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Q8NE71 (ABCF1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 119. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length845 AA.
Sequence statusComplete.
Protein existenceEvidence 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.16

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. Nucleusnucleoplasm. Nucleus envelope Ref.16.

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 componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainRepeat
   LigandATP-binding
Nucleotide-binding
   Molecular functionActivator
   PTMIsopeptide bond
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processinflammatory response

Traceable author statement Ref.1. Source: ProtInc

positive regulation of translation

Inferred from direct assay Ref.16. Source: UniProtKB

translation

Traceable author statement Ref.1. Source: ProtInc

translational initiation

Inferred from mutant phenotype Ref.16. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from direct assay. Source: HPA

nuclear envelope

Inferred from direct assay Ref.16. Source: UniProtKB

nucleoplasm

Inferred from direct assay Ref.16. Source: UniProtKB

polysomal ribosome

Inferred from direct assay Ref.16. Source: UniProtKB

ribosome

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionATP binding

Inferred from direct assay Ref.16. Source: UniProtKB

ATPase activity

Inferred from electronic annotation. Source: InterPro

poly(A) RNA binding

Inferred from direct assay PubMed 22658674PubMed 22681889. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.11. Source: UniProtKB

ribosome binding

Inferred from direct assay Ref.11Ref.16. Source: UniProtKB

translation activator activity

Inferred from direct assay Ref.16. 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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 845845ATP-binding cassette sub-family F member 1
PRO_0000093318

Regions

Domain304 – 548245ABC transporter 1
Domain625 – 840216ABC transporter 2
Nucleotide binding336 – 3438ATP 1 By similarity
Nucleotide binding658 – 6658ATP 2 By similarity
Compositional bias141 – 243103Glu-rich

Amino acid modifications

Modified residue221Phosphoserine Ref.18
Modified residue241Phosphoserine Ref.13
Modified residue1051Phosphoserine Ref.7 Ref.18
Modified residue1081Phosphothreonine Ref.7 Ref.17 Ref.18 Ref.20
Modified residue1091Phosphoserine; by CK2 Ref.7 Ref.11 Ref.17 Ref.18 Ref.20
Modified residue1401Phosphoserine; by CK2 Ref.7 Ref.11 Ref.17 Ref.18 Ref.20
Modified residue1661Phosphoserine Ref.20
Modified residue2281Phosphoserine Ref.7 Ref.8 Ref.13 Ref.14 Ref.17 Ref.18 Ref.20
Modified residue5951Phosphoserine Ref.10
Cross-link573Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.9
Cross-link582Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.9

Natural variations

Alternative sequence226 – 26338Missing in isoform 2.
VSP_012078
Natural variant1981N → D.
Corresponds to variant rs6902544 [ dbSNP | Ensembl ].
VAR_048136

Experimental info

Mutagenesis1091S → 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
Mutagenesis1401S → 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
Mutagenesis3421K → 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.16
Mutagenesis3671Q → E: Does not inhibit ribosome binding. Ref.16
Mutagenesis4541G → D: Does not inhibit ribosome binding. Ref.16
Mutagenesis4771E → Q: Does not inhibit ribosome binding. Reduces protein synthesis; when associated with Q-768. Ref.16
Mutagenesis5061H → L: Does not inhibit ribosome binding. Ref.16
Mutagenesis6641K → 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.16
Mutagenesis6951Q → E: Does not inhibit ribosome binding. Ref.16
Mutagenesis7451G → D: Does not inhibit ribosome binding. Ref.16
Mutagenesis7681E → Q: Does not inhibit ribosome binding. Reduces protein synthesis; when associated with Q-477. Ref.16
Mutagenesis7971H → L: Does not inhibit ribosome binding. Ref.16
Sequence conflict1661S → P in AAH34488. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified December 7, 2004. Version 2.
Checksum: 5C5AA662DF4C99E4

FASTA84595,926
        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 

« Hide

Isoform 2 [UniParc].

Checksum: 1B6547EABEE7FC75
Show »

FASTA80791,680

References

« Hide '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. expand/collapse author list , 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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.
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[15]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"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.
[17]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[18]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[19]"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].
[20]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+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.
CCDSCCDS34380.1. [Q8NE71-1]
CCDS34381.1. [Q8NE71-2]
RefSeqNP_001020262.1. NM_001025091.1. [Q8NE71-1]
NP_001081.1. NM_001090.2. [Q8NE71-2]
UniGeneHs.655285.

3D structure databases

ProteinModelPortalQ8NE71.
SMRQ8NE71. Positions 301-834.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106541. 48 interactions.
IntActQ8NE71. 6 interactions.
MINTMINT-1392646.
STRING9606.ENSP00000412553.

PTM databases

PhosphoSiteQ8NE71.

Polymorphism databases

DMDM56417894.

Proteomic databases

MaxQBQ8NE71.
PaxDbQ8NE71.
PRIDEQ8NE71.

Protocols and materials databases

DNASU23.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000326195; ENSP00000313603; ENSG00000204574. [Q8NE71-1]
ENST00000376545; ENSP00000365728; ENSG00000204574. [Q8NE71-2]
ENST00000383587; ENSP00000373081; ENSG00000206490. [Q8NE71-2]
ENST00000383588; ENSP00000373082; ENSG00000206490. [Q8NE71-1]
ENST00000412443; ENSP00000404726; ENSG00000236342. [Q8NE71-2]
ENST00000419893; ENSP00000389065; ENSG00000232169. [Q8NE71-1]
ENST00000420257; ENSP00000391102; ENSG00000225989. [Q8NE71-2]
ENST00000421042; ENSP00000393143; ENSG00000231129. [Q8NE71-2]
ENST00000423247; ENSP00000411327; ENSG00000225989. [Q8NE71-1]
ENST00000426219; ENSP00000414373; ENSG00000231129. [Q8NE71-1]
ENST00000448939; ENSP00000403526; ENSG00000232169. [Q8NE71-2]
ENST00000452530; ENSP00000389472; ENSG00000236149. [Q8NE71-2]
ENST00000457078; ENSP00000412553; ENSG00000236342. [Q8NE71-1]
ENST00000457111; ENSP00000413319; ENSG00000236149. [Q8NE71-1]
GeneID23.
KEGGhsa:23.
UCSCuc003nqk.2. human. [Q8NE71-1]

Organism-specific databases

CTD23.
GeneCardsGC06P030539.
GC06Pj30529.
GC06Pk30529.
GC06Pl30583.
GC06Pm30617.
GC06Pn30528.
GC06Po30530.
HGNCHGNC:70. ABCF1.
HPAHPA017578.
MIM603429. gene.
neXtProtNX_Q8NE71.
PharmGKBPA24405.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0488.
HOGENOMHOG000271637.
HOVERGENHBG050440.
InParanoidQ8NE71.
KOK06184.
OMAFNELVIP.
PhylomeDBQ8NE71.
TreeFamTF105207.

Gene expression databases

ArrayExpressQ8NE71.
BgeeQ8NE71.
CleanExHS_ABCF1.
GenevestigatorQ8NE71.

Family and domain databases

Gene3D3.40.50.300. 2 hits.
InterProIPR003593. AAA+_ATPase.
IPR003439. ABC_transporter-like.
IPR017871. ABC_transporter_CS.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamPF00005. ABC_tran. 2 hits.
[Graphical view]
SMARTSM00382. AAA. 2 hits.
[Graphical view]
SUPFAMSSF52540. SSF52540. 3 hits.
PROSITEPS00211. ABC_TRANSPORTER_1. 2 hits.
PS50893. ABC_TRANSPORTER_2. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSABCF1. human.
GeneWikiABCF1.
GenomeRNAi23.
NextBio69.
PROQ8NE71.
SOURCESearch...

Entry information

Entry nameABCF1_HUMAN
AccessionPrimary (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: July 9, 2014
This is version 119 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM