IF6_HUMAN
ID IF6_HUMAN Reviewed; 245 AA.
AC P56537; B7ZBG9; Q6IBN8; Q96TD5;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 1.
DT 03-AUG-2022, entry version 208.
DE RecName: Full=Eukaryotic translation initiation factor 6 {ECO:0000255|HAMAP-Rule:MF_03132};
DE Short=eIF-6 {ECO:0000255|HAMAP-Rule:MF_03132};
DE AltName: Full=B(2)GCN homolog;
DE AltName: Full=B4 integrin interactor;
DE AltName: Full=CAB;
DE AltName: Full=p27(BBP);
GN Name=EIF6 {ECO:0000255|HAMAP-Rule:MF_03132, ECO:0000312|HGNC:HGNC:6159};
GN Synonyms=EIF3A, ITGB4BP {ECO:0000255|HAMAP-Rule:MF_03132};
GN ORFNames=OK/SW-cl.27;
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 [MRNA] (ISOFORM 1).
RC TISSUE=Skeletal muscle;
RX PubMed=9405604; DOI=10.1073/pnas.94.26.14285;
RA Si K., Chaudhuri J., Chevesich J., Maitra U.;
RT "Molecular cloning and functional expression of a human cDNA encoding
RT translation initiation factor 6.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:14285-14290(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
RX PubMed=9374518; DOI=10.1074/jbc.272.48.30314;
RA Biffo S., Sanvito F., Costa S., Preve L., Pignatelli R., Spinardi L.,
RA Marchisio P.C.;
RT "Isolation of a novel beta4 integrin-binding protein (p27(BBP)) highly
RT expressed in epithelial cells.";
RL J. Biol. Chem. 272:30314-30321(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RX PubMed=11290417; DOI=10.1016/s0378-1119(01)00370-5;
RA Donadini A., Giodini A., Sanvito F., Marchisio P.C., Biffo S.;
RT "The human ITGB4BP gene is constitutively expressed in vitro, but highly
RT modulated in vivo.";
RL Gene 266:35-43(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Umbilical cord blood;
RX PubMed=9653160; DOI=10.1073/pnas.95.14.8175;
RA Mao M., Fu G., Wu J.-S., Zhang Q.-H., Zhou J., Kan L.-X., Huang Q.-H.,
RA He K.-L., Gu B.-W., Han Z.-G., Shen Y., Gu J., Yu Y.-P., Xu S.-H.,
RA Wang Y.-X., Chen S.-J., Chen Z.;
RT "Identification of genes expressed in human CD34(+) hematopoietic
RT stem/progenitor cells by expressed sequence tags and efficient full-length
RT cDNA cloning.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:8175-8180(1998).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Colon adenocarcinoma;
RA Shichijo S., Itoh K.;
RT "Identification of immuno-peptidmics that are recognized by tumor-reactive
RT CTL generated from TIL of colon cancer patients.";
RL Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung, Muscle, and Ovary;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [11]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=10085284; DOI=10.1083/jcb.144.5.823;
RA Sanvito F., Piatti S., Villa A., Bossi M., Lucchini G., Marchisio P.C.,
RA Biffo S.;
RT "The beta4 integrin interactor p27(BBP/eIF6) is an essential nuclear matrix
RT protein involved in 60S ribosomal subunit assembly.";
RL J. Cell Biol. 144:823-837(1999).
RN [12]
RP PHOSPHORYLATION AT SER-174 AND SER-175, SUBCELLULAR LOCATION, AND
RP NUCLEOCYTOPLASMIC SHUTTLING.
RX PubMed=12917340; DOI=10.1128/mcb.23.17.6187-6199.2003;
RA Basu U., Si K., Deng H., Maitra U.;
RT "Phosphorylation of mammalian eukaryotic translation initiation factor 6
RT and its Saccharomyces cerevisiae homologue Tif6p: evidence that
RT phosphorylation of Tif6p regulates its nucleocytoplasmic distribution and
RT is required for yeast cell growth.";
RL Mol. Cell. Biol. 23:6187-6199(2003).
RN [13]
RP FUNCTION, SUBUNIT, PHOSPHORYLATION AT SER-235, AND INTERACTION WITH RACK1.
RX PubMed=14654845; DOI=10.1038/nature02160;
RA Ceci M., Gaviraghi C., Gorrini C., Sala L.A., Offenhauser N.,
RA Marchisio P.C., Biffo S.;
RT "Release of eIF6 (p27BBP) from the 60S subunit allows 80S ribosome
RT assembly.";
RL Nature 426:579-584(2003).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-113, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [15]
RP FUNCTION, AND INTERACTION WITH AGO2; DICER1; MOV10; RPL7A AND TARBP2.
RX PubMed=17507929; DOI=10.1038/nature05841;
RA Chendrimada T.P., Finn K.J., Ji X., Baillat D., Gregory R.I.,
RA Liebhaber S.A., Pasquinelli A.E., Shiekhattar R.;
RT "MicroRNA silencing through RISC recruitment of eIF6.";
RL Nature 447:823-828(2007).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-239 AND SER-243, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-239, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [19]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [20]
RP FUNCTION.
RX PubMed=21536732; DOI=10.1101/gad.623011;
RA Finch A.J., Hilcenko C., Basse N., Drynan L.F., Goyenechea B., Menne T.F.,
RA Gonzalez Fernandez A., Simpson P., D'Santos C.S., Arends M.J., Donadieu J.,
RA Bellanne-Chantelot C., Costanzo M., Boone C., McKenzie A.N., Freund S.M.,
RA Warren A.J.;
RT "Uncoupling of GTP hydrolysis from eIF6 release on the ribosome causes
RT Shwachman-Diamond syndrome.";
RL Genes Dev. 25:917-929(2011).
RN [21]
RP PHOSPHORYLATION AT SER-174 AND SER-175 BY CSNK1D/CK1, AND SUBCELLULAR
RP LOCATION.
RX PubMed=21084295; DOI=10.1074/jbc.m110.188565;
RA Biswas A., Mukherjee S., Das S., Shields D., Chow C.W., Maitra U.;
RT "Opposing action of casein kinase 1 and calcineurin in nucleo-cytoplasmic
RT shuttling of mammalian translation initiation factor eIF6.";
RL J. Biol. Chem. 286:3129-3138(2011).
RN [22]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [23]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [24] {ECO:0007744|PDB:6LQM, ECO:0007744|PDB:6LSR, ECO:0007744|PDB:6LSS, ECO:0007744|PDB:6LU8}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.09 ANGSTROMS) IN COMPLEX WITH THE 60S
RP RIBOSOME, AND FUNCTION.
RX PubMed=32669547; DOI=10.1038/s41467-020-17237-x;
RA Liang X., Zuo M.Q., Zhang Y., Li N., Ma C., Dong M.Q., Gao N.;
RT "Structural snapshots of human pre-60S ribosomal particles before and after
RT nuclear export.";
RL Nat. Commun. 11:3542-3542(2020).
CC -!- FUNCTION: Binds to the 60S ribosomal subunit and prevents its
CC association with the 40S ribosomal subunit to form the 80S initiation
CC complex in the cytoplasm (PubMed:10085284, PubMed:14654845,
CC PubMed:21536732, PubMed:32669547). Behaves as a stimulatory translation
CC initiation factor downstream insulin/growth factors. Is also involved
CC in ribosome biogenesis. Associates with pre-60S subunits in the nucleus
CC and is involved in its nuclear export. Cytoplasmic release of TIF6 from
CC 60S subunits and nuclear relocalization is promoted by a RACK1 (RACK1)-
CC dependent protein kinase C activity (PubMed:10085284, PubMed:14654845,
CC PubMed:21536732). In tissues responsive to insulin, controls fatty acid
CC synthesis and glycolysis by exerting translational control of
CC adipogenic transcription factors such as CEBPB, CEBPD and ATF4 that
CC have G/C rich or uORF in their 5'UTR. Required for ROS-dependent
CC megakaryocyte maturation and platelets formation, controls the
CC expression of mitochondrial respiratory chain genes involved in
CC reactive oxygen species (ROS) synthesis (By similarity). Involved in
CC miRNA-mediated gene silencing by the RNA-induced silencing complex
CC (RISC). Required for both miRNA-mediated translational repression and
CC miRNA-mediated cleavage of complementary mRNAs by RISC
CC (PubMed:17507929). Modulates cell cycle progression and global
CC translation of pre-B cells, its activation seems to be rate-limiting in
CC tumorigenesis and tumor growth (By similarity). {ECO:0000255|HAMAP-
CC Rule:MF_03132, ECO:0000269|PubMed:10085284,
CC ECO:0000269|PubMed:14654845, ECO:0000269|PubMed:17507929,
CC ECO:0000269|PubMed:21536732, ECO:0000269|PubMed:32669547}.
CC -!- SUBUNIT: Monomer. Associates with the 60S ribosomal subunit. Interacts
CC with RACK1. Interacts with DICER1, AGO2, TARBP2, MOV10 and RPL7A; they
CC form a large RNA-induced silencing complex (RISC) (PubMed:17507929).
CC {ECO:0000255|HAMAP-Rule:MF_03132, ECO:0000269|PubMed:14654845,
CC ECO:0000269|PubMed:17507929}.
CC -!- INTERACTION:
CC P56537; Q96C10: DHX58; NbExp=2; IntAct=EBI-372243, EBI-744193;
CC P56537; P19525: EIF2AK2; NbExp=2; IntAct=EBI-372243, EBI-640775;
CC P56537; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-372243, EBI-16439278;
CC P56537; Q8IXL7-2: MSRB3; NbExp=3; IntAct=EBI-372243, EBI-10699187;
CC P56537; Q16612: NREP; NbExp=5; IntAct=EBI-372243, EBI-718657;
CC P56537; Q9Y6K5: OAS3; NbExp=2; IntAct=EBI-372243, EBI-6115729;
CC P56537; Q08AM6: VAC14; NbExp=3; IntAct=EBI-372243, EBI-2107455;
CC P56537; P68404: Prkcb; Xeno; NbExp=2; IntAct=EBI-372243, EBI-397048;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus, nucleolus. Note=Shuttles
CC between cytoplasm and nucleus/nucleolus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P56537-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P56537-2; Sequence=VSP_046747;
CC -!- TISSUE SPECIFICITY: Expressed at very high levels in colon carcinoma
CC with lower levels in normal colon and ileum and lowest levels in kidney
CC and muscle (at protein level). {ECO:0000269|PubMed:11290417}.
CC -!- PTM: Phosphorylation at Ser-174 and Ser-175 by CSNK1D/CK1 promotes
CC nuclear export. {ECO:0000269|PubMed:12917340,
CC ECO:0000269|PubMed:14654845, ECO:0000269|PubMed:21084295}.
CC -!- PTM: Ufmylated by UFL1. {ECO:0000250|UniProtKB:O55135}.
CC -!- SIMILARITY: Belongs to the eIF-6 family. {ECO:0000255|HAMAP-
CC Rule:MF_03132}.
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DR EMBL; AF022229; AAB97735.1; -; mRNA.
DR EMBL; Y11435; CAA72243.1; -; mRNA.
DR EMBL; AF289541; AAK39426.1; -; Genomic_DNA.
DR EMBL; AF289540; AAK39426.1; JOINED; Genomic_DNA.
DR EMBL; AF047433; AAC39897.1; -; mRNA.
DR EMBL; AK314969; BAG37470.1; -; mRNA.
DR EMBL; AB062289; BAB93472.1; -; mRNA.
DR EMBL; CR456764; CAG33045.1; -; mRNA.
DR EMBL; AL121753; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471077; EAW76221.1; -; Genomic_DNA.
DR EMBL; BC001119; AAH01119.1; -; mRNA.
DR EMBL; BC011845; AAH11845.1; -; mRNA.
DR EMBL; BC019305; AAH19305.1; -; mRNA.
DR CCDS; CCDS13249.1; -. [P56537-1]
DR CCDS; CCDS13250.1; -. [P56537-2]
DR RefSeq; NP_001254739.1; NM_001267810.1. [P56537-1]
DR RefSeq; NP_002203.1; NM_002212.3. [P56537-1]
DR RefSeq; NP_852131.1; NM_181466.2. [P56537-2]
DR RefSeq; NP_852133.1; NM_181468.2. [P56537-1]
DR PDB; 6LQM; EM; 3.09 A; 6=1-245.
DR PDB; 6LSR; EM; 3.13 A; 6=1-245.
DR PDB; 6LSS; EM; 3.23 A; 6=1-245.
DR PDB; 6LU8; EM; 3.13 A; 6=1-245.
DR PDBsum; 6LQM; -.
DR PDBsum; 6LSR; -.
DR PDBsum; 6LSS; -.
DR PDBsum; 6LU8; -.
DR AlphaFoldDB; P56537; -.
DR SMR; P56537; -.
DR BioGRID; 109898; 325.
DR CORUM; P56537; -.
DR IntAct; P56537; 51.
DR MINT; P56537; -.
DR STRING; 9606.ENSP00000363574; -.
DR ChEMBL; CHEMBL4296020; -.
DR DrugBank; DB09130; Copper.
DR Allergome; 8361; Hom s eIF6.
DR GlyGen; P56537; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P56537; -.
DR MetOSite; P56537; -.
DR PhosphoSitePlus; P56537; -.
DR SwissPalm; P56537; -.
DR BioMuta; EIF6; -.
DR OGP; P56537; -.
DR REPRODUCTION-2DPAGE; IPI00010105; -.
DR SWISS-2DPAGE; P56537; -.
DR EPD; P56537; -.
DR jPOST; P56537; -.
DR MassIVE; P56537; -.
DR MaxQB; P56537; -.
DR PaxDb; P56537; -.
DR PeptideAtlas; P56537; -.
DR PRIDE; P56537; -.
DR ProteomicsDB; 56921; -. [P56537-1]
DR ProteomicsDB; 7119; -.
DR TopDownProteomics; P56537-1; -. [P56537-1]
DR Antibodypedia; 35156; 266 antibodies from 35 providers.
DR DNASU; 3692; -.
DR Ensembl; ENST00000374436.7; ENSP00000363559.3; ENSG00000242372.9. [P56537-1]
DR Ensembl; ENST00000374443.7; ENSP00000363566.3; ENSG00000242372.9. [P56537-2]
DR Ensembl; ENST00000374450.8; ENSP00000363574.3; ENSG00000242372.9. [P56537-1]
DR Ensembl; ENST00000675032.1; ENSP00000502429.1; ENSG00000242372.9. [P56537-1]
DR GeneID; 3692; -.
DR KEGG; hsa:3692; -.
DR MANE-Select; ENST00000374450.8; ENSP00000363574.3; NM_002212.4; NP_002203.1.
DR UCSC; uc002xbv.3; human. [P56537-1]
DR CTD; 3692; -.
DR DisGeNET; 3692; -.
DR GeneCards; EIF6; -.
DR HGNC; HGNC:6159; EIF6.
DR HPA; ENSG00000242372; Low tissue specificity.
DR MIM; 602912; gene.
DR neXtProt; NX_P56537; -.
DR OpenTargets; ENSG00000242372; -.
DR PharmGKB; PA29958; -.
DR VEuPathDB; HostDB:ENSG00000242372; -.
DR eggNOG; KOG3185; Eukaryota.
DR GeneTree; ENSGT00390000015972; -.
DR HOGENOM; CLU_071894_0_0_1; -.
DR InParanoid; P56537; -.
DR OMA; GEDTTGP; -.
DR OrthoDB; 1157302at2759; -.
DR PhylomeDB; P56537; -.
DR TreeFam; TF105396; -.
DR PathwayCommons; P56537; -.
DR SignaLink; P56537; -.
DR SIGNOR; P56537; -.
DR BioGRID-ORCS; 3692; 781 hits in 1060 CRISPR screens.
DR ChiTaRS; EIF6; human.
DR GeneWiki; EIF6; -.
DR GenomeRNAi; 3692; -.
DR Pharos; P56537; Tbio.
DR PRO; PR:P56537; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; P56537; protein.
DR Bgee; ENSG00000242372; Expressed in esophagus mucosa and 111 other tissues.
DR ExpressionAtlas; P56537; baseline and differential.
DR Genevisible; P56537; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005638; C:lamin filament; IEA:Ensembl.
DR GO; GO:0005730; C:nucleolus; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0030687; C:preribosome, large subunit precursor; IBA:GO_Central.
DR GO; GO:0043023; F:ribosomal large subunit binding; IBA:GO_Central.
DR GO; GO:0043022; F:ribosome binding; IDA:UniProtKB.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-UniRule.
DR GO; GO:1902626; P:assembly of large subunit precursor of preribosome; IBA:GO_Central.
DR GO; GO:0000460; P:maturation of 5.8S rRNA; IBA:GO_Central.
DR GO; GO:0000470; P:maturation of LSU-rRNA; IBA:GO_Central.
DR GO; GO:0042256; P:mature ribosome assembly; IMP:UniProtKB.
DR GO; GO:0035195; P:miRNA-mediated gene silencing; IMP:UniProtKB.
DR GO; GO:0035278; P:miRNA-mediated gene silencing by inhibition of translation; IMP:UniProtKB.
DR GO; GO:0045727; P:positive regulation of translation; ISS:UniProtKB.
DR GO; GO:0042304; P:regulation of fatty acid biosynthetic process; ISS:UniProtKB.
DR GO; GO:0006110; P:regulation of glycolytic process; ISS:UniProtKB.
DR GO; GO:0045652; P:regulation of megakaryocyte differentiation; ISS:UniProtKB.
DR GO; GO:2000377; P:regulation of reactive oxygen species metabolic process; ISS:UniProtKB.
DR GO; GO:0032868; P:response to insulin; ISS:UniProtKB.
DR GO; GO:0000054; P:ribosomal subunit export from nucleus; IBA:GO_Central.
DR CDD; cd00527; IF6; 1.
DR HAMAP; MF_00032; eIF_6; 1.
DR InterPro; IPR002769; eIF6.
DR PANTHER; PTHR10784; PTHR10784; 1.
DR Pfam; PF01912; eIF-6; 1.
DR PIRSF; PIRSF006413; IF-6; 1.
DR SMART; SM00654; eIF6; 1.
DR TIGRFAMs; TIGR00323; eIF-6; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Initiation factor; Nucleus;
KW Phosphoprotein; Protein biosynthesis; Reference proteome;
KW Ribosome biogenesis; Ubl conjugation.
FT CHAIN 1..245
FT /note="Eukaryotic translation initiation factor 6"
FT /id="PRO_0000153734"
FT MOD_RES 113
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:15592455"
FT MOD_RES 165
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O55135, ECO:0000255|HAMAP-
FT Rule:MF_03132"
FT MOD_RES 166
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O55135, ECO:0000255|HAMAP-
FT Rule:MF_03132"
FT MOD_RES 174
FT /note="Phosphoserine; by CK1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03132,
FT ECO:0000269|PubMed:12917340, ECO:0000269|PubMed:21084295"
FT MOD_RES 175
FT /note="Phosphoserine; by CK1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03132,
FT ECO:0000269|PubMed:12917340, ECO:0000269|PubMed:21084295"
FT MOD_RES 235
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03132,
FT ECO:0000269|PubMed:14654845"
FT MOD_RES 239
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 243
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT VAR_SEQ 36..123
FT /note="SVFEGELSDTIPVVHASIAGCRIIGRMCVGNRHGLLVPNNTTDQELQHIRNS
FT LPDTVQIRRVEERLSALGNVTTCNDYVALVHPDLDR -> RCGGSPGAYGGGEACAGVK
FT SSGSGRVPAPLPRHHRVHVPTVCSRASSPIPSPWCTRLSPAAASSGACVW (in
FT isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_046747"
FT CONFLICT 35..36
FT /note="Missing (in Ref. 3; AAK39426)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 245 AA; 26599 MW; 5BA97CD5DB0C17C3 CRC64;
MAVRASFENN CEIGCFAKLT NTYCLVAIGG SENFYSVFEG ELSDTIPVVH ASIAGCRIIG
RMCVGNRHGL LVPNNTTDQE LQHIRNSLPD TVQIRRVEER LSALGNVTTC NDYVALVHPD
LDRETEEILA DVLKVEVFRQ TVADQVLVGS YCVFSNQGGL VHPKTSIEDQ DELSSLLQVP
LVAGTVNRGS EVIAAGMVVN DWCAFCGLDT TSTELSVVES VFKLNEAQPS TIATSMRDSL
IDSLT
