Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9NZJ5 (E2AK3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 139. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:EIF2AK3
Synonyms:PEK, PERK
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1116 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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) By similarity.

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulation

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.

Subunit structure

Forms dimers with HSPA5/BIP in resting cells. Oligomerizes in ER-stressed cells. Interacts with DNAJC3 By similarity.

Subcellular location

Endoplasmic reticulum membrane; Single-pass type I membrane protein.

Tissue specificity

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

Induction

By endoplasmic reticulum stress.

Domain

The lumenal domain senses perturbations in protein folding in the ER, probably through reversible interaction with HSPA5/BIP By similarity.

Post-translational modification

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. Ref.8

N-glycosylated By similarity.

ADP-ribosylated by PARP16 upon ER stress, which increases kinase activity.

Involvement in disease

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.3

Sequence similarities

Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. GCN2 subfamily.

Contains 1 protein kinase domain.

Ontologies

Keywords
   Biological processStress response
Translation regulation
Unfolded protein response
   Cellular componentEndoplasmic reticulum
Membrane
   Coding sequence diversityPolymorphism
   DiseaseDiabetes mellitus
Disease mutation
   DomainSignal
Transmembrane
Transmembrane helix
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMADP-ribosylation
Glycoprotein
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processER overload response

Inferred from direct assay Ref.2PubMed 11907036. Source: UniProtKB

SREBP signaling pathway

Inferred from electronic annotation. Source: Ensembl

activation of cysteine-type endopeptidase activity involved in apoptotic process

Inferred from sequence or structural similarity. Source: UniProtKB

activation of signaling protein activity involved in unfolded protein response

Traceable author statement. Source: Reactome

bone mineralization

Inferred from sequence or structural similarity. Source: UniProtKB

calcium-mediated signaling

Inferred from sequence or structural similarity. Source: UniProtKB

cellular protein metabolic process

Traceable author statement. Source: Reactome

chondrocyte development

Inferred from sequence or structural similarity. Source: UniProtKB

endocrine pancreas development

Inferred from mutant phenotype PubMed 12086964. Source: UniProtKB

endoplasmic reticulum organization

Inferred from sequence or structural similarity. Source: UniProtKB

endoplasmic reticulum unfolded protein response

Inferred from direct assay Ref.2PubMed 11907036Ref.8. Source: UniProtKB

fat cell differentiation

Inferred from electronic annotation. Source: Ensembl

insulin secretion

Inferred from sequence or structural similarity. Source: UniProtKB

insulin-like growth factor receptor signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress

Inferred from electronic annotation. Source: Ensembl

lactation

Inferred from electronic annotation. Source: Ensembl

negative regulation of myelination

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of translation

Traceable author statement PubMed 12086964. Source: UniProtKB

negative regulation of translational initiation in response to stress

Traceable author statement Ref.2PubMed 12086964. Source: UniProtKB

ossification

Inferred from mutant phenotype PubMed 12086964. Source: UniProtKB

positive regulation of protein binding

Inferred from electronic annotation. Source: Ensembl

positive regulation of signal transduction

Inferred from electronic annotation. Source: Ensembl

protein autophosphorylation

Inferred from direct assay Ref.1PubMed 11907036. Source: UniProtKB

protein homooligomerization

Inferred from mutant phenotype PubMed 11907036. Source: UniProtKB

protein phosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of fatty acid metabolic process

Inferred from electronic annotation. Source: Ensembl

response to endoplasmic reticulum stress

Inferred from mutant phenotype PubMed 19061639. Source: BHF-UCL

skeletal system development

Inferred from sequence or structural similarity. Source: UniProtKB

translation

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

endoplasmic reticulum

Inferred from sequence or structural similarity. Source: UniProtKB

endoplasmic reticulum membrane

Inferred from sequence or structural similarity. Source: UniProtKB

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

enzyme binding

Inferred from physical interaction Ref.10. Source: UniProt

eukaryotic translation initiation factor 2alpha kinase activity

Inferred from direct assay Ref.1Ref.2PubMed 11907036. Source: UniProtKB

identical protein binding

Inferred from physical interaction PubMed 11907036. Source: IntAct

protein kinase activity

Traceable author statement Ref.1. Source: ProtInc

protein phosphatase binding

Inferred from physical interaction Ref.8. Source: UniProtKB

protein serine/threonine kinase activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

itself2EBI-766076,EBI-766076

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2929 Potential
Chain30 – 11161087Eukaryotic translation initiation factor 2-alpha kinase 3
PRO_0000024322

Regions

Topological domain30 – 514485Lumenal Potential
Transmembrane515 – 53521Helical; Potential
Topological domain536 – 1116581Cytoplasmic Potential
Domain593 – 1077485Protein kinase
Nucleotide binding599 – 6079ATP By similarity
Compositional bias49 – 524Poly-Ala

Sites

Active site9371Proton acceptor By similarity
Binding site6221ATP By similarity

Amino acid modifications

Modified residue6191Phosphotyrosine Ref.8
Modified residue7151Phosphoserine Ref.7
Modified residue9821Phosphothreonine By similarity
Modified residue10941Phosphoserine Ref.9
Glycosylation2581N-linked (GlcNAc...) Potential

Natural variations

Natural variant1361S → C. Ref.3 Ref.11
Corresponds to variant rs867529 [ dbSNP | Ensembl ].
VAR_011409
Natural variant1661Q → R. Ref.1 Ref.2 Ref.6
Corresponds to variant rs13045 [ dbSNP | Ensembl ].
VAR_011410
Natural variant5661D → V. Ref.11
Corresponds to variant rs55791823 [ dbSNP | Ensembl ].
VAR_040477
Natural variant5881R → Q in WRS; in a Pakistani family; probable complete loss of activity. Ref.3
VAR_011408
Natural variant7041A → S. Ref.1 Ref.2 Ref.6
Corresponds to variant rs1805165 [ dbSNP | Ensembl ].
VAR_011411
Natural variant7161P → L. Ref.11
VAR_040478

Experimental info

Sequence conflict141Missing in AAD19961. Ref.1
Sequence conflict141Missing in AAF61199. Ref.2
Sequence conflict141Missing in AAF91480. Ref.3
Sequence conflict141Missing in BAG37696. Ref.4
Sequence conflict141Missing in AAI26357. Ref.6
Sequence conflict4901N → H in AAF61199. Ref.2

Secondary structure

.......................................... 1116
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9NZJ5 [UniParc].

Last modified May 18, 2010. Version 3.
Checksum: 95FEB5DAE8D3D452

FASTA1,116125,216
        10         20         30         40         50         60 
MERAISPGLL VRALLLLLLL LGLAARTVAA GRARGLPAPT AEAAFGLGAA AAPTSATRVP 

        70         80         90        100        110        120 
AAGAVAAAEV TVEDAEALPA AAGEQEPRGP EPDDETELRP RGRSLVIIST LDGRIAALDP 

       130        140        150        160        170        180 
ENHGKKQWDL DVGSGSLVSS SLSKPEVFGN KMIIPSLDGA LFQWDQDRES METVPFTVES 

       190        200        210        220        230        240 
LLESSYKFGD DVVLVGGKSL TTYGLSAYSG KVRYICSALG CRQWDSDEME QEEDILLLQR 

       250        260        270        280        290        300 
TQKTVRAVGP RSGNEKWNFS VGHFELRYIP DMETRAGFIE STFKPNENTE ESKIISDVEE 

       310        320        330        340        350        360 
QEAAIMDIVI KVSVADWKVM AFSKKGGHLE WEYQFCTPIA SAWLLKDGKV IPISLFDDTS 

       370        380        390        400        410        420 
YTSNDDVLED EEDIVEAARG ATENSVYLGM YRGQLYLQSS VRISEKFPSS PKALESVTNE 

       430        440        450        460        470        480 
NAIIPLPTIK WKPLIHSPSR TPVLVGSDEF DKCLSNDKFS HEEYSNGALS ILQYPYDNGY 

       490        500        510        520        530        540 
YLPYYKRERN KRSTQITVRF LDNPHYNKNI RKKDPVLLLH WWKEIVATIL FCIIATTFIV 

       550        560        570        580        590        600 
RRLFHPHPHR QRKESETQCQ TENKYDSVSG EANDSSWNDI KNSGYISRYL TDFEPIQCLG 

       610        620        630        640        650        660 
RGGFGVVFEA KNKVDDCNYA IKRIRLPNRE LAREKVMREV KALAKLEHPG IVRYFNAWLE 

       670        680        690        700        710        720 
APPEKWQEKM DEIWLKDEST DWPLSSPSPM DAPSVKIRRM DPFATKEHIE IIAPSPQRSR 

       730        740        750        760        770        780 
SFSVGISCDQ TSSSESQFSP LEFSGMDHED ISESVDAAYN LQDSCLTDCD VEDGTMDGND 

       790        800        810        820        830        840 
EGHSFELCPS EASPYVRSRE RTSSSIVFED SGCDNASSKE EPKTNRLHIG NHCANKLTAF 

       850        860        870        880        890        900 
KPTSSKSSSE ATLSISPPRP TTLSLDLTKN TTEKLQPSSP KVYLYIQMQL CRKENLKDWM 

       910        920        930        940        950        960 
NGRCTIEERE RSVCLHIFLQ IAEAVEFLHS KGLMHRDLKP SNIFFTMDDV VKVGDFGLVT 

       970        980        990       1000       1010       1020 
AMDQDEEEQT VLTPMPAYAR HTGQVGTKLY MSPEQIHGNS YSHKVDIFSL GLILFELLYP 

      1030       1040       1050       1060       1070       1080 
FSTQMERVRT LTDVRNLKFP PLFTQKYPCE YVMVQDMLSP SPMERPEAIN IIENAVFEDL 

      1090       1100       1110 
DFPGKTVLRQ RSRSLSSSGT KHSRQSNNSH SPLPSN 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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. expand/collapse author list , 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.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF110146 mRNA. Translation: AAD19961.1.
AF193339 mRNA. Translation: AAF61199.1.
AF284615 expand/collapse EMBL AC list , 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.
RefSeqNP_004827.4. NM_004836.5.
UniGeneHs.591589.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4G31X-ray2.28A588-1093[»]
4G34X-ray2.70A588-1093[»]
ProteinModelPortalQ9NZJ5.
SMRQ9NZJ5. Positions 588-1112.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114840. 9 interactions.
IntActQ9NZJ5. 4 interactions.
STRING9606.ENSP00000307235.

Chemistry

BindingDBQ9NZJ5.
ChEMBLCHEMBL6030.
GuidetoPHARMACOLOGY2017.

PTM databases

PhosphoSiteQ9NZJ5.

Polymorphism databases

DMDM296439367.

Proteomic databases

PaxDbQ9NZJ5.
PRIDEQ9NZJ5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000303236; ENSP00000307235; ENSG00000172071.
GeneID9451.
KEGGhsa:9451.
UCSCuc002stc.4. human.

Organism-specific databases

CTD9451.
GeneCardsGC02M088857.
H-InvDBHIX0023925.
HIX0030379.
HGNCHGNC:3255. EIF2AK3.
HPACAB009204.
HPA015737.
MIM226980. phenotype.
604032. gene.
neXtProtNX_Q9NZJ5.
Orphanet1667. Wolcott-Rallison syndrome.
PharmGKBPA27687.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOVERGENHBG051431.
InParanoidQ9NZJ5.
KOK08860.
OMAKGLMHRD.
PhylomeDBQ9NZJ5.
TreeFamTF101511.

Enzyme and pathway databases

ReactomeREACT_17015. Metabolism of proteins.
SignaLinkQ9NZJ5.

Gene expression databases

ArrayExpressQ9NZJ5.
BgeeQ9NZJ5.
CleanExHS_EIF2AK3.
GenevestigatorQ9NZJ5.

Family and domain databases

Gene3D2.140.10.10. 1 hit.
InterProIPR011009. 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]
PfamPF00069. Pkinase. 2 hits.
[Graphical view]
SUPFAMSSF50998. SSF50998. 2 hits.
SSF56112. SSF56112. 2 hits.
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSEIF2AK3. human.
GeneWikiEIF2AK3.
GenomeRNAi9451.
NextBio35404.
PROQ9NZJ5.
SOURCESearch...

Entry information

Entry nameE2AK3_HUMAN
AccessionPrimary (citable) accession number: Q9NZJ5
Secondary accession number(s): A0AVH1 expand/collapse secondary AC list , A0AVH2, B2RCU9, O95846, Q53QY0, Q53SB1
Entry history
Integrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: May 18, 2010
Last modified: April 16, 2014
This is version 139 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM