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Protein

Eukaryotic translation initiation factor 3 subunit C-like protein

Gene

EIF3CL

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

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 (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

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 C-like protein
Gene namesi
Name:EIF3CL
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 16

Organism-specific databases

HGNCiHGNC:26347. EIF3CL.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162384693.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 914914Eukaryotic translation initiation factor 3 subunit C-like proteinPRO_0000422825Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei9 – 91PhosphoserineBy similarity
Modified residuei11 – 111PhosphoserineBy similarity
Modified residuei13 – 131PhosphoserineBy similarity
Modified residuei15 – 151PhosphoserineBy similarity
Modified residuei16 – 161PhosphoserineBy similarity
Modified residuei18 – 181PhosphoserineBy similarity
Modified residuei39 – 391PhosphoserineBy similarity
Modified residuei99 – 991N6-acetyllysineBy similarity
Modified residuei166 – 1661PhosphoserineBy similarity
Modified residuei178 – 1781PhosphoserineBy similarity
Modified residuei181 – 1811PhosphoserineBy similarity
Modified residuei182 – 1821PhosphoserineBy similarity
Modified residuei525 – 5251PhosphothreonineBy similarity
Modified residuei644 – 6441N6-acetyllysineBy similarity
Modified residuei910 – 9101PhosphoserineBy similarity

Post-translational modificationi

Phosphorylated. Phosphorylation is enhanced upon serum stimulation (By similarity).By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiB5ME19.
MaxQBiB5ME19.
PaxDbiB5ME19.
PRIDEiB5ME19.

PTM databases

iPTMnetiB5ME19.

Expressioni

Gene expression databases

GenevisibleiB5ME19. HS.

Organism-specific databases

HPAiHPA047097.
HPA049495.
HPA050112.

Interactioni

Subunit structurei

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 (By similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

BioGridi609110. 35 interactions.
IntActiB5ME19. 2 interactions.
STRINGi9606.ENSP00000370258.

Structurei

3D structure databases

ProteinModelPortaliB5ME19.
SMRiB5ME19. Positions 333-860.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini714 – 847134PCIBy similarityAdd
BLAST

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiKOG1076. Eukaryota.
ENOG410XRU3. LUCA.
GeneTreeiENSGT00390000017900.
HOGENOMiHOG000029414.
HOVERGENiHBG035174.
KOiK03252.
OMAiTEEICQI.
OrthoDBiEOG7DC23R.
PhylomeDBiB5ME19.
TreeFamiTF101520.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
HAMAPiMF_03002. eIF3c.
InterProiIPR027516. EIF3C.
IPR008905. EIF3C_N_dom.
IPR000717. PCI_dom.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF05470. eIF-3c_N. 1 hit.
PF01399. PCI. 1 hit.
[Graphical view]
SMARTiSM00088. PINT. 1 hit.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 1 hit.

Sequencei

Sequence statusi: Complete.

B5ME19-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSRFFTTGSD SESESSLSGE ELVTKPVGGN YGKQPLLLSE DEEDTKRVVR
60 70 80 90 100
SAKDKRFEEL TNLIRTIRNA MKIRDVTKCL EEFELLGKAY GKAKSIVDKE
110 120 130 140 150
GVPRFYIRIL ADLEDYLNEL WEDKEGKKKM NKNNAKALST LRQKIRKYNR
160 170 180 190 200
DFESHITSYK QNPEQSADED AEKNEEDSEG SSDEDEDEDG VSAATFLKKK
210 220 230 240 250
SEAPSGESRK FLKKMDDEDE DSEDSEDDED WDTGSTSSDS DSEEEEGKQT
260 270 280 290 300
ALASRFLKKA PTTDEDKKAA EKKREDKAKK KHDRKSKRLD EEEEEDNEGG
310 320 330 340 350
EWERVRGGVP LVKEKPKMFA KGTEITHAVV IKKLNEILQA RGKKGTDRAA
360 370 380 390 400
QIELLQLLVQ IAAENNLGEG VIVKIKFNII ASLYDYNPNL ATYMKPEMWG
410 420 430 440 450
KCLDCINELM DILFANPNIF VGENILEESE NLHNADQPLR VRGCILTLVE
460 470 480 490 500
RMDEEFTKIM QNTDPHSQEY VEHLKDEAQV CAIIERVQRY LEEKGTTEEV
510 520 530 540 550
CRIYLLRILH TYYKFDYKAH QRQLTPPEGS SKSEQDQAEN EGEDSAVLME
560 570 580 590 600
RLCKYIYAKD RTDRIRTCAI LCHIYHHALH SRWYQARDLM LMSHLQDNIQ
610 620 630 640 650
HADPPVQILY NRTMVQLGIC AFRQGLTKDA HNALLDIQSS GRAKELLGQG
660 670 680 690 700
LLLRSLQERN QEQEKVERRR QVPFHLHINL ELLECVYLVS AMLLEIPYMA
710 720 730 740 750
AHESDARRRM ISKQFHHQLR VGERQPLLGP PESMREHVVA ASKAMKMGDW
760 770 780 790 800
KTCHSFIINE KMNGKVWDLF PEADKVRTML VRKIQEESLR TYLFTYSSVY
810 820 830 840 850
DSISMETLSD MFELDLPTVH SIISKMIINE ELMASLDQPT QTVVMHRTEP
860 870 880 890 900
TAQQNLALQL AEKLGSLVEN NERVFDHKQG TYGGYFRDQK DGYRKNEGYM
910
RRGGYRQQQS QTAY
Length:914
Mass (Da):105,473
Last modified:October 14, 2008 - v1
Checksum:iD2B4DA4A546F7915
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC138894 Genomic DNA. No translation available.
CCDSiCCDS42136.1.
RefSeqiNP_001093131.1. NM_001099661.2.
NP_001304785.1. NM_001317856.1.
NP_001304786.1. NM_001317857.1.
UniGeneiHs.567374.

Genome annotation databases

EnsembliENST00000380876; ENSP00000370258; ENSG00000205609.
ENST00000398944; ENSP00000381917; ENSG00000205609.
GeneIDi728689.
KEGGihsa:728689.
UCSCiuc002dpi.6. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC138894 Genomic DNA. No translation available.
CCDSiCCDS42136.1.
RefSeqiNP_001093131.1. NM_001099661.2.
NP_001304785.1. NM_001317856.1.
NP_001304786.1. NM_001317857.1.
UniGeneiHs.567374.

3D structure databases

ProteinModelPortaliB5ME19.
SMRiB5ME19. Positions 333-860.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi609110. 35 interactions.
IntActiB5ME19. 2 interactions.
STRINGi9606.ENSP00000370258.

PTM databases

iPTMnetiB5ME19.

Proteomic databases

EPDiB5ME19.
MaxQBiB5ME19.
PaxDbiB5ME19.
PRIDEiB5ME19.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000380876; ENSP00000370258; ENSG00000205609.
ENST00000398944; ENSP00000381917; ENSG00000205609.
GeneIDi728689.
KEGGihsa:728689.
UCSCiuc002dpi.6. human.

Organism-specific databases

CTDi728689.
GeneCardsiEIF3CL.
HGNCiHGNC:26347. EIF3CL.
HPAiHPA047097.
HPA049495.
HPA050112.
neXtProtiNX_B5ME19.
PharmGKBiPA162384693.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1076. Eukaryota.
ENOG410XRU3. LUCA.
GeneTreeiENSGT00390000017900.
HOGENOMiHOG000029414.
HOVERGENiHBG035174.
KOiK03252.
OMAiTEEICQI.
OrthoDBiEOG7DC23R.
PhylomeDBiB5ME19.
TreeFamiTF101520.

Miscellaneous databases

ChiTaRSiEIF3CL. human.
GenomeRNAii728689.
NextBioi127990.
PROiB5ME19.

Gene expression databases

GenevisibleiB5ME19. HS.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
HAMAPiMF_03002. eIF3c.
InterProiIPR027516. EIF3C.
IPR008905. EIF3C_N_dom.
IPR000717. PCI_dom.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF05470. eIF-3c_N. 1 hit.
PF01399. PCI. 1 hit.
[Graphical view]
SMARTiSM00088. PINT. 1 hit.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "The sequence and analysis of duplication-rich human chromosome 16."
    Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.
    , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
    Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Entry informationi

Entry nameiEIFCL_HUMAN
AccessioniPrimary (citable) accession number: B5ME19
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 26, 2013
Last sequence update: October 14, 2008
Last modified: March 16, 2016
This is version 72 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, Reference proteome

Documents

  1. Human chromosome 16
    Human chromosome 16: entries, gene names and cross-references to MIM
  2. 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.