Reviewed, UniProtKB/Swiss-Prot Q9P2K8 (E2AK4_HUMAN)

Names and origin

Protein names

Recommended name:
    Eukaryotic translation initiation factor 2-alpha kinase 4
    EC=2.7.11.1
Alternative name(s):
    GCN2-like protein

Gene names

Name:	EIF2AK4
Synonyms:	GCN2, KIAA1338

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	1649 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Can phosphorylate the alpha subunit of EIF2 and may mediate translational control By similarity.
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Tissue specificity	Widely expressed. Ref.5
Domain	Kinase domain 1 is a degenerate kinase domain. RWD domain is reported to interact with GCN1L1.
Post-translational modification	Autophosphorylated on threonine residues By similarity.
Sequence similarities	Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. GCN2 subfamily. Contains 2 protein kinase domains. Contains 1 RWD domain.

Ontologies

Keywords
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Gene Ontology (GO)
Biological process	protein amino acid phosphorylation Inferred from sequence or structural similarity. Source: UniProtKB regulation of translational initiation Inferred from sequence or structural similarity. Source: UniProtKB tRNA aminoacylation for protein translation Inferred from electronic annotation. Source: InterPro
Cellular component	cytosolic ribosome Inferred from sequence or structural similarity. Source: UniProtKB
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW aminoacyl-tRNA ligase activity Inferred from electronic annotation. Source: InterPro eukaryotic translation initiation factor 2alpha kinase activity Ref.5 Inferred from sequence or structural similarity. Source: UniProtKB protein binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9P2K8-1)

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.

Isoform 2 (identifier: Q9P2K8-2)

The sequence of this isoform differs from the canonical sequence as follows:
     774-801: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1649	1649	Eukaryotic translation initiation factor 2-alpha kinase 4		PRO_0000085947
Regions
	Domain	25 – 137	113	RWD
	Domain	296 – 539	244	Protein kinase 1
	Domain	590 – 1001	412	Protein kinase 2
	Nucleotide binding	596 – 604	9	ATP By similarity
	Region	1022 – 1493	472	Histidyl-tRNA synthetase-like
	Compositional bias	484 – 491	8	Poly-Leu
Sites
	Active site	848	1	Proton acceptor By similarity
	Binding site	619	1	ATP By similarity
Amino acid modifications
	Modified residue	230	1	Phosphoserine Ref.8 Ref.9
	Modified residue	551	1	Phosphoserine Ref.8
	Modified residue	555	1	Phosphoserine Ref.8
	Modified residue	667	1	Phosphothreonine Ref.8 Ref.6 Ref.7
	Modified residue	899	1	Phosphothreonine; by autocatalysis By similarity
	Modified residue	904	1	Phosphothreonine; by autocatalysis By similarity
Natural variations
	Alternative sequence	774 – 801	28	Missing in isoform 2.		VSP_013038
	Natural variant	137	1	H → R Ref.11		VAR_040479
	Natural variant	166	1	R → W Ref.11		VAR_040480
	Natural variant	441	1	I → L Ref.11 Ref.3		VAR_040481
	Natural variant	872	1	D → V Ref.11		VAR_040482
	Natural variant	939	1	H → Y in a lung neuroendocrine carcinoma sample; somatic mutation. Ref.11		VAR_040483
	Natural variant	1060	1	T → R Ref.11		VAR_040484
	Natural variant	1306	1	G → C Ref.11 Ref.1		VAR_040485
	Natural variant	1336	1	K → R Ref.11		VAR_040486
	Natural variant	1406	1	Q → H Ref.11		VAR_040487
Experimental info
	Sequence conflict	155 – 176	22	QEEQQ…QREIL → LLLFFPLGLQQPLLLLLSPP FQ Ref.2
	Sequence conflict	556	1	G → E in AAH78179. Ref.1
	Sequence conflict	608 – 616	9	QNKLDGCCY → WYRVIPSPL in AAH78179. Ref.1
	Sequence conflict	629	1	Q → K in CAH10626. Ref.3
	Sequence conflict	858	1	S → F Ref.4
	Sequence conflict	1133	1	N → I Ref.5

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified March 15, 2005. Version 2. Checksum: 645947D8DBAE5472	FASTA	1,649	186,838
	10 20 30 40 50 60 MAGGRGAPGR GRDEPPESYP QRQDHELQAL EAIYGADFQD LRPDACGPVK EPPEINLVLY 70 80 90 100 110 120 PQGLTGEEVY VKVDLRVKCP PTYPDVVPEI ELKNAKGLSN ESVNLLKSRL EELAKKHCGE 130 140 150 160 170 180 VMIFELAYHV QSFLSEHNKP PPKSFHEEML ERRAQEEQQR LLEAKRKEEQ EQREILHEIQ 190 200 210 220 230 240 RRKEEIKEEK KRKEMAKQER LEIASLSNQD HTSKKDPGGH RTAAILHGGS PDFVGNGKHR 250 260 270 280 290 300 ANSSGRSRRE RQYSVCNSED SPGSCEILYF NMGSPDQLMV HKGKCIGSDE QLGKLVYNAL 310 320 330 340 350 360 ETATGGFVLL YEWVLQWQKK MGPFLTSQEK EKIDKCKKQI QGTETEFNSL VKLSHPNVVR 370 380 390 400 410 420 YLAMNLKEQD DSIVVDILVE HISGVSLAAH LSHSGPIPVH QLRRYTAQLL SGLDYLHSNS 430 440 450 460 470 480 VVHKVLSASN VLVDAEGTVK ITDYSISKRL ADICKEDVFE QTRVRFSDNA LPYKTGKKGD 490 500 510 520 530 540 VWRLGLLLLS LSQGQECGEY PVTIPSDLPA DFQDFLKKCV CLDDKERWSP QQLLKHSFIN 550 560 570 580 590 600 PQPKMPLVEQ SPEDSGGQDY VETVIPSNRL PSAAFFSETQ RQFSRYFIEF EELQLLGKGA 610 620 630 640 650 660 FGAVIKVQNK LDGCCYAVKR IPINPASRQF RRIKGEVTLL SRLHHENIVR YYNAWIERHE 670 680 690 700 710 720 RPAGPGTPPP DSGPLAKDDR AARGQPASDT DGLDSVEAAA PPPILSSSVE WSTSGERSAS 730 740 750 760 770 780 ARFPATGPGS SDDEDDDEDE HGGVFSQSFL PASDSESDII FDNEDENSKS QNQDEDCNEK 790 800 810 820 830 840 NGCHESEPSV TTEAVHYLYI QMEYCEKSTL RDTIDQGLYR DTVRLWRLFR EILDGLAYIH 850 860 870 880 890 900 EKGMIHRDLK PVNIFLDSDD HVKIGDFGLA TDHLAFSADS KQDDQTGDLI KSDPSGHLTG 910 920 930 940 950 960 MVGTALYVSP EVQGSTKSAY NQKVDLFSLG IIFFEMSYHP MVTASERIFV LNQLRDPTSP 970 980 990 1000 1010 1020 KFPEDFDDGE HAKQKSVISW LLNHDPAKRP TATELLKSEL LPPPQMEESE LHEVLHHTLT 1030 1040 1050 1060 1070 1080 NVDGKAYRTM MAQIFSQRIS PAIDYTYDSD ILKGNFSIRT AKMQQHVCET IIRIFKRHGA 1090 1100 1110 1120 1130 1140 VQLCTPLLLP RNRQIYEHNE AALFMDHSGM LVMLPFDLRI PFARYVARNN ILNLKRYCIE 1150 1160 1170 1180 1190 1200 RVFRPRKLDR FHPKELLECA FDIVTSTTNS FLPTAEIIYT IYEIIQEFPA LQERNYSIYL 1210 1220 1230 1240 1250 1260 NHTMLLKAIL LHCGIPEDKL SQVYIILYDA VTEKLTRREV EAKFCNLSLS SNSLCRLYKF 1270 1280 1290 1300 1310 1320 IEQKGDLQDL MPTINSLIKQ KTGIAQLVKY GLKDLEEVVG LLKKLGIKLQ VLINLGLVYK 1330 1340 1350 1360 1370 1380 VQQHNGIIFQ FVAFIKRRQR AVPEILAAGG RYDLLIPQFR GPQALGPVPT AIGVSIAIDK 1390 1400 1410 1420 1430 1440 ISAAVLNMEE SVTISSCDLL VVSVGQMSMS RAINLTQKLW TAGITAEIMY DWSQSQEELQ 1450 1460 1470 1480 1490 1500 EYCRHHEITY VALVSDKEGS HVKVKSFEKE RQTEKRVLET ELVDHVLQKL RTKVTDERNG 1510 1520 1530 1540 1550 1560 REASDNLAVQ NLKGSFSNAS GLFEIHGATV VPIVSVLAPE KLSASTRRRY ETQVQTRLQT 1570 1580 1590 1600 1610 1620 SLANLHQKSS EIEILAVDLP KETILQFLSL EWDADEQAFN TTVKQLLSRL PKQRYLKLVC 1630 1640 DEIYNIKVEK KVSVLFLYSY RDDYYRILF
	Isoform 2. Checksum: 78523D047D8BEDDA	FASTA	1,621	183,645
	10 20 30 40 50 60 MAGGRGAPGR GRDEPPESYP QRQDHELQAL EAIYGADFQD LRPDACGPVK EPPEINLVLY 70 80 90 100 110 120 PQGLTGEEVY VKVDLRVKCP PTYPDVVPEI ELKNAKGLSN ESVNLLKSRL EELAKKHCGE 130 140 150 160 170 180 VMIFELAYHV QSFLSEHNKP PPKSFHEEML ERRAQEEQQR LLEAKRKEEQ EQREILHEIQ 190 200 210 220 230 240 RRKEEIKEEK KRKEMAKQER LEIASLSNQD HTSKKDPGGH RTAAILHGGS PDFVGNGKHR 250 260 270 280 290 300 ANSSGRSRRE RQYSVCNSED SPGSCEILYF NMGSPDQLMV HKGKCIGSDE QLGKLVYNAL 310 320 330 340 350 360 ETATGGFVLL YEWVLQWQKK MGPFLTSQEK EKIDKCKKQI QGTETEFNSL VKLSHPNVVR 370 380 390 400 410 420 YLAMNLKEQD DSIVVDILVE HISGVSLAAH LSHSGPIPVH QLRRYTAQLL SGLDYLHSNS 430 440 450 460 470 480 VVHKVLSASN VLVDAEGTVK ITDYSISKRL ADICKEDVFE QTRVRFSDNA LPYKTGKKGD 490 500 510 520 530 540 VWRLGLLLLS LSQGQECGEY PVTIPSDLPA DFQDFLKKCV CLDDKERWSP QQLLKHSFIN 550 560 570 580 590 600 PQPKMPLVEQ SPEDSGGQDY VETVIPSNRL PSAAFFSETQ RQFSRYFIEF EELQLLGKGA 610 620 630 640 650 660 FGAVIKVQNK LDGCCYAVKR IPINPASRQF RRIKGEVTLL SRLHHENIVR YYNAWIERHE 670 680 690 700 710 720 RPAGPGTPPP DSGPLAKDDR AARGQPASDT DGLDSVEAAA PPPILSSSVE WSTSGERSAS 730 740 750 760 770 780 ARFPATGPGS SDDEDDDEDE HGGVFSQSFL PASDSESDII FDNEDENSKS QNQMEYCEKS 790 800 810 820 830 840 TLRDTIDQGL YRDTVRLWRL FREILDGLAY IHEKGMIHRD LKPVNIFLDS DDHVKIGDFG 850 860 870 880 890 900 LATDHLAFSA DSKQDDQTGD LIKSDPSGHL TGMVGTALYV SPEVQGSTKS AYNQKVDLFS 910 920 930 940 950 960 LGIIFFEMSY HPMVTASERI FVLNQLRDPT SPKFPEDFDD GEHAKQKSVI SWLLNHDPAK 970 980 990 1000 1010 1020 RPTATELLKS ELLPPPQMEE SELHEVLHHT LTNVDGKAYR TMMAQIFSQR ISPAIDYTYD 1030 1040 1050 1060 1070 1080 SDILKGNFSI RTAKMQQHVC ETIIRIFKRH GAVQLCTPLL LPRNRQIYEH NEAALFMDHS 1090 1100 1110 1120 1130 1140 GMLVMLPFDL RIPFARYVAR NNILNLKRYC IERVFRPRKL DRFHPKELLE CAFDIVTSTT 1150 1160 1170 1180 1190 1200 NSFLPTAEII YTIYEIIQEF PALQERNYSI YLNHTMLLKA ILLHCGIPED KLSQVYIILY 1210 1220 1230 1240 1250 1260 DAVTEKLTRR EVEAKFCNLS LSSNSLCRLY KFIEQKGDLQ DLMPTINSLI KQKTGIAQLV 1270 1280 1290 1300 1310 1320 KYGLKDLEEV VGLLKKLGIK LQVLINLGLV YKVQQHNGII FQFVAFIKRR QRAVPEILAA 1330 1340 1350 1360 1370 1380 GGRYDLLIPQ FRGPQALGPV PTAIGVSIAI DKISAAVLNM EESVTISSCD LLVVSVGQMS 1390 1400 1410 1420 1430 1440 MSRAINLTQK LWTAGITAEI MYDWSQSQEE LQEYCRHHEI TYVALVSDKE GSHVKVKSFE 1450 1460 1470 1480 1490 1500 KERQTEKRVL ETELVDHVLQ KLRTKVTDER NGREASDNLA VQNLKGSFSN ASGLFEIHGA 1510 1520 1530 1540 1550 1560 TVVPIVSVLA PEKLSASTRR RYETQVQTRL QTSLANLHQK SSEIEILAVD LPKETILQFL 1570 1580 1590 1600 1610 1620 SLEWDADEQA FNTTVKQLLS RLPKQRYLKL VCDEIYNIKV EKKVSVLFLY SYRDDYYRIL F

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT CYS-1306. Tissue: Muscle and Uterus.
[2]	"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: 10718198] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 155-1649. Tissue: Brain.
[3]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Blocker H., Heubner D., Hoerlein A., Michel G., Wedler H., Kohrer K., Ottenwalder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed: 17974005] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 196-1649, VARIANT LEU-441. Tissue: Melanoma and Testis.
[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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 831-1649.
[5]	"Characterization of a mammalian homolog of the GCN2 eukaryotic initiation factor 2alpha kinase." Berlanga J.J., Santoyo J., de Haro C. Eur. J. Biochem. 265:754-762(1999) [PubMed: 10504407] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1102-1649, TISSUE SPECIFICITY.
[6]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-667, MASS SPECTROMETRY. Tissue: Epithelium.
[7]	"Proteomics analysis of protein kinases by target class-selective prefractionation and tandem mass spectrometry." Wissing J., Jaensch L., Nimtz M., Dieterich G., Hornberger R., Keri G., Wehland J., Daub H. Mol. Cell. Proteomics 6:537-547(2007) [PubMed: 17192257] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-667, MASS SPECTROMETRY.
[8]	"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: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-230; SER-551; SER-555 AND THR-667, MASS SPECTROMETRY.
[9]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-230, MASS SPECTROMETRY.
[10]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[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: 17344846] [Abstract] Cited for: VARIANTS [LARGE SCALE ANALYSIS] ARG-137; TRP-166; LEU-441; VAL-872; TYR-939; ARG-1060; CYS-1306; ARG-1336 AND HIS-1406.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	BC009350 mRNA. Translation: AAH09350.2. BC078179 mRNA. Translation: AAH78179.1. AB037759 mRNA. Translation: BAA92576.1. AL137627 mRNA. Translation: CAB70849.1. AL157497 mRNA. Translation: CAB75678.1. AL832907 mRNA. Translation: CAH10626.1. AK027011 mRNA. Translation: BAB15625.1. Different initiation. AJ243428 mRNA. Translation: CAB58360.1.
IPI	IPI00163851. IPI00456685.
PIR	T46924.
RefSeq	NP_001013725.2.
UniGene	Hs.656673
3D structure databases
SMR	Q9P2K8. Positions 21-144.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9P2K8. 5 interactions.
PTM databases
PhosphoSite	Q9P2K8.
Proteomic databases
PRIDE	Q9P2K8.
Genome annotation databases
Ensembl	ENSG00000128829. Homo sapiens. [Contig view]
GeneID	440275.
KEGG	hsa:440275.
Organism-specific databases
GeneCards	GC15P038014.
H-InvDB	HIX0012119.
HGNC	HGNC:19687. EIF2AK4.
MIM	609280. gene.
PharmGKB	PA134947616.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
HOVERGEN	Q9P2K8.
Enzyme and pathway databases
BRENDA	2.7.11.1. 247.
Gene expression databases
Bgee	Q9P2K8.
CleanEx	HS_EIF2AK4.
GermOnline	ENSG00000128829. Homo sapiens.
Family and domain databases
InterPro	IPR002314. aa-tRNA-synt_IIb_cons-reg. IPR015515. GCN2. IPR000719. Prot_kinase_core. IPR017441. Protein_kinase_ATP_BS. IPR006575. RWD. IPR017442. Se/Thr_pkinase-rel. IPR016255. Ser/Thr_prot_kinase_GCN2. IPR008271. Ser_thr_pkin_AS. IPR016135. UBQ-conjugat/RWD-like. [Graphical view]
Gene3D	G3DSA:3.10.110.10. UBQ-conjugat_E2. 1 hit.
PANTHER	PTHR11042:SF10. GCN2. 1 hit.
Pfam	PF00069. Pkinase. 3 hits. PF05773. RWD. 1 hit. PF00587. tRNA-synt_2b. 1 hit. [Graphical view]
PIRSF	PIRSF000660. Ser/Thr_PK_GCN2. 1 hit.
ProDom	PD000001. Prot_kinase. 3 hits. [Graphical view] [Entries sharing at least one domain]
SMART	SM00591. RWD. 1 hit. [Graphical view]
PROSITE	PS50862. AA_TRNA_LIGASE_II. False negative. PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 2 hits. PS00108. PROTEIN_KINASE_ST. 1 hit. PS50908. RWD. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	109089.
SOURCE	Search...

Entry information

Entry name

E2AK4_HUMAN

Accession

Primary (citable) accession number: Q9P2K8
Secondary accession number(s): Q69YL7 , Q6DC97, Q96GN6, Q9H5K1, Q9NSQ3, Q9NSZ5, Q9UJ56

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 15, 2005
Last sequence update:	March 15, 2005
Last modified:	June 16, 2009
This is version 73 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)