CTIF_HUMAN
ID CTIF_HUMAN Reviewed; 598 AA.
AC O43310; B3KTR8; Q8IVD5;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=CBP80/20-dependent translation initiation factor;
GN Name=CTIF; Synonyms=KIAA0427;
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 MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=9455477; DOI=10.1093/dnares/4.5.307;
RA Ishikawa K., Nagase T., Nakajima D., Seki N., Ohira M., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. VIII. 78
RT new cDNA clones from brain which code for large proteins in vitro.";
RL DNA Res. 4:307-313(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16177791; DOI=10.1038/nature03983;
RA Nusbaum C., Zody M.C., Borowsky M.L., Kamal M., Kodira C.D., Taylor T.D.,
RA Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X.,
RA Abouelleil A., Allen N.R., Anderson S., Bloom T., Bugalter B., Butler J.,
RA Cook A., DeCaprio D., Engels R., Garber M., Gnirke A., Hafez N., Hall J.L.,
RA Norman C.H., Itoh T., Jaffe D.B., Kuroki Y., Lehoczky J., Lui A.,
RA Macdonald P., Mauceli E., Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C.,
RA Noguchi H., O'Leary S.B., Piqani B., Smith C.L., Talamas J.A., Topham K.,
RA Totoki Y., Toyoda A., Wain H.M., Young S.K., Zeng Q., Zimmer A.R.,
RA Fujiyama A., Hattori M., Birren B.W., Sakaki Y., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 18.";
RL Nature 437:551-555(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 60-578 (ISOFORM 1).
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-299, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [6]
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 [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH NCBP1,
RP AND INTERACTION WITH THE EIF-3 COMPLEX.
RX PubMed=19648179; DOI=10.1101/gad.1823409;
RA Kim K.M., Cho H., Choi K., Kim J., Kim B.-W., Ko Y.-G., Jang S.K.,
RA Kim Y.K.;
RT "A new MIF4G domain-containing protein, CTIF, directs nuclear cap-binding
RT protein CBP80/20-dependent translation.";
RL Genes Dev. 23:2033-2045(2009).
RN [9]
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 [10]
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 [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-289 AND SER-299, AND
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 [14]
RP VARIANTS [LARGE SCALE ANALYSIS] LEU-389 AND ILE-438.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Specifically required for the pioneer round of mRNA
CC translation mediated by the cap-binding complex (CBC), that takes place
CC during or right after mRNA export via the nuclear pore complex (NPC).
CC Acts via its interaction with the NCBP1/CBP80 component of the CBC
CC complex and recruits the 40S small subunit of the ribosome via eIF3. In
CC contrast, it is not involved in steady state translation, that takes
CC place when the CBC complex is replaced by cytoplasmic cap-binding
CC protein eIF4E. Also required for nonsense-mediated mRNA decay (NMD),
CC the pioneer round of mRNA translation mediated by the cap-binding
CC complex playing a central role in nonsense-mediated mRNA decay (NMD).
CC {ECO:0000269|PubMed:19648179}.
CC -!- SUBUNIT: Interacts with NCBP1/CBP80; the interaction is direct.
CC Associates with the eukaryotic translation initiation factor 3 (eIF-3)
CC complex. {ECO:0000269|PubMed:19648179}.
CC -!- INTERACTION:
CC O43310-2; Q8N5M1: ATPAF2; NbExp=3; IntAct=EBI-12180013, EBI-1166928;
CC O43310-2; Q9NUU7: DDX19A; NbExp=4; IntAct=EBI-12180013, EBI-740301;
CC O43310-2; Q9UMR2: DDX19B; NbExp=3; IntAct=EBI-12180013, EBI-719232;
CC O43310-2; Q96MH2: HEXIM2; NbExp=3; IntAct=EBI-12180013, EBI-5460660;
CC O43310-2; Q86VS8: HOOK3; NbExp=3; IntAct=EBI-12180013, EBI-1777078;
CC O43310-2; A9UHW6-2: MIF4GD; NbExp=3; IntAct=EBI-12180013, EBI-9118295;
CC O43310-2; Q6P9E2: RECK; NbExp=3; IntAct=EBI-12180013, EBI-10253121;
CC O43310-2; Q9NZD8: SPG21; NbExp=3; IntAct=EBI-12180013, EBI-742688;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region
CC {ECO:0000269|PubMed:19648179}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O43310-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O43310-2; Sequence=VSP_013774;
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:19648179}.
CC -!- SIMILARITY: Belongs to the CTIF family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA24857.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAG53180.1; Type=Miscellaneous discrepancy; Note=Aberrant splicing.; Evidence={ECO:0000305};
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DR EMBL; AB007887; BAA24857.2; ALT_INIT; mRNA.
DR EMBL; AC022919; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC048380; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC093567; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC042146; AAH42146.1; -; mRNA.
DR EMBL; AK095970; BAG53180.1; ALT_SEQ; mRNA.
DR CCDS; CCDS11935.1; -. [O43310-1]
DR CCDS; CCDS45864.1; -. [O43310-2]
DR RefSeq; NP_001135869.1; NM_001142397.1. [O43310-2]
DR RefSeq; NP_055587.1; NM_014772.2. [O43310-1]
DR RefSeq; XP_006722650.1; XM_006722587.3. [O43310-2]
DR RefSeq; XP_006722651.1; XM_006722588.3. [O43310-2]
DR RefSeq; XP_006722652.1; XM_006722589.3.
DR RefSeq; XP_011524581.1; XM_011526279.2. [O43310-1]
DR RefSeq; XP_016881591.1; XM_017026102.1. [O43310-2]
DR AlphaFoldDB; O43310; -.
DR SMR; O43310; -.
DR BioGRID; 115150; 68.
DR CORUM; O43310; -.
DR IntAct; O43310; 9.
DR STRING; 9606.ENSP00000372459; -.
DR TCDB; 1.I.1.1.3; the nuclear pore complex (npc) family.
DR iPTMnet; O43310; -.
DR PhosphoSitePlus; O43310; -.
DR BioMuta; CTIF; -.
DR EPD; O43310; -.
DR jPOST; O43310; -.
DR MassIVE; O43310; -.
DR MaxQB; O43310; -.
DR PaxDb; O43310; -.
DR PeptideAtlas; O43310; -.
DR PRIDE; O43310; -.
DR ProteomicsDB; 48885; -. [O43310-1]
DR ProteomicsDB; 48886; -. [O43310-2]
DR Antibodypedia; 9256; 56 antibodies from 14 providers.
DR DNASU; 9811; -.
DR Ensembl; ENST00000256413.8; ENSP00000256413.3; ENSG00000134030.14. [O43310-1]
DR Ensembl; ENST00000382998.8; ENSP00000372459.3; ENSG00000134030.14. [O43310-2]
DR Ensembl; ENST00000634350.1; ENSP00000489354.1; ENSG00000282825.2. [O43310-2]
DR Ensembl; ENST00000635228.2; ENSP00000489589.1; ENSG00000282825.2. [O43310-1]
DR GeneID; 9811; -.
DR KEGG; hsa:9811; -.
DR MANE-Select; ENST00000256413.8; ENSP00000256413.3; NM_014772.3; NP_055587.1.
DR UCSC; uc002ldc.4; human. [O43310-1]
DR CTD; 9811; -.
DR DisGeNET; 9811; -.
DR GeneCards; CTIF; -.
DR HGNC; HGNC:23925; CTIF.
DR HPA; ENSG00000134030; Low tissue specificity.
DR MIM; 613178; gene.
DR neXtProt; NX_O43310; -.
DR OpenTargets; ENSG00000134030; -.
DR PharmGKB; PA134974369; -.
DR VEuPathDB; HostDB:ENSG00000134030; -.
DR eggNOG; KOG3942; Eukaryota.
DR GeneTree; ENSGT00940000153432; -.
DR HOGENOM; CLU_031968_1_0_1; -.
DR InParanoid; O43310; -.
DR OMA; DFSMREE; -.
DR OrthoDB; 578545at2759; -.
DR PhylomeDB; O43310; -.
DR TreeFam; TF350740; -.
DR PathwayCommons; O43310; -.
DR SignaLink; O43310; -.
DR BioGRID-ORCS; 9811; 13 hits in 1079 CRISPR screens.
DR ChiTaRS; CTIF; human.
DR GenomeRNAi; 9811; -.
DR Pharos; O43310; Tbio.
DR PRO; PR:O43310; -.
DR Proteomes; UP000005640; Chromosome 18.
DR RNAct; O43310; protein.
DR Bgee; ENSG00000134030; Expressed in primary visual cortex and 98 other tissues.
DR ExpressionAtlas; O43310; baseline and differential.
DR Genevisible; O43310; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0008494; F:translation activator activity; IBA:GO_Central.
DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IMP:UniProtKB.
DR GO; GO:0006446; P:regulation of translational initiation; IMP:UniProtKB.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR003890; MIF4G-like_typ-3.
DR Pfam; PF02854; MIF4G; 1.
DR SMART; SM00543; MIF4G; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cytoplasm; Nonsense-mediated mRNA decay;
KW Phosphoprotein; Reference proteome; Translation regulation.
FT CHAIN 1..598
FT /note="CBP80/20-dependent translation initiation factor"
FT /id="PRO_0000050754"
FT DOMAIN 376..577
FT /note="MIF4G"
FT REGION 1..305
FT /note="Interaction with NCBP1/CBP80"
FT /evidence="ECO:0000269|PubMed:19648179"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 43..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 180..336
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..90
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 254..279
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 320..334
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22814378"
FT MOD_RES 18
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 289
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 299
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18088087,
FT ECO:0007744|PubMed:24275569"
FT VAR_SEQ 357
FT /note="K -> KVP (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_013774"
FT VARIANT 82
FT /note="P -> L (in dbSNP:rs2277712)"
FT /id="VAR_020041"
FT VARIANT 389
FT /note="V -> L (in a breast cancer sample; somatic mutation;
FT dbSNP:rs751006365)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035749"
FT VARIANT 438
FT /note="M -> I (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035750"
SQ SEQUENCE 598 AA; 67587 MW; 9F8776857A7DDC8A CRC64;
MENSSAASAS SEAGSSRSQE IEELERFIDS YVLEYQVQGL LADKTEGDGE SERTQSHISQ
WTADCSEPLD SSCSFSRGRA PPQQNGSKDN SLDMLGTDIW AANTFDSFSG ATWDLQPEKL
DFTQFHRKVR HTPKQPLPHI DREGCGKGKL EDGDGINLND IEKVLPAWQG YHPMPHEVEI
AHTKKLFRRR RNDRRRQQRP PGGNKPQQHG DHQPGSAKHN RDHQKSYQGG SAPHPSGRPT
HHGYSQNRRW HHGNMKHPPG DKGEAGAHRN AKETMTIENP KLEDTAGDTG HSSLEAPRSP
DTLAPVASER LPPQQSGGPE VETKRKDSIL PERIGERPKI TLLQSSKDRL RRRLKEKDEV
AVETTTPQQN KMDKLIEILN SMRNNSSDVD TKLTTFMEEA QNSTNSEEML GEIVRTIYQK
AVSDRSFAFT AAKLCDKMAL FMVEGTKFRS LLLNMLQKDF TVREELQQQD VERWLGFITF
LCEVFGTMRS STGEPFRVLV CPIYTCLREL LQSQDVKEDA VLCCSMELQS TGRLLEEQLP
EMMTELLASA RDKMLCPSES MLTRSLLLEV IELHANSWNP LTPPITQYYN RTIQKLTA
