Reviewed, UniProtKB/Swiss-Prot Q9UH17 (ABC3B_HUMAN)

Names and origin

Protein names

Recommended name:
    Probable DNA dC->dU-editing enzyme APOBEC-3B
    EC=3.5.4.-
Alternative name(s):
    Phorbolin-1-related protein
    Phorbolin-2/3

Gene names

Name:

APOBEC3B

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	382 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Lacks cytidine deaminase activity, at least on RNA molecules (monomeric nucleoside substrates or synthetic apoB, NF1 and NAT1 RNA template). Binds to apoB and AU-rich RNAs. Unable to reduce HIV-1 infectivity in vitro. Ref.2 Ref.7
Cofactor	Zinc.
Subunit structure	Homodimer. Interacts with APOBEC3G. Does not interact with APOBEC1. Ref.5
Tissue specificity	Expressed at high and moderate levels in peripheral blood leukocytes, spleen, testes, heart, thymus, prostate and ovary. Also expressed at low levels in several other tissues and tumor cell lines. Ref.5
Induction	Phorbol 12-myristate 13-acetate (PMA) induces overexpression in keratinocytes. Ref.1
Miscellaneous	It is one of seven related genes or pseudogenes found in a cluster, thought to result from gene duplication, on chromosome 22.
Sequence similarities	Belongs to the cytidine and deoxycytidylate deaminase family.
Sequence caution	The sequence AAD00090.1 differs from that shown. Reason: Frameshift at positions 59 and 134. Frameshifts result in two separate ORFs termed phorbolins 2 and 3.

Ontologies

Keywords
Coding sequence diversity	Alternative splicing Polymorphism
Ligand	Metal-binding RNA-binding Zinc
Molecular function	Hydrolase
Technical term	Complete proteome
Gene Ontology (GO)
Molecular function	RNA binding Inferred from electronic annotation. Source: UniProtKB-KW hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amidines Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9UH17-1)

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 (identifier: Q9UH17-2)

The sequence of this isoform differs from the canonical sequence as follows:
     191-382: YLMDPDTFTF...LRAILQNQGN → LRIFSVAFTA...CVRSFRRTHT

Note: May be due to a competing donor splice site.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 382	382	Probable DNA dC->dU-editing enzyme APOBEC-3B		PRO_0000171753
Sites
	Active site	255	1	Proton donor Potential
	Metal binding	66	1	Zinc By similarity
	Metal binding	97	1	Zinc By similarity
	Metal binding	100	1	Zinc By similarity
	Metal binding	253	1	Zinc By similarity
	Metal binding	284	1	Zinc By similarity
	Metal binding	289	1	Zinc By similarity
Natural variations
	Alternative sequence	191 – 382	192	YLMDP…QNQGN → LRIFSVAFTAAMRSCASWTW FLLCSWTRPRSTGSLGSSPG APASPGAVPGKCVRSFRRTH T in isoform 2.		VSP_009802
	Natural variant	62	1	K → E: dbSNP rs2076109.		VAR_018142
	Natural variant	98	1	P → L: dbSNP rs2076110.		VAR_018143
	Natural variant	109	1	S → A: dbSNP rs17000697.		VAR_033455
	Natural variant	146	1	T → K: dbSNP rs5995649. Ref.1 Ref.4		VAR_018144
	Natural variant	351	1	R → H: dbSNP rs1053813.		VAR_048722
Experimental info
	Sequence conflict	103 – 104	2	KL → NV in AAD00090. Ref.1
	Sequence conflict	227 – 228	2	TW → WM in AAD00089. Ref.1
	Sequence conflict	255 – 256	2	EL → DW in AAD00089. Ref.1
	Sequence conflict	306	1	R → P in AAD00089. Ref.1
	Sequence conflict	356	1	F → S in AAW31743. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: DA6EDD23E8856240	FASTA	382	45,924
	10 20 30 40 50 60 MNPQIRNPME RMYRDTFYDN FENEPILYGR SYTWLCYEVK IKRGRSNLLW DTGVFRGQVY 70 80 90 100 110 120 FKPQYHAEMC FLSWFCGNQL PAYKCFQITW FVSWTPCPDC VAKLAEFLSE HPNVTLTISA 130 140 150 160 170 180 ARLYYYWERD YRRALCRLSQ AGARVTIMDY EEFAYCWENF VYNEGQQFMP WYKFDENYAF 190 200 210 220 230 240 LHRTLKEILR YLMDPDTFTF NFNNDPLVLR RRQTYLCYEV ERLDNGTWVL MDQHMGFLCN 250 260 270 280 290 300 EAKNLLCGFY GRHAELRFLD LVPSLQLDPA QIYRVTWFIS WSPCFSWGCA GEVRAFLQEN 310 320 330 340 350 360 THVRLRIFAA RIYDYDPLYK EALQMLRDAG AQVSIMTYDE FEYCWDTFVY RQGCPFQPWD 370 380 GLEEHSQALS GRLRAILQNQ GN
	Isoform 2. Checksum: 9F2B8220F6689383	FASTA	251	29,798
	10 20 30 40 50 60 MNPQIRNPME RMYRDTFYDN FENEPILYGR SYTWLCYEVK IKRGRSNLLW DTGVFRGQVY 70 80 90 100 110 120 FKPQYHAEMC FLSWFCGNQL PAYKCFQITW FVSWTPCPDC VAKLAEFLSE HPNVTLTISA 130 140 150 160 170 180 ARLYYYWERD YRRALCRLSQ AGARVTIMDY EEFAYCWENF VYNEGQQFMP WYKFDENYAF 190 200 210 220 230 240 LHRTLKEILR LRIFSVAFTA AMRSCASWTW FLLCSWTRPR STGSLGSSPG APASPGAVPG 250 KCVRSFRRTH T

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Psoriasis upregulated phorbolin-1 shares structural but not functional similarity to the mRNA-editing protein apobec-1." Madsen P.P., Anant S., Rasmussen H.H., Gromov P., Vorum H., Dumanski J.P., Tommerup N., Collins J.E., Wright C.L., Dunham I., Macginnitie A.J., Davidson N.O., Celis J.E. J. Invest. Dermatol. 113:162-169(1999) [PubMed: 10469298] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT LYS-146, INDUCTION. Tissue: Keratinocyte.
[2]	"Regulated production and anti-HIV type 1 activities of cytidine deaminases APOBEC3B, 3F, and 3G." Rose K.M., Marin M., Kozak S.L., Kabat D. AIDS Res. Hum. Retroviruses 21:611-619(2005) [PubMed: 16060832] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION.
[3]	"The DNA sequence of human chromosome 22." Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M. , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H. Nature 402:489-495(1999) [PubMed: 10591208] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANT LYS-146. Tissue: Uterus.
[5]	"An anthropoid-specific locus of orphan C to U RNA-editing enzymes on chromosome 22." Jarmuz A., Chester A., Bayliss J., Gisbourne J., Dunham I., Scott J., Navaratnam N. Genomics 79:285-296(2002) [PubMed: 11863358] [Abstract] Cited for: GENE FAMILY ORGANIZATION, TISSUE SPECIFICITY, RNA-BINDING, ZINC-BINDING, INTERACTION WITH APOBEC3G.
[6]	"Messenger RNA editing in mammals: new members of the APOBEC family seeking roles in the family business." Wedekind J.E., Dance G.S.C., Sowden M.P., Smith H.C. Trends Genet. 19:207-216(2003) [PubMed: 12683974] [Abstract] Cited for: REVIEW ON APOBEC FAMILIES.
[7]	"Species-specific exclusion of APOBEC3G from HIV-1 virions by Vif." Mariani R., Chen D., Schroefelbauer B., Navarro F., Koenig R., Bollman B., Muenk C., Nymark-McMahon H., Landau N.R. Cell 114:21-31(2003) [PubMed: 12859895] [Abstract] Cited for: FUNCTION IN HIV-1 INFECTIVITY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U61083 mRNA. Translation: AAD00089.1. Different initiation. U61084 mRNA. Translation: AAD00090.1. Frameshift. AY743217 mRNA. Translation: AAW31743.1. AL022318 Genomic DNA. Translation: CAB45270.1. BC053859 mRNA. Translation: AAH53859.1.
IPI	IPI00005531. IPI00409617.
RefSeq	NP_004891.3.
UniGene	Hs.226307
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q9UH17.
PTM databases
PhosphoSite	Q9UH17.
Proteomic databases
PRIDE	Q9UH17.
Genome annotation databases
Ensembl	ENST00000333467; ENSP00000327459; ENSG00000179750; Homo sapiens. [Genome view]
GeneID	9582.
KEGG	hsa:9582.
UCSC	uc003awo.1. human.
Organism-specific databases
CTD	9582.
GeneCards	GC22P037702.
HGNC	HGNC:17352. APOBEC3B.
MIM	607110. gene.
PharmGKB	PA24892.
GenAtlas	Search...
Phylogenomic databases
HOVERGEN	Q9UH17.
OrthoDB	EOG934ZRM.
Gene expression databases
ArrayExpress	Q9UH17.
Bgee	Q9UH17.
CleanEx	HS_APOBEC3B.
Genevestigator	Q9UH17.
GermOnline	ENSG00000179750. Homo sapiens.
Family and domain databases
InterPro	IPR016192. APOBEC/CMP_deaminase_Zn-bd. IPR007904. APOBEC_C. IPR013158. APOBEC_N. IPR016193. Cytidine_deaminase-like. [Graphical view]
Pfam	PF05240. APOBEC_C. 2 hits. PF08210. APOBEC_N. 2 hits. [Graphical view]
PROSITE	PS00903. CYT_DCMP_DEAMINASES. 2 hits. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	35945.
SOURCE	Search...

Entry information

Entry name

ABC3B_HUMAN

Accession

Primary (citable) accession number: Q9UH17
Secondary accession number(s): O95618 , Q5IFJ4, Q7Z2N3, Q7Z6D6, Q9UE74

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 11, 2001
Last sequence update:	May 1, 2000
Last modified:	December 15, 2009
This is version 80 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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.