ID ABCF1_HUMAN Reviewed; 845 AA. AC Q8NE71; A2BF75; O14897; Q69YP6; DT 07-DEC-2004, integrated into UniProtKB/Swiss-Prot. DT 07-DEC-2004, sequence version 2. DT 27-MAR-2024, entry version 192. DE RecName: Full=ATP-binding cassette sub-family F member 1; DE AltName: Full=ATP-binding cassette 50; DE AltName: Full=TNF-alpha-stimulated ABC protein; GN Name=ABCF1; Synonyms=ABC50; 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 2), AND TISSUE SPECIFICITY. RX PubMed=9790762; DOI=10.1006/geno.1998.5480; RA Richard M., Drouin R., Beaulieu A.D.; RT "ABC50, a novel human ATP-binding cassette protein found in tumor necrosis RT factor-alpha-stimulated synoviocytes."; RL Genomics 53:137-145(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Shiina S., Tamiya G., Oka A., Inoko H.; RT "Homo sapiens 2,229,817bp genomic DNA of 6p21.3 HLA class I region."; RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Shiina T., Ota M., Katsuyama Y., Hashimoto N., Inoko H.; RT "Genome diversity in HLA: a new strategy for detection of genetic RT polymorphisms in expressed genes within the HLA class III and class I RT regions."; RL Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., RA Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Embryonic stem cell, and Testis; 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 [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 160-845 (ISOFORM 1). RC TISSUE=Melanoma; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-105; THR-108; SER-109; RP SER-140 AND SER-228, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-228, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=16964243; DOI=10.1038/nbt1240; RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; RT "A probability-based approach for high-throughput protein phosphorylation RT analysis and site localization."; RL Nat. Biotechnol. 24:1285-1292(2006). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-595, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic kidney; RX PubMed=17525332; DOI=10.1126/science.1140321; RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., RA Gygi S.P., Elledge S.J.; RT "ATM and ATR substrate analysis reveals extensive protein networks RT responsive to DNA damage."; RL Science 316:1160-1166(2007). RN [10] RP INTERACTION WITH EIF2S1, ASSOCIATION WITH RIBOSOMES, PHOSPHORYLATION AT RP SER-109 AND SER-140, IDENTIFICATION BY MASS SPECTROMETRY, AND MUTAGENESIS RP OF SER-109 AND SER-140. RX PubMed=17894550; DOI=10.1042/bj20070811; RA Paytubi S., Morrice N.A., Boudeau J., Proud C.G.; RT "The N-terminal region of ABC50 interacts with eukaryotic initiation factor RT eIF2 and is a target for regulatory phosphorylation by CK2."; RL Biochem. J. 409:223-231(2008). RN [11] RP IDENTIFICATION BY 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 [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24 AND SER-228, 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 [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-228, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=18318008; DOI=10.1002/pmic.200700884; RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., RA Zou H., Gu J.; RT "Large-scale phosphoproteome analysis of human liver tissue by enrichment RT and fractionation of phosphopeptides with strong anion exchange RT chromatography."; RL Proteomics 8:1346-1361(2008). RN [14] RP IDENTIFICATION BY MASS 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 [15] RP FUNCTION, ATP-BINDING, ASSOCIATION WITH RIBOSOMES, MUTAGENESIS OF LYS-342; RP GLN-367; GLY-454; GLU-477; HIS-506; LYS-664; GLN-695; GLY-745; GLU-768 AND RP HIS-797, AND SUBCELLULAR LOCATION. RX PubMed=19570978; DOI=10.1074/jbc.m109.031625; RA Paytubi S., Wang X., Lam Y.W., Izquierdo L., Hunter M.J., Jan E., RA Hundal H.S., Proud C.G.; RT "ABC50 promotes translation initiation in mammalian cells."; RL J. Biol. Chem. 284:24061-24073(2009). RN [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-108; SER-109; SER-140 AND RP SER-228, AND 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 [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22; SER-105; THR-108; RP SER-109; SER-140 AND SER-228, AND IDENTIFICATION BY MASS SPECTROMETRY RP [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 [18] 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 [19] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-108; SER-109; SER-140; RP SER-166 AND SER-228, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [20] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22; SER-105; THR-108; RP SER-109; SER-140; SER-166; SER-228 AND SER-595, AND IDENTIFICATION BY MASS RP 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 [21] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-105 AND THR-108, 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). CC -!- FUNCTION: Isoform 2 is required for efficient Cap- and IRES-mediated CC mRNA translation initiation. Isoform 2 is not involved in the ribosome CC biogenesis. {ECO:0000269|PubMed:19570978}. CC -!- SUBUNIT: Isoform 2 interacts (via N-terminus) with EIF2S1; the CC interaction is independent of its phosphorylated status. Isoform 2 CC associates (via both ABC transporter domains) with the ribosomes. CC {ECO:0000269|PubMed:17894550}. CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm CC {ECO:0000269|PubMed:19570978}. Nucleus, nucleoplasm CC {ECO:0000269|PubMed:19570978}. Nucleus envelope CC {ECO:0000269|PubMed:19570978}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q8NE71-1; Sequence=Displayed; CC Name=2; CC IsoId=Q8NE71-2; Sequence=VSP_012078; CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:9790762}. CC -!- INDUCTION: By TNF in cultured synoviocytes. CC -!- PTM: Isoform 2 is phosphorylated at phosphoserine and phosphothreonine. CC Isoform 2 phosphorylation on Ser-109 and Ser-140 by CK2 inhibits CC association of EIF2 with ribosomes. {ECO:0000269|PubMed:17894550}. CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCF family. CC EF3 subfamily. {ECO:0000305}. CC -!- WEB RESOURCE: Name=ABCMdb; Note=Database for mutations in ABC proteins; CC URL="http://abcm2.hegelab.org/search"; 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; AF027302; AAC70891.1; -; mRNA. DR EMBL; BA000025; BAB63325.1; -; Genomic_DNA. DR EMBL; AB088096; BAC54928.1; -; Genomic_DNA. DR EMBL; AL662800; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL662825; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BX000357; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BX119957; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BX248518; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CR753328; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CR388372; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BX927220; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CR759778; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CR847863; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC034488; AAH34488.1; -; mRNA. DR EMBL; BC112923; AAI12924.1; -; mRNA. DR EMBL; AL832430; CAH10648.1; -; mRNA. DR CCDS; CCDS34380.1; -. [Q8NE71-1] DR CCDS; CCDS34381.1; -. [Q8NE71-2] DR RefSeq; NP_001020262.1; NM_001025091.1. [Q8NE71-1] DR RefSeq; NP_001081.1; NM_001090.2. [Q8NE71-2] DR PDB; 5ZXD; X-ray; 2.29 A; A/B=300-841. DR PDBsum; 5ZXD; -. DR AlphaFoldDB; Q8NE71; -. DR SMR; Q8NE71; -. DR BioGRID; 106541; 173. DR DIP; DIP-50666N; -. DR IntAct; Q8NE71; 48. DR MINT; Q8NE71; -. DR STRING; 9606.ENSP00000313603; -. DR TCDB; 3.A.1.121.8; the atp-binding cassette (abc) superfamily. DR GlyGen; Q8NE71; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q8NE71; -. DR MetOSite; Q8NE71; -. DR PhosphoSitePlus; Q8NE71; -. DR SwissPalm; Q8NE71; -. DR BioMuta; ABCF1; -. DR DMDM; 56417894; -. DR CPTAC; CPTAC-301; -. DR CPTAC; CPTAC-302; -. DR EPD; Q8NE71; -. DR jPOST; Q8NE71; -. DR MassIVE; Q8NE71; -. DR MaxQB; Q8NE71; -. DR PaxDb; 9606-ENSP00000313603; -. DR PeptideAtlas; Q8NE71; -. DR ProteomicsDB; 73130; -. [Q8NE71-1] DR ProteomicsDB; 73131; -. [Q8NE71-2] DR Pumba; Q8NE71; -. DR Antibodypedia; 2796; 350 antibodies from 33 providers. DR DNASU; 23; -. DR Ensembl; ENST00000326195.13; ENSP00000313603.8; ENSG00000204574.14. [Q8NE71-1] DR Ensembl; ENST00000376545.7; ENSP00000365728.3; ENSG00000204574.14. [Q8NE71-2] DR Ensembl; ENST00000383587.8; ENSP00000373081.4; ENSG00000206490.11. [Q8NE71-2] DR Ensembl; ENST00000383588.8; ENSP00000373082.4; ENSG00000206490.11. [Q8NE71-1] DR Ensembl; ENST00000412443.6; ENSP00000404726.2; ENSG00000236342.8. [Q8NE71-2] DR Ensembl; ENST00000419893.6; ENSP00000389065.2; ENSG00000232169.9. [Q8NE71-1] DR Ensembl; ENST00000420257.6; ENSP00000391102.2; ENSG00000225989.9. [Q8NE71-2] DR Ensembl; ENST00000421042.6; ENSP00000393143.2; ENSG00000231129.8. [Q8NE71-2] DR Ensembl; ENST00000423247.6; ENSP00000411327.2; ENSG00000225989.9. [Q8NE71-1] DR Ensembl; ENST00000426219.6; ENSP00000414373.2; ENSG00000231129.8. [Q8NE71-1] DR Ensembl; ENST00000448939.6; ENSP00000403526.2; ENSG00000232169.9. [Q8NE71-2] DR Ensembl; ENST00000452530.6; ENSP00000389472.2; ENSG00000236149.9. [Q8NE71-2] DR Ensembl; ENST00000457078.6; ENSP00000412553.2; ENSG00000236342.8. [Q8NE71-1] DR Ensembl; ENST00000457111.6; ENSP00000413319.2; ENSG00000236149.9. [Q8NE71-1] DR GeneID; 23; -. DR KEGG; hsa:23; -. DR MANE-Select; ENST00000326195.13; ENSP00000313603.8; NM_001025091.2; NP_001020262.1. DR UCSC; uc003nql.4; human. [Q8NE71-1] DR AGR; HGNC:70; -. DR CTD; 23; -. DR DisGeNET; 23; -. DR GeneCards; ABCF1; -. DR HGNC; HGNC:70; ABCF1. DR HPA; ENSG00000204574; Low tissue specificity. DR MIM; 603429; gene. DR neXtProt; NX_Q8NE71; -. DR OpenTargets; ENSG00000204574; -. DR PharmGKB; PA24405; -. DR VEuPathDB; HostDB:ENSG00000204574; -. DR eggNOG; KOG0066; Eukaryota. DR GeneTree; ENSGT00940000158329; -. DR HOGENOM; CLU_000604_36_5_1; -. DR InParanoid; Q8NE71; -. DR OMA; ARLVLCM; -. DR OrthoDB; 25181at2759; -. DR PhylomeDB; Q8NE71; -. DR TreeFam; TF105207; -. DR PathwayCommons; Q8NE71; -. DR Reactome; R-HSA-382556; ABC-family proteins mediated transport. DR SignaLink; Q8NE71; -. DR SIGNOR; Q8NE71; -. DR BioGRID-ORCS; 23; 718 hits in 1167 CRISPR screens. DR ChiTaRS; ABCF1; human. DR GeneWiki; ABCF1; -. DR GenomeRNAi; 23; -. DR Pharos; Q8NE71; Tbio. DR PRO; PR:Q8NE71; -. DR Proteomes; UP000005640; Chromosome 6. DR RNAct; Q8NE71; Protein. DR Bgee; ENSG00000204574; Expressed in sural nerve and 101 other cell types or tissues. DR ExpressionAtlas; Q8NE71; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0005635; C:nuclear envelope; IDA:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB. DR GO; GO:0042788; C:polysomal ribosome; IDA:UniProtKB. DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB. DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro. DR GO; GO:0043022; F:ribosome binding; IDA:UniProtKB. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR GO; GO:0008494; F:translation activator activity; IDA:UniProtKB. DR GO; GO:0008135; F:translation factor activity, RNA binding; TAS:ProtInc. DR GO; GO:0006954; P:inflammatory response; TAS:ProtInc. DR GO; GO:0045727; P:positive regulation of translation; IDA:UniProtKB. DR GO; GO:0006412; P:translation; TAS:ProtInc. DR GO; GO:0006413; P:translational initiation; IMP:UniProtKB. DR CDD; cd03221; ABCF_EF-3; 2. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR003439; ABC_transporter-like_ATP-bd. DR InterPro; IPR017871; ABC_transporter-like_CS. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR19211:SF126; ATP-BINDING CASSETTE SUB-FAMILY F MEMBER 1; 1. DR PANTHER; PTHR19211; ATP-BINDING TRANSPORT PROTEIN-RELATED; 1. DR Pfam; PF00005; ABC_tran; 2. DR SMART; SM00382; AAA; 2. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 2. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2. DR Genevisible; Q8NE71; HS. PE 1: Evidence at protein level; KW 3D-structure; Activator; Alternative splicing; ATP-binding; Cytoplasm; KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat. FT CHAIN 1..845 FT /note="ATP-binding cassette sub-family F member 1" FT /id="PRO_0000093318" FT DOMAIN 304..548 FT /note="ABC transporter 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434" FT DOMAIN 625..840 FT /note="ABC transporter 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434" FT REGION 1..261 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 559..602 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 37..63 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 83..121 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 145..198 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 207..229 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 230..244 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 245..261 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 336..343 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434" FT BINDING 658..665 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434" FT MOD_RES 22 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" FT MOD_RES 24 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 105 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 108 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 109 FT /note="Phosphoserine; by CK2" FT /evidence="ECO:0000269|PubMed:17894550, FT ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 140 FT /note="Phosphoserine; by CK2" FT /evidence="ECO:0000269|PubMed:17894550, FT ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 166 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 228 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:16964243, FT ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18318008, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 595 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17525332, FT ECO:0007744|PubMed:23186163" FT VAR_SEQ 226..263 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:9790762" FT /id="VSP_012078" FT VARIANT 198 FT /note="N -> D (in dbSNP:rs6902544)" FT /id="VAR_048136" FT MUTAGEN 109 FT /note="S->A: Reduces phosphorylation. Inhibits strongly FT phosphorylation by CK2; when associated with S-140. Does FT not inhibit interaction with EIF2; when associated with FT S-140. Does not inhibit association with ribosomes; when FT associated with S-140. Reduces EIF2 interaction with FT ribosomes; when associated with S-140. Does not inhibit FT protein synthesis; when associated with A-140." FT /evidence="ECO:0000269|PubMed:17894550" FT MUTAGEN 140 FT /note="S->A: Reduces phosphorylation. Inhibits strongly FT phosphorylation by CK2; when associated with S-109. Does FT not inhibits interaction with EIF2; when associated with FT S-109. Does not inhibit association with ribosomes; when FT associated with S-109. Reduces EIF2 interaction with FT ribosomes; when associated with S-109. Does not inhibit FT protein synthesis; when associated with A-109." FT /evidence="ECO:0000269|PubMed:17894550" FT MUTAGEN 342 FT /note="K->M: Does not inhibit ribosome binding. Reduces FT ATP-binding. Inhibits ATP-binding and reduces protein FT synthesis; when associated with M-664. Shows an enhanced FT association with polyribosomes; when associated with M-664. FT Does not inhibit IRES-mediated protein synthesis; when FT associated with M-664." FT /evidence="ECO:0000269|PubMed:19570978" FT MUTAGEN 367 FT /note="Q->E: Does not inhibit ribosome binding." FT /evidence="ECO:0000269|PubMed:19570978" FT MUTAGEN 454 FT /note="G->D: Does not inhibit ribosome binding." FT /evidence="ECO:0000269|PubMed:19570978" FT MUTAGEN 477 FT /note="E->Q: Does not inhibit ribosome binding. Reduces FT protein synthesis; when associated with Q-768." FT /evidence="ECO:0000269|PubMed:19570978" FT MUTAGEN 506 FT /note="H->L: Does not inhibit ribosome binding." FT /evidence="ECO:0000269|PubMed:19570978" FT MUTAGEN 664 FT /note="K->M: Does not inhibit ribosome binding. Reduces FT ATP-binding. Inhibits ATP-binding and reduces protein FT synthesis; when associated with M-342. Shows a reduced FT association with polyribosomes; when associated with M-664. FT Does not inhibit IRES-mediated protein synthesis; when FT associated with M-664." FT /evidence="ECO:0000269|PubMed:19570978" FT MUTAGEN 695 FT /note="Q->E: Does not inhibit ribosome binding." FT /evidence="ECO:0000269|PubMed:19570978" FT MUTAGEN 745 FT /note="G->D: Does not inhibit ribosome binding." FT /evidence="ECO:0000269|PubMed:19570978" FT MUTAGEN 768 FT /note="E->Q: Does not inhibit ribosome binding. Reduces FT protein synthesis; when associated with Q-477." FT /evidence="ECO:0000269|PubMed:19570978" FT MUTAGEN 797 FT /note="H->L: Does not inhibit ribosome binding." FT /evidence="ECO:0000269|PubMed:19570978" FT CONFLICT 166 FT /note="S -> P (in Ref. 5; AAH34488)" FT /evidence="ECO:0000305" FT STRAND 304..313 FT /evidence="ECO:0007829|PDB:5ZXD" FT STRAND 316..326 FT /evidence="ECO:0007829|PDB:5ZXD" FT STRAND 331..335 FT /evidence="ECO:0007829|PDB:5ZXD" FT HELIX 342..350 FT /evidence="ECO:0007829|PDB:5ZXD" FT STRAND 361..363 FT /evidence="ECO:0007829|PDB:5ZXD" FT HELIX 374..379 FT /evidence="ECO:0007829|PDB:5ZXD" FT HELIX 383..403 FT /evidence="ECO:0007829|PDB:5ZXD" FT HELIX 408..419 FT /evidence="ECO:0007829|PDB:5ZXD" FT HELIX 424..437 FT /evidence="ECO:0007829|PDB:5ZXD" FT HELIX 442..445 FT /evidence="ECO:0007829|PDB:5ZXD" FT HELIX 449..451 FT /evidence="ECO:0007829|PDB:5ZXD" FT HELIX 454..468 FT /evidence="ECO:0007829|PDB:5ZXD" FT STRAND 471..477 FT /evidence="ECO:0007829|PDB:5ZXD" FT TURN 478..481 FT /evidence="ECO:0007829|PDB:5ZXD" FT HELIX 484..495 FT /evidence="ECO:0007829|PDB:5ZXD" FT STRAND 499..504 FT /evidence="ECO:0007829|PDB:5ZXD" FT HELIX 508..514 FT /evidence="ECO:0007829|PDB:5ZXD" FT STRAND 516..522 FT /evidence="ECO:0007829|PDB:5ZXD" FT STRAND 525..531 FT /evidence="ECO:0007829|PDB:5ZXD" FT HELIX 533..563 FT /evidence="ECO:0007829|PDB:5ZXD" FT STRAND 625..632 FT /evidence="ECO:0007829|PDB:5ZXD" FT STRAND 640..648 FT /evidence="ECO:0007829|PDB:5ZXD" FT STRAND 653..657 FT /evidence="ECO:0007829|PDB:5ZXD" FT HELIX 664..672 FT /evidence="ECO:0007829|PDB:5ZXD" FT STRAND 673..675 FT /evidence="ECO:0007829|PDB:5ZXD" FT STRAND 678..684 FT /evidence="ECO:0007829|PDB:5ZXD" FT STRAND 690..693 FT /evidence="ECO:0007829|PDB:5ZXD" FT HELIX 695..698 FT /evidence="ECO:0007829|PDB:5ZXD" FT HELIX 707..715 FT /evidence="ECO:0007829|PDB:5ZXD" FT HELIX 719..728 FT /evidence="ECO:0007829|PDB:5ZXD" FT HELIX 733..737 FT /evidence="ECO:0007829|PDB:5ZXD" FT HELIX 740..742 FT /evidence="ECO:0007829|PDB:5ZXD" FT HELIX 745..758 FT /evidence="ECO:0007829|PDB:5ZXD" FT STRAND 762..768 FT /evidence="ECO:0007829|PDB:5ZXD" FT TURN 769..772 FT /evidence="ECO:0007829|PDB:5ZXD" FT HELIX 775..787 FT /evidence="ECO:0007829|PDB:5ZXD" FT STRAND 790..795 FT /evidence="ECO:0007829|PDB:5ZXD" FT HELIX 799..804 FT /evidence="ECO:0007829|PDB:5ZXD" FT STRAND 808..813 FT /evidence="ECO:0007829|PDB:5ZXD" FT STRAND 816..820 FT /evidence="ECO:0007829|PDB:5ZXD" FT HELIX 824..834 FT /evidence="ECO:0007829|PDB:5ZXD" SQ SEQUENCE 845 AA; 95926 MW; 5C5AA662DF4C99E4 CRC64; MPKAPKQQPP EPEWIGDGES TSPSDKVVKK GKKDKKIKKT FFEELAVEDK QAGEEEKVLK EKEQQQQQQQ QQQKKKRDTR KGRRKKDVDD DGEEKELMER LKKLSVPTSD EEDEVPAPKP RGGKKTKGGN VFAALIQDQS EEEEEEEKHP PKPAKPEKNR INKAVSEEQQ PALKGKKGKE EKSKGKAKPQ NKFAALDNEE EDKEEEIIKE KEPPKQGKEK AKKAEQGSEE EGEGEEEEEE GGESKADDPY AHLSKKEKKK LKKQMEYERQ VASLKAANAA ENDFSVSQAE MSSRQAMLEN ASDIKLEKFS ISAHGKELFV NADLYIVAGR RYGLVGPNGK GKTTLLKHIA NRALSIPPNI DVLLCEQEVV ADETPAVQAV LRADTKRLKL LEEERRLQGQ LEQGDDTAAE RLEKVYEELR ATGAAAAEAK ARRILAGLGF DPEMQNRPTQ KFSGGWRMRV SLARALFMEP TLLMLDEPTN HLDLNAVIWL NNYLQGWRKT LLIVSHDQGF LDDVCTDIIH LDAQRLHYYR GNYMTFKKMY QQKQKELLKQ YEKQEKKLKE LKAGGKSTKQ AEKQTKEALT RKQQKCRRKN QDEESQEAPE LLKRPKEYTV RFTFPDPPPL SPPVLGLHGV TFGYQGQKPL FKNLDFGIDM DSRICIVGPN GVGKSTLLLL LTGKLTPTHG EMRKNHRLKI GFFNQQYAEQ LRMEETPTEY LQRGFNLPYQ DARKCLGRFG LESHAHTIQI CKLSGGQKAR VVFAELACRE PDVLILDEPT NNLDIESIDA LGEAINEYKG AVIVVSHDAR LITETNCQLW VVEEQSVSQI DGDFEDYKRE VLEALGEVMV SRPRE //