Q14152 (EIF3A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Eukaryotic translation initiation factor 3 subunit A
Short name=eIF3a

Alternative name(s):
Eukaryotic translation initiation factor 3 subunit 10
eIF-3-theta
eIF3 p167
eIF3 p180
eIF3 p185

Gene names

Name:	EIF3A
Synonyms:	EIF3S10, KIAA0139

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	1382 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	Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis. The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S preinitiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation. Ref.7
Subunit structure	Interacts with EIF4G1 By similarity. Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is composed of 13 subunits: EIF3A, EIF3B, EIF3C, EIF3D, EIF3E, EIF3F, EIF3G, EIF3H, EIF3I, EIF3J, EIF3K, EIF3L and EIF3M. The eIF-3 complex appears to include 3 stable modules: module A is composed of EIF3A, EIF3B, EIF3G and EIF3I; module B is composed of EIF3F, EIF3H, and EIF3M; and module C is composed of EIF3C, EIF3D, EIF3E, EIF3L and EIF3K. EIF3C of module C binds EIF3B of module A and EIF3H of module B, thereby linking the three modules. EIF3J is a labile subunit that binds to the eIF-3 complex via EIF3B. The eIF-3 complex interacts with RPS6KB1 under conditions of nutrient depletion. Mitogenic stimulation leads to binding and activation of a complex composed of MTOR and RPTOR, leading to phosphorylation and release of RPS6KB1 and binding of EIF4B to eIF-3. Also interacts with KRT7 and PIWIL2. Ref.7 Ref.8 Ref.9 Ref.11 Ref.13 Ref.14 Ref.16
Subcellular location	Cytoplasm Ref.1.
Post-translational modification	Phosphorylated. Phosphorylation is enhanced upon serum stimulation. Ref.14
Sequence similarities	Belongs to the eIF-3 subunit A family. Contains 1 PCI domain.
Mass spectrometry	Molecular mass is 166758.3 Da from positions 1 - 1382. Ref.14
Sequence caution	The sequence BAA09488.2 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Protein biosynthesis
Cellular component	Cytoplasm
Coding sequence diversity	Polymorphism
Domain	Coiled coil Repeat
Molecular function	Initiation factor
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	formation of translation initiation complex Inferred from direct assay Ref.12. Source: UniProtKB
Cellular_component	cytosol Traceable author statement. Source: Reactome eukaryotic translation initiation factor 3 complex Inferred from direct assay Ref.14Ref.12Ref.16. Source: UniProtKB nucleolus Inferred from direct assay. Source: HPA
Molecular_function	structural molecule activity Non-traceable author statement Ref.1. Source: UniProtKB translation initiation factor activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
EIF3B	P55884	5	EBI-366617,EBI-366696
KRT7	P08729	3	EBI-366617,EBI-297833
ORF	Q9Q2G4	5	EBI-366617,EBI-6248094	From a different organism.
UPF1	Q92900-2	5	EBI-366617,EBI-373492

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.6 Ref.14
	Chain	2 – 1382	1381	Eukaryotic translation initiation factor 3 subunit A HAMAP-Rule MF_03000		PRO_0000123537
Regions
	Domain	366 – 494	129	PCI
	Repeat	925 – 934	10	1 HAMAP-Rule MF_03000
	Repeat	935 – 942	8	2; truncated HAMAP-Rule MF_03000
	Repeat	943 – 952	10	3 HAMAP-Rule MF_03000
	Repeat	953 – 962	10	4 HAMAP-Rule MF_03000
	Repeat	963 – 972	10	5 HAMAP-Rule MF_03000
	Repeat	973 – 982	10	6 HAMAP-Rule MF_03000
	Repeat	983 – 992	10	7 HAMAP-Rule MF_03000
	Repeat	993 – 1002	10	8 HAMAP-Rule MF_03000
	Repeat	1003 – 1012	10	9 HAMAP-Rule MF_03000
	Repeat	1013 – 1022	10	10 HAMAP-Rule MF_03000
	Repeat	1023 – 1032	10	11 HAMAP-Rule MF_03000
	Repeat	1033 – 1042	10	12 HAMAP-Rule MF_03000
	Repeat	1043 – 1052	10	13 HAMAP-Rule MF_03000
	Repeat	1054 – 1063	10	14 HAMAP-Rule MF_03000
	Repeat	1064 – 1073	10	15 HAMAP-Rule MF_03000
	Repeat	1074 – 1083	10	16 HAMAP-Rule MF_03000
	Repeat	1084 – 1093	10	17 HAMAP-Rule MF_03000
	Repeat	1094 – 1103	10	18 HAMAP-Rule MF_03000
	Repeat	1104 – 1113	10	19 HAMAP-Rule MF_03000
	Repeat	1114 – 1123	10	20 HAMAP-Rule MF_03000
	Repeat	1124 – 1133	10	21 HAMAP-Rule MF_03000
	Repeat	1134 – 1143	10	22 HAMAP-Rule MF_03000
	Repeat	1144 – 1152	9	23; truncated HAMAP-Rule MF_03000
	Repeat	1153 – 1162	10	24 HAMAP-Rule MF_03000
	Repeat	1163 – 1172	10	25; approximate HAMAP-Rule MF_03000
	Region	664 – 835	172	Interaction with EIF3B HAMAP-Rule MF_03000
	Region	925 – 1172	248	25 X 10 AA approximate tandem repeats of [DE]-[DE]-[DE]-R-[SEVGFPILV]-[HPSN]-[RSW]-[RL]-[DRGTIHN]-[EPMANLGDT] HAMAP-Rule MF_03000
	Coiled coil	82 – 120	39	Potential
	Compositional bias	576 – 875	300	Glu-rich HAMAP-Rule MF_03000
	Compositional bias	925 – 1294	370	Asp-rich HAMAP-Rule MF_03000
Amino acid modifications
	Modified residue	68	1	N6-acetyllysine Ref.18
	Modified residue	492	1	Phosphoserine Ref.17
	Modified residue	881	1	Phosphoserine Ref.14
	Modified residue	882	1	Phosphoserine Ref.19
	Modified residue	1198	1	Phosphoserine Ref.14
	Modified residue	1336	1	Phosphoserine Ref.14
	Modified residue	1364	1	Phosphoserine Ref.14
Natural variations
	Natural variant	386	1	E → K. Corresponds to variant rs967185 [ dbSNP | Ensembl ].		VAR_024438
	Natural variant	694	1	K → N. Corresponds to variant rs431898 [ dbSNP | Ensembl ].		VAR_048921
	Natural variant	993	1	D → E. Corresponds to variant rs532138 [ dbSNP | Ensembl ].		VAR_048922

Sequences

	Sequence		Length	Mass (Da)
	Q14152 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 485C01B28D67EBBA	FASTA	1,382	166,569
	10 20 30 40 50 60 MPAYFQRPEN ALKRANEFLE VGKKQPALDV LYDVMKSKKH RTWQKIHEPI MLKYLELCVD 70 80 90 100 110 120 LRKSHLAKEG LYQYKNICQQ VNIKSLEDVV RAYLKMAEEK TEAAKEESQQ MVLDIEDLDN 130 140 150 160 170 180 IQTPESVLLS AVSGEDTQDR TDRLLLTPWV KFLWESYRQC LDLLRNNSRV ERLYHDIAQQ 190 200 210 220 230 240 AFKFCLQYTR KAEFRKLCDN LRMHLSQIQR HHNQSTAINL NNPESQSMHL ETRLVQLDSA 250 260 270 280 290 300 ISMELWQEAF KAVEDIHGLF SLSKKPPKPQ LMANYYNKVS TVFWKSGNAL FHASTLHRLY 310 320 330 340 350 360 HLSREMRKNL TQDEMQRMST RVLLATLSIP ITPERTDIAR LLDMDGIIVE KQRRLATLLG 370 380 390 400 410 420 LQAPPTRIGL INDMVRFNVL QYVVPEVKDL YNWLEVEFNP LKLCERVTKV LNWVREQPEK 430 440 450 460 470 480 EPELQQYVPQ LQNNTILRLL QQVSQIYQSI EFSRLTSLVP FVDAFQLERA IVDAARHCDL 490 500 510 520 530 540 QVRIDHTSRT LSFGSDLNYA TREDAPIGPH LQSMPSEQIR NQLTAMSSVL AKALEVIKPA 550 560 570 580 590 600 HILQEKEEQH QLAVTAYLKN SRKEHQRILA RRQTIEERKE RLESLNIQRE KEELEQREAE 610 620 630 640 650 660 LQKVRKAEEE RLRQEAKERE KERILQEHEQ IKKKTVRERL EQIKKTELGA KAFKDIDIED 670 680 690 700 710 720 LEELDPDFIM AKQVEQLEKE KKELQERLKN QEKKIDYFER AKRLEEIPLI KSAYEEQRIK 730 740 750 760 770 780 DMDLWEQQEE ERITTMQLER EKALEHKNRM SRMLEDRDLF VMRLKAARQS VYEEKLKQFE 790 800 810 820 830 840 ERLAEERHNR LEERKRQRKE ERRITYYREK EEEEQRRAEE QMLKEREERE RAERAKREEE 850 860 870 880 890 900 LREYQERVKK LEEVERKKRQ RELEIEERER RREEERRLGD SSLSRKDSRW GDRDSEGTWR 910 920 930 940 950 960 KGPEADSEWR RGPPEKEWRR GEGRDEDRSH RRDEERPRRL GDDEDREPSL RPDDDRVPRR 970 980 990 1000 1010 1020 GMDDDRGPRR GPEEDRFSRR GADDDRPSWR NTDDDRPPRR IADEDRGNWR HADDDRPPRR 1030 1040 1050 1060 1070 1080 GLDEDRGSWR TADEDRGPRR GMDDDRGPRR GGADDERSSW RNADDDRGPR RGLDDDRGPR 1090 1100 1110 1120 1130 1140 RGMDDDRGPR RGMDDDRGPR RGMDDDRGPR RGLDDDRGPW RNADDDRIPR RGAEDDRGPW 1150 1160 1170 1180 1190 1200 RNMDDDRLSR RADDDRFPRR GDDSRPGPWR PLVKPGGWRE KEKAREESWG PPRESRPSEE 1210 1220 1230 1240 1250 1260 REWDREKERD RDNQDREEND KDPERERDRE RDVDREDRFR RPRDEGGWRR GPAEESSSWR 1270 1280 1290 1300 1310 1320 DSSRRDDRDR DDRRRERDDR RDLRERRDLR DDRDRRGPPL RSEREEVSSW RRADDRKDDR 1330 1340 1350 1360 1370 1380 VEERDPPRRV PPPALSRDRE RDRDREREGE KEKASWRAEK DRESLRRTKN ETDEDGWTTV RR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The human p167 gene encodes a unique structural protein that contains centrosomin A homology and associates with a multicomponent complex." Scholler J.K., Kanner S.B. DNA Cell Biol. 16:515-531(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], SUBCELLULAR LOCATION. Tissue: Lymphoblastoma.
[2]	"Identification of cDNA clones for the large subunit of eukaryotic translation initiation factor 3. Comparison of homologues from human, Nicotiana tabacum, Caenorhabditis elegans, and Saccharomyces cerevisiae." Johnson K.R., Merrick W.C., Zoll W.L., Zhu Y. J. Biol. Chem. 272:7106-7113(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Keratinocyte and Liver.
[3]	"Prediction of the coding sequences of unidentified human genes. IV. The coding sequences of 40 new genes (KIAA0121-KIAA0160) deduced by analysis of cDNA clones from human cell line KG-1." Nagase T., Seki N., Tanaka A., Ishikawa K., Nomura N. DNA Res. 2:167-174(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Myelomonocyte.
[4]	"The DNA sequence and comparative analysis of human chromosome 10." Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J. , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J. Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	Bienvenut W.V., Boldt K., von Kriegsheim A.F., Matallanas D., Cooper W.N., Kolch W. Submitted (JUL-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 2-13; 15-36; 69-75; 85-91; 144-151; 173-183; 252-264; 279-298; 309-317; 322-335; 341-351; 368-388; 439-469; 490-546; 582-589; 624-632; 694-711; 719-740; 776-782; 817-824; 838-847; 850-856; 862-868; 877-885; 1071-1080; 1122-1130; 1142-1150 AND 1358-1366, CLEAVAGE OF INITIATOR METHIONINE, MASS SPECTROMETRY. Tissue: Hepatoma and Mammary carcinoma.
[7]	"Molecular interaction between human tumor marker protein p150, the largest subunit of eIF3, and intermediate filament protein K7." Lin L., Holbro T., Alonso G., Gerosa D., Burger M.M. J. Cell. Biochem. 80:483-490(2001) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH EIF3B AND KRT7.
[8]	"Characterization of eIF3k: a newly discovered subunit of mammalian translation initiation factor eIF3." Mayeur G.L., Fraser C.S., Peiretti F., Block K.L., Hershey J.W.B. Eur. J. Biochem. 270:4133-4139(2003) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH EIF3B.
[9]	"The j-subunit of human translation initiation factor eIF3 is required for the stable binding of eIF3 and its subcomplexes to 40 S ribosomal subunits in vitro." Fraser C.S., Lee J.Y., Mayeur G.L., Bushell M., Doudna J.A., Hershey J.W.B. J. Biol. Chem. 279:8946-8956(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH EIF3B.
[10]	"Binding of eukaryotic initiation factor 3 to ribosomal 40S subunits and its role in ribosomal dissociation and anti-association." Kolupaeva V.G., Unbehaun A., Lomakin I.B., Hellen C.U.T., Pestova T.V. RNA 11:470-486(2005) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION OF THE EIF-3 COMPLEX.
[11]	"Translation initiation factor eIF4G-1 binds to eIF3 through the eIF3e subunit." LeFebvre A.K., Korneeva N.L., Trutschl M., Cvek U., Duzan R.D., Bradley C.A., Hershey J.W.B., Rhoads R.E. J. Biol. Chem. 281:22917-22932(2006) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN THE EIF-3 COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
[12]	"Reconstitution reveals the functional core of mammalian eIF3." Masutani M., Sonenberg N., Yokoyama S., Imataka H. EMBO J. 26:3373-3383(2007) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION OF THE EIF-3 COMPLEX.
[13]	"Human INT6/eIF3e is required for nonsense-mediated mRNA decay." Morris C., Wittmann J., Jaeck H.-M., Jalinot P. EMBO Rep. 8:596-602(2007) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH EIF3E.
[14]	"Structural characterization of the human eukaryotic initiation factor 3 protein complex by mass spectrometry." Damoc E., Fraser C.S., Zhou M., Videler H., Mayeur G.L., Hershey J.W.B., Doudna J.A., Robinson C.V., Leary J.A. Mol. Cell. Proteomics 6:1135-1146(2007) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN THE EIF-3 COMPLEX, CHARACTERIZATION OF THE EIF-3 COMPLEX, CLEAVAGE OF INITIATOR METHIONINE, PHOSPHORYLATION AT SER-881; SER-1198; SER-1336 AND SER-1364, MASS SPECTROMETRY.
[15]	"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[16]	"Mass spectrometry reveals modularity and a complete subunit interaction map of the eukaryotic translation factor eIF3." Zhou M., Sandercock A.M., Fraser C.S., Ridlova G., Stephens E., Schenauer M.R., Yokoi-Fong T., Barsky D., Leary J.A., Hershey J.W.B., Doudna J.A., Robinson C.V. Proc. Natl. Acad. Sci. U.S.A. 105:18139-18144(2008) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN THE EIF-3 COMPLEX, CHARACTERIZATION OF THE EIF-3 COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
[17]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-492, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[18]	"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-68, MASS SPECTROMETRY.
[19]	"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-882, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[20]	"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].
[21]	"Structural roles for human translation factor eIF3 in initiation of protein synthesis." Siridechadilok B., Fraser C.S., Hall R.J., Doudna J.A., Nogales E. Science 310:1513-1515(2005) [PubMed] [Europe PMC] [Abstract] Cited for: 3D-STRUCTURE MODELING, ELECTRON MICROSCOPY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U58046 mRNA. Translation: AAB41584.1. U58047 Genomic DNA. Translation: AAB41586.1. U78311 mRNA. Translation: AAB80695.1. D50929 mRNA. Translation: BAA09488.2. Different initiation. AL355598 Genomic DNA. Translation: CAI14127.1. CH471066 Genomic DNA. Translation: EAW49408.1.
IPI	IPI00029012.
RefSeq	NP_003741.1. NM_003750.2.
UniGene	Hs.523299.
3D structure databases
ProteinModelPortal	Q14152.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-31114N.
IntAct	Q14152. 26 interactions.
MINT	MINT-1519859.
STRING	9606.ENSP00000358140.
PTM databases
PhosphoSite	Q14152.
Polymorphism databases
DMDM	6685537.
2D gel databases
UCD-2DPAGE	Q14152.
Proteomic databases
PaxDb	Q14152.
PeptideAtlas	Q14152.
PRIDE	Q14152.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000369144; ENSP00000358140; ENSG00000107581.
GeneID	8661.
KEGG	hsa:8661.
UCSC	uc001ldu.3. human.
Organism-specific databases
CTD	8661.
GeneCards	GC10M120794.
H-InvDB	HIX0170434.
HGNC	HGNC:3271. EIF3A.
HPA	HPA038315. HPA038316.
MIM	602039. gene.
neXtProt	NX_Q14152.
PharmGKB	PA27699.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG236708.
HOGENOM	HOG000246822.
HOVERGEN	HBG006128.
InParanoid	Q14152.
KO	K03254.
OMA	QDRDEND.
OrthoDB	EOG4B2SWM.
PhylomeDB	Q14152.
Enzyme and pathway databases
Pathway_Interaction_DB	il2_pi3kpathway. IL2 signaling events mediated by PI3K. mtor_4pathway. mTOR signaling pathway.
Reactome	REACT_17015. Metabolism of proteins. REACT_1762. 3' -UTR-mediated translational regulation. REACT_71. Gene Expression.
Gene expression databases
ArrayExpress	Q14152.
Bgee	Q14152.
CleanEx	HS_EIF3A.
Genevestigator	Q14152.
GermOnline	ENSG00000107581. Homo sapiens.
Family and domain databases
HAMAP	MF_03000. eIF3a.
InterPro	IPR000717. PCI_dom. [Graphical view]
Pfam	PF01399. PCI. 1 hit. [Graphical view]
SMART	SM00088. PINT. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	EIF3A. human.
GenomeRNAi	8661.
NextBio	32483.
SOURCE	Search...

Entry information

Entry name

EIF3A_HUMAN

Accession

Primary (citable) accession number: Q14152
Secondary accession number(s): B1AMV5, O00653, Q15778

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	November 1, 1996
Last modified:	May 1, 2013
This is version 129 of the entry and version 1 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.