Q9NQ94 (A1CF_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
APOBEC1 complementation factor

Alternative name(s):
APOBEC1-stimulating protein

Gene names

Name:	A1CF
Synonyms:	ACF, ASP

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	594 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.1 Ref.2 Ref.11
Subunit structure	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. Ref.1 Ref.2 Ref.8 Ref.12 UniProtKB Q923K9
Subcellular location	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. Ref.11
Tissue specificity	Widely expressed with highest levels in brain, liver, pancreas, colon and spleen. Ref.2
Domain	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. Ref.10
Sequence similarities	Contains 3 RRM (RNA recognition motif) domains.
Sequence caution	The sequence BAA91086.1 differs from that shown. Reason: Frameshift at position 148.

Ontologies

Keywords
Biological process	mRNA processing
Cellular component	Cytoplasm Endoplasmic reticulum Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat
Ligand	RNA-binding
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cytidine to uridine editing Traceable author statement. Source: Reactome gene expression Traceable author statement. Source: Reactome mRNA modification Traceable author statement. Source: Reactome mRNA processing Inferred from electronic annotation. Source: UniProtKB-KW protein stabilization Inferred from direct assay Ref.11. Source: UniProtKB
Cellular_component	apolipoprotein B mRNA editing enzyme complex Inferred from direct assay Ref.1. Source: UniProtKB cytoplasm Inferred from direct assay Ref.11. Source: UniProtKB endoplasmic reticulum Inferred from electronic annotation. Source: UniProtKB-SubCell nucleoplasm Traceable author statement. Source: Reactome
Molecular_function	nucleotide binding Inferred from electronic annotation. Source: InterPro single-stranded RNA binding Inferred from direct assay Ref.10. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 6 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 Ref.1 (identifier: Q9NQ94-1)

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 Ref.1 Ref.2 Ref.3 (identifier: Q9NQ94-2)

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.

Isoform 3 Ref.3 (identifier: Q9NQ94-3)

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

Isoform 4 (identifier: Q9NQ94-4)

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.

Isoform 5 Ref.9 (identifier: Q9NQ94-5)

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

Note: Does not exhibit APOBEC1 complementation activity.

Isoform 6 Ref.9 (identifier: Q9NQ94-6)

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.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 594

594

APOBEC1 complementation factor

PRO_0000081482

Regions

Domain

56 – 134

79

RRM 1

Domain

136 – 218

83

RRM 2

Domain

231 – 303

73

RRM 3

Region

360 – 409

50

Required for nuclear localization Ref.12

Natural variations

Alternative sequence

1 – 84

84

Missing in isoform 5. Ref.9

VSP_051925

Alternative sequence

1 – 33

33

MESNH…YSLVQ → MLCSPSFCKLCWKRKK in isoform 3. Ref.3

VSP_051926

Alternative sequence

1 – 33

33

MESNH…YSLVQ → MEAVCLGTCPEPEASMSTAI PGLKKGNNALQSIILQTLLE K in isoform 4.

VSP_051927

Alternative sequence

202 – 256

55

Missing in isoform 6. Ref.9

VSP_051928

Alternative sequence

381 – 388

8

Missing in isoform 2, isoform 3 and isoform 4. Ref.1 Ref.2 Ref.3

VSP_051929

Natural variant

555

1

V → M.
Corresponds to variant rs9073 [ dbSNP | Ensembl ].

VAR_052201

Natural variant

558

1

A → S.
Corresponds to variant rs11817448 [ dbSNP | Ensembl ].

VAR_059821

Experimental info

Mutagenesis

59

1

F → A: Greatly reduced RNA binding. Ref.10

Mutagenesis

100

1

F → A: Greatly reduced RNA binding. Ref.10

Mutagenesis

139

1

F → A: Greatly reduced RNA binding. Ref.10

Mutagenesis

183

1

F → A: Greatly reduced RNA binding. Ref.10

Mutagenesis

234

1

Y → A: Slightly reduced RNA binding. Ref.10

Mutagenesis

270

1

F → A: Slightly reduced RNA binding. Ref.10

Sequence conflict

191

1

A → T in AAF34824. Ref.2

Sequence conflict

277

1

E → K Ref.2

Sequence conflict

277

1

E → K Ref.3

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

594

Helix Strand Turn

Details...

Beta strand

232 – 237

6

Helix

244 – 252

9

Beta strand

259 – 264

6

Beta strand

266 – 275

10

Helix

276 – 286

11

Beta strand

287 – 291

5

Beta strand

294 – 299

6

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: AA5EF76BD8815807	FASTA	594	65,202
	10 20 30 40 50 60 MESNHKSGDG LSGTQKEAAL RALVQRTGYS LVQENGQRKY GGPPPGWDAA PPERGCEIFI 70 80 90 100 110 120 GKLPRDLFED ELIPLCEKIG KIYEMRMMMD FNGNNRGYAF VTFSNKVEAK NAIKQLNNYE 130 140 150 160 170 180 IRNGRLLGVC ASVDNCRLFV GGIPKTKKRE EILSEMKKVT EGVVDVIVYP SAADKTKNRG 190 200 210 220 230 240 FAFVEYESHR AAAMARRKLL PGRIQLWGHG IAVDWAEPEV EVDEDTMSSV KILYVRNLML 250 260 270 280 290 300 STSEEMIEKE FNNIKPGAVE RVKKIRDYAF VHFSNREDAV EAMKALNGKV LDGSPIEVTL 310 320 330 340 350 360 AKPVDKDSYV RYTRGTGGRG TMLQGEYTYS LGQVYDPTTT YLGAPVFYAP QTYAAIPSLH 370 380 390 400 410 420 FPATKGHLSN RAIIRAPSVR EIYMNVPVGA AGVRGLGGRG YLAYTGLGRG YQVKGDKRED 430 440 450 460 470 480 KLYDILPGME LTPMNPVTLK PQGIKLAPQI LEEICQKNNW GQPVYQLHSA IGQDQRQLFL 490 500 510 520 530 540 YKITIPALAS QNPAIHPFTP PKLSAFVDEA KTYAAEYTLQ TLGIPTDGGD GTMATAAAAA 550 560 570 580 590 TAFPGYAVPN ATAPVSAAQL KQAVTLGQDL AAYTTYEVYP TFAVTARGDG YGTF
	Isoform 2 [UniParc]. Checksum: A836BBA98FD1BD51	FASTA	586	64,256
	10 20 30 40 50 60 MESNHKSGDG LSGTQKEAAL RALVQRTGYS LVQENGQRKY GGPPPGWDAA PPERGCEIFI 70 80 90 100 110 120 GKLPRDLFED ELIPLCEKIG KIYEMRMMMD FNGNNRGYAF VTFSNKVEAK NAIKQLNNYE 130 140 150 160 170 180 IRNGRLLGVC ASVDNCRLFV GGIPKTKKRE EILSEMKKVT EGVVDVIVYP SAADKTKNRG 190 200 210 220 230 240 FAFVEYESHR AAAMARRKLL PGRIQLWGHG IAVDWAEPEV EVDEDTMSSV KILYVRNLML 250 260 270 280 290 300 STSEEMIEKE FNNIKPGAVE RVKKIRDYAF VHFSNREDAV EAMKALNGKV LDGSPIEVTL 310 320 330 340 350 360 AKPVDKDSYV RYTRGTGGRG TMLQGEYTYS LGQVYDPTTT YLGAPVFYAP QTYAAIPSLH 370 380 390 400 410 420 FPATKGHLSN RAIIRAPSVR GAAGVRGLGG RGYLAYTGLG RGYQVKGDKR EDKLYDILPG 430 440 450 460 470 480 MELTPMNPVT LKPQGIKLAP QILEEICQKN NWGQPVYQLH SAIGQDQRQL FLYKITIPAL 490 500 510 520 530 540 ASQNPAIHPF TPPKLSAFVD EAKTYAAEYT LQTLGIPTDG GDGTMATAAA AATAFPGYAV 550 560 570 580 PNATAPVSAA QLKQAVTLGQ DLAAYTTYEV YPTFAVTARG DGYGTF
	Isoform 3 [UniParc]. Checksum: F185421309CBA29F	FASTA	569	62,682
	10 20 30 40 50 60 MLCSPSFCKL CWKRKKENGQ RKYGGPPPGW DAAPPERGCE IFIGKLPRDL FEDELIPLCE 70 80 90 100 110 120 KIGKIYEMRM MMDFNGNNRG YAFVTFSNKV EAKNAIKQLN NYEIRNGRLL GVCASVDNCR 130 140 150 160 170 180 LFVGGIPKTK KREEILSEMK KVTEGVVDVI VYPSAADKTK NRGFAFVEYE SHRAAAMARR 190 200 210 220 230 240 KLLPGRIQLW GHGIAVDWAE PEVEVDEDTM SSVKILYVRN LMLSTSEEMI EKEFNNIKPG 250 260 270 280 290 300 AVERVKKIRD YAFVHFSNRE DAVEAMKALN GKVLDGSPIE VTLAKPVDKD SYVRYTRGTG 310 320 330 340 350 360 GRGTMLQGEY TYSLGQVYDP TTTYLGAPVF YAPQTYAAIP SLHFPATKGH LSNRAIIRAP 370 380 390 400 410 420 SVRGAAGVRG LGGRGYLAYT GLGRGYQVKG DKREDKLYDI LPGMELTPMN PVTLKPQGIK 430 440 450 460 470 480 LAPQILEEIC QKNNWGQPVY QLHSAIGQDQ RQLFLYKITI PALASQNPAI HPFTPPKLSA 490 500 510 520 530 540 FVDEAKTYAA EYTLQTLGIP TDGGDGTMAT AAAAATAFPG YAVPNATAPV SAAQLKQAVT 550 560 LGQDLAAYTT YEVYPTFAVT ARGDGYGTF
	Isoform 4 [UniParc]. Checksum: 2F2C8897629F9E3C	FASTA	594	65,024
	10 20 30 40 50 60 MEAVCLGTCP EPEASMSTAI PGLKKGNNAL QSIILQTLLE KENGQRKYGG PPPGWDAAPP 70 80 90 100 110 120 ERGCEIFIGK LPRDLFEDEL IPLCEKIGKI YEMRMMMDFN GNNRGYAFVT FSNKVEAKNA 130 140 150 160 170 180 IKQLNNYEIR NGRLLGVCAS VDNCRLFVGG IPKTKKREEI LSEMKKVTEG VVDVIVYPSA 190 200 210 220 230 240 ADKTKNRGFA FVEYESHRAA AMARRKLLPG RIQLWGHGIA VDWAEPEVEV DEDTMSSVKI 250 260 270 280 290 300 LYVRNLMLST SEEMIEKEFN NIKPGAVERV KKIRDYAFVH FSNREDAVEA MKALNGKVLD 310 320 330 340 350 360 GSPIEVTLAK PVDKDSYVRY TRGTGGRGTM LQGEYTYSLG QVYDPTTTYL GAPVFYAPQT 370 380 390 400 410 420 YAAIPSLHFP ATKGHLSNRA IIRAPSVRGA AGVRGLGGRG YLAYTGLGRG YQVKGDKRED 430 440 450 460 470 480 KLYDILPGME LTPMNPVTLK PQGIKLAPQI LEEICQKNNW GQPVYQLHSA IGQDQRQLFL 490 500 510 520 530 540 YKITIPALAS QNPAIHPFTP PKLSAFVDEA KTYAAEYTLQ TLGIPTDGGD GTMATAAAAA 550 560 570 580 590 TAFPGYAVPN ATAPVSAAQL KQAVTLGQDL AAYTTYEVYP TFAVTARGDG YGTF
	Isoform 5 [UniParc]. Checksum: 70E050F5DB3F4DA2	FASTA	510	55,962
	10 20 30 40 50 60 MRMMMDFNGN NRGYAFVTFS NKVEAKNAIK QLNNYEIRNG RLLGVCASVD NCRLFVGGIP 70 80 90 100 110 120 KTKKREEILS EMKKVTEGVV DVIVYPSAAD KTKNRGFAFV EYESHRAAAM ARRKLLPGRI 130 140 150 160 170 180 QLWGHGIAVD WAEPEVEVDE DTMSSVKILY VRNLMLSTSE EMIEKEFNNI KPGAVERVKK 190 200 210 220 230 240 IRDYAFVHFS NREDAVEAMK ALNGKVLDGS PIEVTLAKPV DKDSYVRYTR GTGGRGTMLQ 250 260 270 280 290 300 GEYTYSLGQV YDPTTTYLGA PVFYAPQTYA AIPSLHFPAT KGHLSNRAII RAPSVREIYM 310 320 330 340 350 360 NVPVGAAGVR GLGGRGYLAY TGLGRGYQVK GDKREDKLYD ILPGMELTPM NPVTLKPQGI 370 380 390 400 410 420 KLAPQILEEI CQKNNWGQPV YQLHSAIGQD QRQLFLYKIT IPALASQNPA IHPFTPPKLS 430 440 450 460 470 480 AFVDEAKTYA AEYTLQTLGI PTDGGDGTMA TAAAAATAFP GYAVPNATAP VSAAQLKQAV 490 500 510 TLGQDLAAYT TYEVYPTFAV TARGDGYGTF
	Isoform 6 [UniParc]. Checksum: 924E9C2A43A6788C	FASTA	539	58,871
	10 20 30 40 50 60 MESNHKSGDG LSGTQKEAAL RALVQRTGYS LVQENGQRKY GGPPPGWDAA PPERGCEIFI 70 80 90 100 110 120 GKLPRDLFED ELIPLCEKIG KIYEMRMMMD FNGNNRGYAF VTFSNKVEAK NAIKQLNNYE 130 140 150 160 170 180 IRNGRLLGVC ASVDNCRLFV GGIPKTKKRE EILSEMKKVT EGVVDVIVYP SAADKTKNRG 190 200 210 220 230 240 FAFVEYESHR AAAMARRKLL PGAVERVKKI RDYAFVHFSN REDAVEAMKA LNGKVLDGSP 250 260 270 280 290 300 IEVTLAKPVD KDSYVRYTRG TGGRGTMLQG EYTYSLGQVY DPTTTYLGAP VFYAPQTYAA 310 320 330 340 350 360 IPSLHFPATK GHLSNRAIIR APSVREIYMN VPVGAAGVRG LGGRGYLAYT GLGRGYQVKG 370 380 390 400 410 420 DKREDKLYDI LPGMELTPMN PVTLKPQGIK LAPQILEEIC QKNNWGQPVY QLHSAIGQDQ 430 440 450 460 470 480 RQLFLYKITI PALASQNPAI HPFTPPKLSA FVDEAKTYAA EYTLQTLGIP TDGGDGTMAT 490 500 510 520 530 AAAAATAFPG YAVPNATAPV SAAQLKQAVT LGQDLAAYTT YEVYPTFAVT ARGDGYGTF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases 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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00071360.
IPI00148257.
IPI00299499.
IPI00657723.
IPI00657770.
IPI00981528.

RefSeq

NP_001185747.1. NM_001198818.1.
NP_001185748.1. NM_001198819.1.
NP_001185749.1. NM_001198820.1.
NP_055391.2. NM_014576.3.
NP_620310.1. NM_138932.2.
NP_620311.1. NM_138933.2.

UniGene

Hs.282795.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2CPD	NMR	-	A	223-308	[»]

ProteinModelPortal

Q9NQ94.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9NQ94. 1 interaction.

PTM databases

PhosphoSite

Q9NQ94.

Polymorphism databases

DMDM

74761651.

Proteomic databases

PaxDb

Q9NQ94.

PRIDE

Q9NQ94.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000282641; ENSP00000282641; ENSG00000148584.
ENST00000373993; ENSP00000363105; ENSG00000148584.
ENST00000373995; ENSP00000363107; ENSG00000148584.
ENST00000373997; ENSP00000363109; ENSG00000148584.
ENST00000374001; ENSP00000363113; ENSG00000148584.
ENST00000395495; ENSP00000378873; ENSG00000148584.

GeneID

29974.

KEGG

hsa:29974.

UCSC

uc001jjh.3. human.
uc001jji.3. human.
uc001jjj.3. human.

Organism-specific databases

CTD

29974.

GeneCards

GC10M052566.

HGNC

HGNC:24086. A1CF.

HPA

HPA037779.

neXtProt

NX_Q9NQ94.

PharmGKB

PA162375098.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG258596.

HOVERGEN

HBG051917.

InParanoid

Q9NQ94.

OMA

PGYAVPN.

PhylomeDB

Q9NQ94.

Enzyme and pathway databases

Reactome

REACT_1675. mRNA Processing.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpress

Q9NQ94.

Bgee

Q9NQ94.

CleanEx

HS_A1CF.

Genevestigator

Q9NQ94.

GermOnline

ENSG00000148584. Homo sapiens.

Family and domain databases

Gene3D

3.30.160.20. 1 hit.
3.30.70.330. 2 hits.

InterPro

IPR014720. dsRNA-bd-like_dom.
IPR006535. HnRNP_R/Q_splicing_fac.
IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]

Pfam

PF00076. RRM_1. 2 hits.
[Graphical view]

SMART

SM00360. RRM. 3 hits.
[Graphical view]

TIGRFAMs

TIGR01648. hnRNP-R-Q. 1 hit.

PROSITE

PS50102. RRM. 3 hits.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q9NQ94.

GenomeRNAi

29974.

NextBio

52719.

Entry information

Entry name

A1CF_HUMAN

Accession

Primary (citable) accession number: Q9NQ94
Secondary accession number(s): A1L4F2 , A8K7G7, B7ZM14, Q5SZQ0, Q9NQ93, Q9NQX8, Q9NQX9, Q9NXC9, Q9NZD3

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 20, 2005
Last sequence update:	October 1, 2000
Last modified:	May 1, 2013
This is version 110 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.