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Protein

Eukaryotic translation initiation factor 3 subunit A

Gene

Eif3a

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: 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.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Initiation factor

Keywords - Biological processi

Protein biosynthesis

Enzyme and pathway databases

ReactomeiR-MMU-156827. L13a-mediated translational silencing of Ceruloplasmin expression.
R-MMU-72649. Translation initiation complex formation.
R-MMU-72689. Formation of a pool of free 40S subunits.
R-MMU-72695. Formation of the ternary complex, and subsequently, the 43S complex.
R-MMU-72702. Ribosomal scanning and start codon recognition.
R-MMU-72706. GTP hydrolysis and joining of the 60S ribosomal subunit.

Names & Taxonomyi

Protein namesi
Recommended name:
Eukaryotic translation initiation factor 3 subunit AUniRule annotation
Short name:
eIF3aUniRule annotation
Alternative name(s):
Centrosomin
Eukaryotic translation initiation factor 3 subunit 10UniRule annotation
eIF-3-thetaUniRule annotation
eIF3 p167
eIF3 p180
eIF3 p185
p162
Gene namesi
Name:Eif3a
Synonyms:Csma, Eif3, Eif3s10
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 19

Organism-specific databases

MGIiMGI:95301. Eif3a.

Subcellular locationi

  • Cytoplasm UniRule annotation
  • Cytoplasmcytoskeletonmicrotubule organizing centercentrosome 1 Publication
  • Nucleus 1 Publication

  • Note: Centrosomin-A is found in the centrosome. Centrosomin-B is found in the nucleus.

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 13441343Eukaryotic translation initiation factor 3 subunit APRO_0000123538Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei68 – 681N6-acetyllysineBy similarity
Modified residuei492 – 4921PhosphoserineUniRule annotationBy similarity
Modified residuei584 – 5841PhosphoserineCombined sources
Modified residuei895 – 8951PhosphoserineBy similarity
Modified residuei949 – 9491PhosphoserineBy similarity
Modified residuei1028 – 10281PhosphoserineBy similarity
Modified residuei1149 – 11491PhosphoserineBy similarity
Modified residuei1159 – 11591PhosphoserineUniRule annotationBy similarity
Modified residuei1223 – 12231PhosphoserineBy similarity
Modified residuei1300 – 13001PhosphoserineUniRule annotationBy similarity
Modified residuei1326 – 13261PhosphoserineUniRule annotationBy similarity

Post-translational modificationi

Phosphorylated. Phosphorylation is enhanced upon serum stimulation.UniRule annotation

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP23116.
MaxQBiP23116.
PaxDbiP23116.
PeptideAtlasiP23116.
PRIDEiP23116.

PTM databases

iPTMnetiP23116.
PhosphoSiteiP23116.

Expressioni

Gene expression databases

BgeeiENSMUSG00000024991.
GenevisibleiP23116. MM.

Interactioni

Subunit structurei

Interacts with KRT7 (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 may interact with RPS6KB1 under conditions of nutrient depletion. Mitogenic stimulation may lead 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. Interacts with EIF4G1 and PIWIL2.By similarity3 Publications

Protein-protein interaction databases

BioGridi199415. 126 interactions.
IntActiP23116. 137 interactions.
MINTiMINT-1860578.
STRINGi10090.ENSMUSP00000025955.

Structurei

3D structure databases

SMRiP23116. Positions 7-605.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini366 – 494129PCIUniRule annotationAdd
BLAST
Repeati924 – 93181; truncated
Repeati932 – 941102
Repeati942 – 951103; approximate
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; approximate

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni664 – 835172Interaction with EIF3BUniRule annotationAdd
BLAST
Regioni924 – 113321021 X 10 AA approximate tandem repeats of [DA]-[DE]-[ED]-R-[PLIGFSV]-[RPS]-[RW]-[RL]-[GNIHT]-[DGLPTAM]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 biasi924 – 1258335Asp-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

eggNOGiKOG2072. Eukaryota.
ENOG410XQ37. LUCA.
GeneTreeiENSGT00730000111063.
HOGENOMiHOG000246822.
HOVERGENiHBG006128.
InParanoidiP23116.
KOiK03254.
OMAiAREDSWG.
OrthoDBiEOG091G01VW.
TreeFamiTF101522.

Family and domain databases

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

Sequencei

Sequence statusi: Complete.

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

P23116-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPAYFQRPEN ALKRANEFLE VGKKQPALDV LYDVMKSKKH RTWQKIHEPI
60 70 80 90 100
MLKYLELCVD LRKSHLAKEG LYQYKNICQQ VNIKSLEDVV RAYLKLAEEK
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 TQEEMQRMST RVLLATLSIP ITPERTDIAR LLDMDGIIVE
360 370 380 390 400
KQRRLATLLG LQAPPTRIGL INDMVRFSVL QYVVPEVKDL YNWLEVEFNP
410 420 430 440 450
LKLCERVTKV LNWVREQPEK EPELQQYVPQ LQNNTILRLL QQVAQIYQSI
460 470 480 490 500
EFSRLTSLVP FVDAFQLERA IVDAARHCDL QVRIDHTSRT LSFGSDLNYA
510 520 530 540 550
TREDAPVGPH LQSMPSEQIR NQLTAMSSVL AKALEVIRPA HILQEKEEQH
560 570 580 590 600
QLAVNAYLKN 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 KSAYEEQRVK DMDLWEQQEE ERITTMQLER EKALEHKNRM
760 770 780 790 800
SRMLEDRDLF VMRLKAARQS VYEEKLKQFE ERLAEERHSR LEDRKRQRKE
810 820 830 840 850
ERKITYYREK EEEEQRRAEE QMLKEREERE RAERAKREEE LREYQERVKK
860 870 880 890 900
LEEVERKKRQ RELEIEERER RREEERRLGD DPLSRKDSRW GDRDSEGTWR
910 920 930 940 950
KGPEADSEWR RGPPEKEWRR ETRDDERPHR RDEDRLRRLG GDDEERESSL
960 970 980 990 1000
RPDDDRIPRR GLDDDRGPRR GPDEDRFSRR GTDDDRPSWR NADDDRPPRR
1010 1020 1030 1040 1050
IGDDDRGSWR HTDDDRPPRR GLDDERGSWR TADEDRGPRR GMDDDRGPRR
1060 1070 1080 1090 1100
GGADDERSSW RNADDDRGPR RGMDDDRGPR RGLDDDRGPW RNAAEDRISR
1110 1120 1130 1140 1150
RGADDDRGPW RNMDDDRVPR RGDDARPGPW RPFVKPGGWR EKEKAREESW
1160 1170 1180 1190 1200
GPPRESRPSE EREWDRDKEK DRDNQDREEN DKDLERDRDR ERDGDREDRF
1210 1220 1230 1240 1250
RRPRDEGGWR RGPAEESSSW RDSSRRDDRD REDRRRDRDD RRDLRDLRDR
1260 1270 1280 1290 1300
RDLRDDRDRR GPPLRSEREE ASSWRRTDDR KDDRTEERDP PRRVPPPALS
1310 1320 1330 1340
RDRERERERE GEKEKASWRA EKDRESLRRT KNETDEDGWT TVRR
Length:1,344
Mass (Da):161,936
Last modified:July 27, 2011 - v5
Checksum:i215F5CCB8A2C7296
GO

Sequence cautioni

The sequence CAA35246 differs from that shown. Reason: Frameshift at positions 421, 468, 613, 648 and 787. Curated
The sequence CAA59144 differs from that shown. Reason: Frameshift at positions 421, 468, 613, 648, 962 and 1059. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti534 – 5341L → I in AAA90910 (Ref. 1) Curated
Sequence conflicti534 – 5341L → I in CAA35246 (PubMed:9372446).Curated
Sequence conflicti534 – 5341L → I in CAA59144 (PubMed:9372446).Curated
Sequence conflicti683 – 6842EL → DY in CAA35246 (PubMed:9372446).Curated
Sequence conflicti683 – 6842EL → DY in CAA59144 (PubMed:9372446).Curated
Sequence conflicti717 – 7171Q → H in CAA35246 (PubMed:9372446).Curated
Sequence conflicti717 – 7171Q → H in CAA59144 (PubMed:9372446).Curated
Sequence conflicti766 – 7661A → V in CAA35246 (PubMed:9372446).Curated
Sequence conflicti766 – 7661A → V in CAA59144 (PubMed:9372446).Curated
Sequence conflicti793 – 7931D → E in AAA90910 (Ref. 1) Curated
Sequence conflicti1007 – 10071G → A in CAA59144 (PubMed:9372446).Curated
Sequence conflicti1056 – 10561E → D in CAA59144 (PubMed:9372446).Curated

RNA editingi

Modified position: not applicable.
Some positions are modified by RNA editing via nucleotide deletion, up to position 787. The unedited version gives rise to centrosomin-B (shown here). The fully edited version gives rise to centrosomin-A, in which the C-terminal sequence is replaced up to position 787 by Ser-Ile-Val-Ala-STOP. A combination of alternative splicing and RNA editing resulting in this template G deletion could also explain the generation of centrosomin-A mRNA.1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U14172 mRNA. Translation: AAA90910.1.
AC163019 Genomic DNA. No translation available.
X84651 mRNA. Translation: CAA59144.1. Frameshift.
X17373 mRNA. Translation: CAA35246.1. Frameshift.
CCDSiCCDS38035.1.
PIRiS13800.
T42637.
RefSeqiNP_034253.3. NM_010123.3.
UniGeneiMm.2238.
Mm.482533.

Genome annotation databases

EnsembliENSMUST00000025955; ENSMUSP00000025955; ENSMUSG00000024991.
GeneIDi13669.
KEGGimmu:13669.
UCSCiuc008ibx.1. mouse.

Keywords - Coding sequence diversityi

RNA editing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U14172 mRNA. Translation: AAA90910.1.
AC163019 Genomic DNA. No translation available.
X84651 mRNA. Translation: CAA59144.1. Frameshift.
X17373 mRNA. Translation: CAA35246.1. Frameshift.
CCDSiCCDS38035.1.
PIRiS13800.
T42637.
RefSeqiNP_034253.3. NM_010123.3.
UniGeneiMm.2238.
Mm.482533.

3D structure databases

SMRiP23116. Positions 7-605.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi199415. 126 interactions.
IntActiP23116. 137 interactions.
MINTiMINT-1860578.
STRINGi10090.ENSMUSP00000025955.

PTM databases

iPTMnetiP23116.
PhosphoSiteiP23116.

Proteomic databases

EPDiP23116.
MaxQBiP23116.
PaxDbiP23116.
PeptideAtlasiP23116.
PRIDEiP23116.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000025955; ENSMUSP00000025955; ENSMUSG00000024991.
GeneIDi13669.
KEGGimmu:13669.
UCSCiuc008ibx.1. mouse.

Organism-specific databases

CTDi8661.
MGIiMGI:95301. Eif3a.

Phylogenomic databases

eggNOGiKOG2072. Eukaryota.
ENOG410XQ37. LUCA.
GeneTreeiENSGT00730000111063.
HOGENOMiHOG000246822.
HOVERGENiHBG006128.
InParanoidiP23116.
KOiK03254.
OMAiAREDSWG.
OrthoDBiEOG091G01VW.
TreeFamiTF101522.

Enzyme and pathway databases

ReactomeiR-MMU-156827. L13a-mediated translational silencing of Ceruloplasmin expression.
R-MMU-72649. Translation initiation complex formation.
R-MMU-72689. Formation of a pool of free 40S subunits.
R-MMU-72695. Formation of the ternary complex, and subsequently, the 43S complex.
R-MMU-72702. Ribosomal scanning and start codon recognition.
R-MMU-72706. GTP hydrolysis and joining of the 60S ribosomal subunit.

Miscellaneous databases

ChiTaRSiEif3a. mouse.
PROiP23116.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000024991.
GenevisibleiP23116. MM.

Family and domain databases

HAMAPiMF_03000. eIF3a. 1 hit.
InterProiIPR027512. EIF3A.
IPR000717. PCI_dom.
[Graphical view]
PfamiPF01399. PCI. 1 hit.
[Graphical view]
SMARTiSM00088. PINT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiEIF3A_MOUSE
AccessioniPrimary (citable) accession number: P23116
Secondary accession number(s): E9QQ50, Q60697, Q62162
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: July 27, 2011
Last modified: September 7, 2016
This is version 144 of the entry and version 5 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Translation initiation factors
    List of translation initiation factor entries
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.