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Q9NZJ5

- E2AK3_HUMAN

UniProt

Q9NZJ5 - E2AK3_HUMAN

Protein

Eukaryotic translation initiation factor 2-alpha kinase 3

Gene

EIF2AK3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 144 (01 Oct 2014)
      Sequence version 3 (18 May 2010)
      Previous versions | rss
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    Functioni

    Phosphorylates the alpha subunit of eukaryotic translation-initiation factor 2 (EIF2), leading to its inactivation and thus to a rapid reduction of translational initiation and repression of global protein synthesis. 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.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)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei622 – 6221ATPPROSITE-ProRule annotation
    Active sitei937 – 9371Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi599 – 6079ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. enzyme binding Source: UniProt
    3. eukaryotic translation initiation factor 2alpha kinase activity Source: UniProtKB
    4. identical protein binding Source: IntAct
    5. protein binding Source: UniProtKB
    6. protein kinase activity Source: ProtInc
    7. protein phosphatase binding Source: UniProtKB
    8. protein serine/threonine kinase activity Source: UniProtKB

    GO - Biological processi

    1. activation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
    2. activation of signaling protein activity involved in unfolded protein response Source: Reactome
    3. bone mineralization Source: UniProtKB
    4. calcium-mediated signaling Source: UniProtKB
    5. cellular protein metabolic process Source: Reactome
    6. chondrocyte development Source: UniProtKB
    7. endocrine pancreas development Source: UniProtKB
    8. endoplasmic reticulum organization Source: UniProtKB
    9. endoplasmic reticulum unfolded protein response Source: UniProtKB
    10. ER overload response Source: UniProtKB
    11. fat cell differentiation Source: Ensembl
    12. insulin-like growth factor receptor signaling pathway Source: UniProtKB
    13. insulin secretion Source: UniProtKB
    14. intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress Source: Ensembl
    15. lactation Source: Ensembl
    16. negative regulation of myelination Source: UniProtKB
    17. negative regulation of translation Source: UniProtKB
    18. negative regulation of translational initiation in response to stress Source: UniProtKB
    19. ossification Source: UniProtKB
    20. positive regulation of protein binding Source: Ensembl
    21. positive regulation of signal transduction Source: Ensembl
    22. protein autophosphorylation Source: UniProtKB
    23. protein homooligomerization Source: UniProtKB
    24. protein phosphorylation Source: UniProtKB
    25. regulation of fatty acid metabolic process Source: Ensembl
    26. response to endoplasmic reticulum stress Source: BHF-UCL
    27. skeletal system development Source: UniProtKB
    28. SREBP signaling pathway Source: Ensembl
    29. translation Source: Ensembl

    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

    ReactomeiREACT_18277. PERK regulates gene expression.
    SignaLinkiQ9NZJ5.

    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
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:3255. EIF2AK3.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. endoplasmic reticulum Source: UniProtKB
    3. endoplasmic reticulum membrane Source: UniProtKB
    4. integral component of membrane Source: UniProtKB-KW
    5. membrane Source: UniProtKB

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane

    Pathology & Biotechi

    Involvement in diseasei

    Wolcott-Rallison syndrome (WRS) [MIM:226980]: A 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.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti588 – 5881R → Q in WRS; in a Pakistani family; probable complete loss of activity. 1 Publication
    VAR_011408

    Keywords - Diseasei

    Diabetes mellitus, Disease mutation

    Organism-specific databases

    MIMi226980. phenotype.
    Orphaneti1667. Wolcott-Rallison syndrome.
    PharmGKBiPA27687.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2929Sequence AnalysisAdd
    BLAST
    Chaini30 – 11161087Eukaryotic translation initiation factor 2-alpha kinase 3PRO_0000024322Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi258 – 2581N-linked (GlcNAc...)Sequence Analysis
    Modified residuei619 – 6191Phosphotyrosine1 Publication
    Modified residuei715 – 7151Phosphoserine1 Publication
    Modified residuei982 – 9821PhosphothreonineBy similarity
    Modified residuei1094 – 10941Phosphoserine1 Publication

    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 similarity3 Publications
    N-glycosylated.By similarity
    ADP-ribosylated by PARP16 upon ER stress, which increases kinase activity.

    Keywords - PTMi

    ADP-ribosylation, Glycoprotein, Phosphoprotein

    Proteomic databases

    MaxQBiQ9NZJ5.
    PaxDbiQ9NZJ5.
    PRIDEiQ9NZJ5.

    PTM databases

    PhosphoSiteiQ9NZJ5.

    Expressioni

    Tissue specificityi

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

    Inductioni

    By endoplasmic reticulum stress.

    Gene expression databases

    ArrayExpressiQ9NZJ5.
    BgeeiQ9NZJ5.
    CleanExiHS_EIF2AK3.
    GenevestigatoriQ9NZJ5.

    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.By similarity

    Binary interactionsi

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

    Protein-protein interaction databases

    BioGridi114840. 10 interactions.
    IntActiQ9NZJ5. 4 interactions.
    STRINGi9606.ENSP00000307235.

    Structurei

    Secondary structure

    1
    1116
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi588 – 5925
    Beta strandi593 – 6019
    Beta strandi606 – 6127
    Turni613 – 6153
    Beta strandi618 – 6269
    Helixi630 – 64314
    Beta strandi654 – 6607
    Beta strandi882 – 8898
    Helixi896 – 9016
    Helixi906 – 9083
    Helixi911 – 93020
    Helixi940 – 9423
    Beta strandi943 – 9453
    Beta strandi951 – 9533
    Helixi993 – 9964
    Helixi1004 – 101815
    Helixi1024 – 103512
    Helixi1041 – 10466
    Helixi1048 – 105710
    Helixi1062 – 10643
    Helixi1068 – 10725
    Helixi1075 – 10773

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4G31X-ray2.28A588-1093[»]
    4G34X-ray2.70A588-1093[»]
    ProteinModelPortaliQ9NZJ5.
    SMRiQ9NZJ5. Positions 588-660, 830-1116.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini30 – 514485LumenalSequence AnalysisAdd
    BLAST
    Topological domaini536 – 1116581CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei515 – 53521HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini593 – 1077485Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi49 – 524Poly-Ala

    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

    eggNOGiCOG0515.
    HOVERGENiHBG051431.
    InParanoidiQ9NZJ5.
    KOiK08860.
    OMAiKGLMHRD.
    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. Quinonprotein_ADH-like_fam.
    IPR011047. Quinonprotein_ADH-like_supfam.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view]
    PfamiPF00069. Pkinase. 2 hits.
    [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

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    MERAISPGLL VRALLLLLLL LGLAARTVAA GRARGLPAPT AEAAFGLGAA     50
    AAPTSATRVP AAGAVAAAEV TVEDAEALPA AAGEQEPRGP EPDDETELRP 100
    RGRSLVIIST LDGRIAALDP ENHGKKQWDL DVGSGSLVSS SLSKPEVFGN 150
    KMIIPSLDGA LFQWDQDRES METVPFTVES LLESSYKFGD DVVLVGGKSL 200
    TTYGLSAYSG KVRYICSALG CRQWDSDEME QEEDILLLQR TQKTVRAVGP 250
    RSGNEKWNFS VGHFELRYIP DMETRAGFIE STFKPNENTE ESKIISDVEE 300
    QEAAIMDIVI KVSVADWKVM AFSKKGGHLE WEYQFCTPIA SAWLLKDGKV 350
    IPISLFDDTS YTSNDDVLED EEDIVEAARG ATENSVYLGM YRGQLYLQSS 400
    VRISEKFPSS PKALESVTNE NAIIPLPTIK WKPLIHSPSR TPVLVGSDEF 450
    DKCLSNDKFS HEEYSNGALS ILQYPYDNGY YLPYYKRERN KRSTQITVRF 500
    LDNPHYNKNI RKKDPVLLLH WWKEIVATIL FCIIATTFIV RRLFHPHPHR 550
    QRKESETQCQ TENKYDSVSG EANDSSWNDI KNSGYISRYL TDFEPIQCLG 600
    RGGFGVVFEA KNKVDDCNYA IKRIRLPNRE LAREKVMREV KALAKLEHPG 650
    IVRYFNAWLE APPEKWQEKM DEIWLKDEST DWPLSSPSPM DAPSVKIRRM 700
    DPFATKEHIE IIAPSPQRSR SFSVGISCDQ TSSSESQFSP LEFSGMDHED 750
    ISESVDAAYN LQDSCLTDCD VEDGTMDGND EGHSFELCPS EASPYVRSRE 800
    RTSSSIVFED SGCDNASSKE EPKTNRLHIG NHCANKLTAF KPTSSKSSSE 850
    ATLSISPPRP TTLSLDLTKN TTEKLQPSSP KVYLYIQMQL CRKENLKDWM 900
    NGRCTIEERE RSVCLHIFLQ IAEAVEFLHS KGLMHRDLKP SNIFFTMDDV 950
    VKVGDFGLVT AMDQDEEEQT VLTPMPAYAR HTGQVGTKLY MSPEQIHGNS 1000
    YSHKVDIFSL GLILFELLYP FSTQMERVRT LTDVRNLKFP PLFTQKYPCE 1050
    YVMVQDMLSP SPMERPEAIN IIENAVFEDL DFPGKTVLRQ RSRSLSSSGT 1100
    KHSRQSNNSH SPLPSN 1116
    Length:1,116
    Mass (Da):125,216
    Last modified:May 18, 2010 - v3
    Checksum:i95FEB5DAE8D3D452
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti14 – 141Missing in AAD19961. (PubMed:10026192)Curated
    Sequence conflicti14 – 141Missing in AAF61199. (PubMed:10677345)Curated
    Sequence conflicti14 – 141Missing in AAF91480. (PubMed:10932183)Curated
    Sequence conflicti14 – 141Missing in BAG37696. (PubMed:14702039)Curated
    Sequence conflicti14 – 141Missing in AAI26357. (PubMed:15489334)Curated
    Sequence conflicti490 – 4901N → H in AAF61199. (PubMed:10677345)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti136 – 1361S → C.2 Publications
    Corresponds to variant rs867529 [ dbSNP | Ensembl ].
    VAR_011409
    Natural varianti166 – 1661Q → R.3 Publications
    Corresponds to variant rs13045 [ dbSNP | Ensembl ].
    VAR_011410
    Natural varianti566 – 5661D → V.1 Publication
    Corresponds to variant rs55791823 [ dbSNP | Ensembl ].
    VAR_040477
    Natural varianti588 – 5881R → Q in WRS; in a Pakistani family; probable complete loss of activity. 1 Publication
    VAR_011408
    Natural varianti704 – 7041A → S.3 Publications
    Corresponds to variant rs1805165 [ dbSNP | Ensembl ].
    VAR_011411
    Natural varianti716 – 7161P → L.1 Publication
    VAR_040478

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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_004836.5.
    UniGeneiHs.591589.

    Genome annotation databases

    EnsembliENST00000303236; ENSP00000307235; ENSG00000172071.
    GeneIDi9451.
    KEGGihsa:9451.
    UCSCiuc002stc.4. human.

    Polymorphism databases

    DMDMi296439367.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS33241.1.
    RefSeqi NP_004827.4. NM_004836.5.
    UniGenei Hs.591589.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4G31 X-ray 2.28 A 588-1093 [» ]
    4G34 X-ray 2.70 A 588-1093 [» ]
    ProteinModelPortali Q9NZJ5.
    SMRi Q9NZJ5. Positions 588-660, 830-1116.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114840. 10 interactions.
    IntActi Q9NZJ5. 4 interactions.
    STRINGi 9606.ENSP00000307235.

    Chemistry

    BindingDBi Q9NZJ5.
    ChEMBLi CHEMBL6030.
    GuidetoPHARMACOLOGYi 2017.

    PTM databases

    PhosphoSitei Q9NZJ5.

    Polymorphism databases

    DMDMi 296439367.

    Proteomic databases

    MaxQBi Q9NZJ5.
    PaxDbi Q9NZJ5.
    PRIDEi Q9NZJ5.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000303236 ; ENSP00000307235 ; ENSG00000172071 .
    GeneIDi 9451.
    KEGGi hsa:9451.
    UCSCi uc002stc.4. human.

    Organism-specific databases

    CTDi 9451.
    GeneCardsi GC02M088857.
    H-InvDB HIX0023925.
    HIX0030379.
    HGNCi HGNC:3255. EIF2AK3.
    HPAi CAB009204.
    HPA015737.
    MIMi 226980. phenotype.
    604032. gene.
    neXtProti NX_Q9NZJ5.
    Orphaneti 1667. Wolcott-Rallison syndrome.
    PharmGKBi PA27687.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOVERGENi HBG051431.
    InParanoidi Q9NZJ5.
    KOi K08860.
    OMAi KGLMHRD.
    PhylomeDBi Q9NZJ5.
    TreeFami TF101511.

    Enzyme and pathway databases

    Reactomei REACT_18277. PERK regulates gene expression.
    SignaLinki Q9NZJ5.

    Miscellaneous databases

    ChiTaRSi EIF2AK3. human.
    GeneWikii EIF2AK3.
    GenomeRNAii 9451.
    NextBioi 35404.
    PROi Q9NZJ5.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9NZJ5.
    Bgeei Q9NZJ5.
    CleanExi HS_EIF2AK3.
    Genevestigatori Q9NZJ5.

    Family and domain databases

    Gene3Di 2.140.10.10. 1 hit.
    InterProi IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR027295. Quinonprotein_ADH-like_fam.
    IPR011047. Quinonprotein_ADH-like_supfam.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view ]
    Pfami PF00069. Pkinase. 2 hits.
    [Graphical view ]
    SUPFAMi SSF50998. SSF50998. 2 hits.
    SSF56112. SSF56112. 2 hits.
    PROSITEi PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Characterization of a mutant pancreatic eIF-2alpha kinase, PEK, and co-localization with somatostatin in islet delta cells."
      Shi Y., An J., Liang J., Hayes S.E., Sandusky G.E., Stramm L.E., Yang N.N.
      J. Biol. Chem. 274:5723-5730(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, VARIANTS ARG-166 AND SER-704.
      Tissue: Liver, Pancreas and Testis.
    2. "Pancreatic eukaryotic initiation factor-2alpha kinase (PEK) homologues in humans, Drosophila melanogaster and Caenorhabditis elegans that mediate translational control in response to endoplasmic reticulum stress."
      Sood R., Porter A.C., Ma K., Quilliam L.A., Wek R.C.
      Biochem. J. 346:281-293(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, VARIANTS ARG-166 AND SER-704.
      Tissue: Brain and Pancreas.
    3. "EIF2AK3, encoding translation initiation factor 2-alpha kinase 3, is mutated in patients with Wolcott-Rallison syndrome."
      Delepine M., Nicolino M., Barrett T., Golamaully M., Lathrop G.M., Julier C.
      Nat. Genet. 25:406-409(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT WRS GLN-588, VARIANT CYS-136.
    4. "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].
      Tissue: Brain.
    5. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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], VARIANTS ARG-166 AND SER-704.
    7. "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-715, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. "H2s-induced sulfhydration of the phosphatase PTP1B and its role in the endoplasmic reticulum stress response."
      Krishnan N., Fu C., Pappin D.J., Tonks N.K.
      Sci. Signal. 4:RA86-RA86(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT TYR-619, DEPHOSPHORYLATION AT TYR-619.
    9. "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-1094, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. "PARP16 is a tail-anchored endoplasmic reticulum protein required for the PERK-and IRE1alpha-mediated unfolded protein response."
      Jwa M., Chang P.
      Nat. Cell Biol. 14:1223-1230(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ADP-RIBOSYLATION BY PARP16.
    11. "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] CYS-136; VAL-566 AND LEU-716.

    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: October 1, 2014
    This is version 144 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

    External Data

    Dasty 3