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ATP-binding cassette sub-family F member 1 (ATP-binding cassette 50) (TNF-alpha-stimulated ABC protein)

 ABCF1_HUMAN             Reviewed;         845 AA.
Q8NE71; A2BF75; O14897; Q69YP6;
07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
07-DEC-2004, sequence version 2.
28-MAR-2018, entry version 153.
RecName: Full=ATP-binding cassette sub-family F member 1;
AltName: Full=ATP-binding cassette 50;
AltName: Full=TNF-alpha-stimulated ABC protein;
Name=ABCF1; Synonyms=ABC50;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND TISSUE SPECIFICITY.
PubMed=9790762; DOI=10.1006/geno.1998.5480;
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).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Shiina S., Tamiya G., Oka A., Inoko H.;
"Homo sapiens 2,229,817bp genomic DNA of 6p21.3 HLA class I region.";
Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Shiina T., Ota M., Katsuyama Y., Hashimoto N., Inoko H.;
"Genome diversity in HLA: a new strategy for detection of genetic
polymorphisms in expressed genes within the HLA class III and class I
regions.";
Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=14574404; DOI=10.1038/nature02055;
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Embryonic stem cell, and Testis;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 160-845 (ISOFORM 1).
TISSUE=Melanoma;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-105; THR-108; SER-109;
SER-140 AND SER-228, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-228, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein
phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-595, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic kidney;
PubMed=17525332; DOI=10.1126/science.1140321;
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
"ATM and ATR substrate analysis reveals extensive protein networks
responsive to DNA damage.";
Science 316:1160-1166(2007).
[10]
INTERACTION WITH EIF2S1, ASSOCIATION WITH RIBOSOMES, PHOSPHORYLATION
AT SER-109 AND SER-140, IDENTIFICATION BY MASS SPECTROMETRY, AND
MUTAGENESIS OF SER-109 AND SER-140.
PubMed=17894550; DOI=10.1042/BJ20070811;
Paytubi S., Morrice N.A., Boudeau J., Proud C.G.;
"The N-terminal region of ABC50 interacts with eukaryotic initiation
factor eIF2 and is a target for regulatory phosphorylation by CK2.";
Biochem. J. 409:223-231(2008).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Platelet;
PubMed=18088087; DOI=10.1021/pr0704130;
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
Schuetz C., Walter U., Gambaryan S., Sickmann A.;
"Phosphoproteome of resting human platelets.";
J. Proteome Res. 7:526-534(2008).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24 AND SER-228, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-228, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=18318008; DOI=10.1002/pmic.200700884;
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
Zou H., Gu J.;
"Large-scale phosphoproteome analysis of human liver tissue by
enrichment and fractionation of phosphopeptides with strong anion
exchange chromatography.";
Proteomics 8:1346-1361(2008).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[15]
FUNCTION, ATP-BINDING, ASSOCIATION WITH RIBOSOMES, MUTAGENESIS OF
LYS-342; GLN-367; GLY-454; GLU-477; HIS-506; LYS-664; GLN-695;
GLY-745; GLU-768 AND HIS-797, AND SUBCELLULAR LOCATION.
PubMed=19570978; DOI=10.1074/jbc.M109.031625;
Paytubi S., Wang X., Lam Y.W., Izquierdo L., Hunter M.J., Jan E.,
Hundal H.S., Proud C.G.;
"ABC50 promotes translation initiation in mammalian cells.";
J. Biol. Chem. 284:24061-24073(2009).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-108; SER-109; SER-140
AND SER-228, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22; SER-105; THR-108;
SER-109; SER-140 AND SER-228, AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[18]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-108; SER-109; SER-140;
SER-166 AND SER-228, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22; SER-105; THR-108;
SER-109; SER-140; SER-166; SER-228 AND SER-595, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-105 AND THR-108, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
-!- FUNCTION: Isoform 2 is required for efficient Cap- and IRES-
mediated mRNA translation initiation. Isoform 2 is not involved in
the ribosome biogenesis. {ECO:0000269|PubMed:19570978}.
-!- SUBUNIT: Isoform 2 interacts (via N-terminus) with EIF2S1; the
interaction is independent of its phosphorylated status. Isoform 2
associates (via both ABC transporter domains) with the ribosomes.
{ECO:0000269|PubMed:17894550}.
-!- SUBCELLULAR LOCATION: Isoform 2: Cytoplasm
{ECO:0000269|PubMed:19570978}. Nucleus, nucleoplasm
{ECO:0000269|PubMed:19570978}. Nucleus envelope
{ECO:0000269|PubMed:19570978}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q8NE71-1; Sequence=Displayed;
Name=2;
IsoId=Q8NE71-2; Sequence=VSP_012078;
-!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:9790762}.
-!- INDUCTION: By TNF in cultured synoviocytes.
-!- PTM: Isoform 2 is phosphorylated at phosphoserine and
phosphothreonine. Isoform 2 phosphorylation on Ser-109 and Ser-140
by CK2 inhibits association of EIF2 with ribosomes.
{ECO:0000269|PubMed:17894550}.
-!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCF
family. EF3 subfamily. {ECO:0000305}.
-!- WEB RESOURCE: Name=ABCMdb; Note=Database for mutations in ABC
proteins;
URL="http://abcmutations.hegelab.org/proteinDetails?uniprot_id=Q8NE71";
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EMBL; AF027302; AAC70891.1; -; mRNA.
EMBL; BA000025; BAB63325.1; -; Genomic_DNA.
EMBL; AB088096; BAC54928.1; -; Genomic_DNA.
EMBL; AL662800; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL662825; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BX000357; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BX119957; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BX248518; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CR753328; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CR388372; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BX927220; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CR759778; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CR847863; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC034488; AAH34488.1; -; mRNA.
EMBL; BC112923; AAI12924.1; -; mRNA.
EMBL; AL832430; CAH10648.1; -; mRNA.
CCDS; CCDS34380.1; -. [Q8NE71-1]
CCDS; CCDS34381.1; -. [Q8NE71-2]
RefSeq; NP_001020262.1; NM_001025091.1. [Q8NE71-1]
RefSeq; NP_001081.1; NM_001090.2. [Q8NE71-2]
UniGene; Hs.655285; -.
ProteinModelPortal; Q8NE71; -.
BioGrid; 106541; 64.
DIP; DIP-50666N; -.
IntAct; Q8NE71; 22.
MINT; Q8NE71; -.
STRING; 9606.ENSP00000313603; -.
iPTMnet; Q8NE71; -.
PhosphoSitePlus; Q8NE71; -.
SwissPalm; Q8NE71; -.
BioMuta; ABCF1; -.
DMDM; 56417894; -.
EPD; Q8NE71; -.
MaxQB; Q8NE71; -.
PaxDb; Q8NE71; -.
PeptideAtlas; Q8NE71; -.
PRIDE; Q8NE71; -.
DNASU; 23; -.
Ensembl; ENST00000326195; ENSP00000313603; ENSG00000204574. [Q8NE71-1]
Ensembl; ENST00000376545; ENSP00000365728; ENSG00000204574. [Q8NE71-2]
Ensembl; ENST00000383587; ENSP00000373081; ENSG00000206490. [Q8NE71-2]
Ensembl; ENST00000383588; ENSP00000373082; ENSG00000206490. [Q8NE71-1]
Ensembl; ENST00000412443; ENSP00000404726; ENSG00000236342. [Q8NE71-2]
Ensembl; ENST00000419893; ENSP00000389065; ENSG00000232169. [Q8NE71-1]
Ensembl; ENST00000420257; ENSP00000391102; ENSG00000225989. [Q8NE71-2]
Ensembl; ENST00000421042; ENSP00000393143; ENSG00000231129. [Q8NE71-2]
Ensembl; ENST00000423247; ENSP00000411327; ENSG00000225989. [Q8NE71-1]
Ensembl; ENST00000426219; ENSP00000414373; ENSG00000231129. [Q8NE71-1]
Ensembl; ENST00000448939; ENSP00000403526; ENSG00000232169. [Q8NE71-2]
Ensembl; ENST00000452530; ENSP00000389472; ENSG00000236149. [Q8NE71-2]
Ensembl; ENST00000457078; ENSP00000412553; ENSG00000236342. [Q8NE71-1]
Ensembl; ENST00000457111; ENSP00000413319; ENSG00000236149. [Q8NE71-1]
GeneID; 23; -.
KEGG; hsa:23; -.
UCSC; uc003nql.4; human. [Q8NE71-1]
CTD; 23; -.
DisGeNET; 23; -.
EuPathDB; HostDB:ENSG00000204574.12; -.
GeneCards; ABCF1; -.
HGNC; HGNC:70; ABCF1.
HPA; HPA017578; -.
MIM; 603429; gene.
neXtProt; NX_Q8NE71; -.
OpenTargets; ENSG00000204574; -.
PharmGKB; PA24405; -.
eggNOG; KOG0066; Eukaryota.
eggNOG; COG0488; LUCA.
GeneTree; ENSGT00630000089843; -.
HOGENOM; HOG000271637; -.
HOVERGEN; HBG050440; -.
InParanoid; Q8NE71; -.
KO; K06184; -.
OMA; KEYTVRF; -.
OrthoDB; EOG091G031N; -.
PhylomeDB; Q8NE71; -.
TreeFam; TF105207; -.
Reactome; R-HSA-382556; ABC-family proteins mediated transport.
SIGNOR; Q8NE71; -.
ChiTaRS; ABCF1; human.
GeneWiki; ABCF1; -.
GenomeRNAi; 23; -.
PRO; PR:Q8NE71; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000204574; -.
CleanEx; HS_ABCF1; -.
ExpressionAtlas; Q8NE71; baseline and differential.
Genevisible; Q8NE71; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0005635; C:nuclear envelope; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
GO; GO:0042788; C:polysomal ribosome; IDA:UniProtKB.
GO; GO:0005840; C:ribosome; IEA:Ensembl.
GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
GO; GO:0016887; F:ATPase activity; IEA:InterPro.
GO; GO:0043022; F:ribosome binding; IDA:UniProtKB.
GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
GO; GO:0008494; F:translation activator activity; IDA:UniProtKB.
GO; GO:0008135; F:translation factor activity, RNA binding; TAS:ProtInc.
GO; GO:0006954; P:inflammatory response; TAS:ProtInc.
GO; GO:0045727; P:positive regulation of translation; IDA:UniProtKB.
GO; GO:0006412; P:translation; TAS:ProtInc.
GO; GO:0006413; P:translational initiation; IMP:UniProtKB.
GO; GO:0055085; P:transmembrane transport; TAS:Reactome.
InterPro; IPR003593; AAA+_ATPase.
InterPro; IPR032781; ABC_tran_Xtn.
InterPro; IPR003439; ABC_transporter-like.
InterPro; IPR017871; ABC_transporter_CS.
InterPro; IPR027417; P-loop_NTPase.
Pfam; PF00005; ABC_tran; 2.
Pfam; PF12848; ABC_tran_Xtn; 1.
SMART; SM00382; AAA; 2.
SUPFAM; SSF52540; SSF52540; 3.
PROSITE; PS00211; ABC_TRANSPORTER_1; 2.
PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
1: Evidence at protein level;
Activator; Alternative splicing; ATP-binding; Complete proteome;
Cytoplasm; Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome; Repeat.
CHAIN 1 845 ATP-binding cassette sub-family F member
1.
/FTId=PRO_0000093318.
DOMAIN 304 548 ABC transporter 1. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
DOMAIN 625 840 ABC transporter 2. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
NP_BIND 336 343 ATP 1. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
NP_BIND 658 665 ATP 2. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
COMPBIAS 141 243 Glu-rich.
MOD_RES 22 22 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 24 24 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 105 105 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 108 108 Phosphothreonine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 109 109 Phosphoserine; by CK2.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:17894550}.
MOD_RES 140 140 Phosphoserine; by CK2.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:17894550}.
MOD_RES 166 166 Phosphoserine.
{ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 228 228 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18318008,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 595 595 Phosphoserine.
{ECO:0000244|PubMed:17525332,
ECO:0000244|PubMed:23186163}.
VAR_SEQ 226 263 Missing (in isoform 2).
{ECO:0000303|PubMed:9790762}.
/FTId=VSP_012078.
VARIANT 198 198 N -> D (in dbSNP:rs6902544).
/FTId=VAR_048136.
MUTAGEN 109 109 S->A: Reduces phosphorylation. Inhibits
strongly phosphorylation by CK2; when
associated with S-140. Does not inhibit
interaction with EIF2; when associated
with S-140. Does not inhibit association
with ribosomes; when associated with S-
140. Reduces EIF2 interaction with
ribosomes; when associated with S-140.
Does not inhibit protein synthesis; when
associated with A-140.
{ECO:0000269|PubMed:17894550}.
MUTAGEN 140 140 S->A: Reduces phosphorylation. Inhibits
strongly phosphorylation by CK2; when
associated with S-109. Does not inhibits
interaction with EIF2; when associated
with S-109. Does not inhibit association
with ribosomes; when associated with S-
109. Reduces EIF2 interaction with
ribosomes; when associated with S-109.
Does not inhibit protein synthesis; when
associated with A-109.
{ECO:0000269|PubMed:17894550}.
MUTAGEN 342 342 K->M: Does not inhibit ribosome binding.
Reduces ATP-binding. Inhibits ATP-binding
and reduces protein synthesis; when
associated with M-664. Shows an enhanced
association with polyribosomes; when
associated with M-664. Does not inhibit
IRES-mediated protein synthesis; when
associated with M-664.
{ECO:0000269|PubMed:19570978}.
MUTAGEN 367 367 Q->E: Does not inhibit ribosome binding.
{ECO:0000269|PubMed:19570978}.
MUTAGEN 454 454 G->D: Does not inhibit ribosome binding.
{ECO:0000269|PubMed:19570978}.
MUTAGEN 477 477 E->Q: Does not inhibit ribosome binding.
Reduces protein synthesis; when
associated with Q-768.
{ECO:0000269|PubMed:19570978}.
MUTAGEN 506 506 H->L: Does not inhibit ribosome binding.
{ECO:0000269|PubMed:19570978}.
MUTAGEN 664 664 K->M: Does not inhibit ribosome binding.
Reduces ATP-binding. Inhibits ATP-binding
and reduces protein synthesis; when
associated with M-342. Shows a reduced
association with polyribosomes; when
associated with M-664. Does not inhibit
IRES-mediated protein synthesis; when
associated with M-664.
{ECO:0000269|PubMed:19570978}.
MUTAGEN 695 695 Q->E: Does not inhibit ribosome binding.
{ECO:0000269|PubMed:19570978}.
MUTAGEN 745 745 G->D: Does not inhibit ribosome binding.
{ECO:0000269|PubMed:19570978}.
MUTAGEN 768 768 E->Q: Does not inhibit ribosome binding.
Reduces protein synthesis; when
associated with Q-477.
{ECO:0000269|PubMed:19570978}.
MUTAGEN 797 797 H->L: Does not inhibit ribosome binding.
{ECO:0000269|PubMed:19570978}.
CONFLICT 166 166 S -> P (in Ref. 5; AAH34488).
{ECO:0000305}.
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


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