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Q9BQI3

- E2AK1_HUMAN

UniProt

Q9BQI3 - E2AK1_HUMAN

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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

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
Complete GO annotation...

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-KW
Complete GO annotation...

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

BgeeiQ9BQI3.
CleanExiHS_EIF2AK1.
ExpressionAtlasiQ9BQI3. baseline and differential.
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. 9 interactions.
IntActiQ9BQI3. 4 interactions.
MINTiMINT-4715350.
STRINGi9606.ENSP00000199389.

Structurei

3D structure databases

ProteinModelPortaliQ9BQI3.
SMRiQ9BQI3. Positions 176-227, 316-618.
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.
GeneTreeiENSGT00530000062984.
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

        10         20         30         40         50
MQGGNSGVRK REEEGDGAGA VAAPPAIDFP AEGPDPEYDE SDVPAEIQVL
60 70 80 90 100
KEPLQQPTFP FAVANQLLLV SLLEHLSHVH EPNPLRSRQV FKLLCQTFIK
110 120 130 140 150
MGLLSSFTCS DEFSSLRLHH NRAITHLMRS AKERVRQDPC EDISRIQKIR
160 170 180 190 200
SREVALEAQT SRYLNEFEEL AILGKGGYGR VYKVRNKLDG QYYAIKKILI
210 220 230 240 250
KGATKTVCMK VLREVKVLAG LQHPNIVGYH TAWIEHVHVI QPRADRAAIE
260 270 280 290 300
LPSLEVLSDQ EEDREQCGVK NDESSSSSII FAEPTPEKEK RFGESDTENQ
310 320 330 340 350
NNKSVKYTTN LVIRESGELE STLELQENGL AGLSASSIVE QQLPLRRNSH
360 370 380 390 400
LEESFTSTEE SSEENVNFLG QTEAQYHLML HIQMQLCELS LWDWIVERNK
410 420 430 440 450
RGREYVDESA CPYVMANVAT KIFQELVEGV FYIHNMGIVH RDLKPRNIFL
460 470 480 490 500
HGPDQQVKIG DFGLACTDIL QKNTDWTNRN GKRTPTHTSR VGTCLYASPE
510 520 530 540 550
QLEGSEYDAK SDMYSLGVVL LELFQPFGTE MERAEVLTGL RTGQLPESLR
560 570 580 590 600
KRCPVQAKYI QHLTRRNSSQ RPSAIQLLQS ELFQNSGNVN LTLQMKIIEQ
610 620 630
EKEIAELKKQ LNLLSQDKGV RDDGKDGGVG
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. Curated
The sequence AAF71057.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAA92607.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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, 316-618.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 118002. 9 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.
GeneTreei ENSGT00530000062984.
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

Bgeei Q9BQI3.
CleanExi HS_EIF2AK1.
ExpressionAtlasi Q9BQI3. baseline and differential.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 146 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

Dasty 3