ADDA_HUMAN
ID ADDA_HUMAN Reviewed; 737 AA.
AC P35611; A2A3N8; A2A3P0; B4DI79; D3DVR3; D3DVR4; D3DVR5; Q13734; Q14729;
AC Q16156; Q86XM2; Q9UJB6;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 210.
DE RecName: Full=Alpha-adducin;
DE AltName: Full=Erythrocyte adducin subunit alpha;
GN Name=ADD1; Synonyms=ADDA;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 24-36; 41-47;
RP 516-569 AND 722-729, AND VARIANT CYS-586.
RC TISSUE=Reticulocyte;
RX PubMed=1840603; DOI=10.1083/jcb.115.3.665;
RA Joshi R.L., Gilligan D.M., Otto E., McLaughlin T., Bennett V.D.;
RT "Primary structure and domain organization of human alpha and beta
RT adducin.";
RL J. Cell Biol. 115:665-675(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 6).
RX PubMed=1284592; DOI=10.1093/hmg/1.9.669;
RA Goldberg Y.P., Lin B.Y., Andrew S.E., Nasir J., Graham R., Glaves M.L.,
RA Hutchinson G., Theilmann J., Ginzinger D.G., Schappert K.;
RT "Cloning and mapping of the alpha-adducin gene close to D4S95 and
RT assessment of its relationship to Huntington disease.";
RL Hum. Mol. Genet. 1:669-675(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING.
RX PubMed=7774961; DOI=10.1016/0888-7543(95)80113-z;
RA Lin B., Nasir J., McDonald H., Graham R., Rommens J.M., Goldberg Y.P.,
RA Hayden M.R.;
RT "Genomic organization of the human alpha-adducin gene and its alternately
RT spliced isoforms.";
RL Genomics 25:93-99(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
RC TISSUE=Hippocampus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Testis;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 531-737 (ISOFORMS 1/3).
RX PubMed=1345173; DOI=10.1038/ng1192-223;
RA Taylor S.A., Snell R.G., Buckler A., Ambrose C., Duyao M., Church D.,
RA Lin C.S., Altherr M., Bates G.P., Groot N.;
RT "Cloning of the alpha-adducin gene from the Huntington's disease candidate
RT region of chromosome 4 by exon amplification.";
RL Nat. Genet. 2:223-227(1992).
RN [9]
RP PHOSPHORYLATION AT SER-59; SER-408; SER-436; SER-481; SER-716 AND SER-726,
RP AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=8810272; DOI=10.1074/jbc.271.41.25157;
RA Matsuoka Y., Hughes C.A., Bennett V.;
RT "Adducin regulation. Definition of the calmodulin-binding domain and sites
RT of phosphorylation by protein kinases A and C.";
RL J. Biol. Chem. 271:25157-25166(1996).
RN [10]
RP PHOSPHORYLATION AT THR-445 AND THR-480, AND MUTAGENESIS OF THR-445 AND
RP THR-480.
RX PubMed=10209029; DOI=10.1083/jcb.145.2.347;
RA Fukata Y., Oshiro N., Kinoshita N., Kawano Y., Matsuoka Y., Bennett V.,
RA Matsuura Y., Kaibuchi K.;
RT "Phosphorylation of adducin by Rho-kinase plays a crucial role in cell
RT motility.";
RL J. Cell Biol. 145:347-361(1999).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-707 AND SER-710, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-358, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12; THR-331; SER-334;
RP SER-358; SER-431; SER-436 AND SER-465, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
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 [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-465, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-465, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [17]
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., Buerckstuemmer T.,
RA 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 [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12; SER-358; SER-465;
RP SER-707; SER-710 AND SER-714, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12; SER-353; SER-355;
RP SER-358; SER-366; SER-431 AND SER-465, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-59; SER-64; SER-358; SER-678;
RP SER-707 AND SER-716, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [21]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [22]
RP VARIANT TRP-460.
RX PubMed=9674650; DOI=10.1161/01.hyp.32.1.138;
RA Kamitani A., Wong Z.Y., Fraser R., Davies D.L., Connor J.M., Foy C.J.,
RA Watt G.C., Harrap S.B.;
RT "Human alpha-adducin gene, blood pressure, and sodium metabolism.";
RL Hypertension 32:138-143(1998).
RN [23]
RP VARIANTS TRP-460 AND CYS-586.
RX PubMed=10391210; DOI=10.1038/10297;
RA Halushka M.K., Fan J.-B., Bentley K., Hsie L., Shen N., Weder A.,
RA Cooper R., Lipshutz R., Chakravarti A.;
RT "Patterns of single-nucleotide polymorphisms in candidate genes for blood-
RT pressure homeostasis.";
RL Nat. Genet. 22:239-247(1999).
CC -!- FUNCTION: Membrane-cytoskeleton-associated protein that promotes the
CC assembly of the spectrin-actin network. Binds to calmodulin.
CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit or an alpha and a
CC gamma subunit.
CC -!- INTERACTION:
CC P35611; P02489: CRYAA; NbExp=3; IntAct=EBI-2809187, EBI-6875961;
CC P35611; Q13153: PAK1; NbExp=3; IntAct=EBI-2809187, EBI-1307;
CC P35611-5; Q9NP66: HMG20A; NbExp=3; IntAct=EBI-10206868, EBI-740641;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cell membrane;
CC Peripheral membrane protein; Cytoplasmic side.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Comment=Additional isoforms seem to exist.;
CC Name=1;
CC IsoId=P35611-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P35611-2; Sequence=VSP_000175, VSP_000176;
CC Name=3;
CC IsoId=P35611-3; Sequence=VSP_000174;
CC Name=4;
CC IsoId=P35611-4; Sequence=VSP_054420, VSP_000175, VSP_000176;
CC Name=5;
CC IsoId=P35611-5; Sequence=VSP_055402, VSP_055403;
CC Name=6;
CC IsoId=P35611-6; Sequence=VSP_000174, VSP_000175, VSP_000176;
CC -!- TISSUE SPECIFICITY: Expressed in all tissues. Found in much higher
CC levels in reticulocytes than the beta subunit.
CC -!- DOMAIN: Each subunit is comprised of three regions: a NH2-terminal
CC protease-resistant globular head region, a short connecting subdomain,
CC and a protease-sensitive tail region.
CC -!- SIMILARITY: Belongs to the aldolase class II family. Adducin subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA98970.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; X58141; CAA41149.1; -; mRNA.
DR EMBL; L07261; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; L29296; AAB05645.1; -; Genomic_DNA.
DR EMBL; L29286; AAB05645.1; JOINED; Genomic_DNA.
DR EMBL; L29287; AAB05645.1; JOINED; Genomic_DNA.
DR EMBL; L29289; AAB05645.1; JOINED; Genomic_DNA.
DR EMBL; L29290; AAB05645.1; JOINED; Genomic_DNA.
DR EMBL; L29291; AAB05645.1; JOINED; Genomic_DNA.
DR EMBL; L29292; AAB05645.1; JOINED; Genomic_DNA.
DR EMBL; L29293; AAB05645.1; JOINED; Genomic_DNA.
DR EMBL; L29294; AAB05645.1; JOINED; Genomic_DNA.
DR EMBL; L29295; AAB05645.1; JOINED; Genomic_DNA.
DR EMBL; L29297; AAB05645.1; JOINED; Genomic_DNA.
DR EMBL; L29298; AAB05645.1; JOINED; Genomic_DNA.
DR EMBL; AK295457; BAG58391.1; -; mRNA.
DR EMBL; Z74617; CAA98970.1; ALT_SEQ; Genomic_DNA.
DR EMBL; Z68280; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL390065; CAM21299.1; -; Genomic_DNA.
DR EMBL; AL121750; CAM21299.1; JOINED; Genomic_DNA.
DR EMBL; BX465861; CAM21299.1; JOINED; Genomic_DNA.
DR EMBL; BX465861; CAM25274.1; -; Genomic_DNA.
DR EMBL; AL121750; CAM25274.1; JOINED; Genomic_DNA.
DR EMBL; AL390065; CAM25274.1; JOINED; Genomic_DNA.
DR EMBL; AL121750; CAM28230.1; -; Genomic_DNA.
DR EMBL; AL390065; CAM28230.1; JOINED; Genomic_DNA.
DR EMBL; BX465861; CAM28230.1; JOINED; Genomic_DNA.
DR EMBL; AL121750; CAM28231.1; -; Genomic_DNA.
DR EMBL; AL390065; CAM28231.1; JOINED; Genomic_DNA.
DR EMBL; BX465861; CAM28231.1; JOINED; Genomic_DNA.
DR EMBL; AL121750; CAM28232.1; -; Genomic_DNA.
DR EMBL; AL390065; CAM28232.1; JOINED; Genomic_DNA.
DR EMBL; BX465861; CAM28232.1; JOINED; Genomic_DNA.
DR EMBL; CH471131; EAW82498.1; -; Genomic_DNA.
DR EMBL; CH471131; EAW82499.1; -; Genomic_DNA.
DR EMBL; CH471131; EAW82501.1; -; Genomic_DNA.
DR EMBL; CH471131; EAW82502.1; -; Genomic_DNA.
DR EMBL; CH471131; EAW82503.1; -; Genomic_DNA.
DR EMBL; CH471131; EAW82504.1; -; Genomic_DNA.
DR EMBL; CH471131; EAW82505.1; -; Genomic_DNA.
DR EMBL; BC042998; AAH42998.1; -; mRNA.
DR EMBL; AH004561; AAB30914.2; -; mRNA.
DR CCDS; CCDS3363.1; -. [P35611-3]
DR CCDS; CCDS3364.1; -. [P35611-6]
DR CCDS; CCDS43205.1; -. [P35611-1]
DR CCDS; CCDS75094.1; -. [P35611-4]
DR PIR; S18207; S18207.
DR RefSeq; NP_001110.2; NM_001119.4. [P35611-1]
DR RefSeq; NP_001273574.1; NM_001286645.1. [P35611-4]
DR RefSeq; NP_054908.2; NM_014189.3. [P35611-3]
DR RefSeq; NP_054909.2; NM_014190.3. [P35611-2]
DR RefSeq; NP_789771.1; NM_176801.2. [P35611-6]
DR RefSeq; XP_005247994.1; XM_005247937.2.
DR RefSeq; XP_016863193.1; XM_017007704.1. [P35611-3]
DR RefSeq; XP_016863195.1; XM_017007706.1. [P35611-1]
DR RefSeq; XP_016863196.1; XM_017007707.1.
DR RefSeq; XP_016863197.1; XM_017007708.1.
DR RefSeq; XP_016863198.1; XM_017007709.1. [P35611-2]
DR RefSeq; XP_016863199.1; XM_017007710.1.
DR AlphaFoldDB; P35611; -.
DR SMR; P35611; -.
DR BioGRID; 106631; 119.
DR IntAct; P35611; 63.
DR MINT; P35611; -.
DR STRING; 9606.ENSP00000264758; -.
DR GlyGen; P35611; 7 sites, 2 O-linked glycans (7 sites).
DR iPTMnet; P35611; -.
DR MetOSite; P35611; -.
DR PhosphoSitePlus; P35611; -.
DR SwissPalm; P35611; -.
DR BioMuta; ADD1; -.
DR DMDM; 12644231; -.
DR EPD; P35611; -.
DR jPOST; P35611; -.
DR MassIVE; P35611; -.
DR MaxQB; P35611; -.
DR PaxDb; P35611; -.
DR PeptideAtlas; P35611; -.
DR PRIDE; P35611; -.
DR ProteomicsDB; 289; -.
DR ProteomicsDB; 55102; -. [P35611-1]
DR ProteomicsDB; 55103; -. [P35611-2]
DR ProteomicsDB; 55104; -. [P35611-3]
DR ProteomicsDB; 70300; -.
DR Antibodypedia; 4065; 776 antibodies from 41 providers.
DR DNASU; 118; -.
DR Ensembl; ENST00000264758.11; ENSP00000264758.6; ENSG00000087274.19. [P35611-3]
DR Ensembl; ENST00000355842.7; ENSP00000348100.3; ENSG00000087274.19. [P35611-4]
DR Ensembl; ENST00000398123.6; ENSP00000381191.2; ENSG00000087274.19. [P35611-6]
DR Ensembl; ENST00000398125.5; ENSP00000381193.1; ENSG00000087274.19. [P35611-6]
DR Ensembl; ENST00000398129.5; ENSP00000381197.1; ENSG00000087274.19. [P35611-1]
DR Ensembl; ENST00000651918.1; ENSP00000498269.1; ENSG00000087274.19. [P35611-2]
DR GeneID; 118; -.
DR KEGG; hsa:118; -.
DR UCSC; uc003gfo.4; human. [P35611-1]
DR CTD; 118; -.
DR DisGeNET; 118; -.
DR GeneCards; ADD1; -.
DR HGNC; HGNC:243; ADD1.
DR HPA; ENSG00000087274; Low tissue specificity.
DR MalaCards; ADD1; -.
DR MIM; 102680; gene.
DR neXtProt; NX_P35611; -.
DR OpenTargets; ENSG00000087274; -.
DR PharmGKB; PA31; -.
DR VEuPathDB; HostDB:ENSG00000087274; -.
DR eggNOG; KOG3699; Eukaryota.
DR GeneTree; ENSGT00940000158581; -.
DR InParanoid; P35611; -.
DR OrthoDB; 400524at2759; -.
DR PhylomeDB; P35611; -.
DR TreeFam; TF313003; -.
DR PathwayCommons; P35611; -.
DR Reactome; R-HSA-264870; Caspase-mediated cleavage of cytoskeletal proteins.
DR Reactome; R-HSA-381038; XBP1(S) activates chaperone genes.
DR Reactome; R-HSA-5223345; Miscellaneous transport and binding events.
DR SignaLink; P35611; -.
DR SIGNOR; P35611; -.
DR BioGRID-ORCS; 118; 12 hits in 1076 CRISPR screens.
DR ChiTaRS; ADD1; human.
DR GeneWiki; ADD1; -.
DR GenomeRNAi; 118; -.
DR Pharos; P35611; Tbio.
DR PRO; PR:P35611; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; P35611; protein.
DR Bgee; ENSG00000087274; Expressed in right hemisphere of cerebellum and 206 other tissues.
DR ExpressionAtlas; P35611; baseline and differential.
DR Genevisible; P35611; HS.
DR GO; GO:0005912; C:adherens junction; IDA:CAFA.
DR GO; GO:0005737; C:cytoplasm; IDA:CAFA.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0008290; C:F-actin capping protein complex; IDA:BHF-UCL.
DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR GO; GO:0016604; C:nuclear body; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0014069; C:postsynaptic density; IBA:GO_Central.
DR GO; GO:0003779; F:actin binding; TAS:ProtInc.
DR GO; GO:0051015; F:actin filament binding; IDA:BHF-UCL.
DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0046982; F:protein heterodimerization activity; IPI:BHF-UCL.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:BHF-UCL.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:BHF-UCL.
DR GO; GO:0030507; F:spectrin binding; IDA:BHF-UCL.
DR GO; GO:0030036; P:actin cytoskeleton organization; IC:BHF-UCL.
DR GO; GO:0051017; P:actin filament bundle assembly; IDA:BHF-UCL.
DR GO; GO:0051016; P:barbed-end actin filament capping; IDA:BHF-UCL.
DR GO; GO:0071277; P:cellular response to calcium ion; IDA:CAFA.
DR GO; GO:1903393; P:positive regulation of adherens junction organization; IDA:CAFA.
DR GO; GO:1903142; P:positive regulation of establishment of endothelial barrier; IDA:CAFA.
DR GO; GO:0032092; P:positive regulation of protein binding; IDA:BHF-UCL.
DR DisProt; DP00240; -.
DR Gene3D; 3.40.225.10; -; 1.
DR InterPro; IPR027766; ADD1.
DR InterPro; IPR001303; Aldolase_II/adducin_N.
DR InterPro; IPR036409; Aldolase_II/adducin_N_sf.
DR PANTHER; PTHR10672:SF4; PTHR10672:SF4; 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; Cytoplasm; Cytoskeleton; Direct protein sequencing;
KW Membrane; Phosphoprotein; Reference proteome.
FT CHAIN 1..737
FT /note="Alpha-adducin"
FT /id="PRO_0000218530"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 421..486
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 576..737
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 717..734
FT /note="Interaction with calmodulin"
FT /evidence="ECO:0000255"
FT COMPBIAS 421..436
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 437..453
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 576..602
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 603..617
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 654..669
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 672..688
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:19413330"
FT MOD_RES 12
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 59
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000269|PubMed:8810272,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 64
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 331
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 334
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 353
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 355
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 358
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18088087,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 366
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 408
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000269|PubMed:8810272"
FT MOD_RES 427
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYC0"
FT MOD_RES 429
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYC0"
FT MOD_RES 431
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 436
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000269|PubMed:8810272,
FT ECO:0007744|PubMed:18669648"
FT MOD_RES 445
FT /note="Phosphothreonine; by ROCK2"
FT /evidence="ECO:0000269|PubMed:10209029"
FT MOD_RES 464
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYC0"
FT MOD_RES 465
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 480
FT /note="Phosphothreonine; by ROCK2"
FT /evidence="ECO:0000269|PubMed:10209029"
FT MOD_RES 481
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000269|PubMed:8810272"
FT MOD_RES 586
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYC0"
FT MOD_RES 600
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYC0"
FT MOD_RES 613
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYC0"
FT MOD_RES 614
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYC0"
FT MOD_RES 678
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 707
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569"
FT MOD_RES 710
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 714
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 716
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0000269|PubMed:8810272,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 726
FT /note="Phosphoserine; by PKA and PKC"
FT /evidence="ECO:0000269|PubMed:8810272"
FT VAR_SEQ 471
FT /note="K -> KVWTNITHDHVKPLLQSLSSGVCVPSCITNCL (in isoform 3
FT and isoform 6)"
FT /evidence="ECO:0000303|PubMed:1284592"
FT /id="VSP_000174"
FT VAR_SEQ 472..511
FT /note="WTKEDGHRTSTSAVPNLFVPLNTNPKEVQEMRNKIREQNL -> VWTNITHD
FT HVKPLLQSLSSGVCVPSCITNCLVCAYLTVHS (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055402"
FT VAR_SEQ 512..737
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055403"
FT VAR_SEQ 535
FT /note="Q -> QDAPLSDCTETIEGLELTEQTFSPAKSLSFRK (in isoform
FT 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_054420"
FT VAR_SEQ 621..631
FT /note="DLVPEPTTGDD -> GDGCAREYLLP (in isoform 2, isoform 4
FT and isoform 6)"
FT /evidence="ECO:0000303|PubMed:1284592,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_000175"
FT VAR_SEQ 632..737
FT /note="Missing (in isoform 2, isoform 4 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:1284592,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_000176"
FT VARIANT 6
FT /note="R -> C (in dbSNP:rs2295497)"
FT /id="VAR_022108"
FT VARIANT 270
FT /note="Y -> N (in dbSNP:rs4971)"
FT /id="VAR_014863"
FT VARIANT 376
FT /note="E -> D (in dbSNP:rs4972)"
FT /id="VAR_014864"
FT VARIANT 460
FT /note="G -> W (in dbSNP:rs4961)"
FT /evidence="ECO:0000269|PubMed:10391210,
FT ECO:0000269|PubMed:9674650"
FT /id="VAR_014184"
FT VARIANT 510
FT /note="N -> I (in dbSNP:rs4962)"
FT /id="VAR_014865"
FT VARIANT 586
FT /note="S -> C (in dbSNP:rs4963)"
FT /evidence="ECO:0000269|PubMed:10391210,
FT ECO:0000269|PubMed:1840603"
FT /id="VAR_014185"
FT MUTAGEN 445
FT /note="T->D: Abolishes phosphorylation by ROCK2; when
FT associated with D-480."
FT /evidence="ECO:0000269|PubMed:10209029"
FT MUTAGEN 480
FT /note="T->D: Abolishes phosphorylation by ROCK2; when
FT associated with D-445."
FT /evidence="ECO:0000269|PubMed:10209029"
FT CONFLICT 606
FT /note="A -> E (in Ref. 3; AAB05645)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 737 AA; 80955 MW; DF13AB30B12F20B6 CRC64;
MNGDSRAAVV TSPPPTTAPH KERYFDRVDE NNPEYLRERN MAPDLRQDFN MMEQKKRVSM
ILQSPAFCEE LESMIQEQFK KGKNPTGLLA LQQIADFMTT NVPNVYPAAP QGGMAALNMS
LGMVTPVNDL RGSDSIAYDK GEKLLRCKLA AFYRLADLFG WSQLIYNHIT TRVNSEQEHF
LIVPFGLLYS EVTASSLVKI NLQGDIVDRG STNLGVNQAG FTLHSAIYAA RPDVKCVVHI
HTPAGAAVSA MKCGLLPISP EALSLGEVAY HDYHGILVDE EEKVLIQKNL GPKSKVLILR
NHGLVSVGES VEEAFYYIHN LVVACEIQVR TLASAGGPDN LVLLNPEKYK AKSRSPGSPV
GEGTGSPPKW QIGEQEFEAL MRMLDNLGYR TGYPYRYPAL REKSKKYSDV EVPASVTGYS
FASDGDSGTC SPLRHSFQKQ QREKTRWLNS GRGDEASEEG QNGSSPKSKT KWTKEDGHRT
STSAVPNLFV PLNTNPKEVQ EMRNKIREQN LQDIKTAGPQ SQVLCGVVMD RSLVQGELVT
ASKAIIEKEY QPHVIVSTTG PNPFTTLTDR ELEEYRREVE RKQKGSEENL DEAREQKEKS
PPDQPAVPHP PPSTPIKLEE DLVPEPTTGD DSDAATFKPT LPDLSPDEPS EALGFPMLEK
EEEAHRPPSP TEAPTEASPE PAPDPAPVAE EAAPSAVEEG AAADPGSDGS PGKSPSKKKK
KFRTPSFLKK SKKKSDS
