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Q9BQI3

- E2AK1_HUMAN

UniProt

Q9BQI3 - E2AK1_HUMAN

Protein

Eukaryotic translation initiation factor 2-alpha kinase 1

Gene

EIF2AK1

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 2 (20 Jun 2003)
      Previous versions | rss
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    Functioni

    Inhibits protein synthesis at the translation initiation level, in response to various stress conditions, including oxidative stress, heme deficiency, osmotic shock and heat shock. Exerts its function through the phosphorylation of EIF2S1 at 'Ser-48' and 'Ser-51', thus preventing its recycling. Binds hemin forming a 1:1 complex through a cysteine thiolate and histidine nitrogenous coordination. This binding occurs with moderate affinity, allowing it to sense the heme concentration within the cell. Thanks to this unique heme-sensing capacity, plays a crucial role to shut off protein synthesis during acute heme-deficient conditions. In red blood cells (RBCs), controls hemoglobin synthesis ensuring a coordinated regulation of the synthesis of its heme and globin moieties. Thus plays an essential protective role for RBC survival in anemias of iron deficiency. Similarly, in hepatocytes, involved in heme-mediated translational control of CYP2B and CYP3A and possibly other hepatic P450 cytochromes. May also contain ER stress during acute heme-deficient conditions By similarity.By similarity

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.

    Enzyme regulationi

    Induced by acute heme depletion, that not only increases EIF2AK1 protein levels, but also stimulates kinase activity by autophosphorylation. Inhibited by the heme-degradation products biliverdin and bilirubin. Induced by oxidative stress generated by arsenite treatment. Binding of nitric oxide (NO) to the heme iron in the N-terminal heme-binding domain activates the kinase activity, while binding of carbon monoxide (CO) suppresses kinase activity By similarity.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei80 – 801Heme-bindingBy similarity
    Binding sitei196 – 1961ATPPROSITE-ProRule annotation
    Active sitei442 – 4421Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi173 – 1819ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. eukaryotic translation initiation factor 2alpha kinase activity Source: UniProtKB
    3. heme binding Source: UniProtKB
    4. protein homodimerization activity Source: UniProtKB

    GO - Biological processi

    1. negative regulation of cell proliferation Source: Ensembl
    2. negative regulation of hemoglobin biosynthetic process Source: UniProtKB
    3. negative regulation of translational initiation by iron Source: UniProtKB
    4. protein autophosphorylation Source: UniProtKB
    5. protoporphyrinogen IX metabolic process Source: Ensembl
    6. regulation of eIF2 alpha phosphorylation by heme Source: Ensembl
    7. response to external stimulus Source: UniProtKB
    8. response to stress Source: UniProtKB

    Keywords - Molecular functioni

    Kinase, Protein synthesis inhibitor, Serine/threonine-protein kinase, Transferase

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    SignaLinkiQ9BQI3.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Eukaryotic translation initiation factor 2-alpha kinase 1 (EC:2.7.11.1)
    Alternative name(s):
    Heme-controlled repressor
    Short name:
    HCR
    Heme-regulated eukaryotic initiation factor eIF-2-alpha kinase
    Heme-regulated inhibitor
    Hemin-sensitive initiation factor 2-alpha kinase
    Gene namesi
    Name:EIF2AK1
    Synonyms:HRI, KIAA1369
    ORF Names:PRO1362
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 7

    Organism-specific databases

    HGNCiHGNC:24921. EIF2AK1.

    Subcellular locationi

    Cytoplasm By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA134919097.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 630630Eukaryotic translation initiation factor 2-alpha kinase 1PRO_0000085941Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei486 – 4861Phosphothreonine; by autocatalysisBy similarity
    Modified residuei488 – 4881Phosphothreonine; by autocatalysisBy similarity

    Post-translational modificationi

    Activated by autophosphorylation; phosphorylated predominantly on serine and threonine residues, but also on tyrosine residues. Autophosphorylation at Thr-488 is required for kinase activation. The active autophosphorylated form apparently is largely refractory to cellular heme fluctuations By similarity.By similarity

    Keywords - PTMi

    Disulfide bond, Phosphoprotein

    Proteomic databases

    MaxQBiQ9BQI3.
    PaxDbiQ9BQI3.
    PRIDEiQ9BQI3.

    PTM databases

    PhosphoSiteiQ9BQI3.

    Expressioni

    Tissue specificityi

    Expressed predominantly in erythroid cells. At much lower levels, expressed in hepatocytes (at protein level).1 Publication

    Gene expression databases

    ArrayExpressiQ9BQI3.
    BgeeiQ9BQI3.
    CleanExiHS_EIF2AK1.
    GenevestigatoriQ9BQI3.

    Organism-specific databases

    HPAiCAB022082.
    HPA016496.

    Interactioni

    Subunit structurei

    Synthesized in an inactive form that binds to the N-terminal domain of CDC37. Has to be associated with a multiprotein complex containing Hsp90, CDC37 and PPP5C for maturation and activation by autophosphorylation. The phosphatase PPP5C modulates this activation. Forms oligomers. Has been reported as a non-covalently bound homodimer, as well as a hexamer in the absence of hemin. Converted to an inactive disulfide linked homodimer in the presence of hemin By similarity.By similarity

    Protein-protein interaction databases

    BioGridi118002. 5 interactions.
    IntActiQ9BQI3. 4 interactions.
    MINTiMINT-4715350.
    STRINGi9606.ENSP00000199389.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9BQI3.
    SMRiQ9BQI3. Positions 176-227, 316-614.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini167 – 583417Protein kinasePROSITE-ProRule annotationAdd
    BLAST
    Repeati410 – 4156HRM 1
    Repeati552 – 5576HRM 2

    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

    Repeat

    Phylogenomic databases

    eggNOGiCOG0515.
    HOVERGENiHBG051429.
    InParanoidiQ9BQI3.
    KOiK16194.
    OrthoDBiEOG70GMF6.
    PhylomeDBiQ9BQI3.
    TreeFamiTF329383.

    Family and domain databases

    InterProiIPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view]
    PfamiPF00069. Pkinase. 2 hits.
    [Graphical view]
    SUPFAMiSSF56112. SSF56112. 2 hits.
    PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9BQI3-1) [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

    MQGGNSGVRK REEEGDGAGA VAAPPAIDFP AEGPDPEYDE SDVPAEIQVL    50
    KEPLQQPTFP FAVANQLLLV SLLEHLSHVH EPNPLRSRQV FKLLCQTFIK 100
    MGLLSSFTCS DEFSSLRLHH NRAITHLMRS AKERVRQDPC EDISRIQKIR 150
    SREVALEAQT SRYLNEFEEL AILGKGGYGR VYKVRNKLDG QYYAIKKILI 200
    KGATKTVCMK VLREVKVLAG LQHPNIVGYH TAWIEHVHVI QPRADRAAIE 250
    LPSLEVLSDQ EEDREQCGVK NDESSSSSII FAEPTPEKEK RFGESDTENQ 300
    NNKSVKYTTN LVIRESGELE STLELQENGL AGLSASSIVE QQLPLRRNSH 350
    LEESFTSTEE SSEENVNFLG QTEAQYHLML HIQMQLCELS LWDWIVERNK 400
    RGREYVDESA CPYVMANVAT KIFQELVEGV FYIHNMGIVH RDLKPRNIFL 450
    HGPDQQVKIG DFGLACTDIL QKNTDWTNRN GKRTPTHTSR VGTCLYASPE 500
    QLEGSEYDAK SDMYSLGVVL LELFQPFGTE MERAEVLTGL RTGQLPESLR 550
    KRCPVQAKYI QHLTRRNSSQ RPSAIQLLQS ELFQNSGNVN LTLQMKIIEQ 600
    EKEIAELKKQ LNLLSQDKGV RDDGKDGGVG 630
    Length:630
    Mass (Da):71,106
    Last modified:June 20, 2003 - v2
    Checksum:iD63021651806620B
    GO
    Isoform 2 (identifier: Q9BQI3-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         244-244: Missing.

    Show »
    Length:629
    Mass (Da):71,035
    Checksum:iB90159795D580809
    GO

    Sequence cautioni

    The sequence AAF70289.1 differs from that shown. Reason: Frameshift at positions 24, 26 and 33.
    The sequence AAF71057.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence BAA92607.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti2 – 21Q → L in AAF18391. 1 PublicationCurated
    Sequence conflicti4 – 41G → D in BAF83016. (PubMed:14702039)Curated
    Sequence conflicti24 – 329PPAIDFPAE → RRHRLSRR in AAF70289. (PubMed:11101152)Curated
    Sequence conflicti137 – 1371Q → R in AAF70289. (PubMed:11101152)Curated
    Sequence conflicti149 – 1491I → T in BAF83016. (PubMed:14702039)Curated
    Sequence conflicti171 – 1711A → V in AAF18391. 1 PublicationCurated
    Sequence conflicti206 – 2061T → P in AAF66736. (PubMed:12391722)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti117 – 1171R → T.1 Publication
    Corresponds to variant rs34889754 [ dbSNP | Ensembl ].
    VAR_040466
    Natural varianti132 – 1321K → T.1 Publication
    Corresponds to variant rs34851195 [ dbSNP | Ensembl ].
    VAR_040467
    Natural varianti134 – 1341R → K.1 Publication
    Corresponds to variant rs55744865 [ dbSNP | Ensembl ].
    VAR_040468
    Natural varianti139 – 1391P → S.1 Publication
    Corresponds to variant rs55963745 [ dbSNP | Ensembl ].
    VAR_040469
    Natural varianti145 – 1451R → H.1 Publication
    Corresponds to variant rs55971369 [ dbSNP | Ensembl ].
    VAR_040470
    Natural varianti202 – 2021G → S in a lung adenocarcinoma sample; somatic mutation. 1 Publication
    VAR_040471
    Natural varianti292 – 2921F → L.1 Publication
    Corresponds to variant rs55982710 [ dbSNP | Ensembl ].
    VAR_040472
    Natural varianti319 – 3191L → H.1 Publication
    Corresponds to variant rs34909691 [ dbSNP | Ensembl ].
    VAR_040473
    Natural varianti558 – 5581K → R.3 Publications
    Corresponds to variant rs2640 [ dbSNP | Ensembl ].
    VAR_015732

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei244 – 2441Missing in isoform 2. 3 PublicationsVSP_007589

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF255050 mRNA. Translation: AAF70289.1. Frameshift.
    AF100784 mRNA. Translation: AAP97223.1.
    AF181071 mRNA. Translation: AAF18391.1.
    AB037790 mRNA. Translation: BAA92607.1. Different initiation.
    AF183414 mRNA. Translation: AAG09683.1.
    AL136563 mRNA. Translation: CAB66498.1.
    AF147094 mRNA. Translation: AAF66736.1.
    AK075192 mRNA. Translation: BAC11461.1.
    AK290327 mRNA. Translation: BAF83016.1.
    AL834494 mRNA. Translation: CAD39152.1.
    CH236963 Genomic DNA. Translation: EAL23714.1.
    CH878731 Genomic DNA. Translation: EAW55049.1.
    BC006524 mRNA. Translation: AAH06524.1.
    AF116634 mRNA. Translation: AAF71057.1. Different initiation.
    CCDSiCCDS5345.1. [Q9BQI3-1]
    RefSeqiNP_001127807.1. NM_001134335.1. [Q9BQI3-2]
    NP_055228.2. NM_014413.3. [Q9BQI3-1]
    UniGeneiHs.520205.

    Genome annotation databases

    EnsembliENST00000199389; ENSP00000199389; ENSG00000086232. [Q9BQI3-1]
    GeneIDi27102.
    KEGGihsa:27102.
    UCSCiuc003spp.3. human. [Q9BQI3-1]
    uc003spq.3. human. [Q9BQI3-2]

    Polymorphism databases

    DMDMi32172458.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF255050 mRNA. Translation: AAF70289.1 . Frameshift.
    AF100784 mRNA. Translation: AAP97223.1 .
    AF181071 mRNA. Translation: AAF18391.1 .
    AB037790 mRNA. Translation: BAA92607.1 . Different initiation.
    AF183414 mRNA. Translation: AAG09683.1 .
    AL136563 mRNA. Translation: CAB66498.1 .
    AF147094 mRNA. Translation: AAF66736.1 .
    AK075192 mRNA. Translation: BAC11461.1 .
    AK290327 mRNA. Translation: BAF83016.1 .
    AL834494 mRNA. Translation: CAD39152.1 .
    CH236963 Genomic DNA. Translation: EAL23714.1 .
    CH878731 Genomic DNA. Translation: EAW55049.1 .
    BC006524 mRNA. Translation: AAH06524.1 .
    AF116634 mRNA. Translation: AAF71057.1 . Different initiation.
    CCDSi CCDS5345.1. [Q9BQI3-1 ]
    RefSeqi NP_001127807.1. NM_001134335.1. [Q9BQI3-2 ]
    NP_055228.2. NM_014413.3. [Q9BQI3-1 ]
    UniGenei Hs.520205.

    3D structure databases

    ProteinModelPortali Q9BQI3.
    SMRi Q9BQI3. Positions 176-227, 316-614.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 118002. 5 interactions.
    IntActi Q9BQI3. 4 interactions.
    MINTi MINT-4715350.
    STRINGi 9606.ENSP00000199389.

    Chemistry

    BindingDBi Q9BQI3.
    ChEMBLi CHEMBL6029.
    GuidetoPHARMACOLOGYi 2015.

    PTM databases

    PhosphoSitei Q9BQI3.

    Polymorphism databases

    DMDMi 32172458.

    Proteomic databases

    MaxQBi Q9BQI3.
    PaxDbi Q9BQI3.
    PRIDEi Q9BQI3.

    Protocols and materials databases

    DNASUi 27102.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000199389 ; ENSP00000199389 ; ENSG00000086232 . [Q9BQI3-1 ]
    GeneIDi 27102.
    KEGGi hsa:27102.
    UCSCi uc003spp.3. human. [Q9BQI3-1 ]
    uc003spq.3. human. [Q9BQI3-2 ]

    Organism-specific databases

    CTDi 27102.
    GeneCardsi GC07M006061.
    H-InvDB HIX0003741.
    HGNCi HGNC:24921. EIF2AK1.
    HPAi CAB022082.
    HPA016496.
    neXtProti NX_Q9BQI3.
    PharmGKBi PA134919097.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOVERGENi HBG051429.
    InParanoidi Q9BQI3.
    KOi K16194.
    OrthoDBi EOG70GMF6.
    PhylomeDBi Q9BQI3.
    TreeFami TF329383.

    Enzyme and pathway databases

    SignaLinki Q9BQI3.

    Miscellaneous databases

    ChiTaRSi EIF2AK1. human.
    GeneWikii EIF2AK1.
    GenomeRNAii 27102.
    NextBioi 49763.
    PROi Q9BQI3.

    Gene expression databases

    ArrayExpressi Q9BQI3.
    Bgeei Q9BQI3.
    CleanExi HS_EIF2AK1.
    Genevestigatori Q9BQI3.

    Family and domain databases

    InterProi IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view ]
    Pfami PF00069. Pkinase. 2 hits.
    [Graphical view ]
    SUPFAMi 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. "Cloning of hHRI, human heme-regulated eukaryotic initiation factor 2alpha kinase: down-regulated in epithelial ovarian cancers."
      Hwang S.-Y., Kim M.-K., Kim J.-C.
      Mol. Cells 10:584-591(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Hair follicle dermal papilla.
    2. "Cloning and sequencing of a novel human cDNA homologous to rat hemin-sensitive initiation factor 2a kinase mRNA."
      Tu Q., Yu L., Hu P.R., Fu Q., Cui Y.Y., Zhao S.Y.
      Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    3. "Cloning of the human heme-regulated eukaryotic initiation factor 2-alpha kinase from TNF-alpha stimulated dermal microvascular endothelial cells."
      Cannon G., Naik S.M., Boss J.M., Caughman S.W.
      Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Skin.
    4. "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] (ISOFORM 1).
      Tissue: Brain.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Hypothalamus.
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Amygdala.
    7. "Molecular cloning and sequencing of the human heme-regulated eukaryotic initiation factor 2 alpha (eIF-2 alpha) kinase from bone marrow culture."
      Omasa T., Chen Y.-G., Mantalaris A., Tsai Y.C., Wu J.H.
      DNA Seq. 13:133-137(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
      Tissue: Bone marrow.
    8. "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] (ISOFORM 1), VARIANT ARG-558.
      Tissue: Placenta and Tongue.
    9. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Amygdala.
    10. "Human chromosome 7: DNA sequence and biology."
      Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S.
      , Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C.
      Science 300:767-772(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    11. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    12. "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 1).
      Tissue: Ovary.
    13. "Functional prediction of the coding sequences of 121 new genes deduced by analysis of cDNA clones from human fetal liver."
      Zhang C., Yu Y., Zhang S., Wei H., Zhou G., Ouyang S., Luo L., Bi J., Liu M., He F.
      Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 450-630, VARIANT ARG-558.
      Tissue: Fetal liver.
    14. "Hsp90 regulates p50(cdc37) function during the biogenesis of the active conformation of the heme-regulated eIF2 alpha kinase."
      Shao J., Grammatikakis N., Scroggins B.T., Uma S., Huang W., Chen J.-J., Hartson S.D., Matts R.L.
      J. Biol. Chem. 276:206-214(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CDC37 AND THE HSP90 COMPLEX.
    15. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    16. "Hepatic heme-regulated inhibitor (HRI) eukaryotic initiation factor 2alpha kinase: a protagonist of heme-mediated translational control of CYP2B enzymes and a modulator of basal endoplasmic reticulum stress tone."
      Acharya P., Chen J.J., Correia M.A.
      Mol. Pharmacol. 77:575-592(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. "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] THR-117; THR-132; LYS-134; SER-139; HIS-145; SER-202; LEU-292; HIS-319 AND ARG-558.

    Entry informationi

    Entry nameiE2AK1_HUMAN
    AccessioniPrimary (citable) accession number: Q9BQI3
    Secondary accession number(s): A8K2R2
    , Q549K6, Q8NBW3, Q9HC02, Q9NYE0, Q9P0V6, Q9P1J5, Q9P2H8, Q9UHG4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 11, 2001
    Last sequence update: June 20, 2003
    Last modified: October 1, 2014
    This is version 144 of the entry and version 2 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

    Miscellaneous

    Can bind 1 molecules of heme per polypeptide chain.By similarity

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 7
      Human chromosome 7: 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. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

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