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 27-MAR-2024, entry version 202. 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 69. DR ComplexPortal; CPX-2638; Adducin complex, alpha-beta variant. DR CORUM; P35612; -. DR IntAct; P35612; 20. DR MINT; P35612; -. DR STRING; 9606.ENSP00000264436; -. DR GlyGen; P35612; 2 sites, 1 O-linked glycan (2 sites). 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; 9606-ENSP00000264436; -. DR PeptideAtlas; 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 Pumba; P35612; -. DR Antibodypedia; 4066; 294 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 AGR; HGNC:244; -. 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; TSGFCLH; -. DR OrthoDB; 45123at2759; -. 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 1157 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 171 other cell types or tissues. DR ExpressionAtlas; P35612; baseline and differential. 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:0046983; F:protein dimerization activity; IPI:DisProt. 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 CDD; cd00398; Aldolase_II; 1. DR DisProt; DP00241; -. DR Gene3D; 3.40.225.10; Class II aldolase/adducin N-terminal domain; 1. DR InterPro; IPR001303; Aldolase_II/adducin_N. DR InterPro; IPR036409; Aldolase_II/adducin_N_sf. DR PANTHER; PTHR10672; ADDUCIN; 1. DR PANTHER; PTHR10672:SF6; BETA-ADDUCIN; 1. DR Pfam; PF00596; Aldolase_II; 1. DR SMART; SM01007; Aldolase_II; 1. DR SUPFAM; SSF53639; AraD/HMP-PK domain-like; 1. DR Genevisible; P35612; HS. 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 //