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Protein

Eukaryotic translation initiation factor 2-alpha kinase 3

Gene

EIF2AK3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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/EIF2S1) on 'Ser-52' during the unfolded protein response (UPR) and in response to low amino acid availability. Converts phosphorylated eIF-2-alpha/EIF2S1 either in a global protein synthesis inhibitor, leading to a reduced overall utilization of amino acids, or to a translation initiation activator of specific mRNAs, such as the transcriptional activator ATF4, and hence allowing ATF4-mediated reprogramming of amino acid biosynthetic gene expression to alleviate nutrient depletion. Serves as a critical effector of unfolded protein response (UPR)-induced G1 growth arrest due to the loss of cyclin-D1 (CCND1). Involved in control of mitochondrial morphology and function.By similarity

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulationi

Perturbation in protein folding in the endoplasmic reticulum (ER) promotes reversible dissociation from HSPA5/BIP and oligomerization, resulting in transautophosphorylation and kinase activity induction.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei622ATPPROSITE-ProRule annotation1
Active sitei937Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi599 – 607ATPPROSITE-ProRule annotation9

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • enzyme binding Source: UniProtKB
  • eukaryotic translation initiation factor 2alpha kinase activity Source: UniProtKB
  • protein homodimerization activity Source: ParkinsonsUK-UCL
  • protein kinase activity Source: ProtInc
  • protein phosphatase binding Source: UniProtKB
  • protein serine/threonine kinase activity Source: UniProtKB

GO - Biological processi

  • activation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
  • angiogenesis Source: ParkinsonsUK-UCL
  • bone mineralization Source: UniProtKB
  • calcium-mediated signaling Source: UniProtKB
  • cellular response to amino acid starvation Source: UniProtKB
  • cellular response to cold Source: UniProtKB
  • cellular response to glucose starvation Source: ParkinsonsUK-UCL
  • chondrocyte development Source: UniProtKB
  • eiF2alpha phosphorylation in response to endoplasmic reticulum stress Source: UniProtKB
  • endocrine pancreas development Source: UniProtKB
  • endoplasmic reticulum organization Source: UniProtKB
  • endoplasmic reticulum unfolded protein response Source: UniProtKB
  • ER overload response Source: UniProtKB
  • insulin-like growth factor receptor signaling pathway Source: UniProtKB
  • insulin secretion Source: UniProtKB
  • negative regulation of myelination Source: UniProtKB
  • negative regulation of translation Source: UniProtKB
  • negative regulation of translational initiation in response to stress Source: UniProtKB
  • ossification Source: UniProtKB
  • peptidyl-serine phosphorylation Source: ParkinsonsUK-UCL
  • PERK-mediated unfolded protein response Source: ParkinsonsUK-UCL
  • positive regulation of gene expression Source: ParkinsonsUK-UCL
  • positive regulation of protein localization to nucleus Source: ParkinsonsUK-UCL
  • positive regulation of transcription from RNA polymerase I promoter Source: ParkinsonsUK-UCL
  • positive regulation of vascular endothelial growth factor production Source: ParkinsonsUK-UCL
  • protein autophosphorylation Source: UniProtKB
  • protein homooligomerization Source: UniProtKB
  • protein phosphorylation Source: UniProtKB
  • regulation of endoplasmic reticulum stress-induced eIF2 alpha phosphorylation Source: UniProtKB
  • regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway Source: ParkinsonsUK-UCL
  • regulation of translational initiation by eIF2 alpha phosphorylation Source: ParkinsonsUK-UCL
  • response to endoplasmic reticulum stress Source: BHF-UCL
  • response to manganese-induced endoplasmic reticulum stress Source: Ensembl
  • skeletal system development Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Stress response, Translation regulation, Unfolded protein response

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciZFISH:HS10447-MONOMER.
ReactomeiR-HSA-381042. PERK regulates gene expression.
SignaLinkiQ9NZJ5.
SIGNORiQ9NZJ5.

Names & Taxonomyi

Protein namesi
Recommended name:
Eukaryotic translation initiation factor 2-alpha kinase 3 (EC:2.7.11.1)
Alternative name(s):
PRKR-like endoplasmic reticulum kinase
Pancreatic eIF2-alpha kinase
Short name:
HsPEK
Gene namesi
Name:EIF2AK3
Synonyms:PEK, PERK
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:3255. EIF2AK3.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini30 – 514LumenalSequence analysisAdd BLAST485
Transmembranei515 – 535HelicalSequence analysisAdd BLAST21
Topological domaini536 – 1116CytoplasmicSequence analysisAdd BLAST581

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • endoplasmic reticulum Source: UniProtKB
  • endoplasmic reticulum membrane Source: UniProtKB
  • integral component of endoplasmic reticulum membrane Source: ParkinsonsUK-UCL
  • membrane Source: UniProtKB
  • perinuclear region of cytoplasm Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Involvement in diseasei

Wolcott-Rallison syndrome (WRS)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA rare autosomal recessive disorder, characterized by permanent neonatal or early infancy insulin-dependent diabetes and, at a later age, epiphyseal dysplasia, osteoporosis, growth retardation and other multisystem manifestations, such as hepatic and renal dysfunctions, mental retardation and cardiovascular abnormalities.
See also OMIM:226980
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_011408588R → Q in WRS. 1 PublicationCorresponds to variant rs121908569dbSNPEnsembl.1

Keywords - Diseasei

Diabetes mellitus, Disease mutation

Organism-specific databases

DisGeNETi9451.
MalaCardsiEIF2AK3.
MIMi226980. phenotype.
OpenTargetsiENSG00000172071.
Orphaneti1667. Wolcott-Rallison syndrome.
PharmGKBiPA27687.

Chemistry databases

ChEMBLiCHEMBL6030.
GuidetoPHARMACOLOGYi2017.

Polymorphism and mutation databases

BioMutaiEIF2AK3.
DMDMi296439367.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 29Sequence analysisAdd BLAST29
ChainiPRO_000002432230 – 1116Eukaryotic translation initiation factor 2-alpha kinase 3Add BLAST1087

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi258N-linked (GlcNAc...)Sequence analysis1
Modified residuei619Phosphotyrosine1 Publication1
Modified residuei715PhosphoserineCombined sources1
Modified residuei982PhosphothreonineBy similarity1
Modified residuei1094PhosphoserineCombined sources1

Post-translational modificationi

Oligomerization of the N-terminal ER luminal domain by ER stress promotes PERK trans-autophosphorylation of the C-terminal cytoplasmic kinase domain at multiple residues including Thr-982 on the kinase activation loop (By similarity). Autophosphorylated. Phosphorylated at Tyr-619 following endoplasmic reticulum stress, leading to activate its tyrosine-protein kinase activity. Dephosphorylated by PTPN1/TP1B, leading to inactivate its enzyme activity.By similarity1 Publication
N-glycosylated.By similarity
ADP-ribosylated by PARP16 upon ER stress, which increases kinase activity.

Keywords - PTMi

ADP-ribosylation, Glycoprotein, Phosphoprotein

Proteomic databases

EPDiQ9NZJ5.
MaxQBiQ9NZJ5.
PaxDbiQ9NZJ5.
PeptideAtlasiQ9NZJ5.
PRIDEiQ9NZJ5.

PTM databases

iPTMnetiQ9NZJ5.
PhosphoSitePlusiQ9NZJ5.

Expressioni

Tissue specificityi

Ubiquitous. A high level expression is seen in secretory tissues.

Inductioni

By endoplasmic reticulum stress.

Gene expression databases

BgeeiENSG00000172071.
CleanExiHS_EIF2AK3.
ExpressionAtlasiQ9NZJ5. baseline and differential.
GenevisibleiQ9NZJ5. HS.

Organism-specific databases

HPAiCAB009204.
HPA015737.

Interactioni

Subunit structurei

Forms dimers with HSPA5/BIP in resting cells. Oligomerizes in ER-stressed cells. Interacts with DNAJC3 and MFN2 (By similarity). Interacts with TMEM33 (PubMed:26268696).By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-766076,EBI-766076
HSPA5P110214EBI-766076,EBI-354921

GO - Molecular functioni

  • enzyme binding Source: UniProtKB
  • protein homodimerization activity Source: ParkinsonsUK-UCL
  • protein phosphatase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi114840. 42 interactors.
IntActiQ9NZJ5. 8 interactors.
STRINGi9606.ENSP00000307235.

Chemistry databases

BindingDBiQ9NZJ5.

Structurei

Secondary structure

11116
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi105 – 110Combined sources6
Beta strandi113 – 118Combined sources6
Turni120 – 123Combined sources4
Beta strandi126 – 131Combined sources6
Beta strandi137 – 139Combined sources3
Beta strandi152 – 158Combined sources7
Beta strandi161 – 164Combined sources4
Beta strandi166 – 169Combined sources4
Beta strandi171 – 173Combined sources3
Helixi178 – 182Combined sources5
Beta strandi193 – 204Combined sources12
Beta strandi207 – 209Combined sources3
Beta strandi215 – 217Combined sources3
Beta strandi220 – 222Combined sources3
Beta strandi237 – 248Combined sources12
Turni250 – 252Combined sources3
Beta strandi255 – 267Combined sources13
Beta strandi308 – 310Combined sources3
Turni314 – 317Combined sources4
Beta strandi321 – 323Combined sources3
Turni324 – 326Combined sources3
Beta strandi339 – 346Combined sources8
Beta strandi349 – 352Combined sources4
Helixi375 – 383Combined sources9
Beta strandi387 – 390Combined sources4
Beta strandi392 – 398Combined sources7
Helixi588 – 592Combined sources5
Beta strandi593 – 602Combined sources10
Beta strandi605 – 612Combined sources8
Turni613 – 615Combined sources3
Beta strandi618 – 625Combined sources8
Helixi630 – 644Combined sources15
Beta strandi654 – 660Combined sources7
Beta strandi883 – 889Combined sources7
Helixi896 – 901Combined sources6
Helixi906 – 908Combined sources3
Helixi911 – 930Combined sources20
Helixi940 – 942Combined sources3
Beta strandi943 – 945Combined sources3
Beta strandi951 – 953Combined sources3
Helixi993 – 996Combined sources4
Helixi1004 – 1018Combined sources15
Helixi1024 – 1035Combined sources12
Helixi1041 – 1046Combined sources6
Helixi1048 – 1057Combined sources10
Helixi1062 – 1064Combined sources3
Helixi1068 – 1072Combined sources5
Helixi1075 – 1077Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4G31X-ray2.28A588-1093[»]
4G34X-ray2.70A588-1093[»]
4M7IX-ray2.34A588-1093[»]
4X7HX-ray2.00A575-1094[»]
4X7JX-ray2.30A575-1094[»]
4X7KX-ray1.80A575-1094[»]
4X7LX-ray1.90A575-1094[»]
4X7NX-ray2.35A575-1094[»]
4X7OX-ray2.65A575-1094[»]
4YZSX-ray3.14A/B104-403[»]
ProteinModelPortaliQ9NZJ5.
SMRiQ9NZJ5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini593 – 1077Protein kinasePROSITE-ProRule annotationAdd BLAST485

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi49 – 52Poly-Ala4

Domaini

The lumenal domain senses perturbations in protein folding in the ER, probably through reversible interaction with HSPA5/BIP.By similarity

Sequence similaritiesi

Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. GCN2 subfamily.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG1033. Eukaryota.
ENOG410XS0B. LUCA.
GeneTreeiENSGT00530000062984.
HOVERGENiHBG051431.
InParanoidiQ9NZJ5.
KOiK08860.
OMAiKWKPLIH.
OrthoDBiEOG091G01X1.
PhylomeDBiQ9NZJ5.
TreeFamiTF101511.

Family and domain databases

Gene3Di2.140.10.10. 1 hit.
InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR027295. Quinoprotein_ADH-like_fam.
IPR011047. Quinoprotein_ADH-like_supfam.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 2 hits.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF50998. SSF50998. 2 hits.
SSF56112. SSF56112. 2 hits.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9NZJ5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MERAISPGLL VRALLLLLLL LGLAARTVAA GRARGLPAPT AEAAFGLGAA
60 70 80 90 100
AAPTSATRVP AAGAVAAAEV TVEDAEALPA AAGEQEPRGP EPDDETELRP
110 120 130 140 150
RGRSLVIIST LDGRIAALDP ENHGKKQWDL DVGSGSLVSS SLSKPEVFGN
160 170 180 190 200
KMIIPSLDGA LFQWDQDRES METVPFTVES LLESSYKFGD DVVLVGGKSL
210 220 230 240 250
TTYGLSAYSG KVRYICSALG CRQWDSDEME QEEDILLLQR TQKTVRAVGP
260 270 280 290 300
RSGNEKWNFS VGHFELRYIP DMETRAGFIE STFKPNENTE ESKIISDVEE
310 320 330 340 350
QEAAIMDIVI KVSVADWKVM AFSKKGGHLE WEYQFCTPIA SAWLLKDGKV
360 370 380 390 400
IPISLFDDTS YTSNDDVLED EEDIVEAARG ATENSVYLGM YRGQLYLQSS
410 420 430 440 450
VRISEKFPSS PKALESVTNE NAIIPLPTIK WKPLIHSPSR TPVLVGSDEF
460 470 480 490 500
DKCLSNDKFS HEEYSNGALS ILQYPYDNGY YLPYYKRERN KRSTQITVRF
510 520 530 540 550
LDNPHYNKNI RKKDPVLLLH WWKEIVATIL FCIIATTFIV RRLFHPHPHR
560 570 580 590 600
QRKESETQCQ TENKYDSVSG EANDSSWNDI KNSGYISRYL TDFEPIQCLG
610 620 630 640 650
RGGFGVVFEA KNKVDDCNYA IKRIRLPNRE LAREKVMREV KALAKLEHPG
660 670 680 690 700
IVRYFNAWLE APPEKWQEKM DEIWLKDEST DWPLSSPSPM DAPSVKIRRM
710 720 730 740 750
DPFATKEHIE IIAPSPQRSR SFSVGISCDQ TSSSESQFSP LEFSGMDHED
760 770 780 790 800
ISESVDAAYN LQDSCLTDCD VEDGTMDGND EGHSFELCPS EASPYVRSRE
810 820 830 840 850
RTSSSIVFED SGCDNASSKE EPKTNRLHIG NHCANKLTAF KPTSSKSSSE
860 870 880 890 900
ATLSISPPRP TTLSLDLTKN TTEKLQPSSP KVYLYIQMQL CRKENLKDWM
910 920 930 940 950
NGRCTIEERE RSVCLHIFLQ IAEAVEFLHS KGLMHRDLKP SNIFFTMDDV
960 970 980 990 1000
VKVGDFGLVT AMDQDEEEQT VLTPMPAYAR HTGQVGTKLY MSPEQIHGNS
1010 1020 1030 1040 1050
YSHKVDIFSL GLILFELLYP FSTQMERVRT LTDVRNLKFP PLFTQKYPCE
1060 1070 1080 1090 1100
YVMVQDMLSP SPMERPEAIN IIENAVFEDL DFPGKTVLRQ RSRSLSSSGT
1110
KHSRQSNNSH SPLPSN
Length:1,116
Mass (Da):125,216
Last modified:May 18, 2010 - v3
Checksum:i95FEB5DAE8D3D452
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti14Missing in AAD19961 (PubMed:10026192).Curated1
Sequence conflicti14Missing in AAF61199 (PubMed:10677345).Curated1
Sequence conflicti14Missing in AAF91480 (PubMed:10932183).Curated1
Sequence conflicti14Missing in BAG37696 (PubMed:14702039).Curated1
Sequence conflicti14Missing in AAI26357 (PubMed:15489334).Curated1
Sequence conflicti490N → H in AAF61199 (PubMed:10677345).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_011409136S → C.2 PublicationsCorresponds to variant rs867529dbSNPEnsembl.1
Natural variantiVAR_011410166Q → R.3 PublicationsCorresponds to variant rs13045dbSNPEnsembl.1
Natural variantiVAR_040477566D → V.1 PublicationCorresponds to variant rs55791823dbSNPEnsembl.1
Natural variantiVAR_011408588R → Q in WRS. 1 PublicationCorresponds to variant rs121908569dbSNPEnsembl.1
Natural variantiVAR_011411704A → S.3 PublicationsCorresponds to variant rs1805165dbSNPEnsembl.1
Natural variantiVAR_040478716P → L.1 PublicationCorresponds to variant rs55861585dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF110146 mRNA. Translation: AAD19961.1.
AF193339 mRNA. Translation: AAF61199.1.
AF284615
, AF284604, AF284605, AF284606, AF284607, AF284608, AF284609, AF284610, AF284611, AF284612, AF284613, AF284614 Genomic DNA. Translation: AAF91480.1.
AK315287 mRNA. Translation: BAG37696.1.
AC062029 Genomic DNA. Translation: AAY14777.1.
AC104134 Genomic DNA. Translation: AAY24331.1.
BC126354 mRNA. Translation: AAI26355.1.
BC126356 mRNA. Translation: AAI26357.1.
CCDSiCCDS33241.1.
RefSeqiNP_004827.4. NM_004836.6.
UniGeneiHs.591589.

Genome annotation databases

EnsembliENST00000303236; ENSP00000307235; ENSG00000172071.
GeneIDi9451.
KEGGihsa:9451.
UCSCiuc002stc.5. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF110146 mRNA. Translation: AAD19961.1.
AF193339 mRNA. Translation: AAF61199.1.
AF284615
, AF284604, AF284605, AF284606, AF284607, AF284608, AF284609, AF284610, AF284611, AF284612, AF284613, AF284614 Genomic DNA. Translation: AAF91480.1.
AK315287 mRNA. Translation: BAG37696.1.
AC062029 Genomic DNA. Translation: AAY14777.1.
AC104134 Genomic DNA. Translation: AAY24331.1.
BC126354 mRNA. Translation: AAI26355.1.
BC126356 mRNA. Translation: AAI26357.1.
CCDSiCCDS33241.1.
RefSeqiNP_004827.4. NM_004836.6.
UniGeneiHs.591589.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4G31X-ray2.28A588-1093[»]
4G34X-ray2.70A588-1093[»]
4M7IX-ray2.34A588-1093[»]
4X7HX-ray2.00A575-1094[»]
4X7JX-ray2.30A575-1094[»]
4X7KX-ray1.80A575-1094[»]
4X7LX-ray1.90A575-1094[»]
4X7NX-ray2.35A575-1094[»]
4X7OX-ray2.65A575-1094[»]
4YZSX-ray3.14A/B104-403[»]
ProteinModelPortaliQ9NZJ5.
SMRiQ9NZJ5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114840. 42 interactors.
IntActiQ9NZJ5. 8 interactors.
STRINGi9606.ENSP00000307235.

Chemistry databases

BindingDBiQ9NZJ5.
ChEMBLiCHEMBL6030.
GuidetoPHARMACOLOGYi2017.

PTM databases

iPTMnetiQ9NZJ5.
PhosphoSitePlusiQ9NZJ5.

Polymorphism and mutation databases

BioMutaiEIF2AK3.
DMDMi296439367.

Proteomic databases

EPDiQ9NZJ5.
MaxQBiQ9NZJ5.
PaxDbiQ9NZJ5.
PeptideAtlasiQ9NZJ5.
PRIDEiQ9NZJ5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000303236; ENSP00000307235; ENSG00000172071.
GeneIDi9451.
KEGGihsa:9451.
UCSCiuc002stc.5. human.

Organism-specific databases

CTDi9451.
DisGeNETi9451.
GeneCardsiEIF2AK3.
H-InvDBHIX0023925.
HIX0030379.
HGNCiHGNC:3255. EIF2AK3.
HPAiCAB009204.
HPA015737.
MalaCardsiEIF2AK3.
MIMi226980. phenotype.
604032. gene.
neXtProtiNX_Q9NZJ5.
OpenTargetsiENSG00000172071.
Orphaneti1667. Wolcott-Rallison syndrome.
PharmGKBiPA27687.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1033. Eukaryota.
ENOG410XS0B. LUCA.
GeneTreeiENSGT00530000062984.
HOVERGENiHBG051431.
InParanoidiQ9NZJ5.
KOiK08860.
OMAiKWKPLIH.
OrthoDBiEOG091G01X1.
PhylomeDBiQ9NZJ5.
TreeFamiTF101511.

Enzyme and pathway databases

BioCyciZFISH:HS10447-MONOMER.
ReactomeiR-HSA-381042. PERK regulates gene expression.
SignaLinkiQ9NZJ5.
SIGNORiQ9NZJ5.

Miscellaneous databases

ChiTaRSiEIF2AK3. human.
GeneWikiiEIF2AK3.
GenomeRNAii9451.
PROiQ9NZJ5.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000172071.
CleanExiHS_EIF2AK3.
ExpressionAtlasiQ9NZJ5. baseline and differential.
GenevisibleiQ9NZJ5. HS.

Family and domain databases

Gene3Di2.140.10.10. 1 hit.
InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR027295. Quinoprotein_ADH-like_fam.
IPR011047. Quinoprotein_ADH-like_supfam.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 2 hits.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF50998. SSF50998. 2 hits.
SSF56112. SSF56112. 2 hits.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiE2AK3_HUMAN
AccessioniPrimary (citable) accession number: Q9NZJ5
Secondary accession number(s): A0AVH1
, A0AVH2, B2RCU9, O95846, Q53QY0, Q53SB1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: May 18, 2010
Last modified: November 30, 2016
This is version 168 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  7. SIMILARITY comments
    Index of protein domains and families

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.