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Q9NQ94

- A1CF_HUMAN

UniProt

Q9NQ94 - A1CF_HUMAN

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Protein
APOBEC1 complementation factor
Gene
A1CF, ACF, ASP
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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. RNA binding Source: ProtInc
  2. nucleotide binding Source: InterPro
  3. protein binding Source: UniProtKB
  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
Complete GO annotation...

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, ASP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 10

Organism-specific databases

HGNCiHGNC:24086. A1CF.

Subcellular locationi

Nucleus. Endoplasmic reticulum By similarity. Cytoplasm
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 APOBEC1.1 Publication

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
Complete GO annotation...

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 factor
PRO_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 similarity4 Publications

Protein-protein interaction databases

BioGridi119004. 6 interactions.
IntActiQ9NQ94. 1 interaction.

Structurei

Secondary structure

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.

Miscellaneous databases

EvolutionaryTraceiQ9NQ94.

Family & Domainsi

Domains and Repeats

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

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni360 – 40950Required for nuclear localization1 Publication
Add
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

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 23 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.

Show »
Length:586
Mass (Da):64,256
Checksum:iA836BBA98FD1BD51
GO
Isoform 31 Publication (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 4 (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.

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.

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.

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.

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 Publication
VSP_051925Add
BLAST
Alternative sequencei1 – 3333MESNH…YSLVQ → MLCSPSFCKLCWKRKK in isoform 3. 1 Publication
VSP_051926Add
BLAST
Alternative sequencei1 – 3333MESNH…YSLVQ → MEAVCLGTCPEPEASMSTAI PGLKKGNNALQSIILQTLLE K in isoform 4.
VSP_051927Add
BLAST
Alternative sequencei202 – 25655Missing in isoform 6. 1 Publication
VSP_051928Add
BLAST
Alternative sequencei381 – 3888Missing in isoform 2, isoform 3 and isoform 4. 3 Publications
VSP_051929

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti191 – 1911A → T in AAF34824. 1 Publication
Sequence conflicti277 – 2771E → K1 Publication
Sequence conflicti277 – 2771E → K1 Publication

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

« Hide 'large scale' publications
  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: Liver and Small intestine.
  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: September 3, 2014
This is version 122 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

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