Full text data of ABCF1
ABCF1
(ABC50)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
ATP-binding cassette sub-family F member 1 (ATP-binding cassette 50; TNF-alpha-stimulated ABC protein)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
ATP-binding cassette sub-family F member 1 (ATP-binding cassette 50; TNF-alpha-stimulated ABC protein)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q8NE71
ID ABCF1_HUMAN Reviewed; 845 AA.
AC Q8NE71; A2BF75; O14897; Q69YP6;
DT 07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 07-DEC-2004, sequence version 2.
DT 22-JAN-2014, entry version 113.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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
RT necrosis 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.,
RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
RA 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.,
RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
RA Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
RA Durbin R.M., Hubbard T., Sulston J.E., Dunham I., 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
RT project: 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.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., 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 MASS SPECTROMETRY.
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.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-228, AND MASS
RP SPECTROMETRY.
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
RT phosphorylation analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [9]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-573 AND LYS-582, AND MASS
RP SPECTROMETRY.
RC TISSUE=Mammary cancer;
RX PubMed=17370265; DOI=10.1002/pmic.200600410;
RA Denis N.J., Vasilescu J., Lambert J.-P., Smith J.C., Figeys D.;
RT "Tryptic digestion of ubiquitin standards reveals an improved strategy
RT for identifying ubiquitinated proteins by mass spectrometry.";
RL Proteomics 7:868-874(2007).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-595, AND MASS
RP SPECTROMETRY.
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
RA Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
RA Lerenthal Y., Shiloh Y., 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 [11]
RP INTERACTION WITH EIF2S1, ASSOCIATION WITH RIBOSOMES, PHOSPHORYLATION
RP AT SER-109 AND SER-140, MASS SPECTROMETRY, AND MUTAGENESIS OF SER-109
RP 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
RT factor eIF2 and is a target for regulatory phosphorylation by CK2.";
RL Biochem. J. 409:223-231(2008).
RN [12]
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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24 AND SER-228, AND MASS
RP SPECTROMETRY.
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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-228, AND MASS
RP SPECTROMETRY.
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
RT enrichment and fractionation of phosphopeptides with strong anion
RT exchange chromatography.";
RL Proteomics 8:1346-1361(2008).
RN [15]
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.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [16]
RP FUNCTION, ATP-BINDING, ASSOCIATION WITH RIBOSOMES, MUTAGENESIS OF
RP LYS-342; GLN-367; GLY-454; GLU-477; HIS-506; LYS-664; GLN-695;
RP GLY-745; GLU-768 AND 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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-108; SER-109; SER-140
RP AND SER-228, AND MASS SPECTROMETRY.
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-22; SER-105; THR-108;
RP SER-109; SER-140 AND SER-228, AND MASS SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation 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.,
RA Buerckstuemmer T., 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-108; SER-109; SER-140;
RP SER-166 AND SER-228, AND MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
CC -!- FUNCTION: Isoform 2 is required for efficient Cap- and IRES-
CC mediated mRNA translation initiation. Isoform 2 is not involved in
CC the ribosome biogenesis.
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 -!- SUBCELLULAR LOCATION: Isoform 2: Cytoplasm. Nucleus, nucleoplasm.
CC Nucleus envelope.
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.
CC -!- INDUCTION: By TNF in cultured synoviocytes.
CC -!- PTM: Isoform 2 is phosphorylated at phosphoserine and
CC phosphothreonine. Isoform 2 phosphorylation on Ser-109 and Ser-140
CC by CK2; inhibits association of EIF2 with ribosomes.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCF
CC family. EF3 subfamily.
CC -!- SIMILARITY: Contains 2 ABC transporter domains.
CC -!- WEB RESOURCE: Name=ABCMdb; Note=Database for mutations in ABC
CC proteins;
CC URL="http://abcmutations.hegelab.org/proteinDetails?uniprot_id=Q8NE71";
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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; CAI18158.1; -; Genomic_DNA.
DR EMBL; AL662800; CAI18159.1; -; Genomic_DNA.
DR EMBL; AL662825; CAI17836.1; -; Genomic_DNA.
DR EMBL; AL662825; CAI17837.1; -; Genomic_DNA.
DR EMBL; BX000357; CAI18562.1; -; Genomic_DNA.
DR EMBL; BX000357; CAI18563.1; -; Genomic_DNA.
DR EMBL; BX119957; CAM25907.1; -; Genomic_DNA.
DR EMBL; BX248518; CAM25907.1; JOINED; Genomic_DNA.
DR EMBL; BX248518; CAM26017.1; -; Genomic_DNA.
DR EMBL; BX119957; CAM26017.1; JOINED; Genomic_DNA.
DR EMBL; CR753328; CAQ07804.1; -; Genomic_DNA.
DR EMBL; CR388372; CAQ07804.1; JOINED; Genomic_DNA.
DR EMBL; CR388372; CAQ07873.1; -; Genomic_DNA.
DR EMBL; CR753328; CAQ07873.1; JOINED; Genomic_DNA.
DR EMBL; BX927220; CAQ09058.1; -; Genomic_DNA.
DR EMBL; CR759778; CAQ09401.1; -; Genomic_DNA.
DR EMBL; CR847863; CAQ09401.1; JOINED; Genomic_DNA.
DR EMBL; CR847863; CAQ10059.1; -; Genomic_DNA.
DR EMBL; CR759778; CAQ10059.1; JOINED; Genomic_DNA.
DR EMBL; BC034488; AAH34488.1; -; mRNA.
DR EMBL; BC112923; AAI12924.1; -; mRNA.
DR EMBL; AL832430; CAH10648.1; -; mRNA.
DR RefSeq; NP_001020262.1; NM_001025091.1.
DR RefSeq; NP_001081.1; NM_001090.2.
DR UniGene; Hs.655285; -.
DR ProteinModelPortal; Q8NE71; -.
DR SMR; Q8NE71; 301-843.
DR IntAct; Q8NE71; 6.
DR MINT; MINT-1392646; -.
DR STRING; 9606.ENSP00000412553; -.
DR PhosphoSite; Q8NE71; -.
DR DMDM; 56417894; -.
DR PaxDb; Q8NE71; -.
DR PRIDE; Q8NE71; -.
DR DNASU; 23; -.
DR Ensembl; ENST00000326195; ENSP00000313603; ENSG00000204574.
DR Ensembl; ENST00000376545; ENSP00000365728; ENSG00000204574.
DR Ensembl; ENST00000383587; ENSP00000373081; ENSG00000206490.
DR Ensembl; ENST00000383588; ENSP00000373082; ENSG00000206490.
DR Ensembl; ENST00000412443; ENSP00000404726; ENSG00000236342.
DR Ensembl; ENST00000419893; ENSP00000389065; ENSG00000232169.
DR Ensembl; ENST00000420257; ENSP00000391102; ENSG00000225989.
DR Ensembl; ENST00000421042; ENSP00000393143; ENSG00000231129.
DR Ensembl; ENST00000423247; ENSP00000411327; ENSG00000225989.
DR Ensembl; ENST00000426219; ENSP00000414373; ENSG00000231129.
DR Ensembl; ENST00000448939; ENSP00000403526; ENSG00000232169.
DR Ensembl; ENST00000452530; ENSP00000389472; ENSG00000236149.
DR Ensembl; ENST00000457078; ENSP00000412553; ENSG00000236342.
DR Ensembl; ENST00000457111; ENSP00000413319; ENSG00000236149.
DR GeneID; 23; -.
DR KEGG; hsa:23; -.
DR UCSC; uc003nqk.2; human.
DR CTD; 23; -.
DR GeneCards; GC06P030539; -.
DR GeneCards; GC06Pj30529; -.
DR GeneCards; GC06Pk30529; -.
DR GeneCards; GC06Pl30583; -.
DR GeneCards; GC06Pm30617; -.
DR GeneCards; GC06Pn30528; -.
DR GeneCards; GC06Po30530; -.
DR HGNC; HGNC:70; ABCF1.
DR HPA; HPA017578; -.
DR MIM; 603429; gene.
DR neXtProt; NX_Q8NE71; -.
DR PharmGKB; PA24405; -.
DR eggNOG; COG0488; -.
DR HOGENOM; HOG000271637; -.
DR HOVERGEN; HBG050440; -.
DR InParanoid; Q8NE71; -.
DR KO; K06184; -.
DR OMA; IMRIGNT; -.
DR PhylomeDB; Q8NE71; -.
DR ChiTaRS; ABCF1; human.
DR GeneWiki; ABCF1; -.
DR GenomeRNAi; 23; -.
DR NextBio; 69; -.
DR PRO; PR:Q8NE71; -.
DR ArrayExpress; Q8NE71; -.
DR Bgee; Q8NE71; -.
DR CleanEx; HS_ABCF1; -.
DR Genevestigator; Q8NE71; -.
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:0005840; C:ribosome; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR GO; GO:0016887; F:ATPase activity; IEA:InterPro.
DR GO; GO:0043022; F:ribosome binding; IDA:UniProtKB.
DR GO; GO:0008494; F:translation activator activity; IDA:UniProtKB.
DR GO; GO:0008135; F:translation factor activity, nucleic acid binding; TAS:ProtInc.
DR GO; GO:0006200; P:ATP catabolic process; IEA:GOC.
DR GO; GO:0006954; P:inflammatory response; TAS:ProtInc.
DR GO; GO:0006413; P:translational initiation; IMP:UniProtKB.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003439; ABC_transporter-like.
DR InterPro; IPR017871; ABC_transporter_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00005; ABC_tran; 2.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF52540; SSF52540; 3.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 2.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; ATP-binding; Complete proteome;
KW Cytoplasm; Isopeptide bond; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Polymorphism; Reference proteome; Repeat;
KW Ubl conjugation.
FT CHAIN 1 845 ATP-binding cassette sub-family F member
FT 1.
FT /FTId=PRO_0000093318.
FT DOMAIN 304 548 ABC transporter 1.
FT DOMAIN 625 840 ABC transporter 2.
FT NP_BIND 336 343 ATP 1 (By similarity).
FT NP_BIND 658 665 ATP 2 (By similarity).
FT COMPBIAS 141 243 Glu-rich.
FT MOD_RES 22 22 Phosphoserine.
FT MOD_RES 24 24 Phosphoserine.
FT MOD_RES 105 105 Phosphoserine.
FT MOD_RES 108 108 Phosphothreonine.
FT MOD_RES 109 109 Phosphoserine; by CK2.
FT MOD_RES 140 140 Phosphoserine; by CK2.
FT MOD_RES 166 166 Phosphoserine.
FT MOD_RES 228 228 Phosphoserine.
FT MOD_RES 595 595 Phosphoserine.
FT CROSSLNK 573 573 Glycyl lysine isopeptide (Lys-Gly)
FT (interchain with G-Cter in ubiquitin).
FT CROSSLNK 582 582 Glycyl lysine isopeptide (Lys-Gly)
FT (interchain with G-Cter in ubiquitin).
FT VAR_SEQ 226 263 Missing (in isoform 2).
FT /FTId=VSP_012078.
FT VARIANT 198 198 N -> D (in dbSNP:rs6902544).
FT /FTId=VAR_048136.
FT MUTAGEN 109 109 S->A: Reduces phosphorylation. Inhibits
FT strongly phosphorylation by CK2; when
FT associated with S-140. Does not inhibit
FT interaction with EIF2; when associated
FT with S-140. Does not inhibit association
FT with ribosomes; when associated with S-
FT 140. Reduces EIF2 interaction with
FT ribosomes; when associated with S-140.
FT Does not inhibit protein synthesis; when
FT associated with A-140.
FT MUTAGEN 140 140 S->A: Reduces phosphorylation. Inhibits
FT strongly phosphorylation by CK2; when
FT associated with S-109. Does not inhibits
FT interaction with EIF2; when associated
FT with S-109. Does not inhibit association
FT with ribosomes; when associated with S-
FT 109. Reduces EIF2 interaction with
FT ribosomes; when associated with S-109.
FT Does not inhibit protein synthesis; when
FT associated with A-109.
FT MUTAGEN 342 342 K->M: Does not inhibit ribosome binding.
FT Reduces ATP-binding. Inhibits ATP-binding
FT and reduces protein synthesis; when
FT associated with M-664. Shows an enhanced
FT association with polyribosomes; when
FT associated with M-664. Does not inhibit
FT IRES-mediated protein synthesis; when
FT associated with M-664.
FT MUTAGEN 367 367 Q->E: Does not inhibit ribosome binding.
FT MUTAGEN 454 454 G->D: Does not inhibit ribosome binding.
FT MUTAGEN 477 477 E->Q: Does not inhibit ribosome binding.
FT Reduces protein synthesis; when
FT associated with Q-768.
FT MUTAGEN 506 506 H->L: Does not inhibit ribosome binding.
FT MUTAGEN 664 664 K->M: Does not inhibit ribosome binding.
FT Reduces ATP-binding. Inhibits ATP-binding
FT and reduces protein synthesis; when
FT associated with M-342. Shows a reduced
FT association with polyribosomes; when
FT associated with M-664. Does not inhibit
FT IRES-mediated protein synthesis; when
FT associated with M-664.
FT MUTAGEN 695 695 Q->E: Does not inhibit ribosome binding.
FT MUTAGEN 745 745 G->D: Does not inhibit ribosome binding.
FT MUTAGEN 768 768 E->Q: Does not inhibit ribosome binding.
FT Reduces protein synthesis; when
FT associated with Q-477.
FT MUTAGEN 797 797 H->L: Does not inhibit ribosome binding.
FT CONFLICT 166 166 S -> P (in Ref. 5; AAH34488).
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
//
ID ABCF1_HUMAN Reviewed; 845 AA.
AC Q8NE71; A2BF75; O14897; Q69YP6;
DT 07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 07-DEC-2004, sequence version 2.
DT 22-JAN-2014, entry version 113.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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
RT necrosis 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.,
RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
RA 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.,
RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
RA Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
RA Durbin R.M., Hubbard T., Sulston J.E., Dunham I., 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
RT project: 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.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., 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 MASS SPECTROMETRY.
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.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-228, AND MASS
RP SPECTROMETRY.
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
RT phosphorylation analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [9]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-573 AND LYS-582, AND MASS
RP SPECTROMETRY.
RC TISSUE=Mammary cancer;
RX PubMed=17370265; DOI=10.1002/pmic.200600410;
RA Denis N.J., Vasilescu J., Lambert J.-P., Smith J.C., Figeys D.;
RT "Tryptic digestion of ubiquitin standards reveals an improved strategy
RT for identifying ubiquitinated proteins by mass spectrometry.";
RL Proteomics 7:868-874(2007).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-595, AND MASS
RP SPECTROMETRY.
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
RA Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
RA Lerenthal Y., Shiloh Y., 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 [11]
RP INTERACTION WITH EIF2S1, ASSOCIATION WITH RIBOSOMES, PHOSPHORYLATION
RP AT SER-109 AND SER-140, MASS SPECTROMETRY, AND MUTAGENESIS OF SER-109
RP 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
RT factor eIF2 and is a target for regulatory phosphorylation by CK2.";
RL Biochem. J. 409:223-231(2008).
RN [12]
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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24 AND SER-228, AND MASS
RP SPECTROMETRY.
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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-228, AND MASS
RP SPECTROMETRY.
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
RT enrichment and fractionation of phosphopeptides with strong anion
RT exchange chromatography.";
RL Proteomics 8:1346-1361(2008).
RN [15]
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.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [16]
RP FUNCTION, ATP-BINDING, ASSOCIATION WITH RIBOSOMES, MUTAGENESIS OF
RP LYS-342; GLN-367; GLY-454; GLU-477; HIS-506; LYS-664; GLN-695;
RP GLY-745; GLU-768 AND 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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-108; SER-109; SER-140
RP AND SER-228, AND MASS SPECTROMETRY.
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-22; SER-105; THR-108;
RP SER-109; SER-140 AND SER-228, AND MASS SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation 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.,
RA Buerckstuemmer T., 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-108; SER-109; SER-140;
RP SER-166 AND SER-228, AND MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
CC -!- FUNCTION: Isoform 2 is required for efficient Cap- and IRES-
CC mediated mRNA translation initiation. Isoform 2 is not involved in
CC the ribosome biogenesis.
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 -!- SUBCELLULAR LOCATION: Isoform 2: Cytoplasm. Nucleus, nucleoplasm.
CC Nucleus envelope.
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.
CC -!- INDUCTION: By TNF in cultured synoviocytes.
CC -!- PTM: Isoform 2 is phosphorylated at phosphoserine and
CC phosphothreonine. Isoform 2 phosphorylation on Ser-109 and Ser-140
CC by CK2; inhibits association of EIF2 with ribosomes.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCF
CC family. EF3 subfamily.
CC -!- SIMILARITY: Contains 2 ABC transporter domains.
CC -!- WEB RESOURCE: Name=ABCMdb; Note=Database for mutations in ABC
CC proteins;
CC URL="http://abcmutations.hegelab.org/proteinDetails?uniprot_id=Q8NE71";
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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; CAI18158.1; -; Genomic_DNA.
DR EMBL; AL662800; CAI18159.1; -; Genomic_DNA.
DR EMBL; AL662825; CAI17836.1; -; Genomic_DNA.
DR EMBL; AL662825; CAI17837.1; -; Genomic_DNA.
DR EMBL; BX000357; CAI18562.1; -; Genomic_DNA.
DR EMBL; BX000357; CAI18563.1; -; Genomic_DNA.
DR EMBL; BX119957; CAM25907.1; -; Genomic_DNA.
DR EMBL; BX248518; CAM25907.1; JOINED; Genomic_DNA.
DR EMBL; BX248518; CAM26017.1; -; Genomic_DNA.
DR EMBL; BX119957; CAM26017.1; JOINED; Genomic_DNA.
DR EMBL; CR753328; CAQ07804.1; -; Genomic_DNA.
DR EMBL; CR388372; CAQ07804.1; JOINED; Genomic_DNA.
DR EMBL; CR388372; CAQ07873.1; -; Genomic_DNA.
DR EMBL; CR753328; CAQ07873.1; JOINED; Genomic_DNA.
DR EMBL; BX927220; CAQ09058.1; -; Genomic_DNA.
DR EMBL; CR759778; CAQ09401.1; -; Genomic_DNA.
DR EMBL; CR847863; CAQ09401.1; JOINED; Genomic_DNA.
DR EMBL; CR847863; CAQ10059.1; -; Genomic_DNA.
DR EMBL; CR759778; CAQ10059.1; JOINED; Genomic_DNA.
DR EMBL; BC034488; AAH34488.1; -; mRNA.
DR EMBL; BC112923; AAI12924.1; -; mRNA.
DR EMBL; AL832430; CAH10648.1; -; mRNA.
DR RefSeq; NP_001020262.1; NM_001025091.1.
DR RefSeq; NP_001081.1; NM_001090.2.
DR UniGene; Hs.655285; -.
DR ProteinModelPortal; Q8NE71; -.
DR SMR; Q8NE71; 301-843.
DR IntAct; Q8NE71; 6.
DR MINT; MINT-1392646; -.
DR STRING; 9606.ENSP00000412553; -.
DR PhosphoSite; Q8NE71; -.
DR DMDM; 56417894; -.
DR PaxDb; Q8NE71; -.
DR PRIDE; Q8NE71; -.
DR DNASU; 23; -.
DR Ensembl; ENST00000326195; ENSP00000313603; ENSG00000204574.
DR Ensembl; ENST00000376545; ENSP00000365728; ENSG00000204574.
DR Ensembl; ENST00000383587; ENSP00000373081; ENSG00000206490.
DR Ensembl; ENST00000383588; ENSP00000373082; ENSG00000206490.
DR Ensembl; ENST00000412443; ENSP00000404726; ENSG00000236342.
DR Ensembl; ENST00000419893; ENSP00000389065; ENSG00000232169.
DR Ensembl; ENST00000420257; ENSP00000391102; ENSG00000225989.
DR Ensembl; ENST00000421042; ENSP00000393143; ENSG00000231129.
DR Ensembl; ENST00000423247; ENSP00000411327; ENSG00000225989.
DR Ensembl; ENST00000426219; ENSP00000414373; ENSG00000231129.
DR Ensembl; ENST00000448939; ENSP00000403526; ENSG00000232169.
DR Ensembl; ENST00000452530; ENSP00000389472; ENSG00000236149.
DR Ensembl; ENST00000457078; ENSP00000412553; ENSG00000236342.
DR Ensembl; ENST00000457111; ENSP00000413319; ENSG00000236149.
DR GeneID; 23; -.
DR KEGG; hsa:23; -.
DR UCSC; uc003nqk.2; human.
DR CTD; 23; -.
DR GeneCards; GC06P030539; -.
DR GeneCards; GC06Pj30529; -.
DR GeneCards; GC06Pk30529; -.
DR GeneCards; GC06Pl30583; -.
DR GeneCards; GC06Pm30617; -.
DR GeneCards; GC06Pn30528; -.
DR GeneCards; GC06Po30530; -.
DR HGNC; HGNC:70; ABCF1.
DR HPA; HPA017578; -.
DR MIM; 603429; gene.
DR neXtProt; NX_Q8NE71; -.
DR PharmGKB; PA24405; -.
DR eggNOG; COG0488; -.
DR HOGENOM; HOG000271637; -.
DR HOVERGEN; HBG050440; -.
DR InParanoid; Q8NE71; -.
DR KO; K06184; -.
DR OMA; IMRIGNT; -.
DR PhylomeDB; Q8NE71; -.
DR ChiTaRS; ABCF1; human.
DR GeneWiki; ABCF1; -.
DR GenomeRNAi; 23; -.
DR NextBio; 69; -.
DR PRO; PR:Q8NE71; -.
DR ArrayExpress; Q8NE71; -.
DR Bgee; Q8NE71; -.
DR CleanEx; HS_ABCF1; -.
DR Genevestigator; Q8NE71; -.
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:0005840; C:ribosome; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR GO; GO:0016887; F:ATPase activity; IEA:InterPro.
DR GO; GO:0043022; F:ribosome binding; IDA:UniProtKB.
DR GO; GO:0008494; F:translation activator activity; IDA:UniProtKB.
DR GO; GO:0008135; F:translation factor activity, nucleic acid binding; TAS:ProtInc.
DR GO; GO:0006200; P:ATP catabolic process; IEA:GOC.
DR GO; GO:0006954; P:inflammatory response; TAS:ProtInc.
DR GO; GO:0006413; P:translational initiation; IMP:UniProtKB.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003439; ABC_transporter-like.
DR InterPro; IPR017871; ABC_transporter_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00005; ABC_tran; 2.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF52540; SSF52540; 3.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 2.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; ATP-binding; Complete proteome;
KW Cytoplasm; Isopeptide bond; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Polymorphism; Reference proteome; Repeat;
KW Ubl conjugation.
FT CHAIN 1 845 ATP-binding cassette sub-family F member
FT 1.
FT /FTId=PRO_0000093318.
FT DOMAIN 304 548 ABC transporter 1.
FT DOMAIN 625 840 ABC transporter 2.
FT NP_BIND 336 343 ATP 1 (By similarity).
FT NP_BIND 658 665 ATP 2 (By similarity).
FT COMPBIAS 141 243 Glu-rich.
FT MOD_RES 22 22 Phosphoserine.
FT MOD_RES 24 24 Phosphoserine.
FT MOD_RES 105 105 Phosphoserine.
FT MOD_RES 108 108 Phosphothreonine.
FT MOD_RES 109 109 Phosphoserine; by CK2.
FT MOD_RES 140 140 Phosphoserine; by CK2.
FT MOD_RES 166 166 Phosphoserine.
FT MOD_RES 228 228 Phosphoserine.
FT MOD_RES 595 595 Phosphoserine.
FT CROSSLNK 573 573 Glycyl lysine isopeptide (Lys-Gly)
FT (interchain with G-Cter in ubiquitin).
FT CROSSLNK 582 582 Glycyl lysine isopeptide (Lys-Gly)
FT (interchain with G-Cter in ubiquitin).
FT VAR_SEQ 226 263 Missing (in isoform 2).
FT /FTId=VSP_012078.
FT VARIANT 198 198 N -> D (in dbSNP:rs6902544).
FT /FTId=VAR_048136.
FT MUTAGEN 109 109 S->A: Reduces phosphorylation. Inhibits
FT strongly phosphorylation by CK2; when
FT associated with S-140. Does not inhibit
FT interaction with EIF2; when associated
FT with S-140. Does not inhibit association
FT with ribosomes; when associated with S-
FT 140. Reduces EIF2 interaction with
FT ribosomes; when associated with S-140.
FT Does not inhibit protein synthesis; when
FT associated with A-140.
FT MUTAGEN 140 140 S->A: Reduces phosphorylation. Inhibits
FT strongly phosphorylation by CK2; when
FT associated with S-109. Does not inhibits
FT interaction with EIF2; when associated
FT with S-109. Does not inhibit association
FT with ribosomes; when associated with S-
FT 109. Reduces EIF2 interaction with
FT ribosomes; when associated with S-109.
FT Does not inhibit protein synthesis; when
FT associated with A-109.
FT MUTAGEN 342 342 K->M: Does not inhibit ribosome binding.
FT Reduces ATP-binding. Inhibits ATP-binding
FT and reduces protein synthesis; when
FT associated with M-664. Shows an enhanced
FT association with polyribosomes; when
FT associated with M-664. Does not inhibit
FT IRES-mediated protein synthesis; when
FT associated with M-664.
FT MUTAGEN 367 367 Q->E: Does not inhibit ribosome binding.
FT MUTAGEN 454 454 G->D: Does not inhibit ribosome binding.
FT MUTAGEN 477 477 E->Q: Does not inhibit ribosome binding.
FT Reduces protein synthesis; when
FT associated with Q-768.
FT MUTAGEN 506 506 H->L: Does not inhibit ribosome binding.
FT MUTAGEN 664 664 K->M: Does not inhibit ribosome binding.
FT Reduces ATP-binding. Inhibits ATP-binding
FT and reduces protein synthesis; when
FT associated with M-342. Shows a reduced
FT association with polyribosomes; when
FT associated with M-664. Does not inhibit
FT IRES-mediated protein synthesis; when
FT associated with M-664.
FT MUTAGEN 695 695 Q->E: Does not inhibit ribosome binding.
FT MUTAGEN 745 745 G->D: Does not inhibit ribosome binding.
FT MUTAGEN 768 768 E->Q: Does not inhibit ribosome binding.
FT Reduces protein synthesis; when
FT associated with Q-477.
FT MUTAGEN 797 797 H->L: Does not inhibit ribosome binding.
FT CONFLICT 166 166 S -> P (in Ref. 5; AAH34488).
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
//
MIM
603429
*RECORD*
*FIELD* NO
603429
*FIELD* TI
*603429 ATP-BINDING CASSETTE, SUBFAMILY F, MEMBER 1; ABCF1
;;ATP-BINDING CASSETTE 50; ABC50
read more*FIELD* TX
CLONING
The family of ATP-binding cassette (ABC) proteins (e.g., 601691) is
extensive and is responsible for the transport of a variety of molecules
across biologic membranes. Using differential display PCR to identify
genes that are modulated by TNF-alpha (191160) in synoviocytes, Richard
et al. (1998) isolated a cDNA encoding a novel member of the ABC family,
named ABC50. The deduced 807-amino acid ABC50 protein has 2 ABC
transporter family signature motifs, 2 ATP/GTP-binding site A motifs,
and 3 nuclear localization patterns. The authors found that ABC50 also
contains a signature sequence that is characteristic of yeast cluster IV
ABC proteins. Unlike most previously reported family members, ABC50 does
not contain a transmembrane domain. Northern blot analysis demonstrated
ubiquitous expression of a 3.7-kb ABC50 transcript in human tissues.
TNF-alpha stimulation increased the expression of the ABC50 mRNA in
cultured synoviocytes.
GENE STRUCTURE
Berezikov et al. (2007) determined that intron 13 of the ABCF1 gene
contains the microRNA MIRN877 (611619).
MAPPING
Richard et al. (1998) used fluorescence in situ hybridization to map the
human ABC50 gene to chromosome 6p21.33.
*FIELD* RF
1. Berezikov, E.; Chung, W.-J.; Willis, J.; Cuppen, E.; Lai, E. C.
: Mammalian mirtron genes. Molec. Cell 28: 328-336, 2007.
2. Richard, M.; Drouin, R.; Beaulieu, A. D.: ABC50, a novel human
ATP-binding cassette protein found in tumor necrosis factor-alpha-stimulated
synoviocytes. Genomics 53: 137-145, 1998.
*FIELD* CN
Patricia A. Hartz - updated: 11/26/2007
*FIELD* CD
Sheryl A. Jankowski: 1/13/1999
*FIELD* ED
mgross: 11/26/2007
carol: 11/11/1999
psherman: 1/14/1999
*RECORD*
*FIELD* NO
603429
*FIELD* TI
*603429 ATP-BINDING CASSETTE, SUBFAMILY F, MEMBER 1; ABCF1
;;ATP-BINDING CASSETTE 50; ABC50
read more*FIELD* TX
CLONING
The family of ATP-binding cassette (ABC) proteins (e.g., 601691) is
extensive and is responsible for the transport of a variety of molecules
across biologic membranes. Using differential display PCR to identify
genes that are modulated by TNF-alpha (191160) in synoviocytes, Richard
et al. (1998) isolated a cDNA encoding a novel member of the ABC family,
named ABC50. The deduced 807-amino acid ABC50 protein has 2 ABC
transporter family signature motifs, 2 ATP/GTP-binding site A motifs,
and 3 nuclear localization patterns. The authors found that ABC50 also
contains a signature sequence that is characteristic of yeast cluster IV
ABC proteins. Unlike most previously reported family members, ABC50 does
not contain a transmembrane domain. Northern blot analysis demonstrated
ubiquitous expression of a 3.7-kb ABC50 transcript in human tissues.
TNF-alpha stimulation increased the expression of the ABC50 mRNA in
cultured synoviocytes.
GENE STRUCTURE
Berezikov et al. (2007) determined that intron 13 of the ABCF1 gene
contains the microRNA MIRN877 (611619).
MAPPING
Richard et al. (1998) used fluorescence in situ hybridization to map the
human ABC50 gene to chromosome 6p21.33.
*FIELD* RF
1. Berezikov, E.; Chung, W.-J.; Willis, J.; Cuppen, E.; Lai, E. C.
: Mammalian mirtron genes. Molec. Cell 28: 328-336, 2007.
2. Richard, M.; Drouin, R.; Beaulieu, A. D.: ABC50, a novel human
ATP-binding cassette protein found in tumor necrosis factor-alpha-stimulated
synoviocytes. Genomics 53: 137-145, 1998.
*FIELD* CN
Patricia A. Hartz - updated: 11/26/2007
*FIELD* CD
Sheryl A. Jankowski: 1/13/1999
*FIELD* ED
mgross: 11/26/2007
carol: 11/11/1999
psherman: 1/14/1999