Full text data of ADD3
ADD3
(ADDL)
[Confidence: low (only semi-automatic identification from reviews)]
Gamma-adducin (Adducin-like protein 70)
Gamma-adducin (Adducin-like protein 70)
UniProt
Q9UEY8
ID ADDG_HUMAN Reviewed; 706 AA.
AC Q9UEY8; D3DRA8; O43243; Q5VU09; Q92773; Q9UEY7;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAY-2000, sequence version 1.
DT 22-JAN-2014, entry version 112.
DE RecName: Full=Gamma-adducin;
DE AltName: Full=Adducin-like protein 70;
GN Name=ADD3; Synonyms=ADDL;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RX PubMed=8893809;
RA Katagiri T., Ozaki K., Fujiwara T., Shimizu F., Kawai A., Okuno S.,
RA Suzuki M., Nakamura Y., Takahashi E., Hirai Y.;
RT "Cloning, expression and chromosome mapping of adducin-like 70 (ADDL),
RT a human cDNA highly homologous to human erythrocyte adducin.";
RL Cytogenet. Cell Genet. 74:90-95(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Moorthy S., Bennett V.;
RT "Cloning in the gamma quadrant.";
RL Submitted (SEP-1995) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING.
RX PubMed=10581174; DOI=10.1006/bbrc.1999.1769;
RA Citterio L., Azzani T., Duga S., Bianchi G.;
RT "Genomic organization of the human gamma adducin gene.";
RL Biochem. Biophys. Res. Commun. 266:110-114(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Endometrium;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
RA Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
RA Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
RA Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
RA Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
RA Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
RA Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
RA Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
RA Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
RA Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
RA Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
RA Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
RA Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
RA Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
RA Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
RA Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
RA Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
RA Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Ovary;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP SUMOYLATION.
RX PubMed=15561718; DOI=10.1074/jbc.M411718200;
RA Gocke C.B., Yu H., Kang J.;
RT "Systematic identification and analysis of mammalian small ubiquitin-
RT like modifier substrates.";
RL J. Biol. Chem. 280:5004-5012(2005).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-673, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42, AND MASS
RP SPECTROMETRY.
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-64; SER-423; SER-442;
RP SER-673; SER-677 AND SER-681, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-402; SER-423 AND
RP SER-681, AND MASS SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT SER-42; SER-673 AND SER-677, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-677 AND SER-681, AND
RP MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
CC -!- FUNCTION: Membrane-cytoskeleton-associated protein that promotes
CC the assembly of the spectrin-actin network. Binds to calmodulin.
CC -!- SUBUNIT: Heterodimer of an alpha and a gamma subunit.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cell membrane;
CC Peripheral membrane protein; Cytoplasmic side.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Comment=Additional isoforms seem to exist;
CC Name=2; Synonyms=Long;
CC IsoId=Q9UEY8-1; Sequence=Displayed;
CC Name=1; Synonyms=Short;
CC IsoId=Q9UEY8-2; Sequence=VSP_000188;
CC -!- TISSUE SPECIFICITY: Isoform 1 is ubiquitously expressed.
CC -!- DOMAIN: Comprised of three regions: a N-terminal protease-
CC resistant globular head region, a short connecting subdomain, and
CC a protease-sensitive tail region.
CC -!- PTM: Sumoylated.
CC -!- SIMILARITY: Belongs to the aldolase class II family. Adducin
CC subfamily.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC and Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/ADD3ID520ch10q25.html";
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DR EMBL; D67031; BAA23783.1; -; mRNA.
DR EMBL; U37122; AAB17126.1; -; mRNA.
DR EMBL; Y14372; CAB51805.1; -; Genomic_DNA.
DR EMBL; Y14373; CAB51805.1; JOINED; Genomic_DNA.
DR EMBL; Y14374; CAB51805.1; JOINED; Genomic_DNA.
DR EMBL; Y14375; CAB51805.1; JOINED; Genomic_DNA.
DR EMBL; Y14376; CAB51805.1; JOINED; Genomic_DNA.
DR EMBL; Y14377; CAB51805.1; JOINED; Genomic_DNA.
DR EMBL; Y14378; CAB51805.1; JOINED; Genomic_DNA.
DR EMBL; Y14379; CAB51805.1; JOINED; Genomic_DNA.
DR EMBL; Y14380; CAB51805.1; JOINED; Genomic_DNA.
DR EMBL; Y14381; CAB51805.1; JOINED; Genomic_DNA.
DR EMBL; Y14382; CAB51805.1; JOINED; Genomic_DNA.
DR EMBL; Y14383; CAB51805.1; JOINED; Genomic_DNA.
DR EMBL; Y14384; CAB51805.1; JOINED; Genomic_DNA.
DR EMBL; Y14372; CAB51806.1; -; Genomic_DNA.
DR EMBL; Y14373; CAB51806.1; JOINED; Genomic_DNA.
DR EMBL; Y14374; CAB51806.1; JOINED; Genomic_DNA.
DR EMBL; Y14375; CAB51806.1; JOINED; Genomic_DNA.
DR EMBL; Y14376; CAB51806.1; JOINED; Genomic_DNA.
DR EMBL; Y14377; CAB51806.1; JOINED; Genomic_DNA.
DR EMBL; Y14378; CAB51806.1; JOINED; Genomic_DNA.
DR EMBL; Y14379; CAB51806.1; JOINED; Genomic_DNA.
DR EMBL; Y14380; CAB51806.1; JOINED; Genomic_DNA.
DR EMBL; Y14381; CAB51806.1; JOINED; Genomic_DNA.
DR EMBL; Y14382; CAB51806.1; JOINED; Genomic_DNA.
DR EMBL; Y14384; CAB51806.1; JOINED; Genomic_DNA.
DR EMBL; BX647403; CAI46048.1; -; mRNA.
DR EMBL; AL590628; CAH71739.1; -; Genomic_DNA.
DR EMBL; CH471066; EAW49573.1; -; Genomic_DNA.
DR EMBL; CH471066; EAW49574.1; -; Genomic_DNA.
DR EMBL; BC062559; AAH62559.1; -; mRNA.
DR PIR; JC7164; JC7164.
DR RefSeq; NP_001112.2; NM_001121.2.
DR RefSeq; NP_058432.1; NM_016824.3.
DR RefSeq; NP_063968.1; NM_019903.3.
DR RefSeq; XP_005269586.1; XM_005269529.1.
DR RefSeq; XP_005269587.1; XM_005269530.1.
DR RefSeq; XP_005269588.1; XM_005269531.1.
DR RefSeq; XP_005269589.1; XM_005269532.1.
DR RefSeq; XP_005269590.1; XM_005269533.1.
DR RefSeq; XP_005269591.1; XM_005269534.1.
DR UniGene; Hs.501012; -.
DR ProteinModelPortal; Q9UEY8; -.
DR SMR; Q9UEY8; 153-373.
DR IntAct; Q9UEY8; 4.
DR STRING; 9606.ENSP00000348381; -.
DR PhosphoSite; Q9UEY8; -.
DR DMDM; 12643881; -.
DR PaxDb; Q9UEY8; -.
DR PRIDE; Q9UEY8; -.
DR Ensembl; ENST00000277900; ENSP00000277900; ENSG00000148700.
DR Ensembl; ENST00000356080; ENSP00000348381; ENSG00000148700.
DR Ensembl; ENST00000360162; ENSP00000353286; ENSG00000148700.
DR GeneID; 120; -.
DR KEGG; hsa:120; -.
DR UCSC; uc001kyt.4; human.
DR CTD; 120; -.
DR GeneCards; GC10P111755; -.
DR H-InvDB; HIX0170444; -.
DR HGNC; HGNC:245; ADD3.
DR HPA; CAB009797; -.
DR MIM; 601568; gene.
DR neXtProt; NX_Q9UEY8; -.
DR PharmGKB; PA24567; -.
DR eggNOG; COG0235; -.
DR HOGENOM; HOG000116349; -.
DR HOVERGEN; HBG004180; -.
DR InParanoid; Q9UEY8; -.
DR OMA; VNVPEES; -.
DR OrthoDB; EOG7HF1HR; -.
DR PhylomeDB; Q9UEY8; -.
DR ChiTaRS; ADD3; human.
DR GeneWiki; ADD3; -.
DR GenomeRNAi; 120; -.
DR NextBio; 481; -.
DR PMAP-CutDB; Q9UEY8; -.
DR PRO; PR:Q9UEY8; -.
DR ArrayExpress; Q9UEY8; -.
DR Bgee; Q9UEY8; -.
DR CleanEx; HS_ADD3; -.
DR Genevestigator; Q9UEY8; -.
DR GO; GO:0005938; C:cell cortex; IEA:Ensembl.
DR GO; GO:0005911; C:cell-cell junction; IEA:Ensembl.
DR GO; GO:0000794; C:condensed nuclear chromosome; IEA:Ensembl.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; TAS:ProtInc.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; TAS:ProtInc.
DR Gene3D; 3.40.225.10; -; 1.
DR InterPro; IPR027772; ADD3.
DR InterPro; IPR001303; Aldolase_II/adducin_N.
DR PANTHER; PTHR10672:SF5; PTHR10672:SF5; 1.
DR Pfam; PF00596; Aldolase_II; 1.
DR SMART; SM01007; Aldolase_II; 1.
DR SUPFAM; SSF53639; SSF53639; 1.
PE 1: Evidence at protein level;
KW Acetylation; Actin-binding; Alternative splicing; Calmodulin-binding;
KW Cell membrane; Complete proteome; Cytoplasm; Cytoskeleton; Membrane;
KW Phosphoprotein; Reference proteome; Ubl conjugation.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 706 Gamma-adducin.
FT /FTId=PRO_0000218536.
FT REGION 684 701 Interaction with calmodulin (Potential).
FT MOD_RES 2 2 N-acetylserine.
FT MOD_RES 42 42 Phosphoserine.
FT MOD_RES 64 64 Phosphoserine.
FT MOD_RES 402 402 Phosphoserine.
FT MOD_RES 423 423 Phosphoserine.
FT MOD_RES 442 442 Phosphoserine.
FT MOD_RES 673 673 Phosphoserine.
FT MOD_RES 677 677 Phosphoserine.
FT MOD_RES 681 681 Phosphoserine.
FT MOD_RES 683 683 Phosphoserine; by PKC (By similarity).
FT VAR_SEQ 576 607 Missing (in isoform 1).
FT /FTId=VSP_000188.
FT CONFLICT 49 50 FN -> SS (in Ref. 1; BAA23783).
FT CONFLICT 60 60 Q -> R (in Ref. 1; BAA23783).
FT CONFLICT 362 362 Q -> P (in Ref. 2; AAB17126).
FT CONFLICT 420 420 V -> M (in Ref. 2; AAB17126).
FT CONFLICT 421 421 P -> L (in Ref. 1; BAA23783).
FT CONFLICT 426 433 KYMAQRQQ -> QIHGTRGNK (in Ref. 2;
FT AAB17126).
FT CONFLICT 484 484 K -> Q (in Ref. 2; AAB17126).
SQ SEQUENCE 706 AA; 79155 MW; EB8EAF602A4D7B41 CRC64;
MSSDASQGVI TTPPPPSMPH KERYFDRINE NDPEYIRERN MSPDLRQDFN MMEQRKRVTQ
ILQSPAFRED LECLIQEQMK KGHNPTGLLA LQQIADYIMA NSFSGFSSPP LSLGMVTPIN
DLPGADTSSY VKGEKLTRCK LASLYRLVDL FGWAHLANTY ISVRISKEQD HIIIIPRGLS
FSEATASNLV KVNIIGEVVD QGSTNLKIDH TGFSPHAAIY STRPDVKCVI HIHTLATAAV
SSMKCGILPI SQESLLLGDV AYYDYQGSLE EQEERIQLQK VLGPSCKVLV LRNHGVVALG
ETLEEAFHYI FNVQLACEIQ VQALAGAGGV DNLHVLDFQK YKAFTYTVAA SGGGGVNMGS
HQKWKVGEIE FEGLMRTLDN LGYRTGYAYR HPLIREKPRH KSDVEIPATV TAFSFEDDTV
PLSPLKYMAQ RQQREKTRWL NSPNTYMKVN VPEESRNGET SPRTKITWMK AEDSSKVSGG
TPIKIEDPNQ FVPLNTNPNE VLEKRNKIRE QNRYDLKTAG PQSQLLAGIV VDKPPSTMQF
EDDDHGPPAP PNPFSHLTEG ELEEYKRTIE RKQQGLEDAE QELLSDDASS VSQIQSQTQS
PQNVPEKLEE NHELFSKSFI SMEVPVMVVN GKDDMHDVED ELAKRVSRLS TSTTIENIEI
TIKSPEKIEE VLSPEGSPSK SPSKKKKKFR TPSFLKKNKK KEKVEA
//
ID ADDG_HUMAN Reviewed; 706 AA.
AC Q9UEY8; D3DRA8; O43243; Q5VU09; Q92773; Q9UEY7;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAY-2000, sequence version 1.
DT 22-JAN-2014, entry version 112.
DE RecName: Full=Gamma-adducin;
DE AltName: Full=Adducin-like protein 70;
GN Name=ADD3; Synonyms=ADDL;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RX PubMed=8893809;
RA Katagiri T., Ozaki K., Fujiwara T., Shimizu F., Kawai A., Okuno S.,
RA Suzuki M., Nakamura Y., Takahashi E., Hirai Y.;
RT "Cloning, expression and chromosome mapping of adducin-like 70 (ADDL),
RT a human cDNA highly homologous to human erythrocyte adducin.";
RL Cytogenet. Cell Genet. 74:90-95(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Moorthy S., Bennett V.;
RT "Cloning in the gamma quadrant.";
RL Submitted (SEP-1995) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING.
RX PubMed=10581174; DOI=10.1006/bbrc.1999.1769;
RA Citterio L., Azzani T., Duga S., Bianchi G.;
RT "Genomic organization of the human gamma adducin gene.";
RL Biochem. Biophys. Res. Commun. 266:110-114(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Endometrium;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
RA Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
RA Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
RA Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
RA Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
RA Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
RA Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
RA Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
RA Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
RA Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
RA Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
RA Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
RA Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
RA Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
RA Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
RA Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
RA Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
RA Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Ovary;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP SUMOYLATION.
RX PubMed=15561718; DOI=10.1074/jbc.M411718200;
RA Gocke C.B., Yu H., Kang J.;
RT "Systematic identification and analysis of mammalian small ubiquitin-
RT like modifier substrates.";
RL J. Biol. Chem. 280:5004-5012(2005).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-673, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42, AND MASS
RP SPECTROMETRY.
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-64; SER-423; SER-442;
RP SER-673; SER-677 AND SER-681, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-402; SER-423 AND
RP SER-681, AND MASS SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT SER-42; SER-673 AND SER-677, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-677 AND SER-681, AND
RP MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
CC -!- FUNCTION: Membrane-cytoskeleton-associated protein that promotes
CC the assembly of the spectrin-actin network. Binds to calmodulin.
CC -!- SUBUNIT: Heterodimer of an alpha and a gamma subunit.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cell membrane;
CC Peripheral membrane protein; Cytoplasmic side.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Comment=Additional isoforms seem to exist;
CC Name=2; Synonyms=Long;
CC IsoId=Q9UEY8-1; Sequence=Displayed;
CC Name=1; Synonyms=Short;
CC IsoId=Q9UEY8-2; Sequence=VSP_000188;
CC -!- TISSUE SPECIFICITY: Isoform 1 is ubiquitously expressed.
CC -!- DOMAIN: Comprised of three regions: a N-terminal protease-
CC resistant globular head region, a short connecting subdomain, and
CC a protease-sensitive tail region.
CC -!- PTM: Sumoylated.
CC -!- SIMILARITY: Belongs to the aldolase class II family. Adducin
CC subfamily.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC and Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/ADD3ID520ch10q25.html";
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; D67031; BAA23783.1; -; mRNA.
DR EMBL; U37122; AAB17126.1; -; mRNA.
DR EMBL; Y14372; CAB51805.1; -; Genomic_DNA.
DR EMBL; Y14373; CAB51805.1; JOINED; Genomic_DNA.
DR EMBL; Y14374; CAB51805.1; JOINED; Genomic_DNA.
DR EMBL; Y14375; CAB51805.1; JOINED; Genomic_DNA.
DR EMBL; Y14376; CAB51805.1; JOINED; Genomic_DNA.
DR EMBL; Y14377; CAB51805.1; JOINED; Genomic_DNA.
DR EMBL; Y14378; CAB51805.1; JOINED; Genomic_DNA.
DR EMBL; Y14379; CAB51805.1; JOINED; Genomic_DNA.
DR EMBL; Y14380; CAB51805.1; JOINED; Genomic_DNA.
DR EMBL; Y14381; CAB51805.1; JOINED; Genomic_DNA.
DR EMBL; Y14382; CAB51805.1; JOINED; Genomic_DNA.
DR EMBL; Y14383; CAB51805.1; JOINED; Genomic_DNA.
DR EMBL; Y14384; CAB51805.1; JOINED; Genomic_DNA.
DR EMBL; Y14372; CAB51806.1; -; Genomic_DNA.
DR EMBL; Y14373; CAB51806.1; JOINED; Genomic_DNA.
DR EMBL; Y14374; CAB51806.1; JOINED; Genomic_DNA.
DR EMBL; Y14375; CAB51806.1; JOINED; Genomic_DNA.
DR EMBL; Y14376; CAB51806.1; JOINED; Genomic_DNA.
DR EMBL; Y14377; CAB51806.1; JOINED; Genomic_DNA.
DR EMBL; Y14378; CAB51806.1; JOINED; Genomic_DNA.
DR EMBL; Y14379; CAB51806.1; JOINED; Genomic_DNA.
DR EMBL; Y14380; CAB51806.1; JOINED; Genomic_DNA.
DR EMBL; Y14381; CAB51806.1; JOINED; Genomic_DNA.
DR EMBL; Y14382; CAB51806.1; JOINED; Genomic_DNA.
DR EMBL; Y14384; CAB51806.1; JOINED; Genomic_DNA.
DR EMBL; BX647403; CAI46048.1; -; mRNA.
DR EMBL; AL590628; CAH71739.1; -; Genomic_DNA.
DR EMBL; CH471066; EAW49573.1; -; Genomic_DNA.
DR EMBL; CH471066; EAW49574.1; -; Genomic_DNA.
DR EMBL; BC062559; AAH62559.1; -; mRNA.
DR PIR; JC7164; JC7164.
DR RefSeq; NP_001112.2; NM_001121.2.
DR RefSeq; NP_058432.1; NM_016824.3.
DR RefSeq; NP_063968.1; NM_019903.3.
DR RefSeq; XP_005269586.1; XM_005269529.1.
DR RefSeq; XP_005269587.1; XM_005269530.1.
DR RefSeq; XP_005269588.1; XM_005269531.1.
DR RefSeq; XP_005269589.1; XM_005269532.1.
DR RefSeq; XP_005269590.1; XM_005269533.1.
DR RefSeq; XP_005269591.1; XM_005269534.1.
DR UniGene; Hs.501012; -.
DR ProteinModelPortal; Q9UEY8; -.
DR SMR; Q9UEY8; 153-373.
DR IntAct; Q9UEY8; 4.
DR STRING; 9606.ENSP00000348381; -.
DR PhosphoSite; Q9UEY8; -.
DR DMDM; 12643881; -.
DR PaxDb; Q9UEY8; -.
DR PRIDE; Q9UEY8; -.
DR Ensembl; ENST00000277900; ENSP00000277900; ENSG00000148700.
DR Ensembl; ENST00000356080; ENSP00000348381; ENSG00000148700.
DR Ensembl; ENST00000360162; ENSP00000353286; ENSG00000148700.
DR GeneID; 120; -.
DR KEGG; hsa:120; -.
DR UCSC; uc001kyt.4; human.
DR CTD; 120; -.
DR GeneCards; GC10P111755; -.
DR H-InvDB; HIX0170444; -.
DR HGNC; HGNC:245; ADD3.
DR HPA; CAB009797; -.
DR MIM; 601568; gene.
DR neXtProt; NX_Q9UEY8; -.
DR PharmGKB; PA24567; -.
DR eggNOG; COG0235; -.
DR HOGENOM; HOG000116349; -.
DR HOVERGEN; HBG004180; -.
DR InParanoid; Q9UEY8; -.
DR OMA; VNVPEES; -.
DR OrthoDB; EOG7HF1HR; -.
DR PhylomeDB; Q9UEY8; -.
DR ChiTaRS; ADD3; human.
DR GeneWiki; ADD3; -.
DR GenomeRNAi; 120; -.
DR NextBio; 481; -.
DR PMAP-CutDB; Q9UEY8; -.
DR PRO; PR:Q9UEY8; -.
DR ArrayExpress; Q9UEY8; -.
DR Bgee; Q9UEY8; -.
DR CleanEx; HS_ADD3; -.
DR Genevestigator; Q9UEY8; -.
DR GO; GO:0005938; C:cell cortex; IEA:Ensembl.
DR GO; GO:0005911; C:cell-cell junction; IEA:Ensembl.
DR GO; GO:0000794; C:condensed nuclear chromosome; IEA:Ensembl.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; TAS:ProtInc.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; TAS:ProtInc.
DR Gene3D; 3.40.225.10; -; 1.
DR InterPro; IPR027772; ADD3.
DR InterPro; IPR001303; Aldolase_II/adducin_N.
DR PANTHER; PTHR10672:SF5; PTHR10672:SF5; 1.
DR Pfam; PF00596; Aldolase_II; 1.
DR SMART; SM01007; Aldolase_II; 1.
DR SUPFAM; SSF53639; SSF53639; 1.
PE 1: Evidence at protein level;
KW Acetylation; Actin-binding; Alternative splicing; Calmodulin-binding;
KW Cell membrane; Complete proteome; Cytoplasm; Cytoskeleton; Membrane;
KW Phosphoprotein; Reference proteome; Ubl conjugation.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 706 Gamma-adducin.
FT /FTId=PRO_0000218536.
FT REGION 684 701 Interaction with calmodulin (Potential).
FT MOD_RES 2 2 N-acetylserine.
FT MOD_RES 42 42 Phosphoserine.
FT MOD_RES 64 64 Phosphoserine.
FT MOD_RES 402 402 Phosphoserine.
FT MOD_RES 423 423 Phosphoserine.
FT MOD_RES 442 442 Phosphoserine.
FT MOD_RES 673 673 Phosphoserine.
FT MOD_RES 677 677 Phosphoserine.
FT MOD_RES 681 681 Phosphoserine.
FT MOD_RES 683 683 Phosphoserine; by PKC (By similarity).
FT VAR_SEQ 576 607 Missing (in isoform 1).
FT /FTId=VSP_000188.
FT CONFLICT 49 50 FN -> SS (in Ref. 1; BAA23783).
FT CONFLICT 60 60 Q -> R (in Ref. 1; BAA23783).
FT CONFLICT 362 362 Q -> P (in Ref. 2; AAB17126).
FT CONFLICT 420 420 V -> M (in Ref. 2; AAB17126).
FT CONFLICT 421 421 P -> L (in Ref. 1; BAA23783).
FT CONFLICT 426 433 KYMAQRQQ -> QIHGTRGNK (in Ref. 2;
FT AAB17126).
FT CONFLICT 484 484 K -> Q (in Ref. 2; AAB17126).
SQ SEQUENCE 706 AA; 79155 MW; EB8EAF602A4D7B41 CRC64;
MSSDASQGVI TTPPPPSMPH KERYFDRINE NDPEYIRERN MSPDLRQDFN MMEQRKRVTQ
ILQSPAFRED LECLIQEQMK KGHNPTGLLA LQQIADYIMA NSFSGFSSPP LSLGMVTPIN
DLPGADTSSY VKGEKLTRCK LASLYRLVDL FGWAHLANTY ISVRISKEQD HIIIIPRGLS
FSEATASNLV KVNIIGEVVD QGSTNLKIDH TGFSPHAAIY STRPDVKCVI HIHTLATAAV
SSMKCGILPI SQESLLLGDV AYYDYQGSLE EQEERIQLQK VLGPSCKVLV LRNHGVVALG
ETLEEAFHYI FNVQLACEIQ VQALAGAGGV DNLHVLDFQK YKAFTYTVAA SGGGGVNMGS
HQKWKVGEIE FEGLMRTLDN LGYRTGYAYR HPLIREKPRH KSDVEIPATV TAFSFEDDTV
PLSPLKYMAQ RQQREKTRWL NSPNTYMKVN VPEESRNGET SPRTKITWMK AEDSSKVSGG
TPIKIEDPNQ FVPLNTNPNE VLEKRNKIRE QNRYDLKTAG PQSQLLAGIV VDKPPSTMQF
EDDDHGPPAP PNPFSHLTEG ELEEYKRTIE RKQQGLEDAE QELLSDDASS VSQIQSQTQS
PQNVPEKLEE NHELFSKSFI SMEVPVMVVN GKDDMHDVED ELAKRVSRLS TSTTIENIEI
TIKSPEKIEE VLSPEGSPSK SPSKKKKKFR TPSFLKKNKK KEKVEA
//
MIM
601568
*RECORD*
*FIELD* NO
601568
*FIELD* TI
*601568 ADDUCIN 3; ADD3
;;ADDUCIN, GAMMA;;
ADDUCIN-LIKE; ADDL
ADD3/NUP98 FUSION GENE, INCLUDED
read more*FIELD* TX
CLONING
From a human fetal-brain cDNA library, Katagiri et al. (1996) isolated a
novel human cDNA which they termed adducin-like 70. The predicted amino
acid sequence shows a high degree of homology to adducins alpha (102680)
and beta (102681). In human erythrocytes, adducin is a 200-kD
heterodimeric skeletal component of the cell membrane, where it promotes
the binding of spectrin to actin. This binding is regulated by
calcium/calmodulin (114180). Adducin also is phosphorylated by protein
kinase C. Adducin and its multiple isoforms represent a family of
proteins present in a variety of tissues and cultured cell lines,
including those from brain, kidney, and liver. The gene, symbolized here
ADDL, contains an open reading frame of 2,022 nucleotides encoding 674
amino acids. It shows 54%, 53%, and 59% identity in predicted amino acid
sequence with alpha and beta components of human adducin and rat adducin
63, respectively. Katagiri et al. (1996) stated that human adducin-like
70 is likely to play an important role in the skeletal organization of
the cell membrane. Northern blot analysis indicated ubiquitous
expression of this gene in adult human tissues.
In a comprehensive assay of gene expression, Gilligan et al. (1999)
showed the ubiquitous expression of alpha- and gamma-adducin, in
contrast to the restricted expression of beta-adducin. Beta-adducin was
expressed at high levels in brain and hematopoietic tissues (bone marrow
in humans, spleen in mice).
By RT-PCR of peripheral blood leukocyte RNA, Citterio et al. (1999)
identified a splice variant of ADD3 that includes exon 13. The deduced
706-amino acid protein contains 32 additional amino acids in its
C-terminal tail compared with the protein described by Katagiri et al.
(1996). RT-PCR detected both splice variants in kidney, brain, lung, and
heart.
GENE STRUCTURE
Citterio et al. (1999) determined that the ADD3 gene contains 14 coding
exons and spans over 20 kb.
MAPPING
Katagiri et al. (1996) localized the gene to chromosome 10q24.2-q24.3 by
fluorescence in situ hybridization. By radiation hybrid analysis,
Citterio et al. (1999) mapped the ADD3 gene to chromosome 10q24.1-q24.2.
MOLECULAR GENETICS
Lanzani et al. (2005) analyzed the ADD3 gene in 40 unrelated individuals
and identified a +386A-G polymorphism (dbSNP rs3731366) in intron 11.
The authors then genotyped 512 newly discovered and never-treated
hypertensive patients (see 145500) for IVS11+386A-G, but found no
association between the polymorphism and ambulatory blood pressure or
plasma levels of renin activity and endogenous ouabain. However,
carriers of a 460W polymorphism in the ADD1 gene (102680.0001) who also
carried the ADD3 G allele had an approximately 8 mm Hg greater increase
in blood pressure than those who carried the ADD3 A allele (p = 0.020 to
0.006, depending on the genetic model applied). Lanzani et al. (2005)
suggested that there were epistatic effects between the ADD1 and ADD3
loci affecting variation in blood pressure.
CYTOGENETICS
- ADD3/NUP98 Fusion Gene
Lahortiga et al. (2003) described a translocation t(10;11)(q25;p15) that
resulted in fusion of the ADD3 gene to the NUP98 gene (601021) on
chromosome 11p15 and development of T-cell acute lymphoblastic leukemia.
*FIELD* RF
1. Citterio, L.; Azzani, T.; Duga, S.; Bianchi, G.: Genomic organization
of the human gamma adducin gene. Biochem. Biophys. Res. Commun. 266:
110-114, 1999.
2. Gilligan, D. M.; Lozovatsky, L.; Gwynn, B.; Brugnara, C.; Mohandas,
N.; Peters, L. L.: Targeted disruption of the beta adducin gene (Add2)
causes red blood cell spherocytosis in mice. Proc. Nat. Acad. Sci. 96:
10717-10722, 1999.
3. Katagiri, T.; Ozaki, K.; Fujiwara, T.; Shimizu, F.; Kawai, A.;
Okuno, S.; Suzuki, M.; Nakamura, Y.; Takahashi, E.; Hirai, Y.: Cloning,
expression and chromosome mapping of adducin-like 70 (ADDL), a human
cDNA highly homologous to human erythrocyte adducin. Cytogenet. Cell
Genet. 74: 90-95, 1996.
4. Lahortiga, I.; Vizmanos, J. L.; Agirre, X.; Vazquez, I.; Cigudosa,
J. C.; Larrayoz, M. J.; Sala, F.; Gorosquieta, A.; Perez-Equiza, K.;
Calasanz, M. J.; Odero, M. D.: NUP98 is fused to adducin 3 in a patient
with T-cell acute lymphoblastic leukemia and myeloid markers, with
a new translocation t(10;11)(q25;p15). Cancer Res. 63: 3079-3083,
2003.
5. Lanzani, C.; Citterio, L.; Jankaricova, M.; Sciarrone, M. T.; Barlassina,
C.; Fattori, S.; Messaggio, E.; Di Serio, C.; Zagato, L.; Cusi, D.;
Hamlyn, J. M.; Stella, A.; Bianchi, G.; Manunta, P.: Role of the
adducin family genes in human essential hypertension. J. Hypertension 23:
543-549, 2005.
*FIELD* CN
Patricia A. Hartz - updated: 4/10/2009
Marla J. F. O'Neill - updated: 12/2/2008
Victor A. McKusick - updated: 9/4/2003
Victor A. McKusick - updated: 11/8/1999
*FIELD* CD
Victor A. McKusick: 12/13/1996
*FIELD* ED
mgross: 04/13/2009
terry: 4/10/2009
carol: 12/2/2008
wwang: 3/2/2007
joanna: 3/17/2004
cwells: 9/8/2003
terry: 9/4/2003
mgross: 11/8/1999
carol: 2/18/1999
jenny: 12/17/1996
jenny: 12/16/1996
mark: 12/13/1996
*RECORD*
*FIELD* NO
601568
*FIELD* TI
*601568 ADDUCIN 3; ADD3
;;ADDUCIN, GAMMA;;
ADDUCIN-LIKE; ADDL
ADD3/NUP98 FUSION GENE, INCLUDED
read more*FIELD* TX
CLONING
From a human fetal-brain cDNA library, Katagiri et al. (1996) isolated a
novel human cDNA which they termed adducin-like 70. The predicted amino
acid sequence shows a high degree of homology to adducins alpha (102680)
and beta (102681). In human erythrocytes, adducin is a 200-kD
heterodimeric skeletal component of the cell membrane, where it promotes
the binding of spectrin to actin. This binding is regulated by
calcium/calmodulin (114180). Adducin also is phosphorylated by protein
kinase C. Adducin and its multiple isoforms represent a family of
proteins present in a variety of tissues and cultured cell lines,
including those from brain, kidney, and liver. The gene, symbolized here
ADDL, contains an open reading frame of 2,022 nucleotides encoding 674
amino acids. It shows 54%, 53%, and 59% identity in predicted amino acid
sequence with alpha and beta components of human adducin and rat adducin
63, respectively. Katagiri et al. (1996) stated that human adducin-like
70 is likely to play an important role in the skeletal organization of
the cell membrane. Northern blot analysis indicated ubiquitous
expression of this gene in adult human tissues.
In a comprehensive assay of gene expression, Gilligan et al. (1999)
showed the ubiquitous expression of alpha- and gamma-adducin, in
contrast to the restricted expression of beta-adducin. Beta-adducin was
expressed at high levels in brain and hematopoietic tissues (bone marrow
in humans, spleen in mice).
By RT-PCR of peripheral blood leukocyte RNA, Citterio et al. (1999)
identified a splice variant of ADD3 that includes exon 13. The deduced
706-amino acid protein contains 32 additional amino acids in its
C-terminal tail compared with the protein described by Katagiri et al.
(1996). RT-PCR detected both splice variants in kidney, brain, lung, and
heart.
GENE STRUCTURE
Citterio et al. (1999) determined that the ADD3 gene contains 14 coding
exons and spans over 20 kb.
MAPPING
Katagiri et al. (1996) localized the gene to chromosome 10q24.2-q24.3 by
fluorescence in situ hybridization. By radiation hybrid analysis,
Citterio et al. (1999) mapped the ADD3 gene to chromosome 10q24.1-q24.2.
MOLECULAR GENETICS
Lanzani et al. (2005) analyzed the ADD3 gene in 40 unrelated individuals
and identified a +386A-G polymorphism (dbSNP rs3731366) in intron 11.
The authors then genotyped 512 newly discovered and never-treated
hypertensive patients (see 145500) for IVS11+386A-G, but found no
association between the polymorphism and ambulatory blood pressure or
plasma levels of renin activity and endogenous ouabain. However,
carriers of a 460W polymorphism in the ADD1 gene (102680.0001) who also
carried the ADD3 G allele had an approximately 8 mm Hg greater increase
in blood pressure than those who carried the ADD3 A allele (p = 0.020 to
0.006, depending on the genetic model applied). Lanzani et al. (2005)
suggested that there were epistatic effects between the ADD1 and ADD3
loci affecting variation in blood pressure.
CYTOGENETICS
- ADD3/NUP98 Fusion Gene
Lahortiga et al. (2003) described a translocation t(10;11)(q25;p15) that
resulted in fusion of the ADD3 gene to the NUP98 gene (601021) on
chromosome 11p15 and development of T-cell acute lymphoblastic leukemia.
*FIELD* RF
1. Citterio, L.; Azzani, T.; Duga, S.; Bianchi, G.: Genomic organization
of the human gamma adducin gene. Biochem. Biophys. Res. Commun. 266:
110-114, 1999.
2. Gilligan, D. M.; Lozovatsky, L.; Gwynn, B.; Brugnara, C.; Mohandas,
N.; Peters, L. L.: Targeted disruption of the beta adducin gene (Add2)
causes red blood cell spherocytosis in mice. Proc. Nat. Acad. Sci. 96:
10717-10722, 1999.
3. Katagiri, T.; Ozaki, K.; Fujiwara, T.; Shimizu, F.; Kawai, A.;
Okuno, S.; Suzuki, M.; Nakamura, Y.; Takahashi, E.; Hirai, Y.: Cloning,
expression and chromosome mapping of adducin-like 70 (ADDL), a human
cDNA highly homologous to human erythrocyte adducin. Cytogenet. Cell
Genet. 74: 90-95, 1996.
4. Lahortiga, I.; Vizmanos, J. L.; Agirre, X.; Vazquez, I.; Cigudosa,
J. C.; Larrayoz, M. J.; Sala, F.; Gorosquieta, A.; Perez-Equiza, K.;
Calasanz, M. J.; Odero, M. D.: NUP98 is fused to adducin 3 in a patient
with T-cell acute lymphoblastic leukemia and myeloid markers, with
a new translocation t(10;11)(q25;p15). Cancer Res. 63: 3079-3083,
2003.
5. Lanzani, C.; Citterio, L.; Jankaricova, M.; Sciarrone, M. T.; Barlassina,
C.; Fattori, S.; Messaggio, E.; Di Serio, C.; Zagato, L.; Cusi, D.;
Hamlyn, J. M.; Stella, A.; Bianchi, G.; Manunta, P.: Role of the
adducin family genes in human essential hypertension. J. Hypertension 23:
543-549, 2005.
*FIELD* CN
Patricia A. Hartz - updated: 4/10/2009
Marla J. F. O'Neill - updated: 12/2/2008
Victor A. McKusick - updated: 9/4/2003
Victor A. McKusick - updated: 11/8/1999
*FIELD* CD
Victor A. McKusick: 12/13/1996
*FIELD* ED
mgross: 04/13/2009
terry: 4/10/2009
carol: 12/2/2008
wwang: 3/2/2007
joanna: 3/17/2004
cwells: 9/8/2003
terry: 9/4/2003
mgross: 11/8/1999
carol: 2/18/1999
jenny: 12/17/1996
jenny: 12/16/1996
mark: 12/13/1996