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F5H335 (F5H335_HUMAN) Unreviewed, UniProtKB/TrEMBL

Last modified July 9, 2014. Version 26. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order

Names and origin

Protein namesRecommended name:
Eukaryotic translation initiation factor 3 subunit A HAMAP-Rule MF_03000

Short name=eIF3a HAMAP-Rule MF_03000
Alternative name(s):
Eukaryotic translation initiation factor 3 subunit 10 HAMAP-Rule MF_03000
eIF-3-theta HAMAP-Rule MF_03000
Gene names
Name:EIF3A HAMAP-Rule MF_03000 Ensembl ENSP00000438178
Synonyms:EIF3S10 HAMAP-Rule MF_03000
OrganismHomo sapiens (Human) [Reference proteome] Ensembl ENSP00000438178
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1348 AA.
Sequence statusComplete.
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 By similarity. HAMAP-Rule MF_03000

Subunit structure

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. Interacts with EIF4G1. Also interacts with KRT7 and PIWIL2 By similarity. HAMAP-Rule MF_03000

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_03000.

Post-translational modification

Phosphorylated. Phosphorylation is enhanced upon serum stimulation By similarity. HAMAP-Rule MF_03000

Sequence similarities

Belongs to the eIF-3 subunit A family. HAMAP-Rule MF_03000

Contains 1 PCI domain. HAMAP-Rule MF_03000

Contains PCI domain. SAAS SAAS027512

Caution

The sequence shown here is derived from an Ensembl automatic analysis pipeline and should be considered as preliminary data. Ensembl ENSP00000438178

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Domain332 – 460129PCI By similarity HAMAP-Rule MF_03000
Region630 – 801172Interaction with EIF3B By similarity HAMAP-Rule MF_03000
Coiled coil48 – 8639 By similarity HAMAP-Rule MF_03000
Coiled coil524 – 60582 By similarity HAMAP-Rule MF_03000
Coiled coil633 – 844212 By similarity HAMAP-Rule MF_03000

Amino acid modifications

Modified residue8471Phosphoserine By similarity HAMAP-Rule MF_03000
Modified residue11641Phosphoserine By similarity HAMAP-Rule MF_03000
Modified residue13021Phosphoserine By similarity HAMAP-Rule MF_03000
Modified residue13301Phosphoserine By similarity HAMAP-Rule MF_03000

Sequences

Sequence LengthMass (Da)Tools
F5H335 [UniParc].

Last modified June 28, 2011. Version 1.
Checksum: 97F42E357D8B5405

FASTA1,348162,636
        10         20         30         40         50         60 
MKSKKHRTWQ KIHEPIMLKY LELCVDLRKS HLAKEGLYQY KNICQQVNIK SLEDVVRAYL 

        70         80         90        100        110        120 
KMAEEKTEAA KEESQQMVLD IEDLDNIQTP ESVLLSAVSG EDTQDRTDRL LLTPWVKFLW 

       130        140        150        160        170        180 
ESYRQCLDLL RNNSRVERLY HDIAQQAFKF CLQYTRKAEF RKLCDNLRMH LSQIQRHHNQ 

       190        200        210        220        230        240 
STAINLNNPE SQSMHLETRL VQLDSAISME LWQEAFKAVE DIHGLFSLSK KPPKPQLMAN 

       250        260        270        280        290        300 
YYNKVSTVFW KSGNALFHAS TLHRLYHLSR EMRKNLTQDE MQRMSTRVLL ATLSIPITPE 

       310        320        330        340        350        360 
RTDIARLLDM DGIIVEKQRR LATLLGLQAP PTRIGLINDM VRFNVLQYVV PEVKDLYNWL 

       370        380        390        400        410        420 
EVEFNPLKLC ERVTKVLNWV REQPEKEPEL QQYVPQLQNN TILRLLQQVS QIYQSIEFSR 

       430        440        450        460        470        480 
LTSLVPFVDA FQLERAIVDA ARHCDLQVRI DHTSRTLSFG SDLNYATRED APIGPHLQSM 

       490        500        510        520        530        540 
PSEQIRNQLT AMSSVLAKAL EVIKPAHILQ EKEEQHQLAV TAYLKNSRKE HQRILARRQT 

       550        560        570        580        590        600 
IEERKERLES LNIQREKEEL EQREAELQKV RKAEEERLRQ EAKEREKERI LQEHEQIKKK 

       610        620        630        640        650        660 
TVRERLEQIK KTELGAKAFK DIDIEDLEEL DPDFIMAKQV EQLEKEKKEL QERLKNQEKK 

       670        680        690        700        710        720 
IDYFERAKRL EEIPLIKSAY EEQRIKDMDL WEQQEEERIT TMQLEREKAL EHKNRMSRML 

       730        740        750        760        770        780 
EDRDLFVMRL KAARQSVYEE KLKQFEERLA EERHNRLEER KRQRKEERRI TYYREKEEEE 

       790        800        810        820        830        840 
QRRAEEQMLK EREERERAER AKREEELREY QERVKKLEEV ERKKRQRELE IEERERRREE 

       850        860        870        880        890        900 
ERRLGDSSLS RKDSRWGDRD SEGTWRKGPE ADSEWRRGPP EKEWRRGEGR DEDRSHRRDE 

       910        920        930        940        950        960 
ERPRRLGDDE DREPSLRPDD DRVPRRGMDD DRGPRRGPEE DRFSRRGADD DRPSWRNTDD 

       970        980        990       1000       1010       1020 
DRPPRRIADE DRGNWRHADD DRPPRRGLDE DRGSWRTADE DRGPRRGMDD DRGPRRGGAD 

      1030       1040       1050       1060       1070       1080 
DERSSWRNAD DDRGPRRGLD DDRGPRRGMD DDRGPRRGMD DDRGPRRGMD DDRGPRRGLD 

      1090       1100       1110       1120       1130       1140 
DDRGPWRNAD DDRIPRRGAE DDRGPWRNMD DDRLSRRADD DRFPRRGDDS RPGPWRPLVK 

      1150       1160       1170       1180       1190       1200 
PGGWREKEKA REESWGPPRE SRPSEEREWD REKERDRDNQ DREENDKDPE RERDRERDVD 

      1210       1220       1230       1240       1250       1260 
REDRFRRPRD EGGWRRGPAE ESSSWRDSSR RDDRDRDDRR RERDDRRDLR ERRDLRDDRD 

      1270       1280       1290       1300       1310       1320 
RRGPPLRSER EEVSSWRRAD DRKDDRVEER DPPRRVPPPA LSRDRERDRD REREGEKEKA 

      1330       1340 
SWRAEKDRES LRRTKNETDE DGWTTVRR 

« Hide

References

« Hide 'large scale' references
[1]"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., 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].
[2]"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].
[3]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[4]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[5]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[6]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Burckstummer 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].
[7]Ensembl
Submitted (JUL-2011) to UniProtKB
Cited for: IDENTIFICATION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL355598 Genomic DNA. No translation available.

3D structure databases

ProteinModelPortalF5H335.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000541549; ENSP00000438178; ENSG00000107581.
KEGGhsa:8661.

Organism-specific databases

HGNCHGNC:3271. EIF3A.
GenAtlasSearch...

Gene expression databases

ArrayExpressF5H335.
BgeeF5H335.

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.
GenomeRNAi8661.
NextBio35508544.

Entry information

Entry nameF5H335_HUMAN
AccessionPrimary (citable) accession number: F5H335
Entry history
Integrated into UniProtKB/TrEMBL: June 28, 2011
Last sequence update: June 28, 2011
Last modified: July 9, 2014
This is version 26 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
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.