Q9NZJ5 (E2AK3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	EIF2AK3
Synonyms:	PEK, PERK

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1116 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 process	Stress response Translation regulation Unfolded protein response
Cellular component	Endoplasmic reticulum Membrane
Coding sequence diversity	Polymorphism
Disease	Diabetes mellitus Disease mutation
Domain	Signal Transmembrane Transmembrane helix
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	ADP-ribosylation Glycoprotein Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	ER overload response Inferred from direct assay Ref.2PubMed 11907036. Source: UniProtKB SREBP signaling pathway Inferred from electronic annotation. Source: Compara 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 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 fat cell differentiation Inferred from electronic annotation. Source: Compara 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 lactation Inferred from electronic annotation. Source: Compara negative regulation of myelination Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of translational initiation in response to stress Traceable author statement Ref.2PubMed 12086964. Source: UniProtKB positive regulation of protein binding Inferred from electronic annotation. Source: Compara positive regulation of signal transduction Inferred from electronic annotation. Source: Compara protein autophosphorylation Inferred from direct assay Ref.1PubMed 11907036. Source: UniProtKB protein homooligomerization Inferred from mutant phenotype PubMed 11907036. Source: UniProtKB regulation of fatty acid metabolic process Inferred from electronic annotation. Source: Compara translation Inferred from electronic annotation. Source: Compara virus-infected cell apoptotic process Inferred from electronic annotation. Source: Compara
Cellular_component	endoplasmic reticulum membrane Inferred from sequence or structural similarity. Source: UniProtKB integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW eukaryotic translation initiation factor 2alpha kinase activity Inferred from direct assay Ref.1Ref.2PubMed 11907036. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		2	EBI-766076,EBI-766076

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 29

29

Potential

Chain

30 – 1116

1087

Eukaryotic translation initiation factor 2-alpha kinase 3

PRO_0000024322

Regions

Topological domain

30 – 514

485

Lumenal Potential

Transmembrane

515 – 535

21

Helical; Potential

Topological domain

536 – 1116

581

Cytoplasmic Potential

Domain

593 – 1077

485

Protein kinase

Nucleotide binding

599 – 607

9

ATP By similarity

Compositional bias

49 – 52

4

Poly-Ala

Sites

Active site

937

1

Proton acceptor By similarity

Binding site

622

1

ATP By similarity

Amino acid modifications

Modified residue

619

1

Phosphotyrosine Ref.8

Modified residue

715

1

Phosphoserine Ref.7

Modified residue

982

1

Phosphothreonine By similarity

Modified residue

1094

1

Phosphoserine Ref.9

Glycosylation

258

1

N-linked (GlcNAc...) Potential

Natural variations

Natural variant

136

1

S → C. Ref.3 Ref.11
Corresponds to variant rs867529 [ dbSNP | Ensembl ].

VAR_011409

Natural variant

166

1

Q → R. Ref.1 Ref.2 Ref.6
Corresponds to variant rs13045 [ dbSNP | Ensembl ].

VAR_011410

Natural variant

566

1

D → V. Ref.11

VAR_040477

Natural variant

588

1

R → Q in WRS; in a Pakistani family; probable complete loss of activity. Ref.3

VAR_011408

Natural variant

704

1

A → S. Ref.1 Ref.2 Ref.6
Corresponds to variant rs1805165 [ dbSNP | Ensembl ].

VAR_011411

Natural variant

716

1

P → L. Ref.11

VAR_040478

Experimental info

Sequence conflict

14

1

Missing in AAD19961. Ref.1

Sequence conflict

14

1

Missing in AAF61199. Ref.2

Sequence conflict

14

1

Missing in AAF91480. Ref.3

Sequence conflict

14

1

Missing in BAG37696. Ref.4

Sequence conflict

14

1

Missing in AAI26357. Ref.6

Sequence conflict

490

1

N → H in AAF61199. Ref.2

Secondary structure

1

.

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1116

Helix Strand Turn

Details...

Helix

588 – 592

5

Beta strand

593 – 601

9

Beta strand

606 – 612

7

Turn

613 – 615

3

Beta strand

618 – 626

9

Helix

630 – 643

14

Beta strand

654 – 660

7

Beta strand

882 – 889

8

Helix

896 – 901

6

Helix

906 – 908

3

Helix

911 – 930

20

Helix

940 – 942

3

Beta strand

943 – 945

3

Beta strand

951 – 953

3

Helix

993 – 996

4

Helix

1004 – 1018

15

Helix

1024 – 1035

12

Helix

1041 – 1046

6

Helix

1048 – 1057

10

Helix

1062 – 1064

3

Helix

1068 – 1072

5

Helix

1075 – 1077

3

Sequences

	Sequence		Length	Mass (Da)
	Q9NZJ5 [UniParc]. Last modified May 18, 2010. Version 3. Checksum: 95FEB5DAE8D3D452	FASTA	1,116	125,216
	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

References

	« Hide 'large scale' referencesShow '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. , 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY.
[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.
+	Additional computationally mapped references.

Web resources

GeneReviews

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00303053.

RefSeq

NP_004827.4. NM_004836.5.

UniGene

Hs.591589.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
4G31	X-ray	2.28	A	588-1093	[»]
4G34	X-ray	2.70	A	588-1093	[»]

ProteinModelPortal

Q9NZJ5.

SMR

Q9NZJ5. Positions 588-660, 830-1112.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9NZJ5. 4 interactions.

STRING

9606.ENSP00000307235.

PTM databases

PhosphoSite

Q9NZJ5.

Polymorphism databases

DMDM

296439367.

Proteomic databases

PaxDb

Q9NZJ5.

PRIDE

Q9NZJ5.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000303236; ENSP00000307235; ENSG00000172071.

GeneID

9451.

KEGG

hsa:9451.

UCSC

uc002stc.4. human.

Organism-specific databases

CTD

9451.

GeneCards

GC02M088758.

H-InvDB

HIX0023925.
HIX0030379.

HGNC

HGNC:3255. EIF2AK3.

HPA

CAB009204.
HPA015737.

MIM

226980. phenotype.
604032. gene.

neXtProt

NX_Q9NZJ5.

Orphanet

1667. Wolcott-Rallison syndrome.

PharmGKB

PA27687.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0515.

HOVERGEN

HBG051431.

InParanoid

Q9NZJ5.

KO

K08860.

OMA

SPMDAPS.

Enzyme and pathway databases

Reactome

REACT_116125. Disease.

Gene expression databases

ArrayExpress

Q9NZJ5.

Bgee

Q9NZJ5.

CleanEx

HS_EIF2AK3.

Genevestigator

Q9NZJ5.

GermOnline

ENSG00000172071. Homo sapiens.

Family and domain databases

InterPro

IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_cat_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR011047. Quinonprotein_ADH-like_supfam.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]

Pfam

PF00069. Pkinase. 2 hits.
[Graphical view]

SUPFAM

SSF56112. Kinase_like. 1 hit.
SSF50998. Quin_alc_DH_like. 1 hit.

PROSITE

PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

Q9NZJ5.

ChEMBL

CHEMBL6030.

ChiTaRS

EIF2AK3. human.

GenomeRNAi

9451.

NextBio

35404.

SOURCE

Search...

Entry information

Entry name

E2AK3_HUMAN

Accession

Primary (citable) accession number: Q9NZJ5
Secondary accession number(s): A0AVH1 , A0AVH2, B2RCU9, O95846, Q53QY0, Q53SB1

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 26, 2001
Last sequence update:	May 18, 2010
Last modified:	May 1, 2013
This is version 128 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.