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Q9Z2R9

- E2AK1_MOUSE

UniProt

Q9Z2R9 - E2AK1_MOUSE

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Protein
Eukaryotic translation initiation factor 2-alpha kinase 1
Gene
Eif2ak1, Hri
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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.3 Publications

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.3 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei80 – 801Heme-binding By similarity
Binding sitei196 – 1961ATP By similarity
Active sitei440 – 4401Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi173 – 1819ATP By similarity

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 binding Source: IntAct
  5. protein homodimerization activity Source: UniProtKB
  6. protein kinase activity Source: MGI

GO - Biological processi

  1. negative regulation of cell proliferation Source: UniProtKB
  2. negative regulation of hemoglobin biosynthetic process Source: UniProtKB
  3. negative regulation of translation Source: UniProtKB-KW
  4. protein autophosphorylation Source: UniProtKB
  5. protoporphyrinogen IX metabolic process Source: MGI
  6. regulation of eIF2 alpha phosphorylation by heme Source: MGI
  7. regulation of hemoglobin biosynthetic process Source: MGI
  8. regulation of translation Source: MGI
  9. response to external stimulus Source: UniProtKB
  10. response to stress Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

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

Keywords - Ligandi

ATP-binding, Nucleotide-binding

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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 5

Organism-specific databases

MGIiMGI:1353448. Eif2ak1.

Subcellular locationi

Cytoplasm 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Involvement in diseasei

Defects in Eif2ak1 are a cause of hyperchromic anemia in animals suffering from iron deficiency. The number of red blood cells is decreased due to increased apoptosis of erythroid precursor cells, probably because globins misfold and aggregate in the absence of heme.

Disruption phenotypei

Mice are viable and fertile without gross morphological abnormalities. Dramatically altered response to diet-induced iron deficiency shifting from an adaptive decrease in RBC volume and intracellular hemoglobin content to an increased production of abnormally dense red blood cells (RBCs) with decreasing red cell counts. The decrease in RBC number is the result of increased apoptosis of erythroid precursors. Diminished levels of phosphorylated EIF2S1 in bone marrow-derived macrophages (BMDMs). Impaired maturation of BMDMs and blunted inflammatory response to LPS with a reduced cytokine production. Impaired phagocytosis of senescent RBCs by macrophages, resulting in a lower phagocytosis index and lower percentage of macrophages with ingested RBC. In hepatocytes, cytochromes P450 CYP2B6 and CYP3A induction by phenobarbital is not impaired in response to acute heme depletion and CYP2B6 and CYP3A proteins continue to accumulate to supranormal levels, irrespective of the hepatic heme pool status. These cells also exhibit a weak, albeit significant, elevation of the basal ER-stress as reflected by elevated levels of autophosphorylated EIF2AK3/PERK and EIF2AK4/GCN2, the ER-stress related chaperones HSPA5 and HSP90B1, and total hepatic protein ubiquitination.3 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi196 – 1961K → R: Abolishes kinase activity. 2 Publications
Mutagenesisi483 – 4831T → A: No effect on kinase activity. 1 Publication
Mutagenesisi483 – 4831T → D: No effect on kinase activity. 1 Publication
Mutagenesisi485 – 4851T → A: Abolishes kinase activity. 1 Publication
Mutagenesisi485 – 4851T → D: Constitutively active kinase; loss of regulation by heme and arsenite. 1 Publication
Mutagenesisi490 – 4901T → A: Almost complete loss of kinase activity; even upon arsenite treatment. 1 Publication
Mutagenesisi490 – 4901T → D: Almost complete loss of kinase activity; even upon arsenite treatment. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 619619Eukaryotic translation initiation factor 2-alpha kinase 1
PRO_0000085942Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei483 – 4831Phosphothreonine; by autocatalysis1 Publication
Modified residuei485 – 4851Phosphothreonine; by autocatalysis1 Publication
Modified residuei490 – 4901Phosphothreonine; by autocatalysis1 Publication

Post-translational modificationi

Activated by autophosphorylation; phosphorylated predominantly on serine and threonine residues, but also on tyrosine residues. Autophosphorylation at Thr-485 is required for kinase activation. The active autophosphorylated form apparently is largely refractory to cellular heme fluctuations.3 Publications

Keywords - PTMi

Disulfide bond, Phosphoprotein

Proteomic databases

PRIDEiQ9Z2R9.

PTM databases

PhosphoSiteiQ9Z2R9.

Expressioni

Tissue specificityi

Expressed predominantly in erythroid cells, mature reticulocytes, as well as fetal liver nucleated erythroid cells. At much lower levels, expressed in hepatocytes and bone marrow-derived macrophages (at protein level).3 Publications

Developmental stagei

Highly expressed in fetal liver erythroid precursor cells at 14.5 dpc (at protein level).1 Publication

Inductioni

By phenobarbital.5 Publications

Gene expression databases

ArrayExpressiQ9Z2R9.
BgeeiQ9Z2R9.
GenevestigatoriQ9Z2R9.

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 By similarity. Forms oligomers. Has been reported as a homodimer, as well as a hexamer in the absence of hemin. Converted to an inactive disulfide linked homodimer in the presence of hemin.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
Eif2s1Q6ZWX66EBI-642878,EBI-1202234

Protein-protein interaction databases

BioGridi200421. 1 interaction.
IntActiQ9Z2R9. 2 interactions.
MINTiMINT-1746990.
STRINGi10090.ENSMUSP00000098056.

Structurei

3D structure databases

ProteinModelPortaliQ9Z2R9.
SMRiQ9Z2R9. Positions 162-235, 378-619.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini167 – 580414Protein kinase
Add
BLAST
Repeati408 – 4136HRM 1
Repeati549 – 5546HRM 2

Sequence similaritiesi

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00530000062984.
HOVERGENiHBG051429.
InParanoidiQ69ZK8.
KOiK16194.
OMAiNADWTNR.
OrthoDBiEOG70GMF6.
PhylomeDBiQ9Z2R9.
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]

Sequencei

Sequence statusi: Complete.

Q9Z2R9-1 [UniParc]FASTAAdd to Basket

« Hide

MLGGSSVDGE RDTDDDAAGA VAAPPAIDFP AEVSDPKYDE SDVPAELQVL    50
KEPLQQPTFP FLVANQLLLV SLLEHLSHVH EPNPLHSKQV FKLLCQTFIK 100
MGLLSSFTCS DEFSSLRLHH NRAITHLMRS AKERVRQDPC QDNSYMQKIR 150
SREIAFEAQT SRYLNEFEEL AILGKGGYGR VYKVRNKLDG QHYAIKKILI 200
KSATKTDCMK VLREVKVLAG LQHPNIVGYH TAWIEHVHVV QPQDRVPIQL 250
PSLEVLSEQE GDRDQGGVKD NESSSSIVFA ELTPEKEKPF GESEVKNENN 300
NLVSYTANLV VRNSSESESS IELQEDGLTD LSVRPVVRHQ LPLGHSSELE 350
GNFTSTDESS EGNLNLLGQT EVRYHLMLHI QMQLCELSLW DWITERNKRS 400
REYVDEAACP YVMASVATKI FQELVEGVFY IHNMGIVHRD LKPRNIFLHG 450
PDQQVKIGDF GLACADIIQN ADWTNRNGKG TRTHTSRVGT CLYASPEQLE 500
GSQYDAKSDM YSLGVILLEL FQPFGTEMER ATVLTGVRTG RIPESLSKRC 550
PVQAKYIQLL TGRNVSQRPS ALQLLQSELF QTTGNVNLTL QMKIIEQEKE 600
IEELKKQLSL LSQDRGLKR 619
Length:619
Mass (Da):69,702
Last modified:April 5, 2011 - v2
Checksum:i39DC5FF950C92F2A
GO

Sequence cautioni

The sequence BAD32438.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti20 – 201A → S in BAB32242. 1 Publication
Sequence conflicti71 – 711S → C in BAB32242. 1 Publication
Sequence conflicti138 – 15013DPCQD…MQKIR → VSPTGCTLYDKYI in BAB32242. 1 Publication
Add
BLAST
Sequence conflicti196 – 1972KK → IE in BAB29545. 1 Publication
Sequence conflicti371 – 3711E → D in AAC79201. 1 Publication
Sequence conflicti371 – 3711E → D in AAK55766. 1 Publication
Sequence conflicti565 – 5651V → A in AAH28923. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF028808 mRNA. Translation: AAC79201.1.
AY033898 mRNA. Translation: AAK55766.1.
AK173160 mRNA. Translation: BAD32438.1. Different initiation.
BC028923 mRNA. Translation: AAH28923.1.
BC111035 mRNA. Translation: AAI11036.1.
AK014775 mRNA. Translation: BAB29545.1.
AK020887 mRNA. Translation: BAB32242.1.
AK032508 mRNA. Translation: BAC27901.1.
RefSeqiNP_038585.2. NM_013557.2.
UniGeneiMm.389709.
Mm.431968.

Genome annotation databases

EnsembliENSMUST00000100487; ENSMUSP00000098056; ENSMUSG00000029613.
GeneIDi15467.
KEGGimmu:15467.
UCSCiuc029vqe.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF028808 mRNA. Translation: AAC79201.1 .
AY033898 mRNA. Translation: AAK55766.1 .
AK173160 mRNA. Translation: BAD32438.1 . Different initiation.
BC028923 mRNA. Translation: AAH28923.1 .
BC111035 mRNA. Translation: AAI11036.1 .
AK014775 mRNA. Translation: BAB29545.1 .
AK020887 mRNA. Translation: BAB32242.1 .
AK032508 mRNA. Translation: BAC27901.1 .
RefSeqi NP_038585.2. NM_013557.2.
UniGenei Mm.389709.
Mm.431968.

3D structure databases

ProteinModelPortali Q9Z2R9.
SMRi Q9Z2R9. Positions 162-235, 378-619.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 200421. 1 interaction.
IntActi Q9Z2R9. 2 interactions.
MINTi MINT-1746990.
STRINGi 10090.ENSMUSP00000098056.

Chemistry

ChEMBLi CHEMBL1938213.

PTM databases

PhosphoSitei Q9Z2R9.

Proteomic databases

PRIDEi Q9Z2R9.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000100487 ; ENSMUSP00000098056 ; ENSMUSG00000029613 .
GeneIDi 15467.
KEGGi mmu:15467.
UCSCi uc029vqe.1. mouse.

Organism-specific databases

CTDi 27102.
MGIi MGI:1353448. Eif2ak1.

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00530000062984.
HOVERGENi HBG051429.
InParanoidi Q69ZK8.
KOi K16194.
OMAi NADWTNR.
OrthoDBi EOG70GMF6.
PhylomeDBi Q9Z2R9.
TreeFami TF329383.

Miscellaneous databases

ChiTaRSi EIF2AK1. mouse.
NextBioi 288300.
PROi Q9Z2R9.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9Z2R9.
Bgeei Q9Z2R9.
Genevestigatori Q9Z2R9.

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

« Hide 'large scale' publications
  1. "Characterization of the hemin-sensitive eukaryotic initiation factor 2alpha kinase from mouse nonerythroid cells."
    Berlanga J.J., Herrero S., de Haro C.
    J. Biol. Chem. 273:32340-32346(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], MUTAGENESIS OF LYS-196, AUTOPHOSPHORYLATION.
    Strain: C57BL/6 X CBA.
    Tissue: Liver.
  2. "Heme-regulated eIF2alpha kinase (HRI) is required for translational regulation and survival of erythroid precursors in iron deficiency."
    Han A.-P., Yu C., Lu L., Fujiwara Y., Browne C., Chin G., Fleming M., Leboulch P., Orkin S.H., Chen J.-J.
    EMBO J. 20:6909-6918(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DISRUPTION PHENOTYPE.
    Tissue: Erythroleukemia.
  3. "Prediction of the coding sequences of mouse homologues of KIAA gene: IV. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
    Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H., Nagase T., Ohara O., Koga H.
    DNA Res. 11:205-218(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Pancreatic islet.
  4. "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].
    Strain: C57BL/6J and FVB/N.
    Tissue: Eye and Salivary gland.
  5. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-211 AND 445-619.
    Strain: C57BL/6J.
    Tissue: Head, Olfactory bulb and Retina.
  6. "Multiple autophosphorylation is essential for the formation of the active and stable homodimer of heme-regulated eIF2alpha kinase."
    Bauer B.N., Rafie-Kolpin M., Lu L., Han A., Chen J.-J.
    Biochemistry 40:11543-11551(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: AUTOPHOSPHORYLATION, HEME-BINDING.
  7. "Translation initiation control by heme-regulated eukaryotic initiation factor 2alpha kinase in erythroid cells under cytoplasmic stresses."
    Lu L., Han A.P., Chen J.J.
    Mol. Cell. Biol. 21:7971-7980(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: REGULATION BY HEME DEFICIENCY; HEAT SHOCK; OSMOTIC STRESS AND OXIDATIVE STRESS, TISSUE SPECIFICITY.
  8. "Autophosphorylation of threonine 485 in the activation loop is essential for attaining eIF2alpha kinase activity of HRI."
    Rafie-Kolpin M., Han A.P., Chen J.J.
    Biochemistry 42:6536-6544(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: AUTOPHOSPHORYLATION AT THR-483; THR-485 AND THR-490, ENZYME REGULATION, MUTAGENESIS OF LYS-196; THR-483; THR-485 AND THR-490.
  9. "Activation of heme-regulated eukaryotic initiation factor 2alpha kinase by nitric oxide is induced by the formation of a five-coordinate NO-heme complex: optical absorption, electron spin resonance, and resonance raman spectral studies."
    Igarashi J., Sato A., Kitagawa T., Yoshimura T., Yamauchi S., Sagami I., Shimizu T.
    J. Biol. Chem. 279:15752-15762(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: HEME-BINDING, ENZYME REGULATION.
  10. "Characterization of heme-regulated eIF2alpha kinase: roles of the N-terminal domain in the oligomeric state, heme binding, catalysis, and inhibition."
    Miksanova M., Igarashi J., Minami M., Sagami I., Yamauchi S., Kurokawa H., Shimizu T.
    Biochemistry 45:9894-9905(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, OLIGOMERIZATION, HEME-BINDING, INDUCTION.
  11. "The function of heme-regulated eIF2alpha kinase in murine iron homeostasis and macrophage maturation."
    Liu S., Suragani R.N., Wang F., Han A., Zhao W., Andrews N.C., Chen J.J.
    J. Clin. Invest. 117:3296-3305(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE.
  12. "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: FUNCTION, TISSUE SPECIFICITY, ENZYME REGULATION, DISRUPTION PHENOTYPE.

Entry informationi

Entry nameiE2AK1_MOUSE
AccessioniPrimary (citable) accession number: Q9Z2R9
Secondary accession number(s): Q2TA96
, Q69ZK8, Q8C024, Q8K123, Q9CTP5, Q9D601
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: April 5, 2011
Last modified: June 11, 2014
This is version 129 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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