCombined sources1
Modified residuei882Phosphothreonine; by autocatalysis1 Publication1
Modified residuei887Phosphothreonine; by autocatalysis1 Publication1

Post-translational modificationi

Autophosphorylated, autophosphorylation on Thr-882 and Thr-887 increases kinase activity.6 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP15442
PaxDbiP15442
PRIDEiP15442

PTM databases

iPTMnetiP15442

Interactioni

Subunit structurei

Homodimer; homodimerization is important for kinase activation by uncharged tRNAs (PubMed:9566889, PubMed:10983975, PubMed:11250908, PubMed:17202131, PubMed:15964839). Interacts (via N-terminal RWD domain) with GCN1 (via N- and C-terminus); 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:21849502). Interacts (via N-terminus) with the GCN1-GCN20 complex 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:10775272, PubMed:11101534). Interacts (via C-terminus) with TIF11; this interaction is direct, occurs in amino acid-repleted cells, may be stabilzed in a ribosome-dependent manner, reduces GCN2-mediated eIF-2-alpha phosphorylation but not GCN2 autophosphorylation and is lost in amino acid-starved cells and by uncharged tRNAs (PubMed:21849502). Associates (via C-terminus) with ribosomes (PubMed:2038314, PubMed:9430731, PubMed:10983975, PubMed:22888004).13 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • protein homodimerization activity Source: UniProtKB
  • protein self-association Source: UniProtKB
  • translation initiation factor binding Source: UniProtKB

Protein-protein interaction databases

BioGridi32336, 229 interactors
DIPiDIP-2346N
IntActiP15442, 27 interactors
MINTiP15442
STRINGi4932.YDR283C

Structurei

Secondary structure

11659
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 6Combined sources3
Helixi8 – 23Combined sources16
Beta strandi26 – 31Combined sources6
Beta strandi37 – 40Combined sources4
Beta strandi48 – 53Combined sources6
Beta strandi63 – 69Combined sources7
Beta strandi80 – 84Combined sources5
Helixi92 – 107Combined sources16
Helixi114 – 130Combined sources17
Helixi594 – 598Combined sources5
Beta strandi599 – 607Combined sources9
Beta strandi609 – 618Combined sources10
Turni619 – 621Combined sources3
Beta strandi624 – 633Combined sources10
Helixi634 – 647Combined sources14
Beta strandi653 – 655Combined sources3
Beta strandi658 – 664Combined sources7
Beta strandi781 – 789Combined sources9
Helixi796 – 802Combined sources7
Helixi805 – 807Combined sources3
Helixi809 – 828Combined sources20
Helixi838 – 840Combined sources3
Beta strandi841 – 843Combined sources3
Beta strandi849 – 851Combined sources3
Helixi888 – 890Combined sources3
Helixi893 – 896Combined sources4
Helixi905 – 919Combined sources15
Helixi925 – 936Combined sources12
Turni948 – 950Combined sources3
Helixi952 – 961Combined sources10
Helixi966 – 968Combined sources3
Helixi972 – 977Combined sources6
Helixi986 – 995Combined sources10
Beta strandi1541 – 1543Combined sources3
Beta strandi1551 – 1553Combined sources3
Helixi1560 – 1577Combined sources18
Beta strandi1582 – 1586Combined sources5
Helixi1590 – 1598Combined sources9
Beta strandi1601 – 1603Combined sources3
Helixi1604 – 1612Combined sources9
Helixi1615 – 1617Combined sources3
Helixi1621 – 1636Combined sources16
Beta strandi1641 – 1646Combined sources6
Turni1647 – 1649Combined sources3
Beta strandi1652 – 1656Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1ZXEX-ray2.60A/B/C/D/E/F594-997[»]
1ZY4X-ray1.95A/B594-997[»]
1ZY5X-ray2.00A/B594-997[»]
1ZYCX-ray3.00A/B/C/D594-997[»]
1ZYDX-ray2.75A/B594-997[»]
2YZ0NMR-A1-138[»]
4OTMX-ray1.95A/B1519-1659[»]
ProteinModelPortaliP15442
SMRiP15442
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP15442

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini17 – 128RWDPROSITE-ProRule annotationAdd BLAST112
Domaini256 – 527Protein kinase 1PROSITE-ProRule annotationAdd BLAST272
Domaini599 – 981Protein kinase 2PROSITE-ProRule annotationAdd BLAST383

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni999 – 1519Histidyl-tRNA synthetase-likeAdd BLAST521

Domaini

The C-terminal domain negatively regulates kinase activity via an autoinhibitory association with the protein kinase and histidyl-tRNA synthetase-like domains in amino acid-repleted cells, that is counteracted by uncharged tRNAs in amino acid-starved cells (PubMed:7623840, PubMed:8798780, PubMed:10983975, PubMed:11250908). The C-terminal, histidyl-tRNA synthetase-like region and protein kinase domains are necessary for homodimer formation (PubMed:9566889, PubMed:10983975, PubMed:11250908). The C-terminal and protein kinase domains are necessary for ribosome association (PubMed:9566889, PubMed:10983975). The C-terminal and histidyl-tRNA synthetase-like regions are required for uncharged tRNAs binding in amino acid-starved cells (PubMed:7623840, PubMed:8798780, PubMed:9430731, PubMed:10983975).6 Publications

Sequence similaritiesi

Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. GCN2 subfamily.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

GeneTreeiENSGT00530000062984
HOGENOMiHOG000172724
InParanoidiP15442
KOiK16196
OMAiKCVCLDD
OrthoDBiEOG092C0AG1

Family and domain databases

Gene3Di3.10.110.10, 1 hit
3.40.50.800, 1 hit
InterProiView protein in InterPro
IPR036621 Anticodon-bd_dom_sf
IPR016255 Gcn2
IPR024435 HisRS-related_dom
IPR011009 Kinase-like_dom_sf
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
IPR006575 RWD-domain
IPR008271 Ser/Thr_kinase_AS
IPR016135 UBQ-conjugating_enzyme/RWD
PfamiView protein in Pfam
PF12745 HGTP_anticodon2, 1 hit
PF00069 Pkinase, 3 hits
PF05773 RWD, 1 hit
PIRSFiPIRSF000660 Ser/Thr_PK_GCN2, 1 hit
SMARTiView protein in SMART
SM00591 RWD, 1 hit
SM00220 S_TKc, 1 hit
SUPFAMiSSF54495 SSF54495, 1 hit
SSF56112 SSF56112, 3 hits
PROSITEiView protein in PROSITE
PS00107 PROTEIN_KINASE_ATP, 1 hit
PS50011 PROTEIN_KINASE_DOM, 2 hits
PS00108 PROTEIN_KINASE_ST, 1 hit
PS50908 RWD, 1 hit

Sequencei

Sequence statusi: Complete.

P15442-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSLSHLTLDQ YYEIQCNELE AIRSIYMDDF TDLTKRKSSW DKQPQIIFEI
60 70 80 90 100
TLRSVDKEPV ESSITLHFAM TPMYPYTAPE IEFKNVQNVM DSQLQMLKSE
110 120 130 140 150
FKKIHNTSRG QEIIFEITSF TQEKLDEFQN VVNTQSLEDD RLQRIKETKE
160 170 180 190 200
QLEKEEREKQ QETIKKRSDE QRRIDEIVQR ELEKRQDDDD DLLFNRTTQL
210 220 230 240 250
DLQPPSEWVA SGEAIVFSKT IKAKLPNNSM FKFKAVVNPK PIKLTSDIFS
260 270 280 290 300
FSKQFLVKPY IPPESPLADF LMSSEMMENF YYLLSEIELD NSYFNTSNGK
310 320 330 340 350
KEIANLEKEL ETVLKAKHDN VNRLFGYTVE RMGRNNATFV WKIRLLTEYC
360 370 380 390 400
NYYPLGDLIQ SVGFVNLATA RIWMIRLLEG LEAIHKLGIV HKCINLETVI
410 420 430 440 450
LVKDADFGST IPKLVHSTYG YTVLNMLSRY PNKNGSSVEL SPSTWIAPEL
460 470 480 490 500
LKFNNAKPQR LTDIWQLGVL FIQIISGSDI VMNFETPQEF LDSTSMDETL
510 520 530 540 550
YDLLSKMLNN DPKKRLGTLE LLPMKFLRTN IDSTINRFNL VSESVNSNSL
560 570 580 590 600
ELTPGDTITV RGNGGRTLSQ SSIRRRSFNV GSRFSSINPA TRSRYASDFE
610 620 630 640 650
EIAVLGQGAF GQVVKARNAL DSRYYAIKKI RHTEEKLSTI LSEVMLLASL
660 670 680 690 700
NHQYVVRYYA AWLEEDSMDE NVFESTDEES DLSESSSDFE ENDLLDQSSI
710 720 730 740 750
FKNRTNHDLD NSNWDFISGS GYPDIVFENS SRDDENEDLD HDTSSTSSSE
760 770 780 790 800
SQDDTDKESK SIQNVPRRRN FVKPMTAVKK KSTLFIQMEY CENRTLYDLI
810 820 830 840 850
HSENLNQQRD EYWRLFRQIL EALSYIHSQG IIHRDLKPMN IFIDESRNVK
860 870 880 890 900
IGDFGLAKNV HRSLDILKLD SQNLPGSSDN LTSAIGTAMY VATEVLDGTG
910 920 930 940 950
HYNEKIDMYS LGIIFFEMIY PFSTGMERVN ILKKLRSVSI EFPPDFDDNK
960 970 980 990 1000
MKVEKKIIRL LIDHDPNKRP GARTLLNSGW LPVKHQDEVI KEALKSLSNP
1010 1020 1030 1040 1050
SSPWQQQVRE SLFNQSYSLT NDILFDNSVP TSTPFANILR SQMTEEVVKI
1060 1070 1080 1090 1100
FRKHGGIENN APPRIFPKAP IYGTQNVYEV LDKGGTVLQL QYDLTYPMAR
1110 1120 1130 1140 1150
YLSKNPSLIS KQYRMQHVYR PPDHSRSSLE PRKFGEIDFD IISKSSSESG
1160 1170 1180 1190 1200
FYDAESLKII DEILTVFPVF EKTNTFFILN HADILESVFN FTNIDKAQRP
1210 1220 1230 1240 1250
LVSRMLSQVG FARSFKEVKN ELKAQLNISS TALNDLELFD FRLDFEAAKK
1260 1270 1280 1290 1300
RLYKLMIDSP HLKKIEDSLS HISKVLSYLK PLEVARNVVI SPLSNYNSAF
1310 1320 1330 1340 1350
YKGGIMFHAV YDDGSSRNMI AAGGRYDTLI SFFARPSGKK SSNTRKAVGF
1360 1370 1380 1390 1400
NLAWETIFGI AQNYFKLASG NRIKKRNRFL KDTAVDWKPS RCDVLISSFS
1410 1420 1430 1440 1450
NSLLDTIGVT ILNTLWKQNI KADMLRDCSS VDDVVTGAQQ DGIDWILLIK
1460 1470 1480 1490 1500
QQAYPLTNHK RKYKPLKIKK LSTNVDIDLD LDEFLTLYQQ ETGNKSLIND
1510 1520 1530 1540 1550
SLTLGDKADE FKRWDENSSA GSSQEGDIDD VVAGSTNNQK VIYVPNMATR
1560 1570 1580 1590 1600
SKKANKREKW VYEDAARNSS NMILHNLSNA PIITVDALRD ETLEIISITS
1610 1620 1630 1640 1650
LAQKEEWLRK VFGSGNNSTP RSFATSIYNN LSKEAHKGNR WAILYCHKTG

KSSVIDLQR
Length:1,659
Mass (Da):190,193
Last modified:September 5, 2006 - v3
Checksum:i1F56E4B046D52325
GO

Sequence cautioni

The sequence AAA34636 differs from that shown. Reason: Erroneous initiation.Curated
The sequence AAA34881 differs from that shown. Reason: Frameshift at positions 71, 218, 226, 271, 279, 370, 389, 432, 592, 605, 1052, 1125, 1197, 1255, 1331 and 1428.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti70M → I in AAA34881 (PubMed:3290651).Curated1
Sequence conflicti220 – 226TIKAKLP → NYKGKIA in AAA34881 (PubMed:3290651).Curated7
Sequence conflicti271 – 279LMSSEMMEN → YVFSNHGKS in AAA34881 (PubMed:3290651).Curated9
Sequence conflicti374M → I in AAA34881 (PubMed:3290651).Curated1
Sequence conflicti392K → Q in AAA34881 (PubMed:3290651).Curated1
Sequence conflicti395N → S in AAA34881 (PubMed:3290651).Curated1
Sequence conflicti407F → C in AAA34881 (PubMed:3290651).Curated1
Sequence conflicti411 – 413IPK → MPE in AAA34881 (PubMed:3290651).Curated3
Sequence conflicti475I → M in AAA34881 (PubMed:3290651).Curated1
Sequence conflicti589P → A in AAA34881 (PubMed:3290651).Curated1
Sequence conflicti604 – 605VL → FS in AAA34881 (PubMed:3290651).Curated2
Sequence conflicti622S → T in AAA34881 (PubMed:3290651).Curated1
Sequence conflicti640 – 641IL → MI in AAA34881 (PubMed:3290651).Curated2
Sequence conflicti727F → C in AAA34881 (PubMed:3290651).Curated1
Sequence conflicti839M → K in AAA34881 (PubMed:3290651).Curated1
Sequence conflicti954E → Q in AAA34881 (PubMed:3290651).Curated1
Sequence conflicti1144K → E in AAA34881 (PubMed:3290651).Curated1
Sequence conflicti1328 – 1331TLIS → RFHT in AAA34881 (PubMed:3290651).Curated4
Sequence conflicti1348V → A in AAA34881 (PubMed:3290651).Curated1
Sequence conflicti1356T → I in AAA34881 (PubMed:3290651).Curated1
Sequence conflicti1434V → I in AAA34881 (PubMed:3290651).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M27082 Genomic DNA Translation: AAA34636.1 Different initiation.
U51030 Genomic DNA Translation: AAB64461.1
M20487 Genomic DNA Translation: AAA34881.1 Sequence problems.
BK006938 Genomic DNA Translation: DAA12123.1
PIRiS70139 OKBYN2
RefSeqiNP_010569.3, NM_001180591.3

Genome annotation databases

EnsemblFungiiYDR283C; YDR283C; YDR283C
GeneIDi851877
KEGGisce:YDR283C

Similar proteinsi

Entry informationi

Entry nameiGCN2_YEAST
AccessioniPrimary (citable) accession number: P15442
Secondary accession number(s): D6VSR3
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: September 5, 2006
Last modified: May 23, 2018
This is version 206 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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