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Q9P2K8

- E2AK4_HUMAN

UniProt

Q9P2K8 - E2AK4_HUMAN

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Protein

Eukaryotic translation initiation factor 2-alpha kinase 4

Gene

EIF2AK4

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Can phosphorylate the alpha subunit of EIF2 and may mediate translational control.By similarity

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei619 – 6191ATPPROSITE-ProRule annotation
Active sitei848 – 8481Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi596 – 6049ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. eukaryotic translation initiation factor 2alpha kinase activity Source: UniProtKB
  3. protein serine/threonine kinase activity Source: UniProtKB

GO - Biological processi

  1. cellular response to starvation Source: Ensembl
  2. endoplasmic reticulum unfolded protein response Source: Ensembl
  3. negative regulation of translation Source: Ensembl
  4. protein phosphorylation Source: UniProtKB
  5. regulation of translational initiation Source: UniProtKB
  6. regulation of translational initiation in response to stress Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

SignaLinkiQ9P2K8.

Names & Taxonomyi

Protein namesi
Recommended name:
Eukaryotic translation initiation factor 2-alpha kinase 4 (EC:2.7.11.1)
Alternative name(s):
GCN2-like protein
Gene namesi
Name:EIF2AK4
Synonyms:GCN2, KIAA1338
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 15

Organism-specific databases

HGNCiHGNC:19687. EIF2AK4.

Subcellular locationi

GO - Cellular componenti

  1. cytosolic ribosome Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Involvement in diseasei

Pulmonary venoocclusive disease 2, autosomal recessive (PVOD2) [MIM:234810]: A 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.2 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti585 – 5851R → Q in PVOD2. 1 Publication
VAR_070990
Natural varianti643 – 6431L → R in PVOD2. 1 Publication
VAR_070991

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi234810. phenotype.
Orphaneti199241. Pulmonary capillary hemangiomatosis.
31837. Pulmonary venoocclusive disease.
PharmGKBiPA134947616.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 16491649Eukaryotic translation initiation factor 2-alpha kinase 4PRO_0000085947Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei230 – 2301Phosphoserine4 Publications
Modified residuei667 – 6671Phosphothreonine4 Publications
Modified residuei899 – 8991Phosphothreonine; by autocatalysisBy similarity
Modified residuei904 – 9041Phosphothreonine; by autocatalysisBy similarity
Modified residuei1259 – 12591N6-acetyllysine1 Publication

Post-translational modificationi

Autophosphorylated on threonine residues.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9P2K8.
PaxDbiQ9P2K8.
PRIDEiQ9P2K8.

PTM databases

PhosphoSiteiQ9P2K8.

Expressioni

Tissue specificityi

Widely expressed. Expressed in the lung in smooth muscle cells of the pulmonary vessel wall, interstitial tissue and macrophages.2 Publications

Gene expression databases

BgeeiQ9P2K8.
CleanExiHS_EIF2AK4.
ExpressionAtlasiQ9P2K8. baseline and differential.
GenevestigatoriQ9P2K8.

Organism-specific databases

HPAiHPA011811.

Interactioni

Protein-protein interaction databases

BioGridi136426. 9 interactions.
IntActiQ9P2K8. 15 interactions.
STRINGi9606.ENSP00000263791.

Structurei

3D structure databases

ProteinModelPortaliQ9P2K8.
SMRiQ9P2K8. Positions 21-144, 296-576, 585-658, 735-1050, 1055-1489, 1531-1649.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini25 – 137113RWDPROSITE-ProRule annotationAdd
BLAST
Domaini296 – 539244Protein kinase 1PROSITE-ProRule annotationAdd
BLAST
Domaini590 – 1001412Protein kinase 2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1022 – 1493472Histidyl-tRNA synthetase-likeAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi484 – 4918Poly-Leu

Domaini

Kinase domain 1 is a degenerate kinase domain.
RWD domain is reported to interact with GCN1L1.

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

Repeat

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00530000062984.
HOVERGENiHBG051432.
InParanoidiQ9P2K8.
KOiK16196.
OMAiLNMEEPV.
OrthoDBiEOG780RKP.
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.
IPR016255. Ser/Thr_kinase_GCN2.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view]
PfamiPF12745. HGTP_anticodon2. 1 hit.
PF00069. Pkinase. 3 hits.
PF05773. RWD. 1 hit.
[Graphical view]
PIRSFiPIRSF000660. Ser/Thr_PK_GCN2. 1 hit.
SMARTiSM00591. RWD. 1 hit.
[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. Align

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 BAA92576.1 differs from that shown. Reason: Contaminating sequence. Sequence of unknown origin in the N-terminal part.Curated
The sequence BAB15625.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti556 – 5561E → G in BAA92576. (PubMed:10718198)Curated
Sequence conflicti556 – 5561E → G in CAH10626. (PubMed:17974005)Curated
Sequence conflicti629 – 6291Q → K in CAH10626. (PubMed:17974005)Curated
Sequence conflicti858 – 8581S → F in BAB15625. (PubMed:14702039)Curated
Sequence conflicti1133 – 11331N → I in CAB58360. (PubMed:10504407)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti137 – 1371H → R.1 Publication
VAR_040479
Natural varianti166 – 1661R → W.1 Publication
Corresponds to variant rs34439704 [ dbSNP | Ensembl ].
VAR_040480
Natural varianti441 – 4411I → L.2 Publications
Corresponds to variant rs2291627 [ dbSNP | Ensembl ].
VAR_040481
Natural varianti585 – 5851R → Q in PVOD2. 1 Publication
VAR_070990
Natural varianti643 – 6431L → R in PVOD2. 1 Publication
VAR_070991
Natural varianti872 – 8721D → V.1 Publication
VAR_040482
Natural varianti939 – 9391H → Y in a lung neuroendocrine carcinoma sample; somatic mutation. 1 Publication
VAR_040483
Natural varianti1060 – 10601T → R.1 Publication
VAR_040484
Natural varianti1306 – 13061G → C.2 Publications
Corresponds to variant rs35602605 [ dbSNP | Ensembl ].
VAR_040485
Natural varianti1336 – 13361K → R.1 Publication
Corresponds to variant rs35480871 [ dbSNP | Ensembl ].
VAR_040486
Natural varianti1406 – 14061Q → H.1 Publication
Corresponds to variant rs55721315 [ dbSNP | Ensembl ].
VAR_040487

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei608 – 6169QNKLDGCCY → WYRVIPSPL in isoform 3. 1 PublicationVSP_039185
Alternative sequencei617 – 16491033Missing in isoform 3. 1 PublicationVSP_039186Add
BLAST
Alternative sequencei774 – 80128Missing in isoform 2. CuratedVSP_013038Add
BLAST

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.3. human. [Q9P2K8-3]
uc001zkm.1. human. [Q9P2K8-1]

Polymorphism databases

DMDMi296439368.

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 .
CCDSi CCDS42016.1. [Q9P2K8-1 ]
PIRi T46924.
RefSeqi NP_001013725.2. NM_001013703.3. [Q9P2K8-1 ]
UniGenei Hs.656673.

3D structure databases

ProteinModelPortali Q9P2K8.
SMRi Q9P2K8. Positions 21-144, 296-576, 585-658, 735-1050, 1055-1489, 1531-1649.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 136426. 9 interactions.
IntActi Q9P2K8. 15 interactions.
STRINGi 9606.ENSP00000263791.

Chemistry

BindingDBi Q9P2K8.
ChEMBLi CHEMBL5358.
GuidetoPHARMACOLOGYi 2018.

PTM databases

PhosphoSitei Q9P2K8.

Polymorphism databases

DMDMi 296439368.

Proteomic databases

MaxQBi Q9P2K8.
PaxDbi Q9P2K8.
PRIDEi Q9P2K8.

Protocols and materials databases

DNASUi 440275.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000263791 ; ENSP00000263791 ; ENSG00000128829 . [Q9P2K8-1 ]
ENST00000559624 ; ENSP00000453148 ; ENSG00000128829 . [Q9P2K8-3 ]
GeneIDi 440275.
KEGGi hsa:440275.
UCSCi uc001zkl.3. human. [Q9P2K8-3 ]
uc001zkm.1. human. [Q9P2K8-1 ]

Organism-specific databases

CTDi 440275.
GeneCardsi GC15P040226.
H-InvDB HIX0012119.
HGNCi HGNC:19687. EIF2AK4.
HPAi HPA011811.
MIMi 234810. phenotype.
609280. gene.
neXtProti NX_Q9P2K8.
Orphaneti 199241. Pulmonary capillary hemangiomatosis.
31837. Pulmonary venoocclusive disease.
PharmGKBi PA134947616.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00530000062984.
HOVERGENi HBG051432.
InParanoidi Q9P2K8.
KOi K16196.
OMAi LNMEEPV.
OrthoDBi EOG780RKP.
PhylomeDBi Q9P2K8.
TreeFami TF101512.

Enzyme and pathway databases

SignaLinki Q9P2K8.

Miscellaneous databases

ChiTaRSi EIF2AK4. human.
GeneWikii EIF2AK4.
GenomeRNAii 440275.
NextBioi 109089.
PROi Q9P2K8.
SOURCEi Search...

Gene expression databases

Bgeei Q9P2K8.
CleanExi HS_EIF2AK4.
ExpressionAtlasi Q9P2K8. baseline and differential.
Genevestigatori Q9P2K8.

Family and domain databases

Gene3Di 3.10.110.10. 1 hit.
3.40.50.800. 1 hit.
InterProi IPR004154. 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.
IPR016255. Ser/Thr_kinase_GCN2.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view ]
Pfami PF12745. HGTP_anticodon2. 1 hit.
PF00069. Pkinase. 3 hits.
PF05773. RWD. 1 hit.
[Graphical view ]
PIRSFi PIRSF000660. Ser/Thr_PK_GCN2. 1 hit.
SMARTi SM00591. RWD. 1 hit.
[Graphical view ]
SUPFAMi SSF54495. SSF54495. 1 hit.
SSF56112. SSF56112. 3 hits.
PROSITEi PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 2 hits.
PS00108. PROTEIN_KINASE_ST. 1 hit.
PS50908. RWD. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Analysis of the DNA sequence and duplication history of human chromosome 15."
    Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A.
    , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.
    Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 821-1649 (ISOFORM 1), VARIANT CYS-1306.
    Tissue: Muscle and Uterus.
  3. "Prediction of the coding sequences of unidentified human genes. XVI. The complete sequences of 150 new cDNA clones from brain which code for large proteins in vitro."
    Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.
    DNA Res. 7:65-73(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 177-1649.
    Tissue: Brain.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 196-1649, VARIANT LEU-441.
    Tissue: Melanoma and Testis.
  5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 831-1649.
  6. "Characterization of a mammalian homolog of the GCN2 eukaryotic initiation factor 2alpha kinase."
    Berlanga J.J., Santoyo J., de Haro C.
    Eur. J. Biochem. 265:754-762(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1102-1649, TISSUE SPECIFICITY.
  7. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-667, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-230 AND THR-667, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-230, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-667, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1259, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-230 AND THR-667, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-230, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. Cited for: INVOLVEMENT IN PVOD2.
  16. "EIF2AK4 mutations cause pulmonary veno-occlusive disease, a recessive form of pulmonary hypertension."
    Eyries M., Montani D., Girerd B., Perret C., Leroy A., Lonjou C., Chelghoum N., Coulet F., Bonnet D., Dorfmueller P., Fadel E., Sitbon O., Simonneau G., Tregouet D.A., Humbert M., Soubrier F.
    Nat. Genet. 46:65-69(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, VARIANTS PVOD2 GLN-585 AND ARG-643.
  17. "Patterns of somatic mutation in human cancer genomes."
    Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.
    , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
    Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS [LARGE SCALE ANALYSIS] ARG-137; TRP-166; LEU-441; VAL-872; TYR-939; ARG-1060; CYS-1306; ARG-1336 AND HIS-1406.

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 26, 2014
This is version 131 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

External Data

Dasty 3