位置:首页 > 蛋白库 > EIFCL_HUMAN
EIFCL_HUMAN
ID   EIFCL_HUMAN             Reviewed;         914 AA.
AC   B5ME19;
DT   26-JUN-2013, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2008, sequence version 1.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=Eukaryotic translation initiation factor 3 subunit C-like protein;
GN   Name=EIF3CL;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15616553; DOI=10.1038/nature03187;
RA   Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA   Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA   Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA   Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA   Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA   Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA   Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA   Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA   Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA   Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA   Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA   Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA   Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA   Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA   Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA   Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA   Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA   Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA   Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA   DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA   Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA   Myers R.M., Rubin E.M., Pennacchio L.A.;
RT   "The sequence and analysis of duplication-rich human chromosome 16.";
RL   Nature 432:988-994(2004).
CC   -!- FUNCTION: Component of the eukaryotic translation initiation factor 3
CC       (eIF-3) complex, which is required for several steps in the initiation
CC       of protein synthesis. The eIF-3 complex associates with the 40S
CC       ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-
CC       2:GTP:methionyl-tRNAi and eIF-5 to form the 43S pre-initiation complex
CC       (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC
CC       and scanning of the mRNA for AUG recognition. The eIF-3 complex is also
CC       required for disassembly and recycling of post-termination ribosomal
CC       complexes and subsequently prevents premature joining of the 40S and
CC       60S ribosomal subunits prior to initiation. The eIF-3 complex
CC       specifically targets and initiates translation of a subset of mRNAs
CC       involved in cell proliferation, including cell cycling, differentiation
CC       and apoptosis, and uses different modes of RNA stem-loop binding to
CC       exert either translational activation or repression.
CC       {ECO:0000250|UniProtKB:Q99613}.
CC   -!- SUBUNIT: Component of the eukaryotic translation initiation factor 3
CC       (eIF-3) complex, which is composed of 13 subunits: EIF3A, EIF3B, EIF3C,
CC       EIF3D, EIF3E, EIF3F, EIF3G, EIF3H, EIF3I, EIF3J, EIF3K, EIF3L and
CC       EIF3M. The eIF-3 complex appears to include 3 stable modules: module A
CC       is composed of EIF3A, EIF3B, EIF3G and EIF3I; module B is composed of
CC       EIF3F, EIF3H, and EIF3M; and module C is composed of EIF3C, EIF3D,
CC       EIF3E, EIF3K and EIF3L. EIF3C of module C binds EIF3B of module A and
CC       EIF3H of module B, thereby linking the three modules. EIF3J is a labile
CC       subunit that binds to the eIF-3 complex via EIF3B. The eIF-3 complex
CC       interacts with RPS6KB1 under conditions of nutrient depletion.
CC       Mitogenic stimulation leads to binding and activation of a complex
CC       composed of MTOR and RPTOR, leading to phosphorylation and release of
CC       RPS6KB1 and binding of EIF4B to eIF-3 (By similarity).
CC       {ECO:0000250|UniProtKB:Q99613}.
CC   -!- INTERACTION:
CC       B5ME19; O15372: EIF3H; NbExp=2; IntAct=EBI-8456517, EBI-709735;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q99613}.
CC   -!- PTM: Phosphorylated. Phosphorylation is enhanced upon serum stimulation
CC       (By similarity). {ECO:0000250|UniProtKB:Q99613}.
CC   -!- SIMILARITY: Belongs to the eIF-3 subunit C family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AC138894; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   CCDS; CCDS42136.1; -.
DR   RefSeq; NP_001093131.1; NM_001099661.2.
DR   RefSeq; NP_001304785.1; NM_001317856.1.
DR   RefSeq; NP_001304786.1; NM_001317857.1.
DR   AlphaFoldDB; B5ME19; -.
DR   SMR; B5ME19; -.
DR   BioGRID; 609110; 63.
DR   IntAct; B5ME19; 15.
DR   MINT; B5ME19; -.
DR   STRING; 9606.ENSP00000370258; -.
DR   GlyGen; B5ME19; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; B5ME19; -.
DR   MetOSite; B5ME19; -.
DR   PhosphoSitePlus; B5ME19; -.
DR   SwissPalm; B5ME19; -.
DR   BioMuta; EIF3CL; -.
DR   jPOST; B5ME19; -.
DR   MassIVE; B5ME19; -.
DR   MaxQB; B5ME19; -.
DR   PaxDb; B5ME19; -.
DR   PeptideAtlas; B5ME19; -.
DR   PRIDE; B5ME19; -.
DR   ProteomicsDB; 6205; -.
DR   Antibodypedia; 67070; 13 antibodies from 4 providers.
DR   DNASU; 728689; -.
DR   Ensembl; ENST00000380876.5; ENSP00000370258.5; ENSG00000205609.13.
DR   Ensembl; ENST00000398944.7; ENSP00000381917.3; ENSG00000205609.13.
DR   GeneID; 728689; -.
DR   KEGG; hsa:728689; -.
DR   MANE-Select; ENST00000380876.5; ENSP00000370258.5; NM_001317857.2; NP_001304786.1.
DR   UCSC; uc002dpi.6; human.
DR   CTD; 728689; -.
DR   GeneCards; EIF3CL; -.
DR   HGNC; HGNC:26347; EIF3CL.
DR   HPA; ENSG00000205609; Low tissue specificity.
DR   neXtProt; NX_B5ME19; -.
DR   OpenTargets; ENSG00000205609; -.
DR   PharmGKB; PA162384693; -.
DR   VEuPathDB; HostDB:ENSG00000205609; -.
DR   eggNOG; KOG1076; Eukaryota.
DR   GeneTree; ENSGT00390000017900; -.
DR   HOGENOM; CLU_004304_0_0_1; -.
DR   OMA; VSRTHSI; -.
DR   OrthoDB; 273138at2759; -.
DR   PhylomeDB; B5ME19; -.
DR   TreeFam; TF101520; -.
DR   PathwayCommons; B5ME19; -.
DR   SignaLink; B5ME19; -.
DR   BioGRID-ORCS; 728689; 675 hits in 972 CRISPR screens.
DR   ChiTaRS; EIF3CL; human.
DR   GenomeRNAi; 728689; -.
DR   Pharos; B5ME19; Tdark.
DR   PRO; PR:B5ME19; -.
DR   Proteomes; UP000005640; Chromosome 16.
DR   RNAct; B5ME19; protein.
DR   Bgee; ENSG00000205609; Expressed in apex of heart and 95 other tissues.
DR   Genevisible; B5ME19; HS.
DR   GO; GO:0016282; C:eukaryotic 43S preinitiation complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0033290; C:eukaryotic 48S preinitiation complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0005852; C:eukaryotic translation initiation factor 3 complex; IBA:GO_Central.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0031369; F:translation initiation factor binding; IBA:GO_Central.
DR   GO; GO:0001732; P:formation of cytoplasmic translation initiation complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0006413; P:translational initiation; IBA:GO_Central.
DR   Gene3D; 1.10.10.10; -; 1.
DR   HAMAP; MF_03002; eIF3c; 1.
DR   InterPro; IPR027516; EIF3C.
DR   InterPro; IPR008905; EIF3C_N_dom.
DR   InterPro; IPR000717; PCI_dom.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR13937; PTHR13937; 1.
DR   Pfam; PF05470; eIF-3c_N; 1.
DR   Pfam; PF01399; PCI; 1.
DR   SMART; SM00088; PINT; 1.
DR   SUPFAM; SSF46785; SSF46785; 1.
DR   PROSITE; PS50250; PCI; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Cytoplasm; Initiation factor; Phosphoprotein;
KW   Protein biosynthesis; Reference proteome.
FT   CHAIN           1..914
FT                   /note="Eukaryotic translation initiation factor 3 subunit
FT                   C-like protein"
FT                   /id="PRO_0000422825"
FT   DOMAIN          674..850
FT                   /note="PCI"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT   REGION          1..44
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          157..302
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          523..543
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          886..914
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..20
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        169..190
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        202..217
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        218..240
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        259..277
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         9
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q99613"
FT   MOD_RES         11
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q99613"
FT   MOD_RES         13
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q99613"
FT   MOD_RES         15
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q99613"
FT   MOD_RES         16
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q99613"
FT   MOD_RES         18
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q99613"
FT   MOD_RES         39
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q99613"
FT   MOD_RES         99
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8R1B4"
FT   MOD_RES         166
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q99613"
FT   MOD_RES         178
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8R1B4"
FT   MOD_RES         181
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8R1B4"
FT   MOD_RES         182
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8R1B4"
FT   MOD_RES         525
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q99613"
FT   MOD_RES         644
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8R1B4"
FT   MOD_RES         910
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q99613"
SQ   SEQUENCE   914 AA;  105473 MW;  D2B4DA4A546F7915 CRC64;
     MSRFFTTGSD SESESSLSGE ELVTKPVGGN YGKQPLLLSE DEEDTKRVVR SAKDKRFEEL
     TNLIRTIRNA MKIRDVTKCL EEFELLGKAY GKAKSIVDKE GVPRFYIRIL ADLEDYLNEL
     WEDKEGKKKM NKNNAKALST LRQKIRKYNR DFESHITSYK QNPEQSADED AEKNEEDSEG
     SSDEDEDEDG VSAATFLKKK SEAPSGESRK FLKKMDDEDE DSEDSEDDED WDTGSTSSDS
     DSEEEEGKQT ALASRFLKKA PTTDEDKKAA EKKREDKAKK KHDRKSKRLD EEEEEDNEGG
     EWERVRGGVP LVKEKPKMFA KGTEITHAVV IKKLNEILQA RGKKGTDRAA QIELLQLLVQ
     IAAENNLGEG VIVKIKFNII ASLYDYNPNL ATYMKPEMWG KCLDCINELM DILFANPNIF
     VGENILEESE NLHNADQPLR VRGCILTLVE RMDEEFTKIM QNTDPHSQEY VEHLKDEAQV
     CAIIERVQRY LEEKGTTEEV CRIYLLRILH TYYKFDYKAH QRQLTPPEGS SKSEQDQAEN
     EGEDSAVLME RLCKYIYAKD RTDRIRTCAI LCHIYHHALH SRWYQARDLM LMSHLQDNIQ
     HADPPVQILY NRTMVQLGIC AFRQGLTKDA HNALLDIQSS GRAKELLGQG LLLRSLQERN
     QEQEKVERRR QVPFHLHINL ELLECVYLVS AMLLEIPYMA AHESDARRRM ISKQFHHQLR
     VGERQPLLGP PESMREHVVA ASKAMKMGDW KTCHSFIINE KMNGKVWDLF PEADKVRTML
     VRKIQEESLR TYLFTYSSVY DSISMETLSD MFELDLPTVH SIISKMIINE ELMASLDQPT
     QTVVMHRTEP TAQQNLALQL AEKLGSLVEN NERVFDHKQG TYGGYFRDQK DGYRKNEGYM
     RRGGYRQQQS QTAY
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024