Q9NIV1 · E2AK3_DROME
- ProteinEukaryotic translation initiation factor 2-alpha kinase
- GenePEK
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids1162 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Phosphorylates the alpha subunit of eukaryotic translation-initiation factor 2 (EIF2), leading to its inactivation and thus to a rapid reduction of translational initiation and repression of global protein synthesis.
Catalytic activity
- ATP + L-seryl-[protein] = ADP + H+ + O-phospho-L-seryl-[protein]
Activity regulation
Perturbation in protein folding in the endoplasmic reticulum (ER) promotes reversible dissociation from HSPA5/BIP and oligomerization, resulting in transautophosphorylation and kinase activity induction.
Features
Showing features for binding site, active site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | endoplasmic reticulum | |
Cellular Component | endoplasmic reticulum membrane | |
Cellular Component | nucleus | |
Molecular Function | ATP binding | |
Molecular Function | eukaryotic translation initiation factor 2alpha kinase activity | |
Molecular Function | protein serine kinase activity | |
Biological Process | PERK-mediated unfolded protein response | |
Biological Process | positive regulation of autophagy | |
Biological Process | positive regulation of JNK cascade | |
Biological Process | regulation of G2/M transition of mitotic cell cycle |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameEukaryotic translation initiation factor 2-alpha kinase
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Endopterygota > Diptera > Brachycera > Muscomorpha > Ephydroidea > Drosophilidae > Drosophila > Sophophora
Accessions
- Primary accessionQ9NIV1
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Endoplasmic reticulum membrane ; Single-pass type I membrane protein
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 40-537 | Lumenal | ||||
Sequence: GHPTTDSELQTAGSPRPPGLEHCVDQEERRVARRLLYISTLDGRLSALDIAKSGKLRWSVPTGPGPLISSSIHRLELTNNGQFVRMIPSLSGGIYKFDGDSIDPIPITAEHLLSSSAKFSDDLVISGGKETRSYGVSVRTGQLLYECSLNGCVNSTEEGLAIDDTIREPDEEDQLEDGEQLRDEAGYIVRHDPLLDDVIIVRRQTQTVRAVESRTGVERWNFSVGQHELDLVRPSECQLQPRDELELAVLDVDIKVVVPEGIICAFSKSEPQTMLWKYKFDHPIVSAWNTNADDELQPIDLFSSAQWLWDQDENDTELPNAPQSPPSIYLGMYDKQLYIQESIRLRQEIMDQTKVYQQLTGDTSLMPRIPWKPISASSKSLVIFRKDQEDPEMIAEGAVAQGGELVPYDDENFAVAAQSVLNASEFVNGNGFYFYTTGDLNGPQECSTQNNPTDLPAITAPTSPTNATSEGTEATGNHSVNDDLGFSLDDIDAPVKVV | ||||||
Transmembrane | 538-558 | Helical | ||||
Sequence: ILSLWFWWKEIVVIAFTSAVI | ||||||
Topological domain | 559-1162 | Cytoplasmic | ||||
Sequence: LNIFMGQRNQRVEREYLVIERHVPVQTAIEATEASTQALLGPVVPMQRPGNRFSFPPGQANQRTISESTTHSGEHYTSRFQSDFELMQCLGRGGFGVVFEAKNKLDENRYAIKRITLPNKESSRQRVLREARTLASCEHHNIVRYFHSWTETPPTGWQEEEDRKLLAHELSTSIQIETPDDSTMPSLTEQLKEKRQQQLLSWVSDAANSTACSHDFHLPGESSLKNIREEYDYDEEEDSLIEFRSESQSAALRAEEEDDTDDDYEEDEEQQGDHEKRHRSSVSIDIHSASFDLKNINYSQHQLVSNSFQIESVRPKSSGSDDANDDNKARRKPLTLALAQNHNNNQNGSQPTPSSATILNGTVAKPSKVYLYIQMQLCRKESLRDWLRDNRSETRAAHIGDIFHQIVDAVDYVHLKGLIHRDLKPSNIFFSQDGQIKIGDFGLVTDMADIPNLVAKCGDQSGLPSCARHTQQVGTHLYMSPEQLLGQHYDYKVDIYSLGLIFFELHVYFSTEMERIKTLRSLRDGQYPKDFAVNYPQQYDLLQQMLSAQPEQRPQTKQLKSQLRNILQLPHLLSEGQSEQAELAERARRLSRSRTFSSSSEPHQ |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for signal, chain, glycosylation, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-39 | |||||
Sequence: MQDDLDGIVRHRRRSLSFLQIVTLTMAGLVAFDPAQVLA | ||||||
Chain | PRO_0000024326 | 40-1162 | Eukaryotic translation initiation factor 2-alpha kinase | |||
Sequence: GHPTTDSELQTAGSPRPPGLEHCVDQEERRVARRLLYISTLDGRLSALDIAKSGKLRWSVPTGPGPLISSSIHRLELTNNGQFVRMIPSLSGGIYKFDGDSIDPIPITAEHLLSSSAKFSDDLVISGGKETRSYGVSVRTGQLLYECSLNGCVNSTEEGLAIDDTIREPDEEDQLEDGEQLRDEAGYIVRHDPLLDDVIIVRRQTQTVRAVESRTGVERWNFSVGQHELDLVRPSECQLQPRDELELAVLDVDIKVVVPEGIICAFSKSEPQTMLWKYKFDHPIVSAWNTNADDELQPIDLFSSAQWLWDQDENDTELPNAPQSPPSIYLGMYDKQLYIQESIRLRQEIMDQTKVYQQLTGDTSLMPRIPWKPISASSKSLVIFRKDQEDPEMIAEGAVAQGGELVPYDDENFAVAAQSVLNASEFVNGNGFYFYTTGDLNGPQECSTQNNPTDLPAITAPTSPTNATSEGTEATGNHSVNDDLGFSLDDIDAPVKVVILSLWFWWKEIVVIAFTSAVILNIFMGQRNQRVEREYLVIERHVPVQTAIEATEASTQALLGPVVPMQRPGNRFSFPPGQANQRTISESTTHSGEHYTSRFQSDFELMQCLGRGGFGVVFEAKNKLDENRYAIKRITLPNKESSRQRVLREARTLASCEHHNIVRYFHSWTETPPTGWQEEEDRKLLAHELSTSIQIETPDDSTMPSLTEQLKEKRQQQLLSWVSDAANSTACSHDFHLPGESSLKNIREEYDYDEEEDSLIEFRSESQSAALRAEEEDDTDDDYEEDEEQQGDHEKRHRSSVSIDIHSASFDLKNINYSQHQLVSNSFQIESVRPKSSGSDDANDDNKARRKPLTLALAQNHNNNQNGSQPTPSSATILNGTVAKPSKVYLYIQMQLCRKESLRDWLRDNRSETRAAHIGDIFHQIVDAVDYVHLKGLIHRDLKPSNIFFSQDGQIKIGDFGLVTDMADIPNLVAKCGDQSGLPSCARHTQQVGTHLYMSPEQLLGQHYDYKVDIYSLGLIFFELHVYFSTEMERIKTLRSLRDGQYPKDFAVNYPQQYDLLQQMLSAQPEQRPQTKQLKSQLRNILQLPHLLSEGQSEQAELAERARRLSRSRTFSSSSEPHQ | ||||||
Glycosylation | 193 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 260 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 353 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 461 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 505 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 516 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Modified residue | 624 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 797 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 818 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 1028 | Phosphothreonine | ||||
Sequence: T |
Post-translational modification
Autophosphorylated.
N-glycosylated.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Structure
Family & Domains
Features
Showing features for region, domain, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 498-517 | Disordered | ||||
Sequence: TAPTSPTNATSEGTEATGNH | ||||||
Domain | 642-1130 | Protein kinase | ||||
Sequence: FELMQCLGRGGFGVVFEAKNKLDENRYAIKRITLPNKESSRQRVLREARTLASCEHHNIVRYFHSWTETPPTGWQEEEDRKLLAHELSTSIQIETPDDSTMPSLTEQLKEKRQQQLLSWVSDAANSTACSHDFHLPGESSLKNIREEYDYDEEEDSLIEFRSESQSAALRAEEEDDTDDDYEEDEEQQGDHEKRHRSSVSIDIHSASFDLKNINYSQHQLVSNSFQIESVRPKSSGSDDANDDNKARRKPLTLALAQNHNNNQNGSQPTPSSATILNGTVAKPSKVYLYIQMQLCRKESLRDWLRDNRSETRAAHIGDIFHQIVDAVDYVHLKGLIHRDLKPSNIFFSQDGQIKIGDFGLVTDMADIPNLVAKCGDQSGLPSCARHTQQVGTHLYMSPEQLLGQHYDYKVDIYSLGLIFFELHVYFSTEMERIKTLRSLRDGQYPKDFAVNYPQQYDLLQQMLSAQPEQRPQTKQLKSQLRNILQLPHL | ||||||
Region | 801-839 | Disordered | ||||
Sequence: FRSESQSAALRAEEEDDTDDDYEEDEEQQGDHEKRHRSS | ||||||
Compositional bias | 813-827 | Acidic residues | ||||
Sequence: EEEDDTDDDYEEDEE | ||||||
Region | 1135-1162 | Disordered | ||||
Sequence: QSEQAELAERARRLSRSRTFSSSSEPHQ |
Domain
The lumenal domain senses perturbations in protein folding in the ER, probably through reversible interaction with HSPA5/BIP.
Sequence similarities
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length1,162
- Mass (Da)131,039
- Last updated2003-08-15 v2
- ChecksumF3D6B4C87159D95B
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A0B4KG56 | A0A0B4KG56_DROME | PEK | 1099 | ||
A0A0B4KGJ5 | A0A0B4KGJ5_DROME | PEK | 1110 |
Features
Showing features for sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 629 | in Ref. 1; AAF61200 | ||||
Sequence: H → D | ||||||
Compositional bias | 813-827 | Acidic residues | ||||
Sequence: EEEDDTDDDYEEDEE |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF193340 EMBL· GenBank· DDBJ | AAF61200.1 EMBL· GenBank· DDBJ | mRNA | ||
AJ313085 EMBL· GenBank· DDBJ | CAC85207.1 EMBL· GenBank· DDBJ | mRNA | ||
AE014297 EMBL· GenBank· DDBJ | AAF52028.2 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY094831 EMBL· GenBank· DDBJ | AAM11184.1 EMBL· GenBank· DDBJ | mRNA |