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Protein

eIF-2-alpha kinase GCN2

Gene

EIF2AK4

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' in response to low amino acid availability (PubMed:25329545). Plays a role as an activator of the integrated stress response (ISR) required for adapatation to amino acid starvation. Converts phosphorylated eIF-2-alpha/EIF2S1 either to a competitive inhibitor of the 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 ATF4, and hence allowing ATF4-mediated reprogramming of amino acid biosynthetic gene expression to alleviate nutrient depletion. Binds uncharged tRNAs (By similarity). Involved in cell cycle arrest by promoting cyclin D1 mRNA translation repression after the unfolded protein response pathway (UPR) activation or cell cycle inhibitor CDKN1A/p21 mRNA translation activation in response to amino acid deprivation (PubMed:26102367). Plays a role in the consolidation of synaptic plasticity, learning as well as formation of long-term memory. Plays a role in neurite outgrowth inhibition. Plays a proapoptotic role in response to glucose deprivation. Promotes global cellular protein synthesis repression in response to UV irradiation independently of the stress-activated protein kinase/c-Jun N-terminal kinase (SAPK/JNK) and p38 MAPK signaling pathways (By similarity). Plays a role in the antiviral response against alphavirus infection; impairs early viral mRNA translation of the incoming genomic virus RNA, thus preventing alphavirus replication (By similarity).By similarity2 Publications
(Microbial infection) Plays a role in modulating the adaptive immune response to yellow fever virus infection; promotes dendritic cells to initiate autophagy and antigene presentation to both CD4+ and CD8+ T-cells under amino acid starvation (PubMed:24310610).1 Publication

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei619ATPPROSITE-ProRule annotation1
Active sitei848Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi596 – 604ATPPROSITE-ProRule annotation9

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Activator, Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Activation of host autophagy by virus, Adaptive immunity, Antiviral defense, Cell cycle, Growth arrest, Host-virus interaction, Immunity, Neurogenesis, Stress response, Translation regulation

Keywords - Ligandi

ATP-binding, Nucleotide-binding, RNA-binding, tRNA-binding

Enzyme and pathway databases

BioCyciZFISH:HS05227-MONOMER.
SignaLinkiQ9P2K8.
SIGNORiQ9P2K8.

Names & Taxonomyi

Protein namesi
Recommended name:
eIF-2-alpha kinase GCN2By similarity (EC:2.7.11.1By similarity)
Alternative name(s):
Eukaryotic translation initiation factor 2-alpha kinase 4Imported
GCN2-like protein
Gene namesi
Name:EIF2AK4Imported
Synonyms:GCN2, KIAA1338
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 15

Organism-specific databases

HGNCiHGNC:19687. EIF2AK4.

Subcellular locationi

  • Cytoplasm By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Involvement in diseasei

Pulmonary venoocclusive disease 2, autosomal recessive (PVOD2)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA disease characterized by widespread fibrous obstruction and intimal thickening of septal veins and preseptal venules, a low diffusing capacity for carbon monoxide, occult alveolar hemorrhage, and nodular ground-glass opacities, septal lines and lymph node enlargement showed by high-resolution computed tomography of the chest. It is frequently associated with pulmonary capillary dilatation and proliferation, and is a rare and devastating cause of pulmonary hypertension.
See also OMIM:234810
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_070990585R → Q in PVOD2. 1 PublicationCorresponds to variant rs587777106dbSNPEnsembl.1
Natural variantiVAR_070991643L → R in PVOD2. 1 PublicationCorresponds to variant rs757852728dbSNPEnsembl.1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNETi440275.
MalaCardsiEIF2AK4.
MIMi234810. phenotype.
OpenTargetsiENSG00000128829.
Orphaneti199241. Pulmonary capillary hemangiomatosis.
31837. Pulmonary venoocclusive disease.
PharmGKBiPA134947616.

Chemistry databases

ChEMBLiCHEMBL5358.
GuidetoPHARMACOLOGYi2018.

Polymorphism and mutation databases

BioMutaiEIF2AK4.
DMDMi296439368.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000859471 – 1649eIF-2-alpha kinase GCN2Add BLAST1649

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei230PhosphoserineCombined sources1
Modified residuei667PhosphothreonineCombined sources1
Modified residuei871PhosphothreonineCombined sources1
Modified residuei899Phosphothreonine; by autocatalysisBy similarity1
Modified residuei904Phosphothreonine; by autocatalysisBy similarity1
Modified residuei1259N6-acetyllysineCombined sources1

Post-translational modificationi

Autophosphorylated; autophosphorylation on Thr-899 is increased upon amino acid starvation and in UV irradiation cells and inhibited in presence of IMPACT.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ9P2K8.
MaxQBiQ9P2K8.
PaxDbiQ9P2K8.
PeptideAtlasiQ9P2K8.
PRIDEiQ9P2K8.

PTM databases

iPTMnetiQ9P2K8.
PhosphoSitePlusiQ9P2K8.

Expressioni

Tissue specificityi

Widely expressed (PubMed:10504407). Expressed in lung, smooth muscle cells and macrophages (PubMed:24292273).2 Publications

Gene expression databases

BgeeiENSG00000128829.
CleanExiHS_EIF2AK4.
ExpressionAtlasiQ9P2K8. baseline and differential.
GenevisibleiQ9P2K8. HS.

Organism-specific databases

HPAiHPA011811.

Interactioni

Subunit structurei

Homodimer; homodimerization is important for kinase activation by uncharged tRNAs. Interacts with GCN1; this interaction stimulates EIF2AK4/GCN2 kinase activity and is impaired by IMPACT upon a variety of stress conditions, such as amino acid depletion, UV-C irradiation, proteasome inhibitor treatment and glucose deprivation. Interacts with DNAJC3; this interaction inhibits EIF2AK4/GCN2 kinase activity during endoplasmic reticulum (ER), hypothermic and amino acid-starving stress conditions.By similarity

Protein-protein interaction databases

BioGridi136426. 20 interactors.
IntActiQ9P2K8. 20 interactors.
STRINGi9606.ENSP00000263791.

Chemistry databases

BindingDBiQ9P2K8.

Structurei

3D structure databases

ProteinModelPortaliQ9P2K8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini25 – 137RWDPROSITE-ProRule annotationAdd BLAST113
Domaini296 – 539Protein kinase 1PROSITE-ProRule annotationAdd BLAST244
Domaini590 – 1001Protein kinase 2PROSITE-ProRule annotationAdd BLAST412

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1022 – 1493Histidyl-tRNA synthetase-likeAdd BLAST472

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili146 – 205Sequence analysisAdd BLAST60

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi484 – 491Poly-Leu8

Domaini

The histidyl-tRNA synthetase-like region and protein kinase domains are necessary for eIF-2-alpha kinase activity and eIF-2-alpha-mediated translational control. The histidyl-tRNA synthetase-like domain is necessary for binding to uncharged tRNAs. Kinase domain 1 is a degenerate kinase domain.By similarity

Sequence similaritiesi

Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. GCN2 subfamily.PROSITE-ProRule annotation
Contains 2 protein kinase domains.PROSITE-ProRule annotation
Contains 1 RWD domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, Repeat

Phylogenomic databases

eggNOGiKOG1035. Eukaryota.
COG0124. LUCA.
GeneTreeiENSGT00530000062984.
HOVERGENiHBG051432.
InParanoidiQ9P2K8.
KOiK16196.
OMAiKCVCLDD.
OrthoDBiEOG091G0NNL.
PhylomeDBiQ9P2K8.
TreeFamiTF101512.

Family and domain databases

Gene3Di3.10.110.10. 1 hit.
3.40.50.800. 1 hit.
InterProiIPR004154. Anticodon-bd.
IPR024435. HisRS-related_dom.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR006575. RWD-domain.
IPR008271. Ser/Thr_kinase_AS.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view]
PfamiPF12745. HGTP_anticodon2. 1 hit.
PF00069. Pkinase. 3 hits.
PF05773. RWD. 1 hit.
[Graphical view]
SMARTiSM00591. RWD. 1 hit.
SM00220. S_TKc. 2 hits.
[Graphical view]
SUPFAMiSSF54495. SSF54495. 1 hit.
SSF56112. SSF56112. 3 hits.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 2 hits.
PS00108. PROTEIN_KINASE_ST. 1 hit.
PS50908. RWD. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9P2K8-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAGGRGAPGR GRDEPPESYP QRQDHELQAL EAIYGADFQD LRPDACGPVK
60 70 80 90 100
EPPEINLVLY PQGLTGEEVY VKVDLRVKCP PTYPDVVPEI ELKNAKGLSN
110 120 130 140 150
ESVNLLKSRL EELAKKHCGE VMIFELAYHV QSFLSEHNKP PPKSFHEEML
160 170 180 190 200
ERRAQEEQQR LLEAKRKEEQ EQREILHEIQ RRKEEIKEEK KRKEMAKQER
210 220 230 240 250
LEIASLSNQD HTSKKDPGGH RTAAILHGGS PDFVGNGKHR ANSSGRSRRE
260 270 280 290 300
RQYSVCNSED SPGSCEILYF NMGSPDQLMV HKGKCIGSDE QLGKLVYNAL
310 320 330 340 350
ETATGGFVLL YEWVLQWQKK MGPFLTSQEK EKIDKCKKQI QGTETEFNSL
360 370 380 390 400
VKLSHPNVVR YLAMNLKEQD DSIVVDILVE HISGVSLAAH LSHSGPIPVH
410 420 430 440 450
QLRRYTAQLL SGLDYLHSNS VVHKVLSASN VLVDAEGTVK ITDYSISKRL
460 470 480 490 500
ADICKEDVFE QTRVRFSDNA LPYKTGKKGD VWRLGLLLLS LSQGQECGEY
510 520 530 540 550
PVTIPSDLPA DFQDFLKKCV CLDDKERWSP QQLLKHSFIN PQPKMPLVEQ
560 570 580 590 600
SPEDSEGQDY VETVIPSNRL PSAAFFSETQ RQFSRYFIEF EELQLLGKGA
610 620 630 640 650
FGAVIKVQNK LDGCCYAVKR IPINPASRQF RRIKGEVTLL SRLHHENIVR
660 670 680 690 700
YYNAWIERHE RPAGPGTPPP DSGPLAKDDR AARGQPASDT DGLDSVEAAA
710 720 730 740 750
PPPILSSSVE WSTSGERSAS ARFPATGPGS SDDEDDDEDE HGGVFSQSFL
760 770 780 790 800
PASDSESDII FDNEDENSKS QNQDEDCNEK NGCHESEPSV TTEAVHYLYI
810 820 830 840 850
QMEYCEKSTL RDTIDQGLYR DTVRLWRLFR EILDGLAYIH EKGMIHRDLK
860 870 880 890 900
PVNIFLDSDD HVKIGDFGLA TDHLAFSADS KQDDQTGDLI KSDPSGHLTG
910 920 930 940 950
MVGTALYVSP EVQGSTKSAY NQKVDLFSLG IIFFEMSYHP MVTASERIFV
960 970 980 990 1000
LNQLRDPTSP KFPEDFDDGE HAKQKSVISW LLNHDPAKRP TATELLKSEL
1010 1020 1030 1040 1050
LPPPQMEESE LHEVLHHTLT NVDGKAYRTM MAQIFSQRIS PAIDYTYDSD
1060 1070 1080 1090 1100
ILKGNFSIRT AKMQQHVCET IIRIFKRHGA VQLCTPLLLP RNRQIYEHNE
1110 1120 1130 1140 1150
AALFMDHSGM LVMLPFDLRI PFARYVARNN ILNLKRYCIE RVFRPRKLDR
1160 1170 1180 1190 1200
FHPKELLECA FDIVTSTTNS FLPTAEIIYT IYEIIQEFPA LQERNYSIYL
1210 1220 1230 1240 1250
NHTMLLKAIL LHCGIPEDKL SQVYIILYDA VTEKLTRREV EAKFCNLSLS
1260 1270 1280 1290 1300
SNSLCRLYKF IEQKGDLQDL MPTINSLIKQ KTGIAQLVKY GLKDLEEVVG
1310 1320 1330 1340 1350
LLKKLGIKLQ VLINLGLVYK VQQHNGIIFQ FVAFIKRRQR AVPEILAAGG
1360 1370 1380 1390 1400
RYDLLIPQFR GPQALGPVPT AIGVSIAIDK ISAAVLNMEE SVTISSCDLL
1410 1420 1430 1440 1450
VVSVGQMSMS RAINLTQKLW TAGITAEIMY DWSQSQEELQ EYCRHHEITY
1460 1470 1480 1490 1500
VALVSDKEGS HVKVKSFEKE RQTEKRVLET ELVDHVLQKL RTKVTDERNG
1510 1520 1530 1540 1550
REASDNLAVQ NLKGSFSNAS GLFEIHGATV VPIVSVLAPE KLSASTRRRY
1560 1570 1580 1590 1600
ETQVQTRLQT SLANLHQKSS EIEILAVDLP KETILQFLSL EWDADEQAFN
1610 1620 1630 1640
TTVKQLLSRL PKQRYLKLVC DEIYNIKVEK KVSVLFLYSY RDDYYRILF
Length:1,649
Mass (Da):186,911
Last modified:May 18, 2010 - v3
Checksum:iECF3CFFA51AEE67C
GO
Isoform 2 (identifier: Q9P2K8-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     774-801: Missing.

Note: No experimental confirmation available.
Show »
Length:1,621
Mass (Da):183,717
Checksum:i40B21FA4D721C758
GO
Isoform 3 (identifier: Q9P2K8-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     608-616: QNKLDGCCY → WYRVIPSPL
     617-1649: Missing.

Note: No experimental confirmation available.
Show »
Length:616
Mass (Da):69,797
Checksum:iCBFF2B4F683C5DB3
GO

Sequence cautioni

The sequence BAA92576 differs from that shown. Contaminating sequence. Sequence of unknown origin in the N-terminal part.Curated
The sequence BAB15625 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti556E → G in BAA92576 (PubMed:10718198).Curated1
Sequence conflicti556E → G in CAH10626 (PubMed:17974005).Curated1
Sequence conflicti629Q → K in CAH10626 (PubMed:17974005).Curated1
Sequence conflicti858S → F in BAB15625 (PubMed:14702039).Curated1
Sequence conflicti1133N → I in CAB58360 (PubMed:10504407).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_040479137H → R.1 PublicationCorresponds to variant rs35509999dbSNPEnsembl.1
Natural variantiVAR_040480166R → W.1 PublicationCorresponds to variant rs34439704dbSNPEnsembl.1
Natural variantiVAR_040481441I → L.2 PublicationsCorresponds to variant rs2291627dbSNPEnsembl.1
Natural variantiVAR_070990585R → Q in PVOD2. 1 PublicationCorresponds to variant rs587777106dbSNPEnsembl.1
Natural variantiVAR_070991643L → R in PVOD2. 1 PublicationCorresponds to variant rs757852728dbSNPEnsembl.1
Natural variantiVAR_040482872D → V.1 PublicationCorresponds to variant rs34665481dbSNPEnsembl.1
Natural variantiVAR_040483939H → Y in a lung neuroendocrine carcinoma sample; somatic mutation. 1 Publication1
Natural variantiVAR_0404841060T → R.1 PublicationCorresponds to variant rs55781333dbSNPEnsembl.1
Natural variantiVAR_0404851306G → C.2 PublicationsCorresponds to variant rs35602605dbSNPEnsembl.1
Natural variantiVAR_0404861336K → R.1 PublicationCorresponds to variant rs35480871dbSNPEnsembl.1
Natural variantiVAR_0404871406Q → H.1 PublicationCorresponds to variant rs55721315dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_039185608 – 616QNKLDGCCY → WYRVIPSPL in isoform 3. 1 Publication9
Alternative sequenceiVSP_039186617 – 1649Missing in isoform 3. 1 PublicationAdd BLAST1033
Alternative sequenceiVSP_013038774 – 801Missing in isoform 2. CuratedAdd BLAST28

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC012377 Genomic DNA. No translation available.
AC025168 Genomic DNA. No translation available.
BC009350 mRNA. Translation: AAH09350.2.
BC078179 mRNA. Translation: AAH78179.1.
AB037759 mRNA. Translation: BAA92576.1. Sequence problems.
AL137627 mRNA. Translation: CAB70849.1.
AL157497 mRNA. Translation: CAB75678.1.
AL832907 mRNA. Translation: CAH10626.1.
AK027011 mRNA. Translation: BAB15625.1. Different initiation.
AJ243428 mRNA. Translation: CAB58360.1.
CCDSiCCDS42016.1. [Q9P2K8-1]
PIRiT46924.
RefSeqiNP_001013725.2. NM_001013703.3. [Q9P2K8-1]
UniGeneiHs.656673.

Genome annotation databases

EnsembliENST00000263791; ENSP00000263791; ENSG00000128829. [Q9P2K8-1]
ENST00000559624; ENSP00000453148; ENSG00000128829. [Q9P2K8-3]
GeneIDi440275.
KEGGihsa:440275.
UCSCiuc001zkl.4. human. [Q9P2K8-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC012377 Genomic DNA. No translation available.
AC025168 Genomic DNA. No translation available.
BC009350 mRNA. Translation: AAH09350.2.
BC078179 mRNA. Translation: AAH78179.1.
AB037759 mRNA. Translation: BAA92576.1. Sequence problems.
AL137627 mRNA. Translation: CAB70849.1.
AL157497 mRNA. Translation: CAB75678.1.
AL832907 mRNA. Translation: CAH10626.1.
AK027011 mRNA. Translation: BAB15625.1. Different initiation.
AJ243428 mRNA. Translation: CAB58360.1.
CCDSiCCDS42016.1. [Q9P2K8-1]
PIRiT46924.
RefSeqiNP_001013725.2. NM_001013703.3. [Q9P2K8-1]
UniGeneiHs.656673.

3D structure databases

ProteinModelPortaliQ9P2K8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi136426. 20 interactors.
IntActiQ9P2K8. 20 interactors.
STRINGi9606.ENSP00000263791.

Chemistry databases

BindingDBiQ9P2K8.
ChEMBLiCHEMBL5358.
GuidetoPHARMACOLOGYi2018.

PTM databases

iPTMnetiQ9P2K8.
PhosphoSitePlusiQ9P2K8.

Polymorphism and mutation databases

BioMutaiEIF2AK4.
DMDMi296439368.

Proteomic databases

EPDiQ9P2K8.
MaxQBiQ9P2K8.
PaxDbiQ9P2K8.
PeptideAtlasiQ9P2K8.
PRIDEiQ9P2K8.

Protocols and materials databases

DNASUi440275.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000263791; ENSP00000263791; ENSG00000128829. [Q9P2K8-1]
ENST00000559624; ENSP00000453148; ENSG00000128829. [Q9P2K8-3]
GeneIDi440275.
KEGGihsa:440275.
UCSCiuc001zkl.4. human. [Q9P2K8-1]

Organism-specific databases

CTDi440275.
DisGeNETi440275.
GeneCardsiEIF2AK4.
H-InvDBHIX0012119.
HGNCiHGNC:19687. EIF2AK4.
HPAiHPA011811.
MalaCardsiEIF2AK4.
MIMi234810. phenotype.
609280. gene.
neXtProtiNX_Q9P2K8.
OpenTargetsiENSG00000128829.
Orphaneti199241. Pulmonary capillary hemangiomatosis.
31837. Pulmonary venoocclusive disease.
PharmGKBiPA134947616.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1035. Eukaryota.
COG0124. LUCA.
GeneTreeiENSGT00530000062984.
HOVERGENiHBG051432.
InParanoidiQ9P2K8.
KOiK16196.
OMAiKCVCLDD.
OrthoDBiEOG091G0NNL.
PhylomeDBiQ9P2K8.
TreeFamiTF101512.

Enzyme and pathway databases

BioCyciZFISH:HS05227-MONOMER.
SignaLinkiQ9P2K8.
SIGNORiQ9P2K8.

Miscellaneous databases

ChiTaRSiEIF2AK4. human.
GeneWikiiEIF2AK4.
GenomeRNAii440275.
PROiQ9P2K8.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000128829.
CleanExiHS_EIF2AK4.
ExpressionAtlasiQ9P2K8. baseline and differential.
GenevisibleiQ9P2K8. HS.

Family and domain databases

Gene3Di3.10.110.10. 1 hit.
3.40.50.800. 1 hit.
InterProiIPR004154. Anticodon-bd.
IPR024435. HisRS-related_dom.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR006575. RWD-domain.
IPR008271. Ser/Thr_kinase_AS.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view]
PfamiPF12745. HGTP_anticodon2. 1 hit.
PF00069. Pkinase. 3 hits.
PF05773. RWD. 1 hit.
[Graphical view]
SMARTiSM00591. RWD. 1 hit.
SM00220. S_TKc. 2 hits.
[Graphical view]
SUPFAMiSSF54495. SSF54495. 1 hit.
SSF56112. SSF56112. 3 hits.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 2 hits.
PS00108. PROTEIN_KINASE_ST. 1 hit.
PS50908. RWD. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiE2AK4_HUMAN
AccessioniPrimary (citable) accession number: Q9P2K8
Secondary accession number(s): C9JEC4
, Q69YL7, Q6DC97, Q96GN6, Q9H5K1, Q9NSQ3, Q9NSZ5, Q9UJ56
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: May 18, 2010
Last modified: November 2, 2016
This is version 151 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 15
    Human chromosome 15: 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. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  6. 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.