ABCF1_HUMAN
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 03-AUG-2022, entry version 183.
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";
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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; 139.
DR DIP; DIP-50666N; -.
DR IntAct; Q8NE71; 43.
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; Q8NE71; -.
DR PeptideAtlas; Q8NE71; -.
DR PRIDE; Q8NE71; -.
DR ProteomicsDB; 73130; -. [Q8NE71-1]
DR ProteomicsDB; 73131; -. [Q8NE71-2]
DR Antibodypedia; 2796; 309 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 CTD; 23; -.
DR DisGeNET; 23; -.
DR GeneCards; ABCF1; -.
DR HGNC; HGNC:70; ABCF1.
DR HPA; ENSG00000204574; Tissue enhanced (skeletal).
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; RYFMDKI; -.
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; 686 hits in 1087 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 99 other tissues.
DR ExpressionAtlas; Q8NE71; baseline and differential.
DR Genevisible; Q8NE71; HS.
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: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 Gene3D; 3.40.50.300; -; 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 Pfam; PF00005; ABC_tran; 2.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 2.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
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 S-
FT 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 S-
FT 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
