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Q9NQ94

- A1CF_HUMAN

UniProt

Q9NQ94 - A1CF_HUMAN

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Protein

APOBEC1 complementation factor

Gene

A1CF

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. nucleotide binding Source: InterPro
  2. RNA binding Source: ProtInc
  3. 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, 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-KW
  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 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

BgeeiQ9NQ94.
CleanExiHS_A1CF.
ExpressionAtlasiQ9NQ94. baseline and differential.
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.
GeneTreeiENSGT00550000074366.
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

        10         20         30         40         50
MESNHKSGDG LSGTQKEAAL RALVQRTGYS LVQENGQRKY GGPPPGWDAA
60 70 80 90 100
PPERGCEIFI GKLPRDLFED ELIPLCEKIG KIYEMRMMMD FNGNNRGYAF
110 120 130 140 150
VTFSNKVEAK NAIKQLNNYE IRNGRLLGVC ASVDNCRLFV GGIPKTKKRE
160 170 180 190 200
EILSEMKKVT EGVVDVIVYP SAADKTKNRG FAFVEYESHR AAAMARRKLL
210 220 230 240 250
PGRIQLWGHG IAVDWAEPEV EVDEDTMSSV KILYVRNLML STSEEMIEKE
260 270 280 290 300
FNNIKPGAVE RVKKIRDYAF VHFSNREDAV EAMKALNGKV LDGSPIEVTL
310 320 330 340 350
AKPVDKDSYV RYTRGTGGRG TMLQGEYTYS LGQVYDPTTT YLGAPVFYAP
360 370 380 390 400
QTYAAIPSLH FPATKGHLSN RAIIRAPSVR EIYMNVPVGA AGVRGLGGRG
410 420 430 440 450
YLAYTGLGRG YQVKGDKRED KLYDILPGME LTPMNPVTLK PQGIKLAPQI
460 470 480 490 500
LEEICQKNNW GQPVYQLHSA IGQDQRQLFL YKITIPALAS QNPAIHPFTP
510 520 530 540 550
PKLSAFVDEA KTYAAEYTLQ TLGIPTDGGD GTMATAAAAA TAFPGYAVPN
560 570 580 590
ATAPVSAAQL KQAVTLGQDL AAYTTYEVYP TFAVTARGDG YGTF
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. [Q9NQ94-2]
ENST00000373993; ENSP00000363105; ENSG00000148584. [Q9NQ94-1]
ENST00000373995; ENSP00000363107; ENSG00000148584. [Q9NQ94-4]
ENST00000373997; ENSP00000363109; ENSG00000148584. [Q9NQ94-2]
ENST00000374001; ENSP00000363113; ENSG00000148584. [Q9NQ94-2]
ENST00000395495; ENSP00000378873; ENSG00000148584. [Q9NQ94-4]
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 . [Q9NQ94-2 ]
ENST00000373993 ; ENSP00000363105 ; ENSG00000148584 . [Q9NQ94-1 ]
ENST00000373995 ; ENSP00000363107 ; ENSG00000148584 . [Q9NQ94-4 ]
ENST00000373997 ; ENSP00000363109 ; ENSG00000148584 . [Q9NQ94-2 ]
ENST00000374001 ; ENSP00000363113 ; ENSG00000148584 . [Q9NQ94-2 ]
ENST00000395495 ; ENSP00000378873 ; ENSG00000148584 . [Q9NQ94-4 ]
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.
GeneTreei ENSGT00550000074366.
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

Bgeei Q9NQ94.
CleanExi HS_A1CF.
ExpressionAtlasi Q9NQ94. baseline and differential.
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: 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 29, 2014
This is version 124 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