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Q8NE71 (ABCF1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 94. 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·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)
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.20

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.15

Subcellular location

Isoform 2: Cytoplasm. Nucleusnucleoplasm. Nucleus envelope Ref.20.

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. Phosphorylated upon DNA damage, probably by ATM or ATR. Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.21

Sequence similarities

Belongs to the ABC transporter superfamily. ABCF family. EF3 subfamily.

Contains 2 ABC transporter domains.

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.19
Modified residue241Phosphoserine Ref.17 Ref.19
Modified residue1051Phosphoserine Ref.8 Ref.9 Ref.17
Modified residue1081Phosphothreonine Ref.7 Ref.8 Ref.9 Ref.14 Ref.17 Ref.19 Ref.21
Modified residue1091Phosphoserine; by CK2 Ref.7 Ref.8 Ref.9 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.21
Modified residue1401Phosphoserine; by CK2 Ref.9 Ref.11 Ref.15 Ref.17 Ref.19 Ref.21
Modified residue1661Phosphoserine Ref.17 Ref.21
Modified residue2281Phosphoserine Ref.9 Ref.10 Ref.11 Ref.17 Ref.18 Ref.21
Modified residue5951Phosphoserine Ref.13
Cross-link573Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.12
Cross-link582Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.12

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.15
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.15
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.20
Mutagenesis3671Q → E: Does not inhibit ribosome binding. Ref.20
Mutagenesis4541G → D: Does not inhibit ribosome binding. Ref.20
Mutagenesis4771E → Q: Does not inhibit ribosome binding. Reduces protein synthesis; when associated with Q-768. Ref.20
Mutagenesis5061H → L: Does not inhibit ribosome binding. Ref.20
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.20
Mutagenesis6951Q → E: Does not inhibit ribosome binding. Ref.20
Mutagenesis7451G → D: Does not inhibit ribosome binding. Ref.20
Mutagenesis7681E → Q: Does not inhibit ribosome binding. Reduces protein synthesis; when associated with Q-477. Ref.20
Mutagenesis7971H → L: Does not inhibit ribosome binding. Ref.20
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: 9790762] [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: 14574404] [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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: 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: 17974005] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 160-845 (ISOFORM 1).
Tissue: Melanoma.
[7]"Large-scale characterization of HeLa cell nuclear phosphoproteins."
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-108 AND SER-109, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[8]"Global phosphoproteome of HT-29 human colon adenocarcinoma cells."
Kim J.-E., Tannenbaum S.R., White F.M.
J. Proteome Res. 4:1339-1346(2005) [PubMed: 16083285] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-105; THR-108 AND SER-109, MASS SPECTROMETRY.
Tissue: Colon adenocarcinoma.
[9]"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: 17081983] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-105; THR-108; SER-109; SER-140 AND SER-228, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[10]"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: 16964243] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-228, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[11]"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry."
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-140 AND SER-228, MASS SPECTROMETRY.
Tissue: Embryonic kidney.
[12]"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: 17370265] [Abstract]
Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-573 AND LYS-582, MASS SPECTROMETRY.
Tissue: Mammary cancer.
[13]"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: 17525332] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-595, MASS SPECTROMETRY.
Tissue: Embryonic kidney.
[14]"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column."
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.
Anal. Sci. 24:161-166(2008) [PubMed: 18187866] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-108 AND SER-109, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[15]"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: 17894550] [Abstract]
Cited for: INTERACTION WITH EIF2S1, ASSOCIATION WITH RIBOSOMES, PHOSPHORYLATION AT SER-109 AND SER-140, PHOSPHORYLATION, MASS SPECTROMETRY, MUTAGENESIS OF SER-109 AND SER-140.
[16]"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: 18088087] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-109, MASS SPECTROMETRY.
Tissue: Platelet.
[17]"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: 18669648] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24; SER-105; THR-108; SER-109; SER-140; SER-166 AND SER-228, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[18]"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: 18318008] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-109 AND SER-228, MASS SPECTROMETRY.
Tissue: Liver.
[19]"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: 19413330] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22; SER-24; THR-108; SER-109 AND SER-140, MASS SPECTROMETRY.
Tissue: Embryonic kidney.
[20]"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: 19570978] [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.
[21]"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: 19690332] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-108; SER-109; SER-140; SER-166 AND SER-228, MASS SPECTROMETRY.
Tissue: Leukemic T-cell.
[22]"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: 21269460] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

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.
BC034488 mRNA. Translation: AAH34488.1.
AL832430 mRNA. Translation: CAH10648.1.
IPIIPI00013495.
IPI00873899.
RefSeqNP_001020262.1. NM_001025091.1.
NP_001081.1. NM_001090.2.
UniGeneHs.655285.

3D structure databases

ProteinModelPortalQ8NE71.
SMRQ8NE71. Positions 302-539, 643-826.
ModBaseSearch...

Protein-protein interaction databases

IntActQ8NE71. 1 interaction.
MINTMINT-1392646.
STRINGQ8NE71.

PTM databases

PhosphoSiteQ8NE71.

Polymorphism databases

DMDM56417894.

Proteomic databases

PRIDEQ8NE71.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000326195; ENSP00000313603; ENSG00000204574.
ENST00000383588; ENSP00000373082; ENSG00000206490.
ENST00000419893; ENSP00000389065; ENSG00000232169.
ENST00000423247; ENSP00000411327; ENSG00000225989.
ENST00000426219; ENSP00000414373; ENSG00000231129.
ENST00000457078; ENSP00000412553; ENSG00000236342.
ENST00000457111; ENSP00000413319; ENSG00000236149.
GeneID23.
KEGGhsa:23.
UCSCuc003nql.1. human.
uc003nqm.1. human.

Organism-specific databases

CTD23.
GeneCardsGC06P030539.
HGNCHGNC:70. ABCF1.
HPAHPA017578.
MIM603429. gene.
neXtProtNX_Q8NE71.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG10759.
GeneTreeENSGT00550000074722.
HOGENOMHBG758042.
HOVERGENHBG050440.
InParanoidQ8NE71.
OMAPIPRGGK.
OrthoDBEOG4Z36DF.
PhylomeDBQ8NE71.

Gene expression databases

ArrayExpressQ8NE71.
BgeeQ8NE71.
CleanExHS_ABCF1.
GenevestigatorQ8NE71.
GermOnlineENSG00000204574. Homo sapiens.

Family and domain databases

InterProIPR003439. ABC_transporter-like.
IPR017871. ABC_transporter_CS.
IPR003593. ATPase_AAA+_core.
[Graphical view]
KOK06184.
PfamPF00005. ABC_tran. 2 hits.
[Graphical view]
SMARTSM00382. AAA. 2 hits.
[Graphical view]
PROSITEPS00211. ABC_TRANSPORTER_1. 2 hits.
PS50893. ABC_TRANSPORTER_2. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio69.
SOURCESearch...

Entry information

Entry nameABCF1_HUMAN
AccessionPrimary (citable) accession number: Q8NE71
Secondary accession number(s): O14897, Q69YP6
Entry history
Integrated into UniProtKB/Swiss-Prot: December 7, 2004
Last sequence update: December 7, 2004
Last modified: January 25, 2012
This is version 94 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

Human chromosome 6

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

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

SIMILARITY comments

Index of protein domains and families