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Single-stranded DNA cytosine deaminase (EC 3.5.4.38) (Activation-induced cytidine deaminase) (AID) (Cytidine aminohydrolase)

 AICDA_HUMAN             Reviewed;         198 AA.
Q9GZX7; Q6QJ81; Q8NFC1;
10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
01-MAR-2001, sequence version 1.
30-AUG-2017, entry version 148.
RecName: Full=Single-stranded DNA cytosine deaminase;
EC=3.5.4.38 {ECO:0000269|PubMed:18722174};
AltName: Full=Activation-induced cytidine deaminase;
Short=AID;
AltName: Full=Cytidine aminohydrolase;
Name=AICDA; Synonyms=AID;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
PubMed=10950930; DOI=10.1006/geno.2000.6268;
Muto T., Muramatsu M., Taniwaki M., Kinoshita K., Honjo T.;
"Isolation, tissue distribution, and chromosomal localization of the
human activation-induced cytidine deaminase (hAID) gene.";
Genomics 68:85-88(2000).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), AND VARIANTS
HIGM2 TRP-24; ARG-80; PRO-106; VAL-139 AND SER-151.
PubMed=11007475; DOI=10.1016/S0092-8674(00)00079-9;
Revy P., Muto T., Levy Y., Geissmann F., Plebani A., Sanal O.,
Catalan N., Forveille M., Dufourcq-Lagelouse R., Gennery A.,
Tezcan I., Ersoy F., Kayserili H., Ugazio A.G., Brousse N.,
Muramatsu M., Notarangelo L.D., Kinoshita K., Honjo T., Fischer A.,
Durandy A.;
"Activation-induced cytidine deaminase (AID) deficiency causes the
autosomal recessive form of the Hyper-IgM syndrome (HIGM2).";
Cell 102:565-575(2000).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=12202747; DOI=10.1073/pnas.192442899;
Martin A., Scharff M.D.;
"Somatic hypermutation of the AID transgene in B and non-B cells.";
Proc. Natl. Acad. Sci. U.S.A. 99:12304-12308(2002).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Roa S., Gonzalez-Sarmiento R.;
"Intracellular localization of AID isoforms.";
Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16541075; DOI=10.1038/nature04569;
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
Kucherlapati R., Weinstock G., Gibbs R.A.;
"The finished DNA sequence of human chromosome 12.";
Nature 440:346-351(2006).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=B-cell;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
SUBCELLULAR LOCATION.
PubMed=14769937; DOI=10.1073/pnas.0307335101;
Ito S., Nagaoka H., Shinkura R., Begum N., Muramatsu M., Nakata M.,
Honjo T.;
"Activation-induced cytidine deaminase shuttles between nucleus and
cytoplasm like apolipoprotein B mRNA editing catalytic polypeptide
1.";
Proc. Natl. Acad. Sci. U.S.A. 101:1975-1980(2004).
[9]
PHOSPHORYLATION AT THR-27 AND SER-38, INTERACTION WITH PRKACA AND
PRKAR1A, AND MUTAGENESIS OF THR-27 AND SER-38.
PubMed=16387847; DOI=10.1073/pnas.0509969103;
Pasqualucci L., Kitaura Y., Gu H., Dalla-Favera R.;
"PKA-mediated phosphorylation regulates the function of activation-
induced deaminase (AID) in B cells.";
Proc. Natl. Acad. Sci. U.S.A. 103:395-400(2006).
[10]
INTERACTION WITH CTNNBL1, FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR
LOCATION, PHOSPHORYLATION AT SER-38, IDENTIFICATION BY MASS
SPECTROMETRY, AND MUTAGENESIS OF 39-ALA--PHE-42 AND SER-38.
PubMed=18722174; DOI=10.1016/j.molcel.2008.07.009;
Conticello S.G., Ganesh K., Xue K., Lu M., Rada C., Neuberger M.S.;
"Interaction between antibody-diversification enzyme AID and
spliceosome-associated factor CTNNBL1.";
Mol. Cell 31:474-484(2008).
[11]
FUNCTION IN DNA DEMETHYLATION.
PubMed=21496894; DOI=10.1016/j.cell.2011.03.022;
Guo J.U., Su Y., Zhong C., Ming G.L., Song H.;
"Hydroxylation of 5-methylcytosine by TET1 promotes active DNA
demethylation in the adult brain.";
Cell 145:423-434(2011).
[12]
INTERACTION WITH CTNNBL1, FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS
OF LYS-10; VAL-18; ARG-19; TRP-20; ARG-50; ARG-112 AND PHE-193, AND
CHARACTERIZATION OF VARIANT TRP-24.
PubMed=21385873; DOI=10.1074/jbc.M110.208769;
Ganesh K., Adam S., Taylor B., Simpson P., Rada C., Neuberger M.;
"CTNNBL1 is a novel nuclear localization sequence-binding protein that
recognizes RNA-splicing factors CDC5L and Prp31.";
J. Biol. Chem. 286:17091-17102(2011).
[13]
SUBCELLULAR LOCATION, AND MUTAGENESIS OF THR-27.
PubMed=21659520; DOI=10.1074/jbc.M111.235721;
Demorest Z.L., Li M., Harris R.S.;
"Phosphorylation directly regulates the intrinsic DNA cytidine
deaminase activity of activation-induced deaminase and APOBEC3G
protein.";
J. Biol. Chem. 286:26568-26575(2011).
[14]
FUNCTION, AND INTERACTION WITH SUPT6H.
PubMed=21518874; DOI=10.1073/pnas.1104423108;
Okazaki I.M., Okawa K., Kobayashi M., Yoshikawa K., Kawamoto S.,
Nagaoka H., Shinkura R., Kitawaki Y., Taniguchi H., Natsume T.,
Iemura S., Honjo T.;
"Histone chaperone Spt6 is required for class switch recombination but
not somatic hypermutation.";
Proc. Natl. Acad. Sci. U.S.A. 108:7920-7925(2011).
[15]
INDUCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=23166356; DOI=10.1084/jem.20121387;
Basso K., Schneider C., Shen Q., Holmes A.B., Setty M., Leslie C.,
Dalla-Favera R.;
"BCL6 positively regulates AID and germinal center gene expression via
repression of miR-155.";
J. Exp. Med. 209:2455-2465(2012).
[16]
INTERACTION WITH RNF126, AND UBIQUITINATION BY RNF126.
PubMed=23277564; DOI=10.1073/pnas.1214538110;
Delker R.K., Zhou Y., Strikoudis A., Stebbins C.E., Papavasiliou F.N.;
"Solubility-based genetic screen identifies RING finger protein 126 as
an E3 ligase for activation-induced cytidine deaminase.";
Proc. Natl. Acad. Sci. U.S.A. 110:1029-1034(2013).
[17]
X-RAY CRYSTALLOGRAPHY (2.81 ANGSTROMS) OF 23-183 IN COMPLEX WITH ZINC.
PubMed=27258794; DOI=10.1016/j.dnarep.2016.05.029;
Pham P., Afif S.A., Shimoda M., Maeda K., Sakaguchi N., Pedersen L.C.,
Goodman M.F.;
"Structural analysis of the activation-induced deoxycytidine deaminase
required in immunoglobulin diversification.";
DNA Repair 43:48-56(2016).
[18]
VARIANT CYS-25.
PubMed=11544457; DOI=10.1067/mai.2001.117456;
Noguchi E., Shibasaki M., Inudou M., Kamioka M., Yokouchi Y.,
Yamakawa-Kobayashi K., Hamaguchi H., Matsui A., Arinami T.;
"Association between a new polymorphism in the activation-induced
cytidine deaminase gene and atopic asthma and the regulation of total
serum IgE levels.";
J. Allergy Clin. Immunol. 108:382-386(2001).
[19]
VARIANTS HIGM2 TRP-24; TYR-56; ARG-80; ARG-87; PRO-106; VAL-139;
SER-151 AND SER-174.
PubMed=14962793; DOI=10.1016/j.clim.2003.10.007;
Quartier P., Bustamante J., Sanal O., Plebani A., Debre M.,
Deville A., Litzman J., Levy J., Fermand J.P., Lane P., Horneff G.,
Aksu G., Yalcin I., Davies G., Tezcan I., Ersoy F., Catalan N.,
Imai K., Fischer A., Durandy A.;
"Clinical, immunologic and genetic analysis of 29 patients with
autosomal recessive hyper-IgM syndrome due to activation-induced
cytidine deaminase deficiency.";
Clin. Immunol. 110:22-29(2004).
[20]
VARIANT HIGM2 LEU-15.
PubMed=23803409; DOI=10.1016/j.clim.2013.05.017;
Caratao N., Cortesao C.S., Reis P.H., Freitas R.F., Jacob C.M.,
Pastorino A.C., Carneiro-Sampaio M., Barreto V.M.;
"A novel activation-induced cytidine deaminase (AID) mutation in
Brazilian patients with hyper-IgM type 2 syndrome.";
Clin. Immunol. 148:279-286(2013).
[21]
VARIANTS HIGM2 HIS-31 AND PRO-130.
PubMed=26545377; DOI=10.1007/s00251-015-0878-6;
Ouadani H., Ben-Mustapha I., Ben-ali M., Ben-khemis L., Largueche B.,
Boussoffara R., Maalej S., Fetni I., Hassayoun S., Mahfoudh A.,
Mellouli F., Yalaoui S., Masmoudi H., Bejaoui M., Barbouche M.R.;
"Novel and recurrent AID mutations underlie prevalent autosomal
recessive form of HIGM in consanguineous patients.";
Immunogenetics 68:19-28(2016).
[22]
CHARACTERIZATION OF VARIANTS HIGM2 TYR-56 AND PRO-130, AND FUNCTION.
PubMed=27716525; DOI=10.1016/j.molimm.2016.09.025;
Ouadani H., Ben-Mustapha I., Ben-Ali M., Largueche B., Jovanic T.,
Garcia S., Arcangioli B., Elloumi-Zghal H., Fathallah D., Hachicha M.,
Masmoudi H., Rougeon F., Barbouche M.R.;
"Activation induced cytidine deaminase mutant (AID-His130Pro) from
Hyper IgM 2 patient retained mutagenic activity on SHM artificial
substrate.";
Mol. Immunol. 79:77-82(2016).
-!- FUNCTION: Single-stranded DNA-specific cytidine deaminase.
Involved in somatic hypermutation (SHM), gene conversion, and
class-switch recombination (CSR) in B-lymphocytes by deaminating C
to U during transcription of Ig-variable (V) and Ig-switch (S)
region DNA. Required for several crucial steps of B-cell terminal
differentiation necessary for efficient antibody responses
(PubMed:18722174, PubMed:21385873, PubMed:21518874,
PubMed:27716525). May also play a role in the epigenetic
regulation of gene expression by participating in DNA
demethylation (PubMed:21496894). {ECO:0000269|PubMed:18722174,
ECO:0000269|PubMed:21385873, ECO:0000269|PubMed:21496894,
ECO:0000269|PubMed:21518874, ECO:0000269|PubMed:27716525}.
-!- CATALYTIC ACTIVITY: Cytosine in single-stranded DNA + H(2)O =
uracil in single-stranded DNA + NH(3).
{ECO:0000269|PubMed:18722174}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000269|PubMed:27258794};
-!- SUBUNIT: Interacts with CTNNBL1; the interaction is important for
the immunoglobulin switch activity of AICDA. Interacts (via its
NLS) with KPNA1. Interacts with PKA/PRKACA and PRKAR1A/PKR1.
Interacts with TRIM28 and NCL (By similarity). Interacts with
SUPT6H. Interacts with RNF126. {ECO:0000250,
ECO:0000269|PubMed:16387847, ECO:0000269|PubMed:18722174,
ECO:0000269|PubMed:21385873, ECO:0000269|PubMed:21518874,
ECO:0000269|PubMed:23277564}.
-!- INTERACTION:
Q784Z8:C (xeno); NbExp=2; IntAct=EBI-3834328, EBI-11666471;
P31689:DNAJA1; NbExp=6; IntAct=EBI-3834328, EBI-347834;
O60884:DNAJA2; NbExp=3; IntAct=EBI-3834328, EBI-352957;
P24522:GADD45A; NbExp=5; IntAct=EBI-3834328, EBI-448167;
P11142:HSPA8; NbExp=2; IntAct=EBI-3834328, EBI-351896;
Q13569:TDG; NbExp=5; IntAct=EBI-3834328, EBI-348333;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21385873}.
Cytoplasm {ECO:0000269|PubMed:18722174,
ECO:0000269|PubMed:21385873, ECO:0000269|PubMed:23166356}.
Note=Predominantly cytoplasmic but shuttles between the nucleus
and the cytoplasm. {ECO:0000269|PubMed:21385873}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9GZX7-1; Sequence=Displayed;
Name=2;
IsoId=Q9GZX7-2; Sequence=VSP_047803;
-!- TISSUE SPECIFICITY: Strongly expressed in lymph nodes and tonsils.
{ECO:0000269|PubMed:23166356}.
-!- INDUCTION: Negatively regulated by microRNA-155 (miR-155).
{ECO:0000269|PubMed:23166356}.
-!- PTM: Ser-38 is the major site whereas Thr-27 is the minor site of
phosphorylation. Phosphorylation regulates its class-switch
recombination activity. {ECO:0000269|PubMed:16387847,
ECO:0000269|PubMed:18722174}.
-!- PTM: Probably monoubiquitinated on several residues by RNF126.
{ECO:0000269|PubMed:23277564}.
-!- DISEASE: Immunodeficiency with hyper-IgM 2 (HIGM2) [MIM:605258]: A
rare immunodeficiency syndrome characterized by normal or elevated
serum IgM levels with absence of IgG, IgA, and IgE. It results in
a profound susceptibility to bacterial infections.
{ECO:0000269|PubMed:11007475, ECO:0000269|PubMed:14962793,
ECO:0000269|PubMed:23803409, ECO:0000269|PubMed:26545377,
ECO:0000269|PubMed:27716525}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase
family. {ECO:0000305}.
-!- WEB RESOURCE: Name=AICDAbase; Note=AICDA mutation db;
URL="http://structure.bmc.lu.se/idbase/AICDAbase/";
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EMBL; AB040431; BAB12721.1; -; mRNA.
EMBL; AB040430; BAB12720.1; -; Genomic_DNA.
EMBL; AF529819; AAM95406.1; -; mRNA.
EMBL; AY536516; AAS92920.1; -; mRNA.
EMBL; BT007402; AAP36066.1; -; mRNA.
EMBL; AC092184; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC006296; AAH06296.1; -; mRNA.
CCDS; CCDS41747.1; -. [Q9GZX7-1]
CCDS; CCDS81662.1; -. [Q9GZX7-2]
RefSeq; NP_001317272.1; NM_001330343.1. [Q9GZX7-2]
RefSeq; NP_065712.1; NM_020661.3. [Q9GZX7-1]
UniGene; Hs.149342; -.
PDB; 5JJ4; X-ray; 2.81 A; A/B/C=23-183.
PDBsum; 5JJ4; -.
ProteinModelPortal; Q9GZX7; -.
SMR; Q9GZX7; -.
BioGrid; 121497; 54.
DIP; DIP-48519N; -.
ELM; Q9GZX7; -.
IntAct; Q9GZX7; 24.
MINT; MINT-4717382; -.
STRING; 9606.ENSP00000229335; -.
iPTMnet; Q9GZX7; -.
PhosphoSitePlus; Q9GZX7; -.
BioMuta; AICDA; -.
DMDM; 23813666; -.
MaxQB; Q9GZX7; -.
PaxDb; Q9GZX7; -.
PeptideAtlas; Q9GZX7; -.
PRIDE; Q9GZX7; -.
DNASU; 57379; -.
Ensembl; ENST00000229335; ENSP00000229335; ENSG00000111732. [Q9GZX7-1]
Ensembl; ENST00000537228; ENSP00000445691; ENSG00000111732. [Q9GZX7-2]
GeneID; 57379; -.
KEGG; hsa:57379; -.
UCSC; uc001qur.3; human. [Q9GZX7-1]
CTD; 57379; -.
DisGeNET; 57379; -.
GeneCards; AICDA; -.
HGNC; HGNC:13203; AICDA.
MalaCards; AICDA; -.
MIM; 605257; gene.
MIM; 605258; phenotype.
neXtProt; NX_Q9GZX7; -.
OpenTargets; ENSG00000111732; -.
Orphanet; 101089; Hyper-IgM syndrome type 2.
PharmGKB; PA24644; -.
eggNOG; ENOG410IFHW; Eukaryota.
eggNOG; ENOG4111HYQ; LUCA.
GeneTree; ENSGT00530000062933; -.
HOGENOM; HOG000033754; -.
HOVERGEN; HBG050434; -.
InParanoid; Q9GZX7; -.
KO; K10989; -.
OMA; RNKNGCH; -.
OrthoDB; EOG091G0J2L; -.
PhylomeDB; Q9GZX7; -.
TreeFam; TF331356; -.
BRENDA; 3.5.4.38; 2681.
SIGNOR; Q9GZX7; -.
GeneWiki; AICDA; -.
GenomeRNAi; 57379; -.
PRO; PR:Q9GZX7; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000111732; -.
CleanEx; HS_AICDA; -.
ExpressionAtlas; Q9GZX7; baseline and differential.
Genevisible; Q9GZX7; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0004126; F:cytidine deaminase activity; IDA:UniProtKB.
GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0030183; P:B cell differentiation; NAS:UniProtKB.
GO; GO:0071222; P:cellular response to lipopolysaccharide; IEA:Ensembl.
GO; GO:0042742; P:defense response to bacterium; IEA:Ensembl.
GO; GO:0080111; P:DNA demethylation; IDA:UniProtKB.
GO; GO:0045190; P:isotype switching; IEA:Ensembl.
GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
GO; GO:0090310; P:negative regulation of methylation-dependent chromatin silencing; IDA:UniProtKB.
GO; GO:0016445; P:somatic diversification of immunoglobulins; IDA:UniProtKB.
GO; GO:0016446; P:somatic hypermutation of immunoglobulin genes; IMP:UniProtKB.
InterPro; IPR016192; APOBEC/CMP_deaminase_Zn-bd.
InterPro; IPR013158; APOBEC_N.
InterPro; IPR002125; CMP_dCMP_dom.
InterPro; IPR016193; Cytidine_deaminase-like.
Pfam; PF08210; APOBEC_N; 1.
SUPFAM; SSF53927; SSF53927; 1.
PROSITE; PS00903; CYT_DCMP_DEAMINASES_1; 1.
PROSITE; PS51747; CYT_DCMP_DEAMINASES_2; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome; Cytoplasm;
Disease mutation; Hydrolase; Metal-binding; mRNA processing; Nucleus;
Phosphoprotein; Polymorphism; Reference proteome; Ubl conjugation;
Zinc.
CHAIN 1 198 Single-stranded DNA cytosine deaminase.
/FTId=PRO_0000171687.
DOMAIN 23 129 CMP/dCMP-type deaminase.
{ECO:0000255|PROSITE-ProRule:PRU01083}.
REGION 2 26 Interaction with SUPT6H.
{ECO:0000269|PubMed:21518874}.
REGION 39 42 Important for interaction with CTNNBL1.
{ECO:0000269|PubMed:18722174}.
REGION 88 116 Required for interaction with RNF126.
{ECO:0000269|PubMed:23277564}.
MOTIF 1 30 Bipartite nuclear localization signal.
{ECO:0000269|PubMed:14769937}.
MOTIF 183 198 Nuclear export signal.
{ECO:0000269|PubMed:14769937}.
ACT_SITE 58 58 Proton donor.
{ECO:0000250|UniProtKB:P0ABF6}.
METAL 56 56 Zinc; catalytic.
{ECO:0000269|PubMed:27258794}.
METAL 87 87 Zinc; catalytic.
{ECO:0000269|PubMed:27258794}.
METAL 90 90 Zinc; catalytic.
{ECO:0000269|PubMed:27258794}.
MOD_RES 27 27 Phosphothreonine; by PKA.
{ECO:0000269|PubMed:16387847}.
MOD_RES 38 38 Phosphoserine; by PKA.
{ECO:0000269|PubMed:16387847,
ECO:0000269|PubMed:18722174}.
VAR_SEQ 143 152 Missing (in isoform 2).
{ECO:0000303|Ref.4}.
/FTId=VSP_047803.
VARIANT 15 15 F -> L (in HIGM2).
{ECO:0000269|PubMed:23803409}.
/FTId=VAR_077563.
VARIANT 24 24 R -> W (in HIGM2; completely abolishes
nuclear import and interaction with
CTNNBL1, diminishes interaction with
KPNA1 and abolishes immunoglobulin class
switching; dbSNP:rs104894324).
{ECO:0000269|PubMed:11007475,
ECO:0000269|PubMed:14962793,
ECO:0000269|PubMed:21385873}.
/FTId=VAR_013774.
VARIANT 25 25 R -> C. {ECO:0000269|PubMed:11544457}.
/FTId=VAR_014091.
VARIANT 31 31 Y -> H (in HIGM2).
{ECO:0000269|PubMed:26545377}.
/FTId=VAR_077564.
VARIANT 56 56 H -> Y (in HIGM2; unknown pathological
significance; loss of mutagenic
activity). {ECO:0000269|PubMed:14962793,
ECO:0000269|PubMed:27716525}.
/FTId=VAR_077565.
VARIANT 80 80 W -> R (in HIGM2; dbSNP:rs104894320).
{ECO:0000269|PubMed:11007475,
ECO:0000269|PubMed:14962793}.
/FTId=VAR_013775.
VARIANT 87 87 C -> R (in HIGM2; unknown pathological
significance; dbSNP:rs762590894).
{ECO:0000269|PubMed:14962793}.
/FTId=VAR_077566.
VARIANT 106 106 L -> P (in HIGM2; dbSNP:rs104894321).
{ECO:0000269|PubMed:11007475,
ECO:0000269|PubMed:14962793}.
/FTId=VAR_013776.
VARIANT 130 130 H -> P (in HIGM2; slightly decreased
mutagenic activity).
{ECO:0000269|PubMed:26545377,
ECO:0000269|PubMed:27716525}.
/FTId=VAR_077567.
VARIANT 139 139 M -> V (in HIGM2; dbSNP:rs104894322).
{ECO:0000269|PubMed:11007475,
ECO:0000269|PubMed:14962793}.
/FTId=VAR_013777.
VARIANT 151 151 F -> S (in HIGM2; dbSNP:rs104894327).
{ECO:0000269|PubMed:11007475,
ECO:0000269|PubMed:14962793}.
/FTId=VAR_013778.
VARIANT 174 174 R -> S (in HIGM2; unknown pathological
significance).
{ECO:0000269|PubMed:14962793}.
/FTId=VAR_077568.
MUTAGEN 10 10 K->A: Little effect on nuclear import;
when associated with A-193. No effect on
CTNNBL1 binding.
{ECO:0000269|PubMed:21385873}.
MUTAGEN 18 18 V->S: Greatly impaired nuclear import;
when associated with V-19 and A-193.
Reduced interaction with both CTNNBL1 and
KPNA1, and abolishes immunoglobulin class
switching; when associated with V-19.
{ECO:0000269|PubMed:21385873}.
MUTAGEN 19 19 R->V: Greatly impaired nuclear import;
when associated with S-18 and A-193.
Reduced interaction with both CTNNBL1 and
KPNA1, and abolishes immunoglobulin class
switching; when associated with S-18.
{ECO:0000269|PubMed:21385873}.
MUTAGEN 20 20 W->K: Impaired nuclear import; when
associated with A-193. No effect on
CTNNBL1 binding.
{ECO:0000269|PubMed:21385873}.
MUTAGEN 27 27 T->A: Loss of phosphorylation. No effect
on cytidine deaminase activity. Impaired
class-switch recombination activity.
{ECO:0000269|PubMed:16387847,
ECO:0000269|PubMed:21659520}.
MUTAGEN 27 27 T->E: Phosphomimetic mutant which shows
loss of cytidine deaminase activity and
impaired class-switch recombination
activity. {ECO:0000269|PubMed:16387847,
ECO:0000269|PubMed:21659520}.
MUTAGEN 38 38 S->A: Loss of phosphorylation. Impaired
class-switch recombination activity. No
effect on interaction with CTNNBL1.
{ECO:0000269|PubMed:16387847,
ECO:0000269|PubMed:18722174}.
MUTAGEN 38 38 S->D: No effect on interaction with
CTNNBL1. {ECO:0000269|PubMed:16387847,
ECO:0000269|PubMed:18722174}.
MUTAGEN 39 42 ATSF->GGQV: Greatly reduced interaction
with CTNNBL1 but no effect on subcellular
location, enzyme activity, ability to
oligomerize nor on phosphorylation at
Ser-38. Diminished antibody
diversification.
{ECO:0000269|PubMed:18722174}.
MUTAGEN 50 50 R->G: Some reduced nuclear import; when
associated with A-193.
{ECO:0000269|PubMed:21385873}.
MUTAGEN 112 112 R->D: Greatly reduced nuclear import;
when associated with A-193.
{ECO:0000269|PubMed:21385873}.
MUTAGEN 193 193 F->A: Completely abolishes nuclear
import; when associated with W-24 or D-
112. Little affect on nuclear import;
when associated with A-10. Greatly
impaired nuclear import; when associated
with K-20 or G-50. Almost completely
abolishes nuclear import; when associated
with S-18 and V-19.
{ECO:0000269|PubMed:21385873}.
CONFLICT 119 119 R -> H (in Ref. 3; AAM95406).
{ECO:0000305}.
STRAND 28 36 {ECO:0000244|PDB:5JJ4}.
STRAND 42 50 {ECO:0000244|PDB:5JJ4}.
HELIX 57 68 {ECO:0000244|PDB:5JJ4}.
STRAND 74 84 {ECO:0000244|PDB:5JJ4}.
HELIX 88 99 {ECO:0000244|PDB:5JJ4}.
STRAND 104 112 {ECO:0000244|PDB:5JJ4}.
HELIX 122 131 {ECO:0000244|PDB:5JJ4}.
STRAND 135 138 {ECO:0000244|PDB:5JJ4}.
HELIX 141 150 {ECO:0000244|PDB:5JJ4}.
HELIX 165 179 {ECO:0000244|PDB:5JJ4}.
SEQUENCE 198 AA; 23954 MW; 3C27BB143DB184A9 CRC64;
MDSLLMNRRK FLYQFKNVRW AKGRRETYLC YVVKRRDSAT SFSLDFGYLR NKNGCHVELL
FLRYISDWDL DPGRCYRVTW FTSWSPCYDC ARHVADFLRG NPNLSLRIFT ARLYFCEDRK
AEPEGLRRLH RAGVQIAIMT FKDYFYCWNT FVENHERTFK AWEGLHENSV RLSRQLRRIL
LPLYEVDDLR DAFRTLGL


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