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Q14152 (EIF3A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 139. 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·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

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

Protein attributes

Sequence length1382 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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 processProtein biosynthesis
   Cellular componentCytoplasm
   Coding sequence diversityPolymorphism
   DomainCoiled coil
Repeat
   Molecular functionInitiation factor
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcellular protein metabolic process

Traceable author statement. Source: Reactome

formation of translation initiation complex

Inferred from direct assay Ref.12. Source: UniProtKB

formation of translation preinitiation complex

Inferred from electronic annotation. Source: UniProtKB-HAMAP

gene expression

Traceable author statement. Source: Reactome

regulation of translational initiation

Inferred from electronic annotation. Source: UniProtKB-HAMAP

translation

Traceable author statement. Source: Reactome

translational initiation

Inferred by curator Ref.14Ref.16. Source: UniProtKB

   Cellular_componentcytoplasm

Non-traceable author statement Ref.1. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

eukaryotic 43S preinitiation complex

Inferred from electronic annotation. Source: UniProtKB-HAMAP

eukaryotic 48S preinitiation complex

Inferred from electronic annotation. Source: UniProtKB-HAMAP

eukaryotic translation initiation factor 3 complex

Inferred from direct assay Ref.14Ref.12Ref.16. Source: UniProtKB

nucleolus

Inferred from direct assay. Source: HPA

nucleus

Inferred from direct assay. Source: HPA

   Molecular_functionpoly(A) RNA binding

Inferred from direct assay PubMed 22658674PubMed 22681889. Source: UniProtKB

structural molecule activity

Non-traceable author statement Ref.1. Source: UniProtKB

translation initiation factor activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.6 Ref.14
Chain2 – 13821381Eukaryotic translation initiation factor 3 subunit A HAMAP-Rule MF_03000
PRO_0000123537

Regions

Domain366 – 494129PCI
Repeat925 – 934101 HAMAP-Rule MF_03000
Repeat935 – 94282; truncated HAMAP-Rule MF_03000
Repeat943 – 952103 HAMAP-Rule MF_03000
Repeat953 – 962104 HAMAP-Rule MF_03000
Repeat963 – 972105 HAMAP-Rule MF_03000
Repeat973 – 982106 HAMAP-Rule MF_03000
Repeat983 – 992107 HAMAP-Rule MF_03000
Repeat993 – 1002108 HAMAP-Rule MF_03000
Repeat1003 – 1012109 HAMAP-Rule MF_03000
Repeat1013 – 10221010 HAMAP-Rule MF_03000
Repeat1023 – 10321011 HAMAP-Rule MF_03000
Repeat1033 – 10421012 HAMAP-Rule MF_03000
Repeat1043 – 10521013 HAMAP-Rule MF_03000
Repeat1054 – 10631014 HAMAP-Rule MF_03000
Repeat1064 – 10731015 HAMAP-Rule MF_03000
Repeat1074 – 10831016 HAMAP-Rule MF_03000
Repeat1084 – 10931017 HAMAP-Rule MF_03000
Repeat1094 – 11031018 HAMAP-Rule MF_03000
Repeat1104 – 11131019 HAMAP-Rule MF_03000
Repeat1114 – 11231020 HAMAP-Rule MF_03000
Repeat1124 – 11331021 HAMAP-Rule MF_03000
Repeat1134 – 11431022 HAMAP-Rule MF_03000
Repeat1144 – 1152923; truncated HAMAP-Rule MF_03000
Repeat1153 – 11621024 HAMAP-Rule MF_03000
Repeat1163 – 11721025; approximate HAMAP-Rule MF_03000
Region664 – 835172Interaction with EIF3B HAMAP-Rule MF_03000
Region925 – 117224825 X 10 AA approximate tandem repeats of [DE]-[DE]-[DE]-R-[SEVGFPILV]-[HPSN]-[RSW]-[RL]-[DRGTIHN]-[EPMANLGDT] HAMAP-Rule MF_03000
Coiled coil82 – 12039 Potential
Compositional bias576 – 875300Glu-rich HAMAP-Rule MF_03000
Compositional bias925 – 1294370Asp-rich HAMAP-Rule MF_03000

Amino acid modifications

Modified residue681N6-acetyllysine Ref.18
Modified residue4921Phosphoserine Ref.17
Modified residue8811Phosphoserine Ref.14
Modified residue8821Phosphoserine Ref.19
Modified residue11981Phosphoserine Ref.14
Modified residue13361Phosphoserine Ref.14
Modified residue13641Phosphoserine Ref.14

Natural variations

Natural variant3861E → K.
Corresponds to variant rs967185 [ dbSNP | Ensembl ].
VAR_024438
Natural variant6941K → N.
Corresponds to variant rs431898 [ dbSNP | Ensembl ].
VAR_048921
Natural variant9931D → E.
Corresponds to variant rs532138 [ dbSNP | Ensembl ].
VAR_048922

Sequences

Sequence LengthMass (Da)Tools
Q14152 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 485C01B28D67EBBA

FASTA1,382166,569
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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, IDENTIFICATION BY 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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.
RefSeqNP_003741.1. NM_003750.2.
UniGeneHs.523299.

3D structure databases

ProteinModelPortalQ14152.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114210. 85 interactions.
DIPDIP-31114N.
IntActQ14152. 31 interactions.
MINTMINT-1519859.
STRING9606.ENSP00000358140.

PTM databases

PhosphoSiteQ14152.

Polymorphism databases

DMDM6685537.

2D gel databases

UCD-2DPAGEQ14152.

Proteomic databases

PaxDbQ14152.
PeptideAtlasQ14152.
PRIDEQ14152.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000369144; ENSP00000358140; ENSG00000107581.
GeneID8661.
KEGGhsa:8661.
UCSCuc001ldu.3. human.

Organism-specific databases

CTD8661.
GeneCardsGC10M120794.
H-InvDBHIX0170434.
HGNCHGNC:3271. EIF3A.
HPAHPA038315.
HPA038316.
MIM602039. gene.
neXtProtNX_Q14152.
PharmGKBPA27699.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG236708.
HOGENOMHOG000246822.
HOVERGENHBG006128.
InParanoidQ14152.
KOK03254.
OMARGPWRNT.
OrthoDBEOG7BGHKJ.
PhylomeDBQ14152.
TreeFamTF101522.

Enzyme and pathway databases

ReactomeREACT_17015. Metabolism of proteins.
REACT_1762. 3' -UTR-mediated translational regulation.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpressQ14152.
BgeeQ14152.
CleanExHS_EIF3A.
GenevestigatorQ14152.

Family and domain databases

HAMAPMF_03000. eIF3a.
InterProIPR027512. EIF3A.
IPR000717. PCI_dom.
[Graphical view]
PANTHERPTHR14005:SF0. PTHR14005:SF0. 1 hit.
PfamPF01399. PCI. 1 hit.
[Graphical view]
SMARTSM00088. PINT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSEIF3A. human.
GeneWikiEIF3A.
GenomeRNAi8661.
NextBio32483.
PROQ14152.
SOURCESearch...

Entry information

Entry nameEIF3A_HUMAN
AccessionPrimary (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: April 16, 2014
This is version 139 of the entry and version 1 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

MIM cross-references

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

Translation initiation factors

List of translation initiation factor entries

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 10

Human chromosome 10: entries, gene names and cross-references to MIM