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Q9NZJ5

- E2AK3_HUMAN

UniProt

Q9NZJ5 - E2AK3_HUMAN

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Protein

Eukaryotic translation initiation factor 2-alpha kinase 3

Gene

EIF2AK3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Phosphorylates the alpha subunit of eukaryotic translation-initiation factor 2 (EIF2), leading to its inactivation and thus to a rapid reduction of translational initiation and repression of global protein synthesis. Serves as a critical effector of unfolded protein response (UPR)-induced G1 growth arrest due to the loss of cyclin-D1 (CCND1). Involved in control of mitochondrial morphology and function (By similarity).By similarity

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulationi

Perturbation in protein folding in the endoplasmic reticulum (ER) promotes reversible dissociation from HSPA5/BIP and oligomerization, resulting in transautophosphorylation and kinase activity induction.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei622 – 6221ATPPROSITE-ProRule annotation
Active sitei937 – 9371Proton acceptorPROSITE-ProRule annotation

Regions

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

GO - Molecular functioni

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

GO - Biological processi

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

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Stress response, Translation regulation, Unfolded protein response

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_18277. PERK regulates gene expression.
SignaLinkiQ9NZJ5.

Names & Taxonomyi

Protein namesi
Recommended name:
Eukaryotic translation initiation factor 2-alpha kinase 3 (EC:2.7.11.1)
Alternative name(s):
PRKR-like endoplasmic reticulum kinase
Pancreatic eIF2-alpha kinase
Short name:
HsPEK
Gene namesi
Name:EIF2AK3
Synonyms:PEK, PERK
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:3255. EIF2AK3.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Involvement in diseasei

Wolcott-Rallison syndrome (WRS) [MIM:226980]: A rare autosomal recessive disorder, characterized by permanent neonatal or early infancy insulin-dependent diabetes and, at a later age, epiphyseal dysplasia, osteoporosis, growth retardation and other multisystem manifestations, such as hepatic and renal dysfunctions, mental retardation and cardiovascular abnormalities.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti588 – 5881R → Q in WRS; in a Pakistani family; probable complete loss of activity. 1 Publication
VAR_011408

Keywords - Diseasei

Diabetes mellitus, Disease mutation

Organism-specific databases

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

PTM / Processingi

Molecule processing

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

Amino acid modifications

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

Post-translational modificationi

Oligomerization of the N-terminal ER luminal domain by ER stress promotes PERK trans-autophosphorylation of the C-terminal cytoplasmic kinase domain at multiple residues including Thr-982 on the kinase activation loop (By similarity). Autophosphorylated. Phosphorylated at Tyr-619 following endoplasmic reticulum stress, leading to activate its tyrosine-protein kinase activity. Dephosphorylated by PTPN1/TP1B, leading to inactivate its enzyme activity.By similarity3 Publications
N-glycosylated.By similarity
ADP-ribosylated by PARP16 upon ER stress, which increases kinase activity.

Keywords - PTMi

ADP-ribosylation, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiQ9NZJ5.
PaxDbiQ9NZJ5.
PRIDEiQ9NZJ5.

PTM databases

PhosphoSiteiQ9NZJ5.

Expressioni

Tissue specificityi

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

Inductioni

By endoplasmic reticulum stress.

Gene expression databases

BgeeiQ9NZJ5.
CleanExiHS_EIF2AK3.
ExpressionAtlasiQ9NZJ5. baseline and differential.
GenevestigatoriQ9NZJ5.

Organism-specific databases

HPAiCAB009204.
HPA015737.

Interactioni

Subunit structurei

Forms dimers with HSPA5/BIP in resting cells. Oligomerizes in ER-stressed cells. Interacts with DNAJC3 and MFN2 (By similarity).By similarity

Binary interactionsi

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

Protein-protein interaction databases

BioGridi114840. 16 interactions.
IntActiQ9NZJ5. 4 interactions.
STRINGi9606.ENSP00000307235.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4G31X-ray2.28A588-1093[»]
4G34X-ray2.70A588-1093[»]
4M7IX-ray2.34A588-1093[»]
ProteinModelPortaliQ9NZJ5.
SMRiQ9NZJ5. Positions 588-660, 834-1116.
ModBaseiSearch...
MobiDBiSearch...

Topological domain

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

Transmembrane

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

Family & Domainsi

Domains and Repeats

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

Compositional bias

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

Domaini

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

Sequence similaritiesi

Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. GCN2 subfamily.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00530000062984.
HOVERGENiHBG051431.
InParanoidiQ9NZJ5.
KOiK08860.
OMAiKGLMHRD.
PhylomeDBiQ9NZJ5.
TreeFamiTF101511.

Family and domain databases

Gene3Di2.140.10.10. 1 hit.
InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR027295. Quinonprotein_ADH-like_fam.
IPR011047. Quinonprotein_ADH-like_supfam.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 2 hits.
[Graphical view]
SUPFAMiSSF50998. SSF50998. 2 hits.
SSF56112. SSF56112. 2 hits.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9NZJ5-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MERAISPGLL VRALLLLLLL LGLAARTVAA GRARGLPAPT AEAAFGLGAA
60 70 80 90 100
AAPTSATRVP AAGAVAAAEV TVEDAEALPA AAGEQEPRGP EPDDETELRP
110 120 130 140 150
RGRSLVIIST LDGRIAALDP ENHGKKQWDL DVGSGSLVSS SLSKPEVFGN
160 170 180 190 200
KMIIPSLDGA LFQWDQDRES METVPFTVES LLESSYKFGD DVVLVGGKSL
210 220 230 240 250
TTYGLSAYSG KVRYICSALG CRQWDSDEME QEEDILLLQR TQKTVRAVGP
260 270 280 290 300
RSGNEKWNFS VGHFELRYIP DMETRAGFIE STFKPNENTE ESKIISDVEE
310 320 330 340 350
QEAAIMDIVI KVSVADWKVM AFSKKGGHLE WEYQFCTPIA SAWLLKDGKV
360 370 380 390 400
IPISLFDDTS YTSNDDVLED EEDIVEAARG ATENSVYLGM YRGQLYLQSS
410 420 430 440 450
VRISEKFPSS PKALESVTNE NAIIPLPTIK WKPLIHSPSR TPVLVGSDEF
460 470 480 490 500
DKCLSNDKFS HEEYSNGALS ILQYPYDNGY YLPYYKRERN KRSTQITVRF
510 520 530 540 550
LDNPHYNKNI RKKDPVLLLH WWKEIVATIL FCIIATTFIV RRLFHPHPHR
560 570 580 590 600
QRKESETQCQ TENKYDSVSG EANDSSWNDI KNSGYISRYL TDFEPIQCLG
610 620 630 640 650
RGGFGVVFEA KNKVDDCNYA IKRIRLPNRE LAREKVMREV KALAKLEHPG
660 670 680 690 700
IVRYFNAWLE APPEKWQEKM DEIWLKDEST DWPLSSPSPM DAPSVKIRRM
710 720 730 740 750
DPFATKEHIE IIAPSPQRSR SFSVGISCDQ TSSSESQFSP LEFSGMDHED
760 770 780 790 800
ISESVDAAYN LQDSCLTDCD VEDGTMDGND EGHSFELCPS EASPYVRSRE
810 820 830 840 850
RTSSSIVFED SGCDNASSKE EPKTNRLHIG NHCANKLTAF KPTSSKSSSE
860 870 880 890 900
ATLSISPPRP TTLSLDLTKN TTEKLQPSSP KVYLYIQMQL CRKENLKDWM
910 920 930 940 950
NGRCTIEERE RSVCLHIFLQ IAEAVEFLHS KGLMHRDLKP SNIFFTMDDV
960 970 980 990 1000
VKVGDFGLVT AMDQDEEEQT VLTPMPAYAR HTGQVGTKLY MSPEQIHGNS
1010 1020 1030 1040 1050
YSHKVDIFSL GLILFELLYP FSTQMERVRT LTDVRNLKFP PLFTQKYPCE
1060 1070 1080 1090 1100
YVMVQDMLSP SPMERPEAIN IIENAVFEDL DFPGKTVLRQ RSRSLSSSGT
1110
KHSRQSNNSH SPLPSN
Length:1,116
Mass (Da):125,216
Last modified:May 18, 2010 - v3
Checksum:i95FEB5DAE8D3D452
GO

Experimental Info

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

Natural variant

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

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF110146 mRNA. Translation: AAD19961.1.
AF193339 mRNA. Translation: AAF61199.1.
AF284615
, AF284604, AF284605, AF284606, AF284607, AF284608, AF284609, AF284610, AF284611, AF284612, AF284613, AF284614 Genomic DNA. Translation: AAF91480.1.
AK315287 mRNA. Translation: BAG37696.1.
AC062029 Genomic DNA. Translation: AAY14777.1.
AC104134 Genomic DNA. Translation: AAY24331.1.
BC126354 mRNA. Translation: AAI26355.1.
BC126356 mRNA. Translation: AAI26357.1.
CCDSiCCDS33241.1.
RefSeqiNP_004827.4. NM_004836.5.
UniGeneiHs.591589.

Genome annotation databases

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

Polymorphism databases

DMDMi296439367.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF110146 mRNA. Translation: AAD19961.1 .
AF193339 mRNA. Translation: AAF61199.1 .
AF284615
, AF284604 , AF284605 , AF284606 , AF284607 , AF284608 , AF284609 , AF284610 , AF284611 , AF284612 , AF284613 , AF284614 Genomic DNA. Translation: AAF91480.1 .
AK315287 mRNA. Translation: BAG37696.1 .
AC062029 Genomic DNA. Translation: AAY14777.1 .
AC104134 Genomic DNA. Translation: AAY24331.1 .
BC126354 mRNA. Translation: AAI26355.1 .
BC126356 mRNA. Translation: AAI26357.1 .
CCDSi CCDS33241.1.
RefSeqi NP_004827.4. NM_004836.5.
UniGenei Hs.591589.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4G31 X-ray 2.28 A 588-1093 [» ]
4G34 X-ray 2.70 A 588-1093 [» ]
4M7I X-ray 2.34 A 588-1093 [» ]
ProteinModelPortali Q9NZJ5.
SMRi Q9NZJ5. Positions 588-660, 834-1116.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 114840. 16 interactions.
IntActi Q9NZJ5. 4 interactions.
STRINGi 9606.ENSP00000307235.

Chemistry

BindingDBi Q9NZJ5.
ChEMBLi CHEMBL6030.
GuidetoPHARMACOLOGYi 2017.

PTM databases

PhosphoSitei Q9NZJ5.

Polymorphism databases

DMDMi 296439367.

Proteomic databases

MaxQBi Q9NZJ5.
PaxDbi Q9NZJ5.
PRIDEi Q9NZJ5.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

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

Organism-specific databases

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

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00530000062984.
HOVERGENi HBG051431.
InParanoidi Q9NZJ5.
KOi K08860.
OMAi KGLMHRD.
PhylomeDBi Q9NZJ5.
TreeFami TF101511.

Enzyme and pathway databases

Reactomei REACT_18277. PERK regulates gene expression.
SignaLinki Q9NZJ5.

Miscellaneous databases

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

Gene expression databases

Bgeei Q9NZJ5.
CleanExi HS_EIF2AK3.
ExpressionAtlasi Q9NZJ5. baseline and differential.
Genevestigatori Q9NZJ5.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  1. "Characterization of a mutant pancreatic eIF-2alpha kinase, PEK, and co-localization with somatostatin in islet delta cells."
    Shi Y., An J., Liang J., Hayes S.E., Sandusky G.E., Stramm L.E., Yang N.N.
    J. Biol. Chem. 274:5723-5730(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, VARIANTS ARG-166 AND SER-704.
    Tissue: Liver, Pancreas and Testis.
  2. "Pancreatic eukaryotic initiation factor-2alpha kinase (PEK) homologues in humans, Drosophila melanogaster and Caenorhabditis elegans that mediate translational control in response to endoplasmic reticulum stress."
    Sood R., Porter A.C., Ma K., Quilliam L.A., Wek R.C.
    Biochem. J. 346:281-293(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, VARIANTS ARG-166 AND SER-704.
    Tissue: Brain and Pancreas.
  3. "EIF2AK3, encoding translation initiation factor 2-alpha kinase 3, is mutated in patients with Wolcott-Rallison syndrome."
    Delepine M., Nicolino M., Barrett T., Golamaully M., Lathrop G.M., Julier C.
    Nat. Genet. 25:406-409(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT WRS GLN-588, VARIANT CYS-136.
  4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  5. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANTS ARG-166 AND SER-704.
  7. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-715, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "H2s-induced sulfhydration of the phosphatase PTP1B and its role in the endoplasmic reticulum stress response."
    Krishnan N., Fu C., Pappin D.J., Tonks N.K.
    Sci. Signal. 4:RA86-RA86(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT TYR-619, DEPHOSPHORYLATION AT TYR-619.
  9. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1094, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "PARP16 is a tail-anchored endoplasmic reticulum protein required for the PERK-and IRE1alpha-mediated unfolded protein response."
    Jwa M., Chang P.
    Nat. Cell Biol. 14:1223-1230(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ADP-RIBOSYLATION BY PARP16.
  11. "Patterns of somatic mutation in human cancer genomes."
    Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.
    , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
    Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS [LARGE SCALE ANALYSIS] CYS-136; VAL-566 AND LEU-716.

Entry informationi

Entry nameiE2AK3_HUMAN
AccessioniPrimary (citable) accession number: Q9NZJ5
Secondary accession number(s): A0AVH1
, A0AVH2, B2RCU9, O95846, Q53QY0, Q53SB1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: May 18, 2010
Last modified: October 29, 2014
This is version 145 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3