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Q9NQ94

- A1CF_HUMAN

UniProt

Q9NQ94 - A1CF_HUMAN

Protein

APOBEC1 complementation factor

Gene

A1CF

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 123 (01 Oct 2014)
      Sequence version 1 (01 Oct 2000)
      Previous versions | rss
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    Functioni

    Essential component of the apolipoprotein B mRNA editing enzyme complex which is responsible for the postranscriptional editing of a CAA codon for Gln to a UAA codon for stop in APOB mRNA. Binds to APOB mRNA and is probably responsible for docking the catalytic subunit, APOBEC1, to the mRNA to allow it to deaminate its target cytosine. The complex also protects the edited APOB mRNA from nonsense-mediated decay.3 Publications

    GO - Molecular functioni

    1. nucleotide binding Source: InterPro
    2. protein binding Source: UniProtKB
    3. RNA binding Source: ProtInc
    4. single-stranded RNA binding Source: UniProtKB

    GO - Biological processi

    1. cytidine to uridine editing Source: Reactome
    2. gene expression Source: Reactome
    3. mRNA modification Source: Reactome
    4. mRNA processing Source: UniProtKB-KW
    5. protein stabilization Source: UniProtKB

    Keywords - Biological processi

    mRNA processing

    Keywords - Ligandi

    RNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_1390. Formation of the Editosome.
    REACT_167. mRNA Editing: C to U Conversion.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    APOBEC1 complementation factor
    Alternative name(s):
    APOBEC1-stimulating protein
    Gene namesi
    Name:A1CF
    Synonyms:ACF, ASPImported
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 10

    Organism-specific databases

    HGNCiHGNC:24086. A1CF.

    Subcellular locationi

    Nucleus 1 Publication. Endoplasmic reticulum By similarity. Cytoplasm 1 Publication
    Note: Predominantly nuclear where it localizes to heterochromatin. Also cytoplasmic where it is found at the outer surface of the endoplasmic reticulum By similarity. Shuttles between the nucleus and cytoplasm. May be transported into the nucleus by the nuclear import protein TNPO2/TRN2 or by APOBEC1.By similarity

    GO - Cellular componenti

    1. apolipoprotein B mRNA editing enzyme complex Source: UniProtKB
    2. cytoplasm Source: UniProtKB
    3. endoplasmic reticulum Source: UniProtKB-SubCell
    4. nucleoplasm Source: Reactome
    5. nucleus Source: HPA

    Keywords - Cellular componenti

    Cytoplasm, Endoplasmic reticulum, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi59 – 591F → A: Greatly reduced RNA binding. 1 Publication
    Mutagenesisi100 – 1001F → A: Greatly reduced RNA binding. 1 Publication
    Mutagenesisi139 – 1391F → A: Greatly reduced RNA binding. 1 Publication
    Mutagenesisi183 – 1831F → A: Greatly reduced RNA binding. 1 Publication
    Mutagenesisi234 – 2341Y → A: Slightly reduced RNA binding. 1 Publication
    Mutagenesisi270 – 2701F → A: Slightly reduced RNA binding. 1 Publication

    Organism-specific databases

    PharmGKBiPA162375098.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 594594APOBEC1 complementation factorPRO_0000081482Add
    BLAST

    Proteomic databases

    MaxQBiQ9NQ94.
    PaxDbiQ9NQ94.
    PRIDEiQ9NQ94.

    PTM databases

    PhosphoSiteiQ9NQ94.

    Expressioni

    Tissue specificityi

    Widely expressed with highest levels in brain, liver, pancreas, colon and spleen.1 Publication

    Gene expression databases

    ArrayExpressiQ9NQ94.
    BgeeiQ9NQ94.
    CleanExiHS_A1CF.
    GenevestigatoriQ9NQ94.

    Organism-specific databases

    HPAiHPA037779.
    HPA044079.

    Interactioni

    Subunit structurei

    Part of the apolipoprotein B mRNA editing complex with APOBEC1. Interacts with TNPO2; TNPO2 may be responsible for transport of A1CF into the nucleus. Interacts with SYNCRIP. Interacts with CELF2/CUGBP2 By similarity.By similarity

    Protein-protein interaction databases

    BioGridi119004. 6 interactions.
    IntActiQ9NQ94. 1 interaction.

    Structurei

    Secondary structure

    1
    594
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi232 – 2376
    Helixi244 – 2529
    Beta strandi259 – 2646
    Beta strandi266 – 27510
    Helixi276 – 28611
    Beta strandi287 – 2915
    Beta strandi294 – 2996

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2CPDNMR-A223-308[»]
    ProteinModelPortaliQ9NQ94.
    SMRiQ9NQ94. Positions 57-308.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9NQ94.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini56 – 13479RRM 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini136 – 21883RRM 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini231 – 30373RRM 3PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni360 – 40950Required for nuclear localization1 PublicationAdd
    BLAST

    Domaini

    The RRM domains are necessary but not sufficient for binding to APOB mRNA. Additional residues in the pre-RRM and C-terminal regions are required for RNA-binding and for complementing APOBEC1 activity.1 Publication

    Sequence similaritiesi

    Contains 3 RRM (RNA recognition motif) domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG258596.
    HOVERGENiHBG051917.
    InParanoidiQ9NQ94.
    OMAiLIQRTGY.
    OrthoDBiEOG73JKW2.
    PhylomeDBiQ9NQ94.
    TreeFamiTF314932.

    Family and domain databases

    Gene3Di3.30.160.20. 1 hit.
    3.30.70.330. 2 hits.
    InterProiIPR014720. dsRNA-bd_dom.
    IPR006535. HnRNP_R/Q_splicing_fac.
    IPR012677. Nucleotide-bd_a/b_plait.
    IPR000504. RRM_dom.
    [Graphical view]
    PfamiPF00076. RRM_1. 2 hits.
    [Graphical view]
    SMARTiSM00360. RRM. 3 hits.
    [Graphical view]
    TIGRFAMsiTIGR01648. hnRNP-R-Q. 1 hit.
    PROSITEiPS50102. RRM. 3 hits.
    [Graphical view]

    Sequences (6)i

    Sequence statusi: Complete.

    This entry describes 6 isoformsi produced by alternative splicing. Align

    Isoform 11 Publication (identifier: Q9NQ94-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MESNHKSGDG LSGTQKEAAL RALVQRTGYS LVQENGQRKY GGPPPGWDAA    50
    PPERGCEIFI GKLPRDLFED ELIPLCEKIG KIYEMRMMMD FNGNNRGYAF 100
    VTFSNKVEAK NAIKQLNNYE IRNGRLLGVC ASVDNCRLFV GGIPKTKKRE 150
    EILSEMKKVT EGVVDVIVYP SAADKTKNRG FAFVEYESHR AAAMARRKLL 200
    PGRIQLWGHG IAVDWAEPEV EVDEDTMSSV KILYVRNLML STSEEMIEKE 250
    FNNIKPGAVE RVKKIRDYAF VHFSNREDAV EAMKALNGKV LDGSPIEVTL 300
    AKPVDKDSYV RYTRGTGGRG TMLQGEYTYS LGQVYDPTTT YLGAPVFYAP 350
    QTYAAIPSLH FPATKGHLSN RAIIRAPSVR EIYMNVPVGA AGVRGLGGRG 400
    YLAYTGLGRG YQVKGDKRED KLYDILPGME LTPMNPVTLK PQGIKLAPQI 450
    LEEICQKNNW GQPVYQLHSA IGQDQRQLFL YKITIPALAS QNPAIHPFTP 500
    PKLSAFVDEA KTYAAEYTLQ TLGIPTDGGD GTMATAAAAA TAFPGYAVPN 550
    ATAPVSAAQL KQAVTLGQDL AAYTTYEVYP TFAVTARGDG YGTF 594
    Length:594
    Mass (Da):65,202
    Last modified:October 1, 2000 - v1
    Checksum:iAA5EF76BD8815807
    GO
    Isoform 22 Publications (identifier: Q9NQ94-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         381-388: Missing.

    Note: Major isoform found in 66-78% of cDNA clones.1 Publication

    Show »
    Length:586
    Mass (Da):64,256
    Checksum:iA836BBA98FD1BD51
    GO
    Isoform 3 (identifier: Q9NQ94-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-33: MESNHKSGDGLSGTQKEAALRALVQRTGYSLVQ → MLCSPSFCKLCWKRKK
         381-388: Missing.

    Show »
    Length:569
    Mass (Da):62,682
    Checksum:iF185421309CBA29F
    GO
    Isoform 4Curated (identifier: Q9NQ94-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-33: MESNHKSGDGLSGTQKEAALRALVQRTGYSLVQ → MEAVCLGTCPEPEASMSTAIPGLKKGNNALQSIILQTLLEK
         381-388: Missing.

    Note: Does not exhibit APOBEC1 complementation activity.1 Publication

    Curated

    Show »
    Length:594
    Mass (Da):65,024
    Checksum:i2F2C8897629F9E3C
    GO
    Isoform 51 Publication (identifier: Q9NQ94-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-84: Missing.

    Note: Does not exhibit APOBEC1 complementation activity.1 Publication

    Show »
    Length:510
    Mass (Da):55,962
    Checksum:i70E050F5DB3F4DA2
    GO
    Isoform 61 Publication (identifier: Q9NQ94-6) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         202-256: Missing.

    Note: Minor isoform found in 2-3% of cDNA clones.1 Publication

    Show »
    Length:539
    Mass (Da):58,871
    Checksum:i924E9C2A43A6788C
    GO

    Sequence cautioni

    The sequence BAA91086.1 differs from that shown. Reason: Frameshift at position 148.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti191 – 1911A → T in AAF34824. (PubMed:10669759)Curated
    Sequence conflicti277 – 2771E → K(PubMed:10669759)Curated
    Sequence conflicti277 – 2771E → K1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti555 – 5551V → M.
    Corresponds to variant rs9073 [ dbSNP | Ensembl ].
    VAR_052201
    Natural varianti558 – 5581A → S.
    Corresponds to variant rs11817448 [ dbSNP | Ensembl ].
    VAR_059821

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 8484Missing in isoform 5. 1 PublicationVSP_051925Add
    BLAST
    Alternative sequencei1 – 3333MESNH…YSLVQ → MLCSPSFCKLCWKRKK in isoform 3. 1 PublicationVSP_051926Add
    BLAST
    Alternative sequencei1 – 3333MESNH…YSLVQ → MEAVCLGTCPEPEASMSTAI PGLKKGNNALQSIILQTLLE K in isoform 4. 2 PublicationsVSP_051927Add
    BLAST
    Alternative sequencei202 – 25655Missing in isoform 6. 1 PublicationVSP_051928Add
    BLAST
    Alternative sequencei381 – 3888Missing in isoform 2, isoform 3 and isoform 4. 5 PublicationsVSP_051929

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ272078 mRNA. Translation: CAB94754.1.
    AJ272079 mRNA. Translation: CAB94755.1.
    AF209192 mRNA. Translation: AAF34824.1.
    AF271789 mRNA. Translation: AAF76221.1.
    AF271790 mRNA. Translation: AAF76222.1.
    AK000324 mRNA. Translation: BAA91086.1. Frameshift.
    AK291982 mRNA. Translation: BAF84671.1.
    AL512366, AL589794 Genomic DNA. Translation: CAI14233.1.
    AL512366, AL589794 Genomic DNA. Translation: CAI14235.1.
    AL512366, AL589794 Genomic DNA. Translation: CAI14236.1.
    AL589794, AL512366 Genomic DNA. Translation: CAI15762.1.
    AL589794, AL512366 Genomic DNA. Translation: CAI15763.1.
    AL589794, AL512366 Genomic DNA. Translation: CAI15764.1.
    CH471083 Genomic DNA. Translation: EAW54133.1.
    CH471083 Genomic DNA. Translation: EAW54134.1.
    CH471083 Genomic DNA. Translation: EAW54135.1.
    BC130519 mRNA. Translation: AAI30520.1.
    BC144196 mRNA. Translation: AAI44197.1.
    CCDSiCCDS7241.1. [Q9NQ94-2]
    CCDS7242.1. [Q9NQ94-1]
    CCDS7243.1. [Q9NQ94-4]
    RefSeqiNP_001185747.1. NM_001198818.1. [Q9NQ94-2]
    NP_001185748.1. NM_001198819.1.
    NP_001185749.1. NM_001198820.1. [Q9NQ94-4]
    NP_055391.2. NM_014576.3. [Q9NQ94-2]
    NP_620310.1. NM_138932.2. [Q9NQ94-1]
    NP_620311.1. NM_138933.2. [Q9NQ94-4]
    XP_005269775.1. XM_005269718.1. [Q9NQ94-1]
    XP_005269776.1. XM_005269719.1. [Q9NQ94-1]
    XP_005269777.1. XM_005269720.1. [Q9NQ94-1]
    XP_006717871.1. XM_006717808.1. [Q9NQ94-1]
    XP_006717872.1. XM_006717809.1. [Q9NQ94-4]
    UniGeneiHs.282795.

    Genome annotation databases

    EnsembliENST00000282641; ENSP00000282641; ENSG00000148584. [Q9NQ94-1]
    ENST00000373993; ENSP00000363105; ENSG00000148584. [Q9NQ94-1]
    ENST00000373995; ENSP00000363107; ENSG00000148584. [Q9NQ94-4]
    ENST00000373997; ENSP00000363109; ENSG00000148584. [Q9NQ94-2]
    ENST00000374001; ENSP00000363113; ENSG00000148584. [Q9NQ94-2]
    ENST00000395495; ENSP00000378873; ENSG00000148584. [Q9NQ94-6]
    GeneIDi29974.
    KEGGihsa:29974.
    UCSCiuc001jjh.3. human. [Q9NQ94-4]
    uc001jji.3. human. [Q9NQ94-2]
    uc001jjj.3. human. [Q9NQ94-1]

    Polymorphism databases

    DMDMi74761651.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ272078 mRNA. Translation: CAB94754.1 .
    AJ272079 mRNA. Translation: CAB94755.1 .
    AF209192 mRNA. Translation: AAF34824.1 .
    AF271789 mRNA. Translation: AAF76221.1 .
    AF271790 mRNA. Translation: AAF76222.1 .
    AK000324 mRNA. Translation: BAA91086.1 . Frameshift.
    AK291982 mRNA. Translation: BAF84671.1 .
    AL512366 , AL589794 Genomic DNA. Translation: CAI14233.1 .
    AL512366 , AL589794 Genomic DNA. Translation: CAI14235.1 .
    AL512366 , AL589794 Genomic DNA. Translation: CAI14236.1 .
    AL589794 , AL512366 Genomic DNA. Translation: CAI15762.1 .
    AL589794 , AL512366 Genomic DNA. Translation: CAI15763.1 .
    AL589794 , AL512366 Genomic DNA. Translation: CAI15764.1 .
    CH471083 Genomic DNA. Translation: EAW54133.1 .
    CH471083 Genomic DNA. Translation: EAW54134.1 .
    CH471083 Genomic DNA. Translation: EAW54135.1 .
    BC130519 mRNA. Translation: AAI30520.1 .
    BC144196 mRNA. Translation: AAI44197.1 .
    CCDSi CCDS7241.1. [Q9NQ94-2 ]
    CCDS7242.1. [Q9NQ94-1 ]
    CCDS7243.1. [Q9NQ94-4 ]
    RefSeqi NP_001185747.1. NM_001198818.1. [Q9NQ94-2 ]
    NP_001185748.1. NM_001198819.1.
    NP_001185749.1. NM_001198820.1. [Q9NQ94-4 ]
    NP_055391.2. NM_014576.3. [Q9NQ94-2 ]
    NP_620310.1. NM_138932.2. [Q9NQ94-1 ]
    NP_620311.1. NM_138933.2. [Q9NQ94-4 ]
    XP_005269775.1. XM_005269718.1. [Q9NQ94-1 ]
    XP_005269776.1. XM_005269719.1. [Q9NQ94-1 ]
    XP_005269777.1. XM_005269720.1. [Q9NQ94-1 ]
    XP_006717871.1. XM_006717808.1. [Q9NQ94-1 ]
    XP_006717872.1. XM_006717809.1. [Q9NQ94-4 ]
    UniGenei Hs.282795.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2CPD NMR - A 223-308 [» ]
    ProteinModelPortali Q9NQ94.
    SMRi Q9NQ94. Positions 57-308.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 119004. 6 interactions.
    IntActi Q9NQ94. 1 interaction.

    PTM databases

    PhosphoSitei Q9NQ94.

    Polymorphism databases

    DMDMi 74761651.

    Proteomic databases

    MaxQBi Q9NQ94.
    PaxDbi Q9NQ94.
    PRIDEi Q9NQ94.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000282641 ; ENSP00000282641 ; ENSG00000148584 . [Q9NQ94-1 ]
    ENST00000373993 ; ENSP00000363105 ; ENSG00000148584 . [Q9NQ94-1 ]
    ENST00000373995 ; ENSP00000363107 ; ENSG00000148584 . [Q9NQ94-4 ]
    ENST00000373997 ; ENSP00000363109 ; ENSG00000148584 . [Q9NQ94-2 ]
    ENST00000374001 ; ENSP00000363113 ; ENSG00000148584 . [Q9NQ94-2 ]
    ENST00000395495 ; ENSP00000378873 ; ENSG00000148584 . [Q9NQ94-6 ]
    GeneIDi 29974.
    KEGGi hsa:29974.
    UCSCi uc001jjh.3. human. [Q9NQ94-4 ]
    uc001jji.3. human. [Q9NQ94-2 ]
    uc001jjj.3. human. [Q9NQ94-1 ]

    Organism-specific databases

    CTDi 29974.
    GeneCardsi GC10M052566.
    HGNCi HGNC:24086. A1CF.
    HPAi HPA037779.
    HPA044079.
    neXtProti NX_Q9NQ94.
    PharmGKBi PA162375098.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG258596.
    HOVERGENi HBG051917.
    InParanoidi Q9NQ94.
    OMAi LIQRTGY.
    OrthoDBi EOG73JKW2.
    PhylomeDBi Q9NQ94.
    TreeFami TF314932.

    Enzyme and pathway databases

    Reactomei REACT_1390. Formation of the Editosome.
    REACT_167. mRNA Editing: C to U Conversion.

    Miscellaneous databases

    EvolutionaryTracei Q9NQ94.
    GeneWikii ACF_(gene).
    GenomeRNAii 29974.
    NextBioi 52719.
    PROi Q9NQ94.

    Gene expression databases

    ArrayExpressi Q9NQ94.
    Bgeei Q9NQ94.
    CleanExi HS_A1CF.
    Genevestigatori Q9NQ94.

    Family and domain databases

    Gene3Di 3.30.160.20. 1 hit.
    3.30.70.330. 2 hits.
    InterProi IPR014720. dsRNA-bd_dom.
    IPR006535. HnRNP_R/Q_splicing_fac.
    IPR012677. Nucleotide-bd_a/b_plait.
    IPR000504. RRM_dom.
    [Graphical view ]
    Pfami PF00076. RRM_1. 2 hits.
    [Graphical view ]
    SMARTi SM00360. RRM. 3 hits.
    [Graphical view ]
    TIGRFAMsi TIGR01648. hnRNP-R-Q. 1 hit.
    PROSITEi PS50102. RRM. 3 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Purification and molecular cloning of a novel essential component of the apolipoprotein B mRNA editing enzyme-complex."
      Lellek H., Kirsten R., Diehl I., Apostel F., Buck F., Greeve J.
      J. Biol. Chem. 275:19848-19856(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, INTERACTION WITH APOBEC1.
      Tissue: LiverImported and Small intestineImported.
    2. "Molecular cloning of APOBEC-1 complementation factor, a novel RNA-binding protein involved in the editing of apolipoprotein B mRNA."
      Mehta A., Kinter M.T., Sherman N.E., Driscoll D.M.
      Mol. Cell. Biol. 20:1846-1854(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, INTERACTION WITH APOBEC1, TISSUE SPECIFICITY.
    3. "Human APOBEC-1 complementation factor related protein."
      Sowden M.P., Smith H.C.
      Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3).
      Tissue: Liver.
    4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 4).
      Tissue: Small intestine.
    5. "The DNA sequence and comparative analysis of human chromosome 10."
      Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
      , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
      Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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] (ISOFORMS 1 AND 4).
    8. "Identification of GRY-RBP as an apolipoprotein B RNA-binding protein that interacts with both apobec-1 and apobec-1 complementation factor to modulate C to U editing."
      Blanc V., Navaratnam N., Henderson J.O., Anant S., Kennedy S., Jarmuz A., Scott J., Davidson N.O.
      J. Biol. Chem. 276:10272-10283(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SYNCRIP.
    9. "Isolation, characterization and developmental regulation of the human apobec-1 complementation factor (ACF) gene."
      Henderson J.O., Blanc V., Davidson N.O.
      Biochim. Biophys. Acta 1522:22-30(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: GENE STRUCTURE, ALTERNATIVE SPLICING.
    10. "Identification of domains in apobec-1 complementation factor required for RNA binding and apolipoprotein-B mRNA editing."
      Mehta A., Driscoll D.M.
      RNA 8:69-82(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: RNA-BINDING DOMAIN, MUTAGENESIS OF PHE-59; PHE-100; PHE-139; PHE-183; TYR-234 AND PHE-270.
    11. "The apolipoprotein B mRNA editing complex performs a multifunctional cycle and suppresses nonsense-mediated decay."
      Chester A., Somasekaram A., Tzimina M., Jarmuz A., Gisbourne J., O'Keefe R., Scott J., Navaratnam N.
      EMBO J. 22:3971-3982(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    12. "A novel nuclear localization signal in the auxiliary domain of apobec-1 complementation factor regulates nucleocytoplasmic import and shuttling."
      Blanc V., Kennedy S., Davidson N.O.
      J. Biol. Chem. 278:41198-41204(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEAR LOCALIZATION SIGNAL, INTERACTION WITH TNPO2.
    13. "Solution structure of the RNA recognition motif of human APOBEC-1 complementation factor, ACF."
      RIKEN structural genomics initiative (RSGI)
      Submitted (NOV-2005) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 223-308.

    Entry informationi

    Entry nameiA1CF_HUMAN
    AccessioniPrimary (citable) accession number: Q9NQ94
    Secondary accession number(s): A1L4F2
    , A8K7G7, B7ZM14, Q5SZQ0, Q9NQ93, Q9NQX8, Q9NQX9, Q9NXC9, Q9NZD3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 20, 2005
    Last sequence update: October 1, 2000
    Last modified: October 1, 2014
    This is version 123 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 10
      Human chromosome 10: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3