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Q99613 (EIF3C_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 152. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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 C

Short name=eIF3c
Alternative name(s):
Eukaryotic translation initiation factor 3 subunit 8
eIF3 p110
Gene names
Name:EIF3C
Synonyms:EIF3S8
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length913 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. HAMAP-Rule MF_03002

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, EIF3K and EIF3L. 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. Identified in a HCV IRES-mediated translation complex, at least composed of EIF3C, IGF2BP1, RPS3 and HCV RNA-replicon. Interacts with ALKBH4, IFIT1 and IFIT2. Ref.7 Ref.8 Ref.10 Ref.11 Ref.12 Ref.14 Ref.15 Ref.16 Ref.17 Ref.19

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_03002.

Post-translational modification

Phosphorylated. Phosphorylation is enhanced upon serum stimulation. Ref.15

Sequence similarities

Belongs to the eIF-3 subunit C family.

Contains 1 PCI domain.

Mass spectrometry

Molecular mass is 106143.8 Da from positions 1 - 913. Ref.15

Molecular mass is 106855±40 Da from positions 1 - 913. Determined by MALDI. Ref.16

Binary interactions

With

Entry

#Exp.

IntAct

Notes

DDX3XO005713EBI-353741,EBI-353779
ORFQ9Q2G45EBI-353741,EBI-6248094From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 913913Eukaryotic translation initiation factor 3 subunit C HAMAP-Rule MF_03002
PRO_0000123525

Regions

Domain712 – 846135PCI
Compositional bias164 – 18926Asp/Glu-rich (acidic) HAMAP-Rule MF_03002
Compositional bias243 – 2464Poly-Glu HAMAP-Rule MF_03002
Compositional bias291 – 2944Poly-Glu HAMAP-Rule MF_03002

Amino acid modifications

Modified residue91Phosphoserine Ref.15
Modified residue111Phosphoserine Ref.15
Modified residue131Phosphoserine Ref.15
Modified residue151Phosphoserine Ref.15
Modified residue161Phosphoserine Ref.15
Modified residue181Phosphoserine Ref.15
Modified residue391Phosphoserine Ref.15
Modified residue991N6-acetyllysine By similarity
Modified residue1661Phosphoserine Ref.15
Modified residue5241Phosphothreonine Ref.15
Modified residue6431N6-acetyllysine By similarity
Modified residue9091Phosphoserine Ref.15

Experimental info

Sequence conflict313 – 3142EK → VR in AAC27674. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q99613 [UniParc].

Last modified May 1, 1997. Version 1.
Checksum: CE5029F4EB51C1AA

FASTA913105,344
        10         20         30         40         50         60 
MSRFFTTGSD SESESSLSGE ELVTKPVGGN YGKQPLLLSE DEEDTKRVVR SAKDKRFEEL 

        70         80         90        100        110        120 
TNLIRTIRNA MKIRDVTKCL EEFELLGKAY GKAKSIVDKE GVPRFYIRIL ADLEDYLNEL 

       130        140        150        160        170        180 
WEDKEGKKKM NKNNAKALST LRQKIRKYNR DFESHITSYK QNPEQSADED AEKNEEDSEG 

       190        200        210        220        230        240 
SSDEDEDEDG VSAATFLKKK SEAPSGESRK FLKKMDDEDE DSEDSEDDED WDTGSTSSDS 

       250        260        270        280        290        300 
DSEEEEGKQT ALASRFLKKA PTTDEDKKAA EKKREDKAKK KHDRKSKRLD EEEEDNEGGE 

       310        320        330        340        350        360 
WERVRGGVPL VKEKPKMFAK GTEITHAVVI KKLNEILQAR GKKGTDRAAQ IELLQLLVQI 

       370        380        390        400        410        420 
AAENNLGEGV IVKIKFNIIA SLYDYNPNLA TYMKPEMWGK CLDCINELMD ILFANPNIFV 

       430        440        450        460        470        480 
GENILEESEN LHNADQPLRV RGCILTLVER MDEEFTKIMQ NTDPHSQEYV EHLKDEAQVC 

       490        500        510        520        530        540 
AIIERVQRYL EEKGTTEEVC RIYLLRILHT YYKFDYKAHQ RQLTPPEGSS KSEQDQAENE 

       550        560        570        580        590        600 
GEDSAVLMER LCKYIYAKDR TDRIRTCAIL CHIYHHALHS RWYQARDLML MSHLQDNIQH 

       610        620        630        640        650        660 
ADPPVQILYN RTMVQLGICA FRQGLTKDAH NALLDIQSSG RAKELLGQGL LLRSLQERNQ 

       670        680        690        700        710        720 
EQEKVERRRQ VPFHLHINLE LLECVYLVSA MLLEIPYMAA HESDARRRMI SKQFHHQLRV 

       730        740        750        760        770        780 
GERQPLLGPP ESMREHVVAA SKAMKMGDWK TCHSFIINEK MNGKVWDLFP EADKVRTMLV 

       790        800        810        820        830        840 
RKIQEESLRT YLFTYSSVYD SISMETLSDM FELDLPTVHS IISKMIINEE LMASLDQPTQ 

       850        860        870        880        890        900 
TVVMHRTEPT AQQNLALQLA EKLGSLVENN ERVFDHKQGT YGGYFRDQKD GYRKNEGYMR 

       910 
RGGYRQQQSQ TAY 

« Hide

References

« Hide 'large scale' references
[1]"Conservation and diversity of eukaryotic translation initiation factor eIF3."
Asano K., Kinzy T.G., Merrick W.C., Hershey J.W.B.
J. Biol. Chem. 272:1101-1109(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Genome duplications and other features in 12 Mb of DNA sequence from human chromosome 16p and 16q."
Loftus B.J., Kim U.-J., Sneddon V.P., Kalush F., Brandon R., Fuhrmann J., Mason T., Crosby M.L., Barnstead M., Cronin L., Mays A.D., Cao Y., Xu R.X., Kang H.-L., Mitchell S., Eichler E.E., Harris P.C., Venter J.C., Adams M.D.
Genomics 60:295-308(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"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. expand/collapse author list , 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].
Tissue: Synovium.
[4]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 (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain, Lymph and Placenta.
[6]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 589-913.
[7]"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.
[8]"mTOR and S6K1 mediate assembly of the translation preinitiation complex through dynamic protein interchange and ordered phosphorylation events."
Holz M.K., Ballif B.A., Gygi S.P., Blenis J.
Cell 123:569-580(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MTOR; RPTOR AND RPS6KB1.
[9]"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.
[10]"Induction and mode of action of the viral stress-inducible murine proteins, P56 and P54."
Terenzi F., Pal S., Sen G.C.
Virology 340:116-124(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH IFIT1 AND IFIT2.
[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]"Distinct induction patterns and functions of two closely related interferon-inducible human genes, ISG54 and ISG56."
Terenzi F., Hui D.J., Merrick W.C., Sen G.C.
J. Biol. Chem. 281:34064-34071(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH IFIT2.
[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, PHOSPHORYLATION AT SER-9; SER-11; SER-13; SER-15; SER-16; SER-18; SER-39; SER-166; THR-524 AND SER-909, MASS SPECTROMETRY.
[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, MASS SPECTROMETRY.
[17]"IGF2BP1 enhances HCV IRES-mediated translation initiation via the 3'UTR."
Weinlich S., Huettelmaier S., Schierhorn A., Behrens S.-E., Ostareck-Lederer A., Ostareck D.H.
RNA 15:1528-1542(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A HCV IRES-MEDIATED TRANSLATION COMPLEX.
[18]"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].
[19]"Human ALKBH4 interacts with proteins associated with transcription."
Bjornstad L.G., Meza T.J., Otterlei M., Olafsrud S.M., Meza-Zepeda L.A., Falnes P.O.
PLoS ONE 7:E49045-E49045(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ALKBH4.
[20]"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
U46025 Genomic DNA. Translation: AAD03462.1.
AC002544 Genomic DNA. Translation: AAC27426.1.
U91326 Genomic DNA. Translation: AAC27674.1.
AK000739 mRNA. Translation: BAA91352.1.
AK292155 mRNA. Translation: BAF84844.1.
BC000533 mRNA. Translation: AAH00533.1.
BC001571 mRNA. Translation: AAH01571.1.
BC071705 mRNA. Translation: AAH71705.1.
BC157842 mRNA. Translation: AAI57843.1.
BC157849 mRNA. Translation: AAI57850.1.
CH878380 Genomic DNA. Translation: EAW50492.1.
BT007335 mRNA. Translation: AAP35999.1.
CCDSCCDS10638.1.
RefSeqNP_001032897.1. NM_001037808.2.
NP_001186071.1. NM_001199142.1.
NP_001254503.1. NM_001267574.2.
NP_001273407.1. NM_001286478.1.
NP_003743.1. NM_003752.4.
UniGeneHs.567374.

3D structure databases

ProteinModelPortalQ99613.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114212. 71 interactions.
DIPDIP-32865N.
IntActQ99613. 23 interactions.
MINTMINT-5000313.
STRING9606.ENSP00000332604.

PTM databases

PhosphoSiteQ99613.

Polymorphism databases

DMDM6685539.

Proteomic databases

MaxQBQ99613.
PaxDbQ99613.
PeptideAtlasQ99613.
PRIDEQ99613.

Protocols and materials databases

DNASU8663.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000331666; ENSP00000332604; ENSG00000184110.
ENST00000395587; ENSP00000378953; ENSG00000184110.
ENST00000566501; ENSP00000457963; ENSG00000184110.
ENST00000566866; ENSP00000457418; ENSG00000184110.
GeneID8663.
KEGGhsa:8663.
UCSCuc002dpg.5. human.

Organism-specific databases

CTD8663.
GeneCardsGC16P028700.
H-InvDBHIX0038592.
HGNCHGNC:3279. EIF3C.
HPACAB034045.
MIM603916. gene.
neXtProtNX_Q99613.
PharmGKBPA162384646.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG305883.
HOGENOMHOG000029414.
HOVERGENHBG035174.
InParanoidQ99613.
KOK03252.
OMAENLHNVD.
OrthoDBEOG7DC23R.
PhylomeDBQ99613.
TreeFamTF101520.

Enzyme and pathway databases

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

Gene expression databases

ArrayExpressQ99613.
BgeeQ99613.
CleanExHS_EIF3C.
HS_EIF3CL.
GenevestigatorQ99613.

Family and domain databases

Gene3D1.10.10.10. 1 hit.
HAMAPMF_03002. eIF3c.
InterProIPR027516. EIF3C.
IPR008905. EIF3C_N_dom.
IPR000717. PCI_dom.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamPF05470. eIF-3c_N. 2 hits.
PF01399. PCI. 1 hit.
[Graphical view]
SMARTSM00088. PINT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSEIF3CL. human.
GeneWikiEIF3C.
GenomeRNAi8663.
NextBio32493.
PROQ99613.
SOURCESearch...

Entry information

Entry nameEIF3C_HUMAN
AccessionPrimary (citable) accession number: Q99613
Secondary accession number(s): A8K7Z0 expand/collapse secondary AC list , B2RXG3, O00215, Q9BW98
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 1, 1997
Last modified: July 9, 2014
This is version 152 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 chromosome 16

Human chromosome 16: entries, gene names and cross-references to MIM