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P23116

- EIF3A_MOUSE

UniProt

P23116 - EIF3A_MOUSE

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Protein

Eukaryotic translation initiation factor 3 subunit A

Gene
Eif3a, Csma, Eif3, Eif3s10
Organism
Mus musculus (Mouse)
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.UniRule annotation

GO - Molecular functioni

  1. protein binding Source: UniProtKB
  2. translation initiation factor activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. formation of translation initiation complex Source: UniProtKB
  2. formation of translation preinitiation complex Source: UniProtKB-HAMAP
  3. regulation of translational initiation Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Initiation factor

Keywords - Biological processi

Protein biosynthesis

Names & Taxonomyi

Protein namesi
Recommended name:
Eukaryotic translation initiation factor 3 subunit A
Short name:
eIF3a
Alternative name(s):
Centrosomin
Eukaryotic translation initiation factor 3 subunit 10
eIF-3-theta
eIF3 p167
eIF3 p180
eIF3 p185
p162
Gene namesi
Name:Eif3a
Synonyms:Csma, Eif3, Eif3s10
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 19

Organism-specific databases

MGIiMGI:95301. Eif3a.

Subcellular locationi

Cytoplasm By similarity. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome. Nucleus
Note: Centrosomin-A is found in the centrosome. Centrosomin-B is found in the nucleus.1 Publication

GO - Cellular componenti

  1. eukaryotic 43S preinitiation complex Source: UniProtKB-HAMAP
  2. eukaryotic 48S preinitiation complex Source: UniProtKB-HAMAP
  3. eukaryotic translation initiation factor 3 complex Source: UniProtKB
  4. eukaryotic translation initiation factor 3 complex, eIF3m Source: MGI
  5. microtubule organizing center Source: UniProtKB-SubCell
  6. nucleolus Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By similarity
Chaini2 – 13441343Eukaryotic translation initiation factor 3 subunit AUniRule annotationPRO_0000123538Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei68 – 681N6-acetyllysine By similarity
Modified residuei492 – 4921Phosphoserine By similarity
Modified residuei1159 – 11591Phosphoserine By similarity
Modified residuei1300 – 13001Phosphoserine By similarity
Modified residuei1326 – 13261Phosphoserine By similarity

Post-translational modificationi

Phosphorylated. Phosphorylation is enhanced upon serum stimulation By similarity.UniRule annotation

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP23116.
PaxDbiP23116.
PRIDEiP23116.

PTM databases

PhosphoSiteiP23116.

Expressioni

Gene expression databases

ArrayExpressiP23116.
BgeeiP23116.
GenevestigatoriP23116.

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 PIWIL2.3 Publications

Protein-protein interaction databases

BioGridi199415. 21 interactions.
IntActiP23116. 33 interactions.
MINTiMINT-1860578.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini366 – 494129PCIAdd
BLAST
Repeati924 – 93181; truncatedUniRule annotation
Repeati932 – 941102UniRule annotation
Repeati942 – 951103; approximateUniRule annotation
Repeati953 – 962104UniRule annotation
Repeati963 – 972105UniRule annotation
Repeati973 – 982106UniRule annotation
Repeati983 – 992107UniRule annotation
Repeati993 – 1002108UniRule annotation
Repeati1003 – 1012109UniRule annotation
Repeati1013 – 10221010UniRule annotation
Repeati1023 – 10321011UniRule annotation
Repeati1033 – 10421012UniRule annotation
Repeati1043 – 10521013UniRule annotation
Repeati1054 – 10631014UniRule annotation
Repeati1064 – 10731015UniRule annotation
Repeati1074 – 10831016UniRule annotation
Repeati1084 – 10931017UniRule annotation
Repeati1094 – 11031018UniRule annotation
Repeati1104 – 11131019UniRule annotation
Repeati1114 – 11231020UniRule annotation
Repeati1124 – 11331021; approximateUniRule annotation

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni664 – 835172Interaction with EIF3B By similarityAdd
BLAST
Regioni924 – 113321021 X 10 AA approximate tandem repeats of [DA]-[DE]-[ED]-R-[PLIGFSV]-[RPS]-[RW]-[RL]-[GNIHT]-[DGLPTAM]UniRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili82 – 12039 Reviewed predictionAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi576 – 875300Glu-richUniRule annotationAdd
BLAST
Compositional biasi924 – 1258335Asp-richUniRule annotationAdd
BLAST

Sequence similaritiesi

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

Keywords - Domaini

Coiled coil, Repeat

Phylogenomic databases

eggNOGiNOG236708.
GeneTreeiENSGT00730000111063.
HOGENOMiHOG000246822.
HOVERGENiHBG006128.
InParanoidiP23116.
KOiK03254.
OMAiRGPWRNT.
OrthoDBiEOG7BGHKJ.
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]

Sequencei

Sequence statusi: Complete.

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

P23116-1 [UniParc]FASTAAdd to Basket

« Hide

MPAYFQRPEN ALKRANEFLE VGKKQPALDV LYDVMKSKKH RTWQKIHEPI     50
MLKYLELCVD LRKSHLAKEG LYQYKNICQQ VNIKSLEDVV RAYLKLAEEK 100
TEAAKEESQQ MVLDIEDLDN IQTPESVLLS AVSGEDTQDR TDRLLLTPWV 150
KFLWESYRQC LDLLRNNSRV ERLYHDIAQQ AFKFCLQYTR KAEFRKLCDN 200
LRMHLSQIQR HHNQSTAINL NNPESQSMHL ETRLVQLDSA ISMELWQEAF 250
KAVEDIHGLF SLSKKPPKPQ LMANYYNKVS TVFWKSGNAL FHASTLHRLY 300
HLSREMRKNL TQEEMQRMST RVLLATLSIP ITPERTDIAR LLDMDGIIVE 350
KQRRLATLLG LQAPPTRIGL INDMVRFSVL QYVVPEVKDL YNWLEVEFNP 400
LKLCERVTKV LNWVREQPEK EPELQQYVPQ LQNNTILRLL QQVAQIYQSI 450
EFSRLTSLVP FVDAFQLERA IVDAARHCDL QVRIDHTSRT LSFGSDLNYA 500
TREDAPVGPH LQSMPSEQIR NQLTAMSSVL AKALEVIRPA HILQEKEEQH 550
QLAVNAYLKN SRKEHQRILA RRQTIEERKE RLESLNIQRE KEELEQREAE 600
LQKVRKAEEE RLRQEAKERE KERILQEHEQ IKKKTVRERL EQIKKTELGA 650
KAFKDIDIED LEELDPDFIM AKQVEQLEKE KKELQERLKN QEKKIDYFER 700
AKRLEEIPLI KSAYEEQRVK DMDLWEQQEE ERITTMQLER EKALEHKNRM 750
SRMLEDRDLF VMRLKAARQS VYEEKLKQFE ERLAEERHSR LEDRKRQRKE 800
ERKITYYREK EEEEQRRAEE QMLKEREERE RAERAKREEE LREYQERVKK 850
LEEVERKKRQ RELEIEERER RREEERRLGD DPLSRKDSRW GDRDSEGTWR 900
KGPEADSEWR RGPPEKEWRR ETRDDERPHR RDEDRLRRLG GDDEERESSL 950
RPDDDRIPRR GLDDDRGPRR GPDEDRFSRR GTDDDRPSWR NADDDRPPRR 1000
IGDDDRGSWR HTDDDRPPRR GLDDERGSWR TADEDRGPRR GMDDDRGPRR 1050
GGADDERSSW RNADDDRGPR RGMDDDRGPR RGLDDDRGPW RNAAEDRISR 1100
RGADDDRGPW RNMDDDRVPR RGDDARPGPW RPFVKPGGWR EKEKAREESW 1150
GPPRESRPSE EREWDRDKEK DRDNQDREEN DKDLERDRDR ERDGDREDRF 1200
RRPRDEGGWR RGPAEESSSW RDSSRRDDRD REDRRRDRDD RRDLRDLRDR 1250
RDLRDDRDRR GPPLRSEREE ASSWRRTDDR KDDRTEERDP PRRVPPPALS 1300
RDRERERERE GEKEKASWRA EKDRESLRRT KNETDEDGWT TVRR 1344
Length:1,344
Mass (Da):161,936
Last modified:July 27, 2011 - v5
Checksum:i215F5CCB8A2C7296
GO

Sequence cautioni

The sequence CAA35246.1 differs from that shown. Reason: Frameshift at positions 421, 468, 613, 648 and 787.
The sequence CAA59144.1 differs from that shown. Reason: Frameshift at positions 421, 468, 613, 648, 962 and 1059.

RNA editingi

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 conflict

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

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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.
CCDSi CCDS38035.1.
PIRi S13800.
T42637.
RefSeqi NP_034253.3. NM_010123.3.
UniGenei Mm.2238.
Mm.482533.

3D structure databases

ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 199415. 21 interactions.
IntActi P23116. 33 interactions.
MINTi MINT-1860578.

PTM databases

PhosphoSitei P23116.

Proteomic databases

MaxQBi P23116.
PaxDbi P23116.
PRIDEi P23116.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000025955 ; ENSMUSP00000025955 ; ENSMUSG00000024991 .
GeneIDi 13669.
KEGGi mmu:13669.
UCSCi uc008ibx.1. mouse.

Organism-specific databases

CTDi 8661.
MGIi MGI:95301. Eif3a.

Phylogenomic databases

eggNOGi NOG236708.
GeneTreei ENSGT00730000111063.
HOGENOMi HOG000246822.
HOVERGENi HBG006128.
InParanoidi P23116.
KOi K03254.
OMAi RGPWRNT.
OrthoDBi EOG7BGHKJ.
TreeFami TF101522.

Miscellaneous databases

ChiTaRSi EIF3A. mouse.
NextBioi 284428.
PROi P23116.
SOURCEi Search...

Gene expression databases

ArrayExpressi P23116.
Bgeei P23116.
Genevestigatori P23116.

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. "Molecular cloning and characterization of the 162 kDa component of a multi-protein complex phosphorylated by Src."
    Fisher R., Fillmore H., Reynolds A.B.
    Submitted (SEP-1994) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Lymphoma.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. "The centrosomal protein centrosomin A and the nuclear protein centrosomin B derive from one gene by post-transcriptional processes involving RNA editing."
    Petzelt C., Joswig G., Mincheva A., Lichter P., Stammer H., Werner D.
    J. Cell Sci. 110:2573-2578(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 401-1142 (CENTROSOMIN B), SUBCELLULAR LOCATION, RNA EDITING.
    Tissue: Ehrlich ascites tumor cell.
  4. "Murine cDNAs coding for the centrosomal antigen centrosomin A."
    Joswig G., Petzelt C., Werner D.
    J. Cell Sci. 98:37-43(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 514-790 (CENTROSOMIN A).
    Tissue: Ehrlich ascites tumor cell.
  5. Joswig G., Petzelt C., Werner D.
    Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION.
  6. "mTOR-dependent stimulation of the association of eIF4G and eIF3 by insulin."
    Harris T.E., Chi A., Shabanowitz J., Hunt D.F., Rhoads R.E., Lawrence J.C. Jr.
    EMBO J. 25:1659-1668(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH EIF3B AND EIF4G1.
  7. "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, IDENTIFICATION IN THE EIF-3 COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
  8. "MILI, a PIWI-interacting RNA-binding protein, is required for germ Line stem cell self-renewal and appears to positively regulate translation."
    Unhavaithaya Y., Hao Y., Beyret E., Yin H., Kuramochi-Miyagawa S., Nakano T., Lin H.
    J. Biol. Chem. 284:6507-6519(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PIWIL2.

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: July 9, 2014
This is version 125 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

External Data

Dasty 3

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