Q8NE71 (ABCF1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
ATP-binding cassette sub-family F member 1

Alternative name(s):
ATP-binding cassette 50
TNF-alpha-stimulated ABC protein

Gene names

Name:	ABCF1
Synonyms:	ABC50

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	845 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Isoform 2 is required for efficient Cap- and IRES-mediated mRNA translation initiation. Isoform 2 is not involved in the ribosome biogenesis. Ref.15
Subunit structure	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. Ref.11
Subcellular location	Isoform 2: Cytoplasm. Nucleus › nucleoplasm. Nucleus envelope Ref.15.
Tissue specificity	Ubiquitous. Ref.1
Induction	By TNF in cultured synoviocytes.
Post-translational modification	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. Ref.11
Sequence similarities	Belongs to the ABC transporter superfamily. ABCF family. EF3 subfamily. Contains 2 ABC transporter domains.

Ontologies

Keywords
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat
Ligand	ATP-binding Nucleotide-binding
Molecular function	Activator
PTM	Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	ATP catabolic process Inferred from electronic annotation. Source: GOC inflammatory response Traceable author statement Ref.1. Source: ProtInc translational initiation Inferred from mutant phenotype Ref.15. Source: UniProtKB
Cellular_component	nuclear envelope Inferred from direct assay Ref.15. Source: UniProtKB nucleoplasm Inferred from direct assay Ref.15. Source: UniProtKB polysomal ribosome Inferred from direct assay Ref.15. Source: UniProtKB ribosome Inferred from electronic annotation. Source: Compara
Molecular_function	ATP binding Inferred from direct assay Ref.15. Source: UniProtKB ATPase activity Inferred from electronic annotation. Source: InterPro ribosome binding Inferred from direct assay Ref.11Ref.15. Source: UniProtKB translation activator activity Inferred from direct assay Ref.15. Source: UniProtKB translation factor activity, nucleic acid binding Traceable author statement Ref.1. Source: ProtInc
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q8NE71-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q8NE71-2)

The sequence of this isoform differs from the canonical sequence as follows:
     226-263: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 845	845	ATP-binding cassette sub-family F member 1		PRO_0000093318
Regions
	Domain	304 – 548	245	ABC transporter 1
	Domain	625 – 840	216	ABC transporter 2
	Nucleotide binding	336 – 343	8	ATP 1 By similarity
	Nucleotide binding	658 – 665	8	ATP 2 By similarity
	Compositional bias	141 – 243	103	Glu-rich
Amino acid modifications
	Modified residue	22	1	Phosphoserine Ref.17
	Modified residue	24	1	Phosphoserine Ref.13
	Modified residue	105	1	Phosphoserine Ref.7 Ref.17
	Modified residue	108	1	Phosphothreonine Ref.7 Ref.16 Ref.17 Ref.19
	Modified residue	109	1	Phosphoserine; by CK2 Ref.7 Ref.11 Ref.16 Ref.17 Ref.19
	Modified residue	140	1	Phosphoserine; by CK2 Ref.7 Ref.11 Ref.16 Ref.17 Ref.19
	Modified residue	166	1	Phosphoserine Ref.19
	Modified residue	228	1	Phosphoserine Ref.7 Ref.8 Ref.13 Ref.14 Ref.16 Ref.17 Ref.19
	Modified residue	595	1	Phosphoserine Ref.10
	Cross-link	573		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.9
	Cross-link	582		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.9
Natural variations
	Alternative sequence	226 – 263	38	Missing in isoform 2.		VSP_012078
	Natural variant	198	1	N → D. Corresponds to variant rs6902544 [ dbSNP | Ensembl ].		VAR_048136
Experimental info
	Mutagenesis	109	1	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. Ref.11
	Mutagenesis	140	1	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. Ref.11
	Mutagenesis	342	1	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. Ref.15
	Mutagenesis	367	1	Q → E: Does not inhibit ribosome binding. Ref.15
	Mutagenesis	454	1	G → D: Does not inhibit ribosome binding. Ref.15
	Mutagenesis	477	1	E → Q: Does not inhibit ribosome binding. Reduces protein synthesis; when associated with Q-768. Ref.15
	Mutagenesis	506	1	H → L: Does not inhibit ribosome binding. Ref.15
	Mutagenesis	664	1	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. Ref.15
	Mutagenesis	695	1	Q → E: Does not inhibit ribosome binding. Ref.15
	Mutagenesis	745	1	G → D: Does not inhibit ribosome binding. Ref.15
	Mutagenesis	768	1	E → Q: Does not inhibit ribosome binding. Reduces protein synthesis; when associated with Q-477. Ref.15
	Mutagenesis	797	1	H → L: Does not inhibit ribosome binding. Ref.15
	Sequence conflict	166	1	S → P in AAH34488. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified December 7, 2004. Version 2. Checksum: 5C5AA662DF4C99E4	FASTA	845	95,926
	10 20 30 40 50 60 MPKAPKQQPP EPEWIGDGES TSPSDKVVKK GKKDKKIKKT FFEELAVEDK QAGEEEKVLK 70 80 90 100 110 120 EKEQQQQQQQ QQQKKKRDTR KGRRKKDVDD DGEEKELMER LKKLSVPTSD EEDEVPAPKP 130 140 150 160 170 180 RGGKKTKGGN VFAALIQDQS EEEEEEEKHP PKPAKPEKNR INKAVSEEQQ PALKGKKGKE 190 200 210 220 230 240 EKSKGKAKPQ NKFAALDNEE EDKEEEIIKE KEPPKQGKEK AKKAEQGSEE EGEGEEEEEE 250 260 270 280 290 300 GGESKADDPY AHLSKKEKKK LKKQMEYERQ VASLKAANAA ENDFSVSQAE MSSRQAMLEN 310 320 330 340 350 360 ASDIKLEKFS ISAHGKELFV NADLYIVAGR RYGLVGPNGK GKTTLLKHIA NRALSIPPNI 370 380 390 400 410 420 DVLLCEQEVV ADETPAVQAV LRADTKRLKL LEEERRLQGQ LEQGDDTAAE RLEKVYEELR 430 440 450 460 470 480 ATGAAAAEAK ARRILAGLGF DPEMQNRPTQ KFSGGWRMRV SLARALFMEP TLLMLDEPTN 490 500 510 520 530 540 HLDLNAVIWL NNYLQGWRKT LLIVSHDQGF LDDVCTDIIH LDAQRLHYYR GNYMTFKKMY 550 560 570 580 590 600 QQKQKELLKQ YEKQEKKLKE LKAGGKSTKQ AEKQTKEALT RKQQKCRRKN QDEESQEAPE 610 620 630 640 650 660 LLKRPKEYTV RFTFPDPPPL SPPVLGLHGV TFGYQGQKPL FKNLDFGIDM DSRICIVGPN 670 680 690 700 710 720 GVGKSTLLLL LTGKLTPTHG EMRKNHRLKI GFFNQQYAEQ LRMEETPTEY LQRGFNLPYQ 730 740 750 760 770 780 DARKCLGRFG LESHAHTIQI CKLSGGQKAR VVFAELACRE PDVLILDEPT NNLDIESIDA 790 800 810 820 830 840 LGEAINEYKG AVIVVSHDAR LITETNCQLW VVEEQSVSQI DGDFEDYKRE VLEALGEVMV SRPRE
	Isoform 2 [UniParc]. Checksum: 1B6547EABEE7FC75	FASTA	807	91,680
	10 20 30 40 50 60 MPKAPKQQPP EPEWIGDGES TSPSDKVVKK GKKDKKIKKT FFEELAVEDK QAGEEEKVLK 70 80 90 100 110 120 EKEQQQQQQQ QQQKKKRDTR KGRRKKDVDD DGEEKELMER LKKLSVPTSD EEDEVPAPKP 130 140 150 160 170 180 RGGKKTKGGN VFAALIQDQS EEEEEEEKHP PKPAKPEKNR INKAVSEEQQ PALKGKKGKE 190 200 210 220 230 240 EKSKGKAKPQ NKFAALDNEE EDKEEEIIKE KEPPKQGKEK AKKAEQMEYE RQVASLKAAN 250 260 270 280 290 300 AAENDFSVSQ AEMSSRQAML ENASDIKLEK FSISAHGKEL FVNADLYIVA GRRYGLVGPN 310 320 330 340 350 360 GKGKTTLLKH IANRALSIPP NIDVLLCEQE VVADETPAVQ AVLRADTKRL KLLEEERRLQ 370 380 390 400 410 420 GQLEQGDDTA AERLEKVYEE LRATGAAAAE AKARRILAGL GFDPEMQNRP TQKFSGGWRM 430 440 450 460 470 480 RVSLARALFM EPTLLMLDEP TNHLDLNAVI WLNNYLQGWR KTLLIVSHDQ GFLDDVCTDI 490 500 510 520 530 540 IHLDAQRLHY YRGNYMTFKK MYQQKQKELL KQYEKQEKKL KELKAGGKST KQAEKQTKEA 550 560 570 580 590 600 LTRKQQKCRR KNQDEESQEA PELLKRPKEY TVRFTFPDPP PLSPPVLGLH GVTFGYQGQK 610 620 630 640 650 660 PLFKNLDFGI DMDSRICIVG PNGVGKSTLL LLLTGKLTPT HGEMRKNHRL KIGFFNQQYA 670 680 690 700 710 720 EQLRMEETPT EYLQRGFNLP YQDARKCLGR FGLESHAHTI QICKLSGGQK ARVVFAELAC 730 740 750 760 770 780 REPDVLILDE PTNNLDIESI DALGEAINEY KGAVIVVSHD ARLITETNCQ LWVVEEQSVS 790 800 QIDGDFEDYK REVLEALGEV MVSRPRE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"ABC50, a novel human ATP-binding cassette protein found in tumor necrosis factor-alpha-stimulated synoviocytes." Richard M., Drouin R., Beaulieu A.D. Genomics 53:137-145(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY.
[2]	"Homo sapiens 2,229,817bp genomic DNA of 6p21.3 HLA class I region." Shiina S., Tamiya G., Oka A., Inoko H. Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"Genome diversity in HLA: a new strategy for detection of genetic polymorphisms in expressed genes within the HLA class III and class I regions." Shiina T., Ota M., Katsuyama Y., Hashimoto N., Inoko H. Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"The DNA sequence and analysis of human chromosome 6." 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. Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Embryonic stem cell and Testis.
[6]	"The full-ORF clone resource of the German cDNA consortium." 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. BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 160-845 (ISOFORM 1). Tissue: Melanoma.
[7]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-105; THR-108; SER-109; SER-140 AND SER-228, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[8]	"A probability-based approach for high-throughput protein phosphorylation analysis and site localization." Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P. Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-228, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[9]	"Tryptic digestion of ubiquitin standards reveals an improved strategy for identifying ubiquitinated proteins by mass spectrometry." Denis N.J., Vasilescu J., Lambert J.-P., Smith J.C., Figeys D. Proteomics 7:868-874(2007) [PubMed] [Europe PMC] [Abstract] Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-573 AND LYS-582, MASS SPECTROMETRY. Tissue: Mammary cancer.
[10]	"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage." 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. Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-595, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[11]	"The N-terminal region of ABC50 interacts with eukaryotic initiation factor eIF2 and is a target for regulatory phosphorylation by CK2." Paytubi S., Morrice N.A., Boudeau J., Proud C.G. Biochem. J. 409:223-231(2008) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH EIF2S1, ASSOCIATION WITH RIBOSOMES, PHOSPHORYLATION AT SER-109 AND SER-140, MASS SPECTROMETRY, MUTAGENESIS OF SER-109 AND SER-140.
[12]	"Phosphoproteome of resting human platelets." Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A. J. Proteome Res. 7:526-534(2008) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Platelet.
[13]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24 AND SER-228, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[14]	"Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography." Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J. Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-228, MASS SPECTROMETRY. Tissue: Liver.
[15]	"ABC50 promotes translation initiation in mammalian cells." Paytubi S., Wang X., Lam Y.W., Izquierdo L., Hunter M.J., Jan E., Hundal H.S., Proud C.G. J. Biol. Chem. 284:24061-24073(2009) [PubMed] [Europe PMC] [Abstract] Cited for: 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, SUBCELLULAR LOCATION.
[16]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-108; SER-109; SER-140 AND SER-228, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[17]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." 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. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22; SER-105; THR-108; SER-109; SER-140 AND SER-228, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[18]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-108; SER-109; SER-140; SER-166 AND SER-228, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Web resources

ABCMdb

Database for mutations in ABC proteins

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF027302 mRNA. Translation: AAC70891.1. BA000025 Genomic DNA. Translation: BAB63325.1. AB088096 Genomic DNA. Translation: BAC54928.1. AL662800 Genomic DNA. Translation: CAI18158.1. AL662800 Genomic DNA. Translation: CAI18159.1. AL662825 Genomic DNA. Translation: CAI17836.1. AL662825 Genomic DNA. Translation: CAI17837.1. BX000357 Genomic DNA. Translation: CAI18562.1. BX000357 Genomic DNA. Translation: CAI18563.1. BX119957, BX248518 Genomic DNA. Translation: CAM25907.1. BX248518, BX119957 Genomic DNA. Translation: CAM26017.1. CR753328, CR388372 Genomic DNA. Translation: CAQ07804.1. CR388372, CR753328 Genomic DNA. Translation: CAQ07873.1. BX927220 Genomic DNA. Translation: CAQ09058.1. CR759778, CR847863 Genomic DNA. Translation: CAQ09401.1. CR847863, CR759778 Genomic DNA. Translation: CAQ10059.1. BC034488 mRNA. Translation: AAH34488.1. BC112923 mRNA. Translation: AAI12924.1. AL832430 mRNA. Translation: CAH10648.1.
IPI	IPI00013495. IPI00873899.
RefSeq	NP_001020262.1. NM_001025091.1. NP_001081.1. NM_001090.2.
UniGene	Hs.655285.
3D structure databases
ProteinModelPortal	Q8NE71.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q8NE71. 3 interactions.
MINT	MINT-1392646.
STRING	9606.ENSP00000412553.
PTM databases
PhosphoSite	Q8NE71.
Polymorphism databases
DMDM	56417894.
Proteomic databases
PaxDb	Q8NE71.
PRIDE	Q8NE71.
Protocols and materials databases
DNASU	23.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000326195; ENSP00000313603; ENSG00000204574. ENST00000376545; ENSP00000365728; ENSG00000204574. ENST00000383587; ENSP00000373081; ENSG00000206490. ENST00000383588; ENSP00000373082; ENSG00000206490. ENST00000412443; ENSP00000404726; ENSG00000236342. ENST00000419893; ENSP00000389065; ENSG00000232169. ENST00000420257; ENSP00000391102; ENSG00000225989. ENST00000421042; ENSP00000393143; ENSG00000231129. ENST00000423247; ENSP00000411327; ENSG00000225989. ENST00000426219; ENSP00000414373; ENSG00000231129. ENST00000448939; ENSP00000403526; ENSG00000232169. ENST00000452530; ENSP00000389472; ENSG00000236149. ENST00000457078; ENSP00000412553; ENSG00000236342. ENST00000457111; ENSP00000413319; ENSG00000236149.
GeneID	23.
KEGG	hsa:23.
UCSC	uc003nqk.2. human.
Organism-specific databases
CTD	23.
GeneCards	GC06P030539.
HGNC	HGNC:70. ABCF1.
HPA	HPA017578.
MIM	603429. gene.
neXtProt	NX_Q8NE71.
PharmGKB	PA24405.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0488.
HOGENOM	HOG000271637.
HOVERGEN	HBG050440.
InParanoid	Q8NE71.
KO	K06184.
OMA	IMRIGNT.
OrthoDB	EOG4Z36DF.
PhylomeDB	Q8NE71.
Gene expression databases
ArrayExpress	Q8NE71.
Bgee	Q8NE71.
CleanEx	HS_ABCF1.
Genevestigator	Q8NE71.
GermOnline	ENSG00000204574. Homo sapiens.
Family and domain databases
InterPro	IPR003593. AAA+_ATPase. IPR003439. ABC_transporter-like. IPR017871. ABC_transporter_CS. [Graphical view]
Pfam	PF00005. ABC_tran. 2 hits. [Graphical view]
SMART	SM00382. AAA. 2 hits. [Graphical view]
PROSITE	PS00211. ABC_TRANSPORTER_1. 2 hits. PS50893. ABC_TRANSPORTER_2. 2 hits. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	ABCF1. human.
GenomeRNAi	23.
NextBio	69.
SOURCE	Search...

Entry information

Entry name

ABCF1_HUMAN

Accession

Primary (citable) accession number: Q8NE71
Secondary accession number(s): A2BF75, O14897, Q69YP6

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 7, 2004
Last sequence update:	December 7, 2004
Last modified:	May 1, 2013
This is version 107 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.