ADDB_HUMAN
ID ADDB_HUMAN Reviewed; 726 AA.
AC P35612; A8K4P2; B4DM17; D6W5G7; D6W5G8; Q13482; Q16412; Q59G82; Q5U5P4;
AC Q6P0P2; Q6PGQ4; Q7Z688; Q7Z689; Q7Z690; Q7Z691;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 193.
DE RecName: Full=Beta-adducin;
DE AltName: Full=Erythrocyte adducin subunit beta;
GN Name=ADD2; Synonyms=ADDB;
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), AND PARTIAL PROTEIN SEQUENCE.
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] (ISOFORMS 4; 5; 6 AND 7), TISSUE SPECIFICITY,
RP AND DEVELOPMENTAL STAGE.
RC TISSUE=Fetal kidney, and Umbilical vein endothelial cell;
RX PubMed=12951058; DOI=10.1016/j.bbrc.2003.08.011;
RA Citterio L., Tizzoni L., Catalano M., Zerbini G., Bianchi G.,
RA Barlassina C.;
RT "Expression analysis of the human adducin gene family and evidence of ADD2
RT beta4 multiple splicing variants.";
RL Biochem. Biophys. Res. Commun. 309:359-367(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 8 AND 9).
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno R.F.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=21697133; DOI=10.1167/iovs.11-7479;
RA Oshikawa M., Tsutsui C., Ikegami T., Fuchida Y., Matsubara M., Toyama S.,
RA Usami R., Ohtoko K., Kato S.;
RT "Full-length transcriptome analysis of human retina-derived cell lines
RT ARPE-19 and Y79 using the vector-capping method.";
RL Invest. Ophthalmol. Vis. Sci. 52:6662-6670(2011).
RN [6]
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 [7]
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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), AND VARIANT
RP ALA-439.
RC TISSUE=Eye;
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 [9]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 332-726 (ISOFORM 3).
RC TISSUE=Bone marrow;
RA Sinard J.H., Stewart G.W., Argent A.C., Gilligan D.M., Morrow J.S.;
RT "A novel isoform of beta adducin utilizes an alternatively spliced exon
RT near the C-terminus.";
RL Mol. Biol. Cell 6:269-269(1995).
RN [10]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 462-559 (ISOFORM 2), AND ALTERNATIVE
RP SPLICING.
RX PubMed=8566798; DOI=10.1016/0378-1119(95)00591-9;
RA Tisminetzky S., Devescovi G., Tripodi G., Muro A., Bianchi G., Colombi M.,
RA Moro L., Barlati S., Tuteja R., Baralle F.E.;
RT "Genomic organisation and chromosomal localisation of the gene encoding
RT human beta adducin.";
RL Gene 167:313-316(1995).
RN [11]
RP PHOSPHORYLATION AT THR-55; SER-703 AND SER-713, AND PARTIAL PROTEIN
RP 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 [12]
RP FUNCTION, IDENTIFICATION IN A COMPLEX WITH DMTN AND SLC2A1, AND INTERACTION
RP WITH SLC2A1.
RX PubMed=18347014; DOI=10.1074/jbc.m707818200;
RA Khan A.A., Hanada T., Mohseni M., Jeong J.J., Zeng L., Gaetani M., Li D.,
RA Reed B.C., Speicher D.W., Chishti A.H.;
RT "Dematin and adducin provide a novel link between the spectrin cytoskeleton
RT and human erythrocyte membrane by directly interacting with glucose
RT transporter-1.";
RL J. Biol. Chem. 283:14600-14609(2008).
RN [13]
RP IDENTIFICATION BY MASS 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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-530; SER-592; SER-596;
RP SER-600; SER-604; THR-611; SER-613; SER-617; SER-693 AND SER-697, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11; SER-530; SER-532;
RP SER-592; SER-596; SER-600; SER-613; SER-617; SER-621; THR-675; SER-693 AND
RP SER-697, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-596, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE 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).
CC -!- FUNCTION: Membrane-cytoskeleton-associated protein that promotes the
CC assembly of the spectrin-actin network. Binds to the erythrocyte
CC membrane receptor SLC2A1/GLUT1 and may therefore provide a link between
CC the spectrin cytoskeleton to the plasma membrane. Binds to calmodulin.
CC Calmodulin binds preferentially to the beta subunit.
CC {ECO:0000269|PubMed:18347014}.
CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit. Found in a complex
CC with ADD2, DMTN and SLC2A1. Interacts with SLC2A1.
CC {ECO:0000269|PubMed:18347014}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cell membrane;
CC Peripheral membrane protein; Cytoplasmic side.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=9;
CC Comment=Additional isoforms seem to exist.;
CC Name=1;
CC IsoId=P35612-1; Sequence=Displayed;
CC Name=2; Synonyms=Adducin 63;
CC IsoId=P35612-2; Sequence=VSP_000181, VSP_000182;
CC Name=3; Synonyms=Beta-4, E;
CC IsoId=P35612-3; Sequence=VSP_000183;
CC Name=4; Synonyms=Beta-4a;
CC IsoId=P35612-4; Sequence=VSP_017244, VSP_017246;
CC Name=5; Synonyms=Beta-4b;
CC IsoId=P35612-5; Sequence=VSP_017242, VSP_017243, VSP_017245;
CC Name=6; Synonyms=Beta-4c;
CC IsoId=P35612-6; Sequence=VSP_017242, VSP_017244, VSP_017246;
CC Name=7; Synonyms=Beta-4d;
CC IsoId=P35612-7; Sequence=VSP_017241, VSP_017244, VSP_017246;
CC Name=8;
CC IsoId=P35612-8; Sequence=VSP_043625, VSP_000181, VSP_000182;
CC Name=9;
CC IsoId=P35612-9; Sequence=VSP_055309, VSP_000181, VSP_000182;
CC -!- TISSUE SPECIFICITY: Expressed mainly in brain, spleen, kidney cortex
CC and medulla, and heart. Also expressed in human umbilical vein
CC endothelial cells, human vascular smooth muscle cells, kidney tubular
CC cells and K-562 cell line. {ECO:0000269|PubMed:12951058}.
CC -!- DEVELOPMENTAL STAGE: Fetal kidney expresses isoforms 3, 4, 5, 6 and 7,
CC and fetal liver expresses isoforms 3 and 4.
CC {ECO:0000269|PubMed:12951058}.
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 -!- PTM: The N-terminus is blocked.
CC -!- SIMILARITY: Belongs to the aldolase class II family. Adducin subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD92464.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X58199; CAA41176.1; -; mRNA.
DR EMBL; AF486420; AAP71863.1; -; mRNA.
DR EMBL; AF486421; AAP71864.1; -; mRNA.
DR EMBL; AF486422; AAP71865.1; -; mRNA.
DR EMBL; AF486423; AAP71866.1; -; mRNA.
DR EMBL; AK291007; BAF83696.1; -; mRNA.
DR EMBL; AK297250; BAG59729.1; -; mRNA.
DR EMBL; AK309773; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AB209227; BAD92464.1; ALT_INIT; mRNA.
DR EMBL; AB593080; BAJ84020.1; -; mRNA.
DR EMBL; AC005234; AAD12715.1; -; Genomic_DNA.
DR EMBL; AC007395; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471053; EAW99801.1; -; Genomic_DNA.
DR EMBL; CH471053; EAW99806.1; -; Genomic_DNA.
DR EMBL; CH471053; EAW99807.1; -; Genomic_DNA.
DR EMBL; CH471053; EAW99808.1; -; Genomic_DNA.
DR EMBL; BC041666; AAH41666.1; -; mRNA.
DR EMBL; BC051882; AAH51882.1; -; mRNA.
DR EMBL; BC056881; AAH56881.1; -; mRNA.
DR EMBL; BC065525; AAH65525.1; -; mRNA.
DR EMBL; U43959; AAA86421.1; -; mRNA.
DR EMBL; S81079; AAD14349.1; -; Genomic_DNA.
DR EMBL; S81077; AAD14349.1; JOINED; Genomic_DNA.
DR CCDS; CCDS1906.1; -. [P35612-1]
DR CCDS; CCDS1909.1; -. [P35612-3]
DR CCDS; CCDS46318.1; -. [P35612-2]
DR CCDS; CCDS54365.1; -. [P35612-9]
DR PIR; S18208; S18208.
DR RefSeq; NP_001171983.1; NM_001185054.1. [P35612-1]
DR RefSeq; NP_001171984.1; NM_001185055.1. [P35612-9]
DR RefSeq; NP_001608.1; NM_001617.3. [P35612-1]
DR RefSeq; NP_059516.2; NM_017482.3. [P35612-2]
DR RefSeq; NP_059522.1; NM_017488.3. [P35612-3]
DR RefSeq; XP_011530804.1; XM_011532502.2. [P35612-1]
DR AlphaFoldDB; P35612; -.
DR SMR; P35612; -.
DR BioGRID; 106632; 62.
DR CORUM; P35612; -.
DR IntAct; P35612; 16.
DR MINT; P35612; -.
DR STRING; 9606.ENSP00000264436; -.
DR iPTMnet; P35612; -.
DR PhosphoSitePlus; P35612; -.
DR BioMuta; ADD2; -.
DR DMDM; 543774; -.
DR EPD; P35612; -.
DR jPOST; P35612; -.
DR MassIVE; P35612; -.
DR MaxQB; P35612; -.
DR PaxDb; P35612; -.
DR PeptideAtlas; P35612; -.
DR PRIDE; P35612; -.
DR ProteomicsDB; 55105; -. [P35612-1]
DR ProteomicsDB; 55106; -. [P35612-2]
DR ProteomicsDB; 55107; -. [P35612-3]
DR ProteomicsDB; 55108; -. [P35612-4]
DR ProteomicsDB; 55109; -. [P35612-5]
DR ProteomicsDB; 55110; -. [P35612-6]
DR ProteomicsDB; 55111; -. [P35612-7]
DR ProteomicsDB; 55112; -. [P35612-8]
DR Antibodypedia; 4066; 244 antibodies from 29 providers.
DR DNASU; 119; -.
DR Ensembl; ENST00000264436.9; ENSP00000264436.3; ENSG00000075340.23. [P35612-1]
DR Ensembl; ENST00000355733.7; ENSP00000347972.3; ENSG00000075340.23. [P35612-3]
DR Ensembl; ENST00000403045.6; ENSP00000384303.2; ENSG00000075340.23. [P35612-1]
DR Ensembl; ENST00000407644.6; ENSP00000384677.2; ENSG00000075340.23. [P35612-1]
DR Ensembl; ENST00000413157.6; ENSP00000388072.2; ENSG00000075340.23. [P35612-2]
DR Ensembl; ENST00000430656.5; ENSP00000398112.1; ENSG00000075340.23. [P35612-9]
DR GeneID; 119; -.
DR KEGG; hsa:119; -.
DR MANE-Select; ENST00000264436.9; ENSP00000264436.3; NM_001617.4; NP_001608.1.
DR UCSC; uc002sgy.4; human. [P35612-1]
DR CTD; 119; -.
DR DisGeNET; 119; -.
DR GeneCards; ADD2; -.
DR HGNC; HGNC:244; ADD2.
DR HPA; ENSG00000075340; Tissue enhanced (bone marrow, brain).
DR MIM; 102681; gene.
DR neXtProt; NX_P35612; -.
DR OpenTargets; ENSG00000075340; -.
DR PharmGKB; PA24566; -.
DR VEuPathDB; HostDB:ENSG00000075340; -.
DR eggNOG; KOG3699; Eukaryota.
DR GeneTree; ENSGT00940000159299; -.
DR HOGENOM; CLU_006033_9_2_1; -.
DR InParanoid; P35612; -.
DR OMA; PFVQEKA; -.
DR PhylomeDB; P35612; -.
DR TreeFam; TF313003; -.
DR PathwayCommons; P35612; -.
DR Reactome; R-HSA-5223345; Miscellaneous transport and binding events.
DR SignaLink; P35612; -.
DR SIGNOR; P35612; -.
DR BioGRID-ORCS; 119; 24 hits in 1080 CRISPR screens.
DR ChiTaRS; ADD2; human.
DR GeneWiki; ADD2; -.
DR GenomeRNAi; 119; -.
DR Pharos; P35612; Tbio.
DR PRO; PR:P35612; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; P35612; protein.
DR Bgee; ENSG00000075340; Expressed in Brodmann (1909) area 10 and 170 other tissues.
DR ExpressionAtlas; P35612; baseline and differential.
DR Genevisible; P35612; HS.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:UniProtKB.
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:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0044853; C:plasma membrane raft; IMP:CAFA.
DR GO; GO:0014069; C:postsynaptic density; IBA:GO_Central.
DR GO; GO:0003779; F:actin binding; IMP:CAFA.
DR GO; GO:0051015; F:actin filament binding; IDA: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:0019901; F:protein kinase binding; IPI:CAFA.
DR GO; GO:0030507; F:spectrin binding; IDA:BHF-UCL.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; IEA:Ensembl.
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:0030097; P:hemopoiesis; IEA:Ensembl.
DR GO; GO:0050900; P:leukocyte migration; IMP:CAFA.
DR GO; GO:0050901; P:leukocyte tethering or rolling; IMP:CAFA.
DR GO; GO:0032092; P:positive regulation of protein binding; IDA:BHF-UCL.
DR GO; GO:0065003; P:protein-containing complex assembly; IDA:UniProtKB.
DR GO; GO:0007416; P:synapse assembly; IEA:Ensembl.
DR DisProt; DP00241; -.
DR Gene3D; 3.40.225.10; -; 1.
DR InterPro; IPR027773; ADD2.
DR InterPro; IPR001303; Aldolase_II/adducin_N.
DR InterPro; IPR036409; Aldolase_II/adducin_N_sf.
DR PANTHER; PTHR10672:SF6; PTHR10672:SF6; 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 Actin-binding; Alternative splicing; Calmodulin-binding; Cell membrane;
KW Cytoplasm; Cytoskeleton; Direct protein sequencing; Membrane;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..726
FT /note="Beta-adducin"
FT /id="PRO_0000218533"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 425..444
FT /note="Interaction with calmodulin"
FT /evidence="ECO:0000255"
FT REGION 525..726
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 704..721
FT /note="Interaction with calmodulin"
FT /evidence="ECO:0000255"
FT COMPBIAS 563..589
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 661..675
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 684..699
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 703..717
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 11
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 25
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q05764"
FT MOD_RES 55
FT /note="Phosphothreonine; by PKA"
FT /evidence="ECO:0000269|PubMed:8810272"
FT MOD_RES 60
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYB8"
FT MOD_RES 344
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYB8"
FT MOD_RES 530
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 532
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 533
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYB8"
FT MOD_RES 535
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYB8"
FT MOD_RES 592
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 596
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 600
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 604
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 611
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 613
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 617
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 619
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYB8"
FT MOD_RES 621
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 675
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 686
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q05764"
FT MOD_RES 689
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYB8"
FT MOD_RES 693
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 697
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 699
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYB8"
FT MOD_RES 701
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYB8"
FT MOD_RES 703
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0000269|PubMed:8810272"
FT MOD_RES 713
FT /note="Phosphoserine; by PKA and PKC"
FT /evidence="ECO:0000269|PubMed:8810272"
FT VAR_SEQ 1
FT /note="M -> MPRRRVPGANCKPTGK (in isoform 8)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043625"
FT VAR_SEQ 1
FT /note="M -> MPRRRVPGANCKPTGKM (in isoform 9)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055309"
FT VAR_SEQ 78..566
FT /note="Missing (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:12951058"
FT /id="VSP_017241"
FT VAR_SEQ 188..493
FT /note="Missing (in isoform 5 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:12951058"
FT /id="VSP_017242"
FT VAR_SEQ 532..559
FT /note="STESQLMSKGDEDTKDDSEETVPNPFSQ -> VEQRLPLTGGETCLPSGSSV
FT PGAGLQDP (in isoform 2, isoform 8 and isoform 9)"
FT /evidence="ECO:0000303|PubMed:14702039, ECO:0000303|Ref.4"
FT /id="VSP_000181"
FT VAR_SEQ 560..726
FT /note="Missing (in isoform 2, isoform 8 and isoform 9)"
FT /evidence="ECO:0000303|PubMed:14702039, ECO:0000303|Ref.4"
FT /id="VSP_000182"
FT VAR_SEQ 581..726
FT /note="GEKETAPEEPGSPAKSAPASPVQSPAKEAETKSPLVSPSKSLEEGTKKTETS
FT KAATTEPETTQPEGVVVNGREEEQTAEEILSKGLSQMTTSADTDVDTSKDKTESVTSGP
FT MSPEGSPSKSPSKKKKKFRTPSFLKKSKKKEKVES -> ETGQEREPGSGPAVCEFFSV
FT ALHIWSNILERKKLPQKSLAHLQSLHLLLQCRAQRRRQRQRAL (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.9"
FT /id="VSP_000183"
FT VAR_SEQ 581..587
FT /note="GEKETAP -> APGWFSS (in isoform 4, isoform 6 and
FT isoform 7)"
FT /evidence="ECO:0000303|PubMed:12951058"
FT /id="VSP_017244"
FT VAR_SEQ 581..586
FT /note="GEKETA -> ETGQER (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:12951058"
FT /id="VSP_017243"
FT VAR_SEQ 587..726
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:12951058"
FT /id="VSP_017245"
FT VAR_SEQ 588..726
FT /note="Missing (in isoform 4, isoform 6 and isoform 7)"
FT /evidence="ECO:0000303|PubMed:12951058"
FT /id="VSP_017246"
FT VARIANT 28
FT /note="D -> N (in dbSNP:rs4986)"
FT /id="VAR_014866"
FT VARIANT 98
FT /note="S -> C (in dbSNP:rs4987)"
FT /id="VAR_048195"
FT VARIANT 335
FT /note="E -> D (in dbSNP:rs4982)"
FT /id="VAR_014867"
FT VARIANT 439
FT /note="T -> A (in dbSNP:rs17855969)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_025318"
FT VARIANT 663
FT /note="S -> R (in dbSNP:rs4985)"
FT /id="VAR_014868"
SQ SEQUENCE 726 AA; 80854 MW; B07F7303D929DBA4 CRC64;
MSEETVPEAA SPPPPQGQPY FDRFSEDDPE YMRLRNRAAD LRQDFNLMEQ KKRVTMILQS
PSFREELEGL IQEQMKKGNN SSNIWALRQI ADFMASTSHA VFPTSSMNVS MMTPINDLHT
ADSLNLAKGE RLMRCKISSV YRLLDLYGWA QLSDTYVTLR VSKEQDHFLI SPKGVSCSEV
TASSLIKVNI LGEVVEKGSS CFPVDTTGFC LHSAIYAARP DVRCIIHLHT PATAAVSAMK
WGLLPVSHNA LLVGDMAYYD FNGEMEQEAD RINLQKCLGP TCKILVLRNH GVVALGDTVE
EAFYKIFHLQ AACEIQVSAL SSAGGVENLI LLEQEKHRPH EVGSVQWAGS TFGPMQKSRL
GEHEFEALMR MLDNLGYRTG YTYRHPFVQE KTKHKSEVEI PATVTAFVFE EDGAPVPALR
QHAQKQQKEK TRWLNTPNTY LRVNVADEVQ RSMGSPRPKT TWMKADEVEK SSSGMPIRIE
NPNQFVPLYT DPQEVLEMRN KIREQNRQDV KSAGPQSQLL ASVIAEKSRS PSTESQLMSK
GDEDTKDDSE ETVPNPFSQL TDQELEEYKK EVERKKLELD GEKETAPEEP GSPAKSAPAS
PVQSPAKEAE TKSPLVSPSK SLEEGTKKTE TSKAATTEPE TTQPEGVVVN GREEEQTAEE
ILSKGLSQMT TSADTDVDTS KDKTESVTSG PMSPEGSPSK SPSKKKKKFR TPSFLKKSKK
KEKVES
