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Q14152

- EIF3A_HUMAN

UniProt

Q14152 - EIF3A_HUMAN

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Protein

Eukaryotic translation initiation factor 3 subunit A

Gene

EIF3A

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.1 PublicationUniRule annotation

GO - Molecular functioni

  1. poly(A) RNA binding Source: UniProtKB
  2. structural molecule activity Source: UniProtKB
  3. translation initiation factor activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. cellular protein metabolic process Source: Reactome
  2. formation of translation initiation complex Source: UniProtKB
  3. formation of translation preinitiation complex Source: UniProtKB-HAMAP
  4. gene expression Source: Reactome
  5. regulation of translational initiation Source: UniProtKB-HAMAP
  6. translation Source: Reactome
  7. translational initiation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Initiation factor

Keywords - Biological processi

Protein biosynthesis

Enzyme and pathway databases

ReactomeiREACT_1079. Formation of the ternary complex, and subsequently, the 43S complex.
REACT_1797. Formation of a pool of free 40S subunits.
REACT_1979. Translation initiation complex formation.
REACT_2085. GTP hydrolysis and joining of the 60S ribosomal subunit.
REACT_79. L13a-mediated translational silencing of Ceruloplasmin expression.
REACT_931. Ribosomal scanning and start codon recognition.

Names & Taxonomyi

Protein namesi
Recommended name:
Eukaryotic translation initiation factor 3 subunit AUniRule annotation
Short name:
eIF3aUniRule annotation
Alternative name(s):
Eukaryotic translation initiation factor 3 subunit 10UniRule annotation
eIF-3-thetaUniRule annotation
eIF3 p167
eIF3 p180
eIF3 p185
Gene namesi
Name:EIF3AUniRule annotation
Synonyms:EIF3S10UniRule annotation, KIAA0139
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 10

Organism-specific databases

HGNCiHGNC:3271. EIF3A.

Subcellular locationi

Cytoplasm 1 PublicationUniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytosol Source: Reactome
  3. eukaryotic 43S preinitiation complex Source: UniProtKB-HAMAP
  4. eukaryotic 48S preinitiation complex Source: UniProtKB-HAMAP
  5. eukaryotic translation initiation factor 3 complex Source: UniProtKB
  6. eukaryotic translation initiation factor 3 complex, eIF3m Source: Ensembl
  7. membrane Source: UniProtKB
  8. nucleolus Source: HPA
  9. nucleus Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA27699.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 PublicationsUniRule annotation
Chaini2 – 13821381Eukaryotic translation initiation factor 3 subunit APRO_0000123537Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei68 – 681N6-acetyllysine1 Publication
Modified residuei492 – 4921Phosphoserine1 PublicationUniRule annotation
Modified residuei881 – 8811Phosphoserine1 PublicationUniRule annotation
Modified residuei882 – 8821Phosphoserine1 PublicationUniRule annotation
Modified residuei1198 – 11981Phosphoserine1 PublicationUniRule annotation
Modified residuei1336 – 13361Phosphoserine1 PublicationUniRule annotation
Modified residuei1364 – 13641Phosphoserine1 PublicationUniRule annotation

Post-translational modificationi

Phosphorylated. Phosphorylation is enhanced upon serum stimulation.3 PublicationsUniRule annotation

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ14152.
PaxDbiQ14152.
PeptideAtlasiQ14152.
PRIDEiQ14152.

2D gel databases

UCD-2DPAGEQ14152.

PTM databases

PhosphoSiteiQ14152.

Expressioni

Gene expression databases

BgeeiQ14152.
CleanExiHS_EIF3A.
ExpressionAtlasiQ14152. baseline and differential.
GenevestigatoriQ14152.

Organism-specific databases

HPAiHPA038315.
HPA038316.

Interactioni

Subunit structurei

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.By similarity7 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
EIF3BP558846EBI-366617,EBI-366696
KRT7P087293EBI-366617,EBI-297833
ORFQ9Q2G45EBI-366617,EBI-6248094From a different organism.
UPF1Q92900-25EBI-366617,EBI-373492

Protein-protein interaction databases

BioGridi114210. 91 interactions.
DIPiDIP-31114N.
IntActiQ14152. 32 interactions.
MINTiMINT-1519859.
STRINGi9606.ENSP00000358140.

Structurei

3D structure databases

ProteinModelPortaliQ14152.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini366 – 494129PCIUniRule annotationAdd
BLAST
Repeati925 – 934101
Repeati935 – 94282; truncated
Repeati943 – 952103
Repeati953 – 962104
Repeati963 – 972105
Repeati973 – 982106
Repeati983 – 992107
Repeati993 – 1002108
Repeati1003 – 1012109
Repeati1013 – 10221010
Repeati1023 – 10321011
Repeati1033 – 10421012
Repeati1043 – 10521013
Repeati1054 – 10631014
Repeati1064 – 10731015
Repeati1074 – 10831016
Repeati1084 – 10931017
Repeati1094 – 11031018
Repeati1104 – 11131019
Repeati1114 – 11231020
Repeati1124 – 11331021
Repeati1134 – 11431022
Repeati1144 – 1152923; truncated
Repeati1153 – 11621024
Repeati1163 – 11721025; approximate

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni664 – 835172Interaction with EIF3BAdd
BLAST
Regioni925 – 117224825 X 10 AA approximate tandem repeats of [DE]-[DE]-[DE]-R-[SEVGFPILV]-[HPSN]-[RSW]-[RL]-[DRGTIHN]-[EPMANLGDT]Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili82 – 12039UniRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi576 – 875300Glu-richAdd
BLAST
Compositional biasi925 – 1294370Asp-richAdd
BLAST

Sequence similaritiesi

Belongs to the eIF-3 subunit A family.UniRule annotation
Contains 1 PCI domain.UniRule annotation

Keywords - Domaini

Coiled coil, Repeat

Phylogenomic databases

eggNOGiNOG236708.
GeneTreeiENSGT00730000111063.
HOGENOMiHOG000246822.
HOVERGENiHBG006128.
InParanoidiQ14152.
KOiK03254.
OMAiRGPWRNT.
OrthoDBiEOG7BGHKJ.
PhylomeDBiQ14152.
TreeFamiTF101522.

Family and domain databases

HAMAPiMF_03000. eIF3a.
InterProiIPR027512. EIF3A.
IPR000717. PCI_dom.
[Graphical view]
PANTHERiPTHR14005:SF0. PTHR14005:SF0. 1 hit.
PfamiPF01399. PCI. 1 hit.
[Graphical view]
SMARTiSM00088. PINT. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q14152) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MPAYFQRPEN ALKRANEFLE VGKKQPALDV LYDVMKSKKH RTWQKIHEPI
60 70 80 90 100
MLKYLELCVD LRKSHLAKEG LYQYKNICQQ VNIKSLEDVV RAYLKMAEEK
110 120 130 140 150
TEAAKEESQQ MVLDIEDLDN IQTPESVLLS AVSGEDTQDR TDRLLLTPWV
160 170 180 190 200
KFLWESYRQC LDLLRNNSRV ERLYHDIAQQ AFKFCLQYTR KAEFRKLCDN
210 220 230 240 250
LRMHLSQIQR HHNQSTAINL NNPESQSMHL ETRLVQLDSA ISMELWQEAF
260 270 280 290 300
KAVEDIHGLF SLSKKPPKPQ LMANYYNKVS TVFWKSGNAL FHASTLHRLY
310 320 330 340 350
HLSREMRKNL TQDEMQRMST RVLLATLSIP ITPERTDIAR LLDMDGIIVE
360 370 380 390 400
KQRRLATLLG LQAPPTRIGL INDMVRFNVL QYVVPEVKDL YNWLEVEFNP
410 420 430 440 450
LKLCERVTKV LNWVREQPEK EPELQQYVPQ LQNNTILRLL QQVSQIYQSI
460 470 480 490 500
EFSRLTSLVP FVDAFQLERA IVDAARHCDL QVRIDHTSRT LSFGSDLNYA
510 520 530 540 550
TREDAPIGPH LQSMPSEQIR NQLTAMSSVL AKALEVIKPA HILQEKEEQH
560 570 580 590 600
QLAVTAYLKN SRKEHQRILA RRQTIEERKE RLESLNIQRE KEELEQREAE
610 620 630 640 650
LQKVRKAEEE RLRQEAKERE KERILQEHEQ IKKKTVRERL EQIKKTELGA
660 670 680 690 700
KAFKDIDIED LEELDPDFIM AKQVEQLEKE KKELQERLKN QEKKIDYFER
710 720 730 740 750
AKRLEEIPLI KSAYEEQRIK DMDLWEQQEE ERITTMQLER EKALEHKNRM
760 770 780 790 800
SRMLEDRDLF VMRLKAARQS VYEEKLKQFE ERLAEERHNR LEERKRQRKE
810 820 830 840 850
ERRITYYREK EEEEQRRAEE QMLKEREERE RAERAKREEE LREYQERVKK
860 870 880 890 900
LEEVERKKRQ RELEIEERER RREEERRLGD SSLSRKDSRW GDRDSEGTWR
910 920 930 940 950
KGPEADSEWR RGPPEKEWRR GEGRDEDRSH RRDEERPRRL GDDEDREPSL
960 970 980 990 1000
RPDDDRVPRR GMDDDRGPRR GPEEDRFSRR GADDDRPSWR NTDDDRPPRR
1010 1020 1030 1040 1050
IADEDRGNWR HADDDRPPRR GLDEDRGSWR TADEDRGPRR GMDDDRGPRR
1060 1070 1080 1090 1100
GGADDERSSW RNADDDRGPR RGLDDDRGPR RGMDDDRGPR RGMDDDRGPR
1110 1120 1130 1140 1150
RGMDDDRGPR RGLDDDRGPW RNADDDRIPR RGAEDDRGPW RNMDDDRLSR
1160 1170 1180 1190 1200
RADDDRFPRR GDDSRPGPWR PLVKPGGWRE KEKAREESWG PPRESRPSEE
1210 1220 1230 1240 1250
REWDREKERD RDNQDREEND KDPERERDRE RDVDREDRFR RPRDEGGWRR
1260 1270 1280 1290 1300
GPAEESSSWR DSSRRDDRDR DDRRRERDDR RDLRERRDLR DDRDRRGPPL
1310 1320 1330 1340 1350
RSEREEVSSW RRADDRKDDR VEERDPPRRV PPPALSRDRE RDRDREREGE
1360 1370 1380
KEKASWRAEK DRESLRRTKN ETDEDGWTTV RR
Length:1,382
Mass (Da):166,569
Last modified:November 1, 1996 - v1
Checksum:i485C01B28D67EBBA
GO
Isoform 2 (identifier: Q14152-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-34: Missing.

Note: No experimental confirmation available.

Show »
Length:1,348
Mass (Da):162,636
Checksum:i97F42E357D8B5405
GO

Sequence cautioni

The sequence BAA09488.2 differs from that shown. Reason: Erroneous initiation.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti520 – 5201R → G in BAG63833. (PubMed:14702039)Curated
Sequence conflicti983 – 9831D → G in BAG63833. (PubMed:14702039)Curated
Sequence conflicti1272 – 12721D → G in BAG63833. (PubMed:14702039)Curated

Mass spectrometryi

Molecular mass is 166758.3 Da from positions 1 - 1382. 1 Publication

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti386 – 3861E → K.1 Publication
Corresponds to variant rs967185 [ dbSNP | Ensembl ].
VAR_024438
Natural varianti694 – 6941K → N.
Corresponds to variant rs431898 [ dbSNP | Ensembl ].
VAR_048921
Natural varianti993 – 9931D → E.
Corresponds to variant rs532138 [ dbSNP | Ensembl ].
VAR_048922

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 3434Missing in isoform 2. 1 PublicationVSP_055471Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U58046 mRNA. Translation: AAB41584.1.
U58047 Genomic DNA. Translation: AAB41586.1.
U78311 mRNA. Translation: AAB80695.1.
D50929 mRNA. Translation: BAA09488.2. Different initiation.
AK302575 mRNA. Translation: BAG63833.1.
AL355598 Genomic DNA. Translation: CAI14127.1.
CH471066 Genomic DNA. Translation: EAW49408.1.
CCDSiCCDS7608.1. [Q14152-1]
RefSeqiNP_003741.1. NM_003750.2. [Q14152-1]
UniGeneiHs.523299.

Genome annotation databases

EnsembliENST00000369144; ENSP00000358140; ENSG00000107581. [Q14152-1]
ENST00000541549; ENSP00000438178; ENSG00000107581. [Q14152-1]
GeneIDi8661.
KEGGihsa:8661.
UCSCiuc001ldu.3. human. [Q14152-1]

Polymorphism databases

DMDMi6685537.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U58046 mRNA. Translation: AAB41584.1 .
U58047 Genomic DNA. Translation: AAB41586.1 .
U78311 mRNA. Translation: AAB80695.1 .
D50929 mRNA. Translation: BAA09488.2 . Different initiation.
AK302575 mRNA. Translation: BAG63833.1 .
AL355598 Genomic DNA. Translation: CAI14127.1 .
CH471066 Genomic DNA. Translation: EAW49408.1 .
CCDSi CCDS7608.1. [Q14152-1 ]
RefSeqi NP_003741.1. NM_003750.2. [Q14152-1 ]
UniGenei Hs.523299.

3D structure databases

ProteinModelPortali Q14152.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 114210. 91 interactions.
DIPi DIP-31114N.
IntActi Q14152. 32 interactions.
MINTi MINT-1519859.
STRINGi 9606.ENSP00000358140.

PTM databases

PhosphoSitei Q14152.

Polymorphism databases

DMDMi 6685537.

2D gel databases

UCD-2DPAGE Q14152.

Proteomic databases

MaxQBi Q14152.
PaxDbi Q14152.
PeptideAtlasi Q14152.
PRIDEi Q14152.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000369144 ; ENSP00000358140 ; ENSG00000107581 . [Q14152-1 ]
ENST00000541549 ; ENSP00000438178 ; ENSG00000107581 . [Q14152-1 ]
GeneIDi 8661.
KEGGi hsa:8661.
UCSCi uc001ldu.3. human. [Q14152-1 ]

Organism-specific databases

CTDi 8661.
GeneCardsi GC10M120794.
H-InvDB HIX0170434.
HGNCi HGNC:3271. EIF3A.
HPAi HPA038315.
HPA038316.
MIMi 602039. gene.
neXtProti NX_Q14152.
PharmGKBi PA27699.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG236708.
GeneTreei ENSGT00730000111063.
HOGENOMi HOG000246822.
HOVERGENi HBG006128.
InParanoidi Q14152.
KOi K03254.
OMAi RGPWRNT.
OrthoDBi EOG7BGHKJ.
PhylomeDBi Q14152.
TreeFami TF101522.

Enzyme and pathway databases

Reactomei REACT_1079. Formation of the ternary complex, and subsequently, the 43S complex.
REACT_1797. Formation of a pool of free 40S subunits.
REACT_1979. Translation initiation complex formation.
REACT_2085. GTP hydrolysis and joining of the 60S ribosomal subunit.
REACT_79. L13a-mediated translational silencing of Ceruloplasmin expression.
REACT_931. Ribosomal scanning and start codon recognition.

Miscellaneous databases

ChiTaRSi EIF3A. human.
GeneWikii EIF3A.
GenomeRNAii 8661.
NextBioi 32483.
PROi Q14152.
SOURCEi Search...

Gene expression databases

Bgeei Q14152.
CleanExi HS_EIF3A.
ExpressionAtlasi Q14152. baseline and differential.
Genevestigatori Q14152.

Family and domain databases

HAMAPi MF_03000. eIF3a.
InterProi IPR027512. EIF3A.
IPR000717. PCI_dom.
[Graphical view ]
PANTHERi PTHR14005:SF0. PTHR14005:SF0. 1 hit.
Pfami PF01399. PCI. 1 hit.
[Graphical view ]
SMARTi SM00088. PINT. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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] (ISOFORM 1), 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] (ISOFORM 1).
    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] (ISOFORM 1).
    Tissue: Myelomonocyte.
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANT LYS-386.
    Tissue: Testis.
  5. "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].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. 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.
  8. "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.
  9. "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.
  10. "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.
  11. "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.
  12. "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.
  13. "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.
  14. "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.
  15. "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.
  16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  17. "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.
  18. "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.
  19. "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].
  20. "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.
  21. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  22. "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.

Entry informationi

Entry nameiEIF3A_HUMAN
AccessioniPrimary (citable) accession number: Q14152
Secondary accession number(s): B1AMV5
, B4DYS1, F5H335, O00653, Q15778
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1996
Last modified: October 29, 2014
This is version 145 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 10
    Human chromosome 10: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. Translation initiation factors
    List of translation initiation factor entries
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3