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Q9P2K8 (E2AK4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 125. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1649 AA.
Sequence statusComplete.
Protein existenceEvidence 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.

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 16491649Eukaryotic translation initiation factor 2-alpha kinase 4
PRO_0000085947

Regions

Domain25 – 137113RWD
Domain296 – 539244Protein kinase 1
Domain590 – 1001412Protein kinase 2
Nucleotide binding596 – 6049ATP By similarity
Region1022 – 1493472Histidyl-tRNA synthetase-like
Compositional bias484 – 4918Poly-Leu

Sites

Active site8481Proton acceptor By similarity
Binding site6191ATP By similarity

Amino acid modifications

Modified residue2301Phosphoserine Ref.8 Ref.9 Ref.12 Ref.14
Modified residue6671Phosphothreonine Ref.7 Ref.8 Ref.10 Ref.12
Modified residue8991Phosphothreonine; by autocatalysis By similarity
Modified residue9041Phosphothreonine; by autocatalysis By similarity
Modified residue12591N6-acetyllysine Ref.11

Natural variations

Alternative sequence608 – 6169QNKLDGCCY → WYRVIPSPL in isoform 3.
VSP_039185
Alternative sequence617 – 16491033Missing in isoform 3.
VSP_039186
Alternative sequence774 – 80128Missing in isoform 2.
VSP_013038
Natural variant1371H → R. Ref.15
VAR_040479
Natural variant1661R → W. Ref.15
Corresponds to variant rs34439704 [ dbSNP | Ensembl ].
VAR_040480
Natural variant4411I → L. Ref.4 Ref.15
Corresponds to variant rs2291627 [ dbSNP | Ensembl ].
VAR_040481
Natural variant8721D → V. Ref.15
VAR_040482
Natural variant9391H → Y in a lung neuroendocrine carcinoma sample; somatic mutation. Ref.15
VAR_040483
Natural variant10601T → R. Ref.15
VAR_040484
Natural variant13061G → C. Ref.2 Ref.15
Corresponds to variant rs35602605 [ dbSNP | Ensembl ].
VAR_040485
Natural variant13361K → R. Ref.15
Corresponds to variant rs35480871 [ dbSNP | Ensembl ].
VAR_040486
Natural variant14061Q → H. Ref.15
Corresponds to variant rs55721315 [ dbSNP | Ensembl ].
VAR_040487

Experimental info

Sequence conflict5561E → G in BAA92576. Ref.3
Sequence conflict5561E → G in CAH10626. Ref.4
Sequence conflict6291Q → K in CAH10626. Ref.4
Sequence conflict8581S → F in BAB15625. Ref.5
Sequence conflict11331N → I in CAB58360. Ref.6

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 18, 2010. Version 3.
Checksum: ECF3CFFA51AEE67C

FASTA1,649186,911
        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 

« Hide

Isoform 2 [UniParc].

Checksum: 40B21FA4D721C758
Show »

FASTA1,621183,717
Isoform 3 [UniParc].

Checksum: CBFF2B4F683C5DB3
Show »

FASTA61669,797

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[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. expand/collapse author list , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] 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.
PIRT46924.
RefSeqNP_001013725.2. NM_001013703.2.
UniGeneHs.656673.

3D structure databases

ProteinModelPortalQ9P2K8.
SMRQ9P2K8. Positions 21-144, 291-576, 585-1050, 1055-1489.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid136426. 5 interactions.
IntActQ9P2K8. 3 interactions.
STRING9606.ENSP00000263791.

Chemistry

ChEMBLCHEMBL5358.
GuidetoPHARMACOLOGY2018.

PTM databases

PhosphoSiteQ9P2K8.

Polymorphism databases

DMDM296439368.

Proteomic databases

PaxDbQ9P2K8.
PRIDEQ9P2K8.

Protocols and materials databases

DNASU440275.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000263791; ENSP00000263791; ENSG00000128829. [Q9P2K8-1]
ENST00000382727; ENSP00000372174; ENSG00000128829. [Q9P2K8-2]
ENST00000559624; ENSP00000453148; ENSG00000128829. [Q9P2K8-3]
GeneID440275.
KEGGhsa:440275.
UCSCuc001zkl.3. human. [Q9P2K8-3]
uc001zkm.1. human. [Q9P2K8-1]

Organism-specific databases

CTD440275.
GeneCardsGC15P040226.
H-InvDBHIX0012119.
HGNCHGNC:19687. EIF2AK4.
HPAHPA011811.
MIM609280. gene.
neXtProtNX_Q9P2K8.
PharmGKBPA134947616.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOVERGENHBG051432.
InParanoidQ9P2K8.
KOK16196.
OMALNMEEPV.
OrthoDBEOG780RKP.
PhylomeDBQ9P2K8.
TreeFamTF101512.

Enzyme and pathway databases

SignaLinkQ9P2K8.

Gene expression databases

ArrayExpressQ9P2K8.
BgeeQ9P2K8.
CleanExHS_EIF2AK4.
GenevestigatorQ9P2K8.

Family and domain databases

Gene3D3.10.110.10. 1 hit.
3.40.50.800. 1 hit.
InterProIPR004154. Anticodon-bd.
IPR024435. HisRS-related_dom.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_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]
PfamPF12745. HGTP_anticodon2. 1 hit.
PF00069. Pkinase. 3 hits.
PF05773. RWD. 1 hit.
[Graphical view]
PIRSFPIRSF000660. Ser/Thr_PK_GCN2. 1 hit.
SMARTSM00591. RWD. 1 hit.
[Graphical view]
SUPFAMSSF54495. SSF54495. 1 hit.
SSF56112. SSF56112. 3 hits.
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 2 hits.
PS00108. PROTEIN_KINASE_ST. 1 hit.
PS50908. RWD. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiEIF2AK4.
GenomeRNAi440275.
NextBio109089.
PROQ9P2K8.
SOURCESearch...

Entry information

Entry nameE2AK4_HUMAN
AccessionPrimary (citable) accession number: Q9P2K8
Secondary accession number(s): C9JEC4 expand/collapse secondary AC list , 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: April 16, 2014
This is version 125 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 15

Human chromosome 15: entries, gene names and cross-references to MIM