Q9Y235 (ABEC2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Probable C->U-editing enzyme APOBEC-2
EC=3.5.4.-

Gene names

Name:

APOBEC2

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	224 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Probable C to U editing enzyme whose physiological substrate is not yet known. Does not display detectable apoB mRNA editing. Has a low intrinsic cytidine deaminase activity. May play a role in the epigenetic regulation of gene expression through the process of active DNA demethylation. Ref.7
Cofactor	Zinc By similarity. Ref.8
Subunit structure	Homotetramer. Ref.8
Tissue specificity	Expressed exclusively in heart and skeletal muscle.
Sequence similarities	Belongs to the cytidine and deoxycytidylate deaminase family.

Ontologies

Keywords
Biological process	mRNA processing
Coding sequence diversity	Polymorphism
Ligand	Metal-binding Zinc
Molecular function	Hydrolase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA demethylation Inferred from direct assay Ref.7. Source: UniProtKB mRNA modification Inferred from electronic annotation. Source: Compara mRNA processing Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	RNA binding Traceable author statement Ref.1. Source: ProtInc cytidine deaminase activity Traceable author statement Ref.1. Source: ProtInc zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 224

224

Probable C->U-editing enzyme APOBEC-2

PRO_0000171749

Sites

Active site

100

1

Proton donor Ref.8

Metal binding

60

1

Zinc; catalytic

Metal binding

98

1

Zinc; catalytic

Metal binding

128

1

Zinc; catalytic

Metal binding

131

1

Zinc; catalytic

Natural variations

Natural variant

136

1

I → T. Ref.3
Corresponds to variant rs2076472 [ dbSNP | Ensembl ].

VAR_024406

Secondary structure

1

.

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224

Helix Strand Turn

Details...

Helix

48 – 53

6

Turn

54 – 56

3

Beta strand

62 – 64

3

Beta strand

68 – 77

10

Beta strand

83 – 94

12

Helix

99 – 106

8

Beta strand

116 – 125

10

Helix

129 – 141

13

Beta strand

145 – 153

9

Helix

160 – 171

12

Beta strand

175 – 178

4

Helix

181 – 191

11

Helix

208 – 223

16

Sequences

	Sequence		Length	Mass (Da)
	Q9Y235 [UniParc]. Last modified November 1, 1999. Version 1. Checksum: CA0905AFAA8C8FA1	FASTA	224	25,703
	10 20 30 40 50 60 MAQKEEAAVA TEAASQNGED LENLDDPEKL KELIELPPFE IVTGERLPAN FFKFQFRNVE 70 80 90 100 110 120 YSSGRNKTFL CYVVEAQGKG GQVQASRGYL EDEHAAAHAE EAFFNTILPA FDPALRYNVT 130 140 150 160 170 180 WYVSSSPCAA CADRIIKTLS KTKNLRLLIL VGRLFMWEEP EIQAALKKLK EAGCKLRIMK 190 200 210 220 PQDFEYVWQN FVEQEEGESK AFQPWEDIQE NFLYYEEKLA DILK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"APOBEC-2, a cardiac- and skeletal muscle-specific member of the cytidine deaminase supergene family." Liao W., Hong S.-H., Chan B.H.-J., Rudolph F.B., Clark S.C., Chan L. Biochem. Biophys. Res. Commun. 260:398-404(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Heart.
[2]	"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]. Tissue: Skeletal muscle.
[3]	Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S. Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT THR-136. Tissue: Pancreas.
[4]	"The DNA sequence and analysis of human chromosome 6." Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S. Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	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].
[6]	"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]. Tissue: PNS.
[7]	"Hydroxylation of 5-methylcytosine by TET1 promotes active DNA demethylation in the adult brain." Guo J.U., Su Y., Zhong C., Ming G.L., Song H. Cell 145:423-434(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN DNA DEMETHYLATION.
[8]	"The APOBEC-2 crystal structure and functional implications for the deaminase AID." Prochnow C., Bransteitter R., Klein M.G., Goodman M.F., Chen X.S. Nature 445:447-451(2007) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 41-224, SUBUNIT, COFACTOR, ACTIVE SITE, ZINC-BINDING SITES.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF161698 mRNA. Translation: AAD45360.1.
AK223461 mRNA. Translation: BAD97181.1.
AK313288 mRNA. Translation: BAG36096.1.
AL031778 Genomic DNA. Translation: CAB44740.1.
CH471081 Genomic DNA. Translation: EAX04009.1.
BC047767 mRNA. Translation: AAH47767.1.
BC069688 mRNA. Translation: AAH69688.1.
BC069764 mRNA. Translation: AAH69764.1.

IPI

IPI00009550.

RefSeq

NP_006780.1. NM_006789.3.

UniGene

Hs.555915.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2NYT	X-ray	2.50	A/B/C/D	41-224	[»]

ProteinModelPortal

Q9Y235.

ModBase

Search...

Protein-protein interaction databases

STRING

9606.ENSP00000244669.

PTM databases

PhosphoSite

Q9Y235.

Polymorphism databases

DMDM

23396446.

Proteomic databases

PaxDb

Q9Y235.

PRIDE

Q9Y235.

Protocols and materials databases

DNASU

10930.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000244669; ENSP00000244669; ENSG00000124701.

GeneID

10930.

KEGG

hsa:10930.

UCSC

uc003opl.3. human.

Organism-specific databases

CTD

10930.

GeneCards

GC06P041020.

HGNC

HGNC:605. APOBEC2.

HPA

HPA014252.
HPA017957.

MIM

604797. gene.

neXtProt

NX_Q9Y235.

PharmGKB

PA24890.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG44965.

HOGENOM

HOG000033754.

HOVERGEN

HBG107155.

InParanoid

Q9Y235.

KO

K01500.

OMA

QDFEYIW.

OrthoDB

EOG47H5QZ.

PhylomeDB

Q9Y235.

Gene expression databases

Bgee

Q9Y235.

CleanEx

HS_APOBEC2.

Genevestigator

Q9Y235.

GermOnline

ENSG00000124701. Homo sapiens.

Family and domain databases

InterPro

IPR007904. APOBEC_C.
IPR013158. APOBEC_N.
IPR016193. Cytidine_deaminase-like.
[Graphical view]

Pfam

PF05240. APOBEC_C. 1 hit.
PF08210. APOBEC_N. 1 hit.
[Graphical view]

SUPFAM

SSF53927. Cytidine_deaminase-like. 1 hit.

PROSITE

PS00903. CYT_DCMP_DEAMINASES. False negative.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q9Y235.

GenomeRNAi

10930.

NextBio

41523.

SOURCE

Search...

Entry information

Entry name

ABEC2_HUMAN

Accession

Primary (citable) accession number: Q9Y235
Secondary accession number(s): B2R899 , Q53F28, Q5TGU5, Q5TGU6

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 19, 2002
Last sequence update:	November 1, 1999
Last modified:	May 1, 2013
This is version 98 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.