Q9P2K8 (E2AK4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

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) [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	1649 AA.
Sequence status	Complete.
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.6
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.
Sequence caution	The sequence BAA92576.1 differs from that shown. Reason: Contaminating sequence. Sequence of unknown origin in the N-terminal part. The sequence BAB15625.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cellular response to starvation Inferred from electronic annotation. Source: Compara endoplasmic reticulum unfolded protein response Inferred from electronic annotation. Source: Compara negative regulation of translation Inferred from electronic annotation. Source: Compara regulation of translational initiation Inferred from sequence or structural similarity. Source: UniProtKB regulation of translational initiation in response to stress Inferred from electronic annotation. Source: Compara
Cellular_component	cytosolic ribosome Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW eukaryotic translation initiation factor 2alpha kinase activity Inferred from sequence or structural similarity Ref.6. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 3 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.

Isoform 3 (identifier: Q9P2K8-3)

The sequence of this isoform differs from the canonical sequence as follows:
     608-616: QNKLDGCCY → WYRVIPSPL
     617-1649: 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 Ref.12 Ref.14
	Modified residue	667	1	Phosphothreonine Ref.7 Ref.8 Ref.10 Ref.12
	Modified residue	899	1	Phosphothreonine; by autocatalysis By similarity
	Modified residue	904	1	Phosphothreonine; by autocatalysis By similarity
	Modified residue	1259	1	N6-acetyllysine Ref.11
Natural variations
	Alternative sequence	608 – 616	9	QNKLDGCCY → WYRVIPSPL in isoform 3.		VSP_039185
	Alternative sequence	617 – 1649	1033	Missing in isoform 3.		VSP_039186
	Alternative sequence	774 – 801	28	Missing in isoform 2.		VSP_013038
	Natural variant	137	1	H → R. Ref.15		VAR_040479
	Natural variant	166	1	R → W. Ref.15		VAR_040480
	Natural variant	441	1	I → L. Ref.4 Ref.15 Corresponds to variant rs2291627 [ dbSNP | Ensembl ].		VAR_040481
	Natural variant	872	1	D → V. Ref.15		VAR_040482
	Natural variant	939	1	H → Y in a lung neuroendocrine carcinoma sample; somatic mutation. Ref.15		VAR_040483
	Natural variant	1060	1	T → R. Ref.15		VAR_040484
	Natural variant	1306	1	G → C. Ref.2 Ref.15 Corresponds to variant rs35602605 [ dbSNP | Ensembl ].		VAR_040485
	Natural variant	1336	1	K → R. Ref.15 Corresponds to variant rs35480871 [ dbSNP | Ensembl ].		VAR_040486
	Natural variant	1406	1	Q → H. Ref.15		VAR_040487
Experimental info
	Sequence conflict	556	1	E → G in BAA92576. Ref.3
	Sequence conflict	556	1	E → G in CAH10626. Ref.4
	Sequence conflict	629	1	Q → K in CAH10626. Ref.4
	Sequence conflict	858	1	S → F in BAB15625. Ref.5
	Sequence conflict	1133	1	N → I in CAB58360. Ref.6

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 18, 2010. Version 3. Checksum: ECF3CFFA51AEE67C	FASTA	1,649	186,911
	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 SPEDSEGQDY 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 [UniParc]. Checksum: 40B21FA4D721C758	FASTA	1,621	183,717
	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 SPEDSEGQDY 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
	Isoform 3 [UniParc]. Checksum: CBFF2B4F683C5DB3	FASTA	616	69,797
	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 SPEDSEGQDY VETVIPSNRL PSAAFFSETQ RQFSRYFIEF EELQLLGKGA 610 FGAVIKVWYR VIPSPL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Analysis of the DNA sequence and duplication history of human chromosome 15." Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A. , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C. Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 821-1649 (ISOFORM 1), VARIANT CYS-1306. Tissue: Muscle and Uterus.
[3]	"Prediction of the coding sequences of unidentified human genes. XVI. The complete sequences of 150 new cDNA clones from brain which code for large proteins in vitro." Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O. DNA Res. 7:65-73(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 177-1649. Tissue: Brain.
[4]	"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., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 196-1649, VARIANT LEU-441. Tissue: Melanoma and Testis.
[5]	"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] OF 831-1649.
[6]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1102-1649, TISSUE SPECIFICITY.
[7]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-667, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-230 AND THR-667, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-230, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"Large-scale proteomics analysis of the human kinome." Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H. Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-667, MASS SPECTROMETRY.
[11]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1259, MASS SPECTROMETRY.
[12]	"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-230 AND THR-667, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[13]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]	"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-230, MASS SPECTROMETRY.
[15]	"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] 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
EMBL GenBank DDBJ	AC012377 Genomic DNA. No translation available. AC025168 Genomic DNA. No translation available. BC009350 mRNA. Translation: AAH09350.2. BC078179 mRNA. Translation: AAH78179.1. AB037759 mRNA. Translation: BAA92576.1. Sequence problems. 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. IPI00966834.
PIR	T46924.
RefSeq	NP_001013725.2. NM_001013703.2.
UniGene	Hs.656673.
3D structure databases
ProteinModelPortal	Q9P2K8.
SMR	Q9P2K8. Positions 21-144, 291-576, 585-658, 735-1050, 1055-1489.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9P2K8. 3 interactions.
STRING	9606.ENSP00000263791.
PTM databases
PhosphoSite	Q9P2K8.
Polymorphism databases
DMDM	296439368.
Proteomic databases
PaxDb	Q9P2K8.
PRIDE	Q9P2K8.
Protocols and materials databases
DNASU	440275.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000263791; ENSP00000263791; ENSG00000128829. ENST00000382727; ENSP00000372174; ENSG00000128829. ENST00000559624; ENSP00000453148; ENSG00000128829.
GeneID	440275.
KEGG	hsa:440275.
UCSC	uc001zkl.3. human. uc001zkm.1. human. uc010bbj.1. human.
Organism-specific databases
CTD	440275.
GeneCards	GC15P040226.
H-InvDB	HIX0012119.
HGNC	HGNC:19687. EIF2AK4.
MIM	609280. gene.
neXtProt	NX_Q9P2K8.
PharmGKB	PA134947616.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0515.
HOVERGEN	HBG051432.
InParanoid	Q9P2K8.
KO	K16196.
OMA	CCYAVKR.
OrthoDB	EOG4J6RQ0.
Gene expression databases
ArrayExpress	Q9P2K8.
Bgee	Q9P2K8.
CleanEx	HS_EIF2AK4.
Genevestigator	Q9P2K8.
GermOnline	ENSG00000128829. Homo sapiens.
Family and domain databases
Gene3D	3.10.110.10. 1 hit. 3.40.50.800. 1 hit.
InterPro	IPR004154. Anticodon-bd. IPR026920. EIF2AK4. IPR024435. HisRS-related_dom. IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_cat_dom. IPR017441. Protein_kinase_ATP_BS. IPR006575. RWD-domain. IPR008271. Ser/Thr_kinase_AS. IPR016255. Ser/Thr_kinase_GCN2. IPR016135. UBQ-conjugating_enzyme/RWD. [Graphical view]
PANTHER	PTHR11042:SF10. PTHR11042:SF10. 1 hit.
Pfam	PF12745. HGTP_anticodon2. 1 hit. PF00069. Pkinase. 3 hits. PF05773. RWD. 1 hit. [Graphical view]
PIRSF	PIRSF000660. Ser/Thr_PK_GCN2. 1 hit.
SMART	SM00591. RWD. 1 hit. [Graphical view]
SUPFAM	SSF56112. Kinase_like. 2 hits. SSF54495. UBQ-conjugat/RWD-like. 1 hit.
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
ChEMBL	CHEMBL5358.
GenomeRNAi	440275.
NextBio	109089.
SOURCE	Search...

Entry information

Entry name

E2AK4_HUMAN

Accession

Primary (citable) accession number: Q9P2K8
Secondary accession number(s): C9JEC4 , Q69YL7, Q6DC97, Q96GN6, Q9H5K1, Q9NSQ3, Q9NSZ5, Q9UJ56

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 15, 2005
Last sequence update:	May 18, 2010
Last modified:	May 1, 2013
This is version 114 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.