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Q9P2K8

- E2AK4_HUMAN

UniProt

Q9P2K8 - E2AK4_HUMAN

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
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    • History
      Entry version 129 (01 Oct 2014)
      Sequence version 3 (18 May 2010)
      Previous versions | rss
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    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

    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

    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

    ArrayExpressiQ9P2K8.
    BgeeiQ9P2K8.
    CleanExiHS_EIF2AK4.
    GenevestigatoriQ9P2K8.

    Organism-specific databases

    HPAiHPA011811.

    Interactioni

    Protein-protein interaction databases

    BioGridi136426. 5 interactions.
    IntActiQ9P2K8. 16 interactions.
    STRINGi9606.ENSP00000263791.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9P2K8.
    SMRiQ9P2K8. Positions 21-144, 296-576, 585-658, 735-1031, 1055-1489.
    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.
    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

    MAGGRGAPGR GRDEPPESYP QRQDHELQAL EAIYGADFQD LRPDACGPVK     50
    EPPEINLVLY PQGLTGEEVY VKVDLRVKCP PTYPDVVPEI ELKNAKGLSN 100
    ESVNLLKSRL EELAKKHCGE VMIFELAYHV QSFLSEHNKP PPKSFHEEML 150
    ERRAQEEQQR LLEAKRKEEQ EQREILHEIQ RRKEEIKEEK KRKEMAKQER 200
    LEIASLSNQD HTSKKDPGGH RTAAILHGGS PDFVGNGKHR ANSSGRSRRE 250
    RQYSVCNSED SPGSCEILYF NMGSPDQLMV HKGKCIGSDE QLGKLVYNAL 300
    ETATGGFVLL YEWVLQWQKK MGPFLTSQEK EKIDKCKKQI QGTETEFNSL 350
    VKLSHPNVVR YLAMNLKEQD DSIVVDILVE HISGVSLAAH LSHSGPIPVH 400
    QLRRYTAQLL SGLDYLHSNS VVHKVLSASN VLVDAEGTVK ITDYSISKRL 450
    ADICKEDVFE QTRVRFSDNA LPYKTGKKGD VWRLGLLLLS LSQGQECGEY 500
    PVTIPSDLPA DFQDFLKKCV CLDDKERWSP QQLLKHSFIN PQPKMPLVEQ 550
    SPEDSEGQDY VETVIPSNRL PSAAFFSETQ RQFSRYFIEF EELQLLGKGA 600
    FGAVIKVQNK LDGCCYAVKR IPINPASRQF RRIKGEVTLL SRLHHENIVR 650
    YYNAWIERHE RPAGPGTPPP DSGPLAKDDR AARGQPASDT DGLDSVEAAA 700
    PPPILSSSVE WSTSGERSAS ARFPATGPGS SDDEDDDEDE HGGVFSQSFL 750
    PASDSESDII FDNEDENSKS QNQDEDCNEK NGCHESEPSV TTEAVHYLYI 800
    QMEYCEKSTL RDTIDQGLYR DTVRLWRLFR EILDGLAYIH EKGMIHRDLK 850
    PVNIFLDSDD HVKIGDFGLA TDHLAFSADS KQDDQTGDLI KSDPSGHLTG 900
    MVGTALYVSP EVQGSTKSAY NQKVDLFSLG IIFFEMSYHP MVTASERIFV 950
    LNQLRDPTSP KFPEDFDDGE HAKQKSVISW LLNHDPAKRP TATELLKSEL 1000
    LPPPQMEESE LHEVLHHTLT NVDGKAYRTM MAQIFSQRIS PAIDYTYDSD 1050
    ILKGNFSIRT AKMQQHVCET IIRIFKRHGA VQLCTPLLLP RNRQIYEHNE 1100
    AALFMDHSGM LVMLPFDLRI PFARYVARNN ILNLKRYCIE RVFRPRKLDR 1150
    FHPKELLECA FDIVTSTTNS FLPTAEIIYT IYEIIQEFPA LQERNYSIYL 1200
    NHTMLLKAIL LHCGIPEDKL SQVYIILYDA VTEKLTRREV EAKFCNLSLS 1250
    SNSLCRLYKF IEQKGDLQDL MPTINSLIKQ KTGIAQLVKY GLKDLEEVVG 1300
    LLKKLGIKLQ VLINLGLVYK VQQHNGIIFQ FVAFIKRRQR AVPEILAAGG 1350
    RYDLLIPQFR GPQALGPVPT AIGVSIAIDK ISAAVLNMEE SVTISSCDLL 1400
    VVSVGQMSMS RAINLTQKLW TAGITAEIMY DWSQSQEELQ EYCRHHEITY 1450
    VALVSDKEGS HVKVKSFEKE RQTEKRVLET ELVDHVLQKL RTKVTDERNG 1500
    REASDNLAVQ NLKGSFSNAS GLFEIHGATV VPIVSVLAPE KLSASTRRRY 1550
    ETQVQTRLQT SLANLHQKSS EIEILAVDLP KETILQFLSL EWDADEQAFN 1600
    TTVKQLLSRL PKQRYLKLVC DEIYNIKVEK KVSVLFLYSY RDDYYRILF 1649
    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.
    The sequence BAB15625.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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, 735-1031, 1055-1489.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 136426. 5 interactions.
    IntActi Q9P2K8. 16 interactions.
    STRINGi 9606.ENSP00000263791.

    Chemistry

    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.
    HOVERGENi HBG051432.
    InParanoidi Q9P2K8.
    KOi K16196.
    OMAi LNMEEPV.
    OrthoDBi EOG780RKP.
    PhylomeDBi Q9P2K8.
    TreeFami TF101512.

    Enzyme and pathway databases

    SignaLinki Q9P2K8.

    Miscellaneous databases

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

    Gene expression databases

    ArrayExpressi Q9P2K8.
    Bgeei Q9P2K8.
    CleanExi HS_EIF2AK4.
    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

    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: October 1, 2014
    This is version 129 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