ID SPTB1_HUMAN Reviewed; 2137 AA. AC P11277; Q15510; Q15519; DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot. DT 25-NOV-2008, sequence version 5. DT 02-SEP-2026, entry version 238. DE RecName: Full=Spectrin beta chain, erythrocytic; DE AltName: Full=Beta-I spectrin; GN Name=SPTB; Synonyms=SPTB1; 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] (ISOFORMS 1 AND 3), AND VARIANTS ASN-439 AND RP ASP-1151. RX PubMed=2195026; DOI=10.1016/s0021-9258(19)38473-x; RA Winkelmann J.C., Chang J.G., Tse W.T., Scarpa A.L., Marchesi V.T., RA Forget B.G.; RT "Full-length sequence of the cDNA for human erythroid beta-spectrin."; RL J. Biol. Chem. 265:11827-11832(1990). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12508121; DOI=10.1038/nature01348; RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., RA Waterston R., Hood L., Weissenbach J.; RT "The DNA sequence and analysis of human chromosome 14."; RL Nature 421:601-607(2003). RN [3] RP PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3), AND ALTERNATIVE RP SPLICING. RX PubMed=2056132; DOI=10.1172/jci115307; RA Garbarz M., Tse W.T., Gallagher P.G., Picat C., Lecomte M.C., Galibert F., RA Dhermy D., Forget B.G.; RT "Spectrin Rouen (beta 220-218), a novel shortened beta-chain variant in a RT kindred with hereditary elliptocytosis. Characterization of the molecular RT defect as exon skipping due to a splice site mutation."; RL J. Clin. Invest. 88:76-81(1991). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1055-2137 (ISOFORM 2), AND VARIANT ASP-1151. RC TISSUE=Skeletal muscle; RX PubMed=2243099; DOI=10.1016/s0021-9258(17)30525-2; RA Winkelmann J.C., Costa F.F., Linzie B.L., Forget B.G.; RT "Beta spectrin in human skeletal muscle. Tissue-specific differential RT processing of 3' beta spectrin pre-mRNA generates a beta spectrin isoform RT with a unique carboxyl terminus."; RL J. Biol. Chem. 265:20449-20454(1990). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] OF 2002-2137 (ISOFORM 1). RX PubMed=1840591; DOI=10.1016/s0021-9258(18)98598-4; RA Gallagher P.G., Tse W.T., Costa F., Scarpa A., Boivin P., Delaunay J., RA Forget B.G.; RT "A splice site mutation of the beta-spectrin gene causing exon skipping in RT hereditary elliptocytosis associated with a truncated beta-spectrin RT chain."; RL J. Biol. Chem. 266:15154-15159(1991). RN [6] RP NUCLEOTIDE SEQUENCE [MRNA] OF 928-1756 (ISOFORMS 1/2/3), AND VARIANT RP ASP-1151. RX PubMed=1976574; DOI=10.1016/0378-1119(90)90104-y; RA Yoon S.H., Kentros C.G., Prchal J.T.; RT "Identification of an unusual deletion within homologous repeats of human RT reticulocyte beta-spectrin and probable peptide polymorphism."; RL Gene 91:297-302(1990). RN [7] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1334-1432 (ISOFORMS 1/2/3), NUCLEOTIDE RP SEQUENCE [MRNA] OF 1909-2137 (ISOFORM 1), AND VARIANT ARG-1374. RX PubMed=3390609; DOI=10.1182/blood.v72.1.328.328; RA Winkelmann J.C., Leto T.L., Watkins P.C., Eddy R., Shows T.B., RA Linnenbach A.J., Sahr K.E., Kathuria N., Marchesi V.T., Forget B.G.; RT "Molecular cloning of the cDNA for human erythrocyte beta-spectrin."; RL Blood 72:328-334(1988). RN [8] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1209-1482 (ISOFORMS 1/2/3). RX PubMed=3478706; DOI=10.1073/pnas.84.21.7468; RA Prchal J.T., Morley B.J., Yoon S.-H., Coetzer T.L., Palek J., Conboy J.G., RA Kan Y.W.; RT "Isolation and characterization of cDNA clones for human erythrocyte beta- RT spectrin."; RL Proc. Natl. Acad. Sci. U.S.A. 84:7468-7472(1987). RN [9] RP PROTEIN SEQUENCE OF 2-18. RC TISSUE=Platelet; RX PubMed=12665801; DOI=10.1038/nbt810; RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., RA Vandekerckhove J.; RT "Exploring proteomes and analyzing protein processing by mass spectrometric RT identification of sorted N-terminal peptides."; RL Nat. Biotechnol. 21:566-569(2003). RN [10] RP DOMAINS. RX PubMed=6472478; DOI=10.1038/311177a0; RA Speicher D.W., Marchesi V.T.; RT "Erythrocyte spectrin is comprised of many homologous triple helical RT segments."; RL Nature 311:177-180(1984). RN [11] RP PHOSPHORYLATION AT THR-2110; SER-2114; SER-2117; SER-2123; SER-2125 AND RP SER-2128. RX PubMed=15065869; DOI=10.1021/bi036092x; RA Tang H.Y., Speicher D.W.; RT "In vivo phosphorylation of human erythrocyte spectrin occurs in a RT sequential manner."; RL Biochemistry 43:4251-4262(2004). RN [12] RP INTERACTION WITH BCAM. RX PubMed=15238148; DOI=10.1111/j.1365-2141.2004.05010.x; RA Kroviarski Y., El Nemer W., Gane P., Rahuel C., Gauthier E., Lecomte M.C., RA Cartron J.P., Colin Y., Le Van Kim C.; RT "Direct interaction between the Lu/B-CAM adhesion glycoproteins and RT erythroid spectrin."; RL Br. J. Haematol. 126:255-264(2004). RN [13] RP INVOLVEMENT IN SPH2. RX PubMed=19538529; DOI=10.1111/j.1365-2141.2009.07759.x; RA Maciag M., Plochocka D., Adamowicz-Salach A., Burzynska B.; RT "Novel beta-spectrin mutations in hereditary spherocytosis associated with RT decreased levels of mRNA."; RL Br. J. Haematol. 146:326-332(2009). RN [14] 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 [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-104; THR-2073; SER-2123 AND RP SER-2125, 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-2043, 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). RN [17] RP PROTEOLYTIC CLEAVAGE (MICROBIAL INFECTION). RX PubMed=29459732; DOI=10.1038/s41564-018-0111-0; RA Thomas J.A., Tan M.S.Y., Bisson C., Borg A., Umrekar T.R., Hackett F., RA Hale V.L., Vizcay-Barrena G., Fleck R.A., Snijders A.P., Saibil H.R., RA Blackman M.J.; RT "A protease cascade regulates release of the human malaria parasite RT Plasmodium falciparum from host red blood cells."; RL Nat. Microbiol. 3:447-455(2018). RN [18] RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1064-1275. RX PubMed=15062087; DOI=10.1016/j.str.2004.02.022; RA Kusunoki H., MacDonald R.I., Mondragon A.; RT "Structural insights into the stability and flexibility of unusual RT erythroid spectrin repeats."; RL Structure 12:645-656(2004). RN [19] RP REVIEW ON VARIANTS. RX PubMed=8844207; RX DOI=10.1002/(sici)1098-1004(1996)8:2<97::aid-humu1>3.0.co;2-m; RA Maillet P., Alloisio N., Morle L., Delaunay J.; RT "Spectrin mutations in hereditary elliptocytosis and hereditary RT spherocytosis."; RL Hum. Mutat. 8:97-107(1996). RN [20] RP VARIANT EL3 PRO-2053. RX PubMed=1975598; DOI=10.1172/jci114792; RA Tse W.T., Lecomte M.-C., Costa F.F., Garbarz M., Feo C., Boivin P., RA Dhermy D., Forget B.G.; RT "Point mutation in the beta-spectrin gene associated with alpha I/74 RT hereditary elliptocytosis. Implications for the mechanism of spectrin dimer RT self-association."; RL J. Clin. Invest. 86:909-916(1990). RN [21] RP VARIANT EL3 CAGLIARI GLY-2018. RX PubMed=8226774; DOI=10.1016/s0021-9258(18)41578-5; RA Sahr K.E., Coetzer T.L., Moy L.S., Derick L.H., Chishti A.H., Jarolim P., RA Lorenzo F., del Giudice E.M., Iolascon A., Gallanello R., Cao A., RA Delaunay J., Liu S.-C., Palek J.; RT "Spectrin Cagliari: an Ala-->Gly substitution in helix 1 of beta spectrin RT repeat 17 that severely disrupts the structure and self-association of the RT erythrocyte spectrin heterodimer."; RL J. Biol. Chem. 268:22656-22662(1993). RN [22] RP INVOLVEMENT IN SPH2, AND VARIANT SPH2 ARG-202. RX PubMed=8102379; DOI=10.1172/jci116628; RA Becker P.S., Tse W.T., Lux S.E., Forget B.G.; RT "Beta spectrin Kissimmee: a spectrin variant associated with autosomal RT dominant hereditary spherocytosis and defective binding to protein 4.1."; RL J. Clin. Invest. 92:612-616(1993). RN [23] RP VARIANTS EL3 VAL-2023 AND ARG-2024. RX PubMed=8018926; DOI=10.1182/blood.v84.1.303.303; RA Parquet N., Devaux I., Boulanger L., Galand C., Boivin P., Lecomte M.-C., RA Dhermy D., Garbarz M.; RT "Identification of three novel spectrin alpha I/74 mutations in hereditary RT elliptocytosis: further support for a triple-stranded folding unit model of RT the spectrin heterodimer contact site."; RL Blood 84:303-308(1994). RN [24] RP VARIANT EL3 PROVIDENCE PRO-2019. RX PubMed=7883966; DOI=10.1172/jci117766; RA Gallagher P.G., Weed S.A., Tse W.T., Benoit L., Morrow J.S., Marchesi S.L., RA Mohandas N., Forget B.G.; RT "Recurrent fatal hydrops fetalis associated with a nucleotide substitution RT in the erythrocyte beta-spectrin gene."; RL J. Clin. Invest. 95:1174-1182(1995). RN [25] RP VARIANT EL3 ARG-2025. RX PubMed=9005995; DOI=10.1172/jci119155; RA Gallagher P.G., Petruzzi M.J., Weed S.A., Zhang Z., Marchesi S.L., RA Mohandas N., Morrow J.S., Forget B.G.; RT "Mutation of a highly conserved residue of betaI spectrin associated with RT fatal and near-fatal neonatal hemolytic anemia."; RL J. Clin. Invest. 99:267-277(1997). CC -!- FUNCTION: Spectrin is the major constituent of the cytoskeletal network CC underlying the erythrocyte plasma membrane. It associates with band 4.1 CC and actin to form the cytoskeletal superstructure of the erythrocyte CC plasma membrane. CC -!- SUBUNIT: Composed of nonhomologous chains, alpha and beta, which CC aggregate to form dimers, tetramers, and higher polymers. Interacts CC with BCAM (PubMed:15238148). {ECO:0000269|PubMed:15238148}. CC -!- INTERACTION: CC P11277; P05067: APP; NbExp=6; IntAct=EBI-514908, EBI-77613; CC P11277; O95295: SNAPIN; NbExp=3; IntAct=EBI-514908, EBI-296723; CC P11277; P02549: SPTA1; NbExp=5; IntAct=EBI-514908, EBI-375617; CC P11277; P50463: Csrp3; Xeno; NbExp=6; IntAct=EBI-514908, EBI-12502290; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cytoplasm, cell cortex. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=P11277-1; Sequence=Displayed; CC Name=2; Synonyms=Muscle-specific; CC IsoId=P11277-2; Sequence=VSP_000719; CC Name=3; CC IsoId=P11277-3; Sequence=VSP_007242; CC -!- PTM: The first phosphorylation event occurs on Ser-2114, followed by CC Ser-2125, Ser-2123, Ser-2128, Ser-2117, and Thr-2110. CC {ECO:0000269|PubMed:15065869}. CC -!- PTM: (Microbial infection) Probably cleaved by P.falciparum SERA6; the CC cleavage results in SPTB solubilization causing the disruption of the CC actin cytoskeleton and the rupture of the erythrocyte cell membrane CC releasing the merozoites. {ECO:0000269|PubMed:29459732}. CC -!- DISEASE: Elliptocytosis 3 (EL3) [MIM:617948]: A Rhesus-unlinked form of CC hereditary elliptocytosis, a genetically heterogeneous hematologic CC disorder characterized by variable hemolytic anemia and elliptical or CC oval red cell shape. Inheritance can be autosomal dominant or autosomal CC recessive. {ECO:0000269|PubMed:1975598, ECO:0000269|PubMed:7883966, CC ECO:0000269|PubMed:8018926, ECO:0000269|PubMed:8226774, CC ECO:0000269|PubMed:9005995}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- DISEASE: Spherocytosis 2 (SPH2) [MIM:616649]: An autosomal dominant CC form of hereditary spherocytosis, a group of hematologic disorders CC characterized by numerous abnormally shaped erythrocytes which are CC generally spheroidal. Clinical manifestations include chronic hemolytic CC anemia, jaundice, and splenomegaly, with variable severity. CC {ECO:0000269|PubMed:19538529, ECO:0000269|PubMed:8102379}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- MISCELLANEOUS: This complex is anchored to the cytoplasmic face of the CC plasma membrane via another protein, ankyrin, which binds to beta- CC spectrin and mediates the binding of the whole complex to a CC transmembrane protein band 3. The interaction of erythrocyte spectrin CC with other proteins through specific binding domains lead to the CC formation of an extensive subplasmalemmal meshwork which is thought to CC be responsible for the maintenance of the biconcave shape of human CC erythrocytes, for the regulation of plasma membrane components and for CC the maintenance of the lipid asymmetry of the plasma membrane. CC -!- MISCELLANEOUS: [Isoform 3]: Due to exon skipping. {ECO:0000305}. CC -!- SIMILARITY: Belongs to the spectrin family. {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; J05500; AAA60578.1; -; mRNA. DR EMBL; J05500; AAA60579.1; -; mRNA. DR EMBL; AL121774; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; M37884; AAA63259.1; -; mRNA. DR EMBL; M37885; AAA60571.1; -; mRNA. DR EMBL; M57948; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; X59510; CAA42097.1; -; mRNA. DR EMBL; X59511; CAA42098.1; -; mRNA. DR EMBL; M18054; AAA60572.1; -; mRNA. DR CCDS; CCDS32099.1; -. [P11277-2] DR CCDS; CCDS32100.1; -. [P11277-1] DR PIR; A37064; SJHUB. DR RefSeq; NP_001020029.1; NM_001024858.4. [P11277-2] DR RefSeq; NP_001342365.1; NM_001355436.2. [P11277-2] DR RefSeq; NP_001342366.1; NM_001355437.2. [P11277-1] DR RefSeq; XP_016877101.1; XM_017021612.3. [P11277-2] DR RefSeq; XP_024305467.1; XM_024449699.2. [P11277-2] DR RefSeq; XP_047287680.1; XM_047431724.1. [P11277-2] DR RefSeq; XP_047287681.1; XM_047431725.1. [P11277-2] DR RefSeq; XP_054232616.1; XM_054376641.1. [P11277-2] DR RefSeq; XP_054232617.1; XM_054376642.1. [P11277-2] DR RefSeq; XP_054232618.1; XM_054376643.1. [P11277-2] DR RefSeq; XP_054232619.1; XM_054376644.1. [P11277-2] DR PDB; 1S35; X-ray; 2.40 A; A=1063-1275. DR PDB; 3EDU; X-ray; 2.10 A; A=1692-1907. DR PDB; 3F57; X-ray; 2.90 A; A/B=1686-1907. DR PDB; 3KBT; X-ray; 2.75 A; A/B=1583-1906. DR PDB; 3KBU; X-ray; 2.75 A; A/B=1583-1906. DR PDB; 3LBX; X-ray; 2.80 A; B=1902-2084. DR AlphaFoldDB; P11277; -. DR SMR; P11277; -. DR BioGRID; 112588; 104. DR ComplexPortal; CPX-2499; Erythrocyte spectrin complex. DR DIP; DIP-1021N; -. DR FunCoup; P11277; 210. DR IntAct; P11277; 50. DR STRING; 9606.ENSP00000495909; -. DR CarbonylDB; P11277; -. DR GlyConnect; P11277; 1 O-GlcNAc glycan (5 sites). DR GlyCosmos; P11277; 5 sites, 1 glycan. DR GlyGen; P11277; 8 sites, 1 O-linked glycan (6 sites). DR iPTMnet; P11277; -. DR MetOSite; P11277; -. DR PhosphoSitePlus; P11277; -. DR BioMuta; SPTB; -. DR DMDM; 215274269; -. DR jPOST; P11277; -. DR MassIVE; P11277; -. DR PaxDb; 9606-ENSP00000495909; -. DR PeptideAtlas; P11277; -. DR ProteomicsDB; 52731; -. [P11277-1] DR ProteomicsDB; 52732; -. [P11277-2] DR ProteomicsDB; 52733; -. [P11277-3] DR Pumba; P11277; -. DR ABCD; P11277; 1 sequenced antibody. DR Antibodypedia; 183; 125 antibodies from 25 providers. DR DNASU; 6710; -. DR Ensembl; ENST00000389720.4; ENSP00000374370.4; ENSG00000070182.22. [P11277-1] DR Ensembl; ENST00000389722.7; ENSP00000374372.3; ENSG00000070182.22. [P11277-2] DR Ensembl; ENST00000644917.1; ENSP00000495909.1; ENSG00000070182.22. [P11277-2] DR Ensembl; ENST00000961380.1; ENSP00000631439.1; ENSG00000070182.22. [P11277-2] DR Ensembl; ENST00000961381.1; ENSP00000631440.1; ENSG00000070182.22. [P11277-2] DR Ensembl; ENST00000961382.1; ENSP00000631441.1; ENSG00000070182.22. [P11277-2] DR GeneID; 6710; -. DR KEGG; hsa:6710; -. DR MANE-Select; ENST00000644917.1; ENSP00000495909.1; NM_001355436.2; NP_001342365.1. [P11277-2] DR UCSC; uc001xhr.4; human. [P11277-1] DR AGR; HGNC:11274; -. DR ClinPGx; PA36103; -. DR CTD; 6710; -. DR DisGeNET; 6710; -. DR GeneCards; SPTB; -. DR HGNC; HGNC:11274; SPTB. DR HPA; ENSG00000070182; Tissue enhanced (bone marrow, skeletal muscle, tongue). DR MalaCards; SPTB; -. DR MIM; 182870; gene. DR MIM; 616649; phenotype. DR MIM; 617948; phenotype. DR OpenTargets; ENSG00000070182; -. DR Orphanet; 288; Hereditary elliptocytosis. DR Orphanet; 822; Hereditary spherocytosis. DR VEuPathDB; HostDB:ENSG00000070182; -. DR eggNOG; KOG0517; Eukaryota. DR GeneTree; ENSGT00940000158908; -. DR HOGENOM; CLU_000146_1_2_1; -. DR InParanoid; P11277; -. DR OMA; EPADMTS; -. DR OrthoDB; 5865767at2759; -. DR PAN-GO; P11277; 6 GO annotations based on evolutionary models. DR PhylomeDB; P11277; -. DR PathwayCommons; P11277; -. DR Reactome; R-HSA-375165; NCAM signaling for neurite out-growth. DR Reactome; R-HSA-445095; Interaction between L1 and Ankyrins. DR Reactome; R-HSA-5673001; RAF/MAP kinase cascade. DR Reactome; R-HSA-6807878; COPI-mediated anterograde transport. DR SignaLink; P11277; -. DR SIGNOR; P11277; -. DR Agora; ENSG00000070182; Agora Nominated Target for Alzheimer's Disease. DR BioGRID-ORCS; 6710; 16 hits in 1153 CRISPR screens. DR CD-CODE; FB4E32DD; Presynaptic clusters and postsynaptic densities. DR ChiTaRS; SPTB; human. DR EvolutionaryTrace; P11277; -. DR GeneWiki; SPTB; -. DR GenomeRNAi; 6710; -. DR Pharos; P11277; Tbio. DR PRO; PR:P11277; -. DR Proteomes; UP000005640; Chromosome 14. DR RNAct; P11277; protein. DR Bgee; ENSG00000070182; Expressed in gastrocnemius and 153 other cell types or tissues. DR ExpressionAtlas; P11277; baseline and differential. DR GO; GO:0015629; C:actin cytoskeleton; TAS:BHF-UCL. DR GO; GO:0030054; C:cell junction; IBA:GO_Central. DR GO; GO:0009986; C:cell surface; IDA:UniProtKB. DR GO; GO:0030864; C:cortical actin cytoskeleton; IBA:GO_Central. DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; TAS:BHF-UCL. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0098794; C:postsynapse; IEA:Ensembl. DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB. DR GO; GO:0008091; C:spectrin; IPI:ComplexPortal. DR GO; GO:0014731; C:spectrin-associated cytoskeleton; IDA:BHF-UCL. DR GO; GO:0003779; F:actin binding; TAS:ProtInc. DR GO; GO:0051015; F:actin filament binding; IDA:UniProtKB. DR GO; GO:0030506; F:ankyrin binding; IPI:BHF-UCL. DR GO; GO:0005200; F:structural constituent of cytoskeleton; IEA:InterPro. DR GO; GO:0030036; P:actin cytoskeleton organization; IBA:GO_Central. DR GO; GO:0098885; P:modification of postsynaptic actin cytoskeleton; IDA:SynGO. DR GO; GO:0008360; P:regulation of cell shape; NAS:ComplexPortal. DR CDD; cd21319; CH_SPTB_rpt2; 1. DR CDD; cd21317; CH_SPTBN2_rpt1; 1. DR CDD; cd00176; SPEC; 8. DR FunFam; 1.10.418.10:FF:000003; Spectrin beta chain; 1. DR FunFam; 1.10.418.10:FF:000004; Spectrin beta chain; 1. DR FunFam; 1.20.58.60:FF:000011; Spectrin beta chain; 1. DR FunFam; 1.20.58.60:FF:000018; Spectrin beta chain; 1. DR FunFam; 1.20.58.60:FF:000019; Spectrin beta chain; 1. DR FunFam; 1.20.58.60:FF:000028; Spectrin beta chain; 1. DR FunFam; 1.20.58.60:FF:000033; Spectrin beta chain; 1. DR FunFam; 1.20.58.60:FF:000049; Spectrin beta chain; 1. DR FunFam; 1.20.58.60:FF:000059; Spectrin beta chain; 1. DR FunFam; 1.20.58.60:FF:000083; Spectrin beta chain; 1. DR FunFam; 1.20.58.60:FF:000099; Spectrin beta chain; 1. DR FunFam; 1.20.58.60:FF:000214; Spectrin beta chain; 1. DR FunFam; 1.20.58.60:FF:000243; Spectrin beta chain; 1. DR FunFam; 1.20.58.60:FF:000252; Spectrin beta chain; 1. DR Gene3D; 1.20.58.60; -; 12. DR Gene3D; 1.10.418.10; Calponin-like domain; 2. DR InterPro; IPR001589; Actinin_actin-bd_CS. DR InterPro; IPR001715; CH_dom. DR InterPro; IPR036872; CH_dom_sf. DR InterPro; IPR018159; Spectrin/alpha-actinin. DR InterPro; IPR016343; Spectrin_bsu. DR InterPro; IPR002017; Spectrin_repeat. DR PANTHER; PTHR11915; SPECTRIN/FILAMIN RELATED CYTOSKELETAL PROTEIN; 1. DR Pfam; PF00307; CH; 2. DR Pfam; PF00435; Spectrin; 17. DR PIRSF; PIRSF002297; Spectrin_beta_subunit; 1. DR SMART; SM00033; CH; 2. DR SMART; SM00150; SPEC; 17. DR SUPFAM; SSF47576; Calponin-homology domain, CH-domain; 1. DR SUPFAM; SSF46966; Spectrin repeat; 13. DR PROSITE; PS00019; ACTININ_1; 1. DR PROSITE; PS00020; ACTININ_2; 1. DR PROSITE; PS50021; CH; 2. DR PDBsum; 1S35; -. DR PDBsum; 3EDU; -. DR PDBsum; 3F57; -. DR PDBsum; 3KBT; -. DR PDBsum; 3KBU; -. DR PDBsum; 3LBX; -. PE 1: Evidence at protein level; KW 3D-structure; Actin capping; Actin-binding; Alternative splicing; KW Cytoplasm; Cytoskeleton; Direct protein sequencing; Disease variant; KW Elliptocytosis; Hereditary hemolytic anemia; Phosphoprotein; KW Proteomics identification; Reference proteome; Repeat. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:12665801" FT CHAIN 2..2137 FT /note="Spectrin beta chain, erythrocytic" FT /id="PRO_0000073459" FT DOMAIN 54..158 FT /note="Calponin-homology (CH) 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044" FT DOMAIN 173..278 FT /note="Calponin-homology (CH) 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044" FT REPEAT 303..411 FT /note="Spectrin 1" FT /evidence="ECO:0000255" FT REPEAT 423..525 FT /note="Spectrin 2" FT /evidence="ECO:0000255" FT REPEAT 529..635 FT /note="Spectrin 3" FT /evidence="ECO:0000255" FT REPEAT 638..741 FT /note="Spectrin 4" FT /evidence="ECO:0000255" FT REPEAT 744..846 FT /note="Spectrin 5" FT /evidence="ECO:0000255" FT REPEAT 851..950 FT /note="Spectrin 6" FT /evidence="ECO:0000255" FT REPEAT 956..1058 FT /note="Spectrin 7" FT /evidence="ECO:0000255" FT REPEAT 1062..1165 FT /note="Spectrin 8" FT /evidence="ECO:0000255" FT REPEAT 1170..1257 FT /note="Spectrin 9" FT /evidence="ECO:0000255" FT REPEAT 1275..1375 FT /note="Spectrin 10" FT /evidence="ECO:0000255" FT REPEAT 1389..1465 FT /note="Spectrin 11" FT /evidence="ECO:0000255" FT REPEAT 1481..1582 FT /note="Spectrin 12" FT /evidence="ECO:0000255" FT REPEAT 1585..1688 FT /note="Spectrin 13" FT /evidence="ECO:0000255" FT REPEAT 1690..1793 FT /note="Spectrin 14" FT /evidence="ECO:0000255" FT REPEAT 1797..1899 FT /note="Spectrin 15" FT /evidence="ECO:0000255" FT REPEAT 1906..2006 FT /note="Spectrin 16" FT /evidence="ECO:0000255" FT REPEAT 2013..2075 FT /note="Spectrin 17" FT /evidence="ECO:0000255" FT REGION 1..30 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2..275 FT /note="Actin-binding" FT REGION 2074..2117 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1..15 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2075..2087 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT SITE 165..166 FT /note="(Microbial infection) Cleavage; by P.falciparum FT SERA6" FT /evidence="ECO:0000269|PubMed:29459732" FT SITE 167..168 FT /note="(Microbial infection) Cleavage; by P.falciparum FT SERA6" FT /evidence="ECO:0000269|PubMed:29459732" FT MOD_RES 36 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P15508" FT MOD_RES 104 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1297 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P15508" FT MOD_RES 2043 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 2073 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 2110 FT /note="Phosphothreonine" FT /evidence="ECO:0000269|PubMed:15065869" FT MOD_RES 2114 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:15065869" FT MOD_RES 2117 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:15065869" FT MOD_RES 2123 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:15065869, FT ECO:0007744|PubMed:23186163" FT MOD_RES 2125 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:15065869, FT ECO:0007744|PubMed:23186163" FT MOD_RES 2128 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:15065869" FT VAR_SEQ 2074..2137 FT /note="LELKERQIAERPAEETGPQEEEGETAGEAPVSHHAATERTSPVSLWSRLSSS FT WESLQPEPSHPY -> ASRGGRRDSRGGSSFPPCGHRENVPGQSLVSFV (in FT isoform 3)" FT /evidence="ECO:0000303|PubMed:2195026" FT /id="VSP_007242" FT VAR_SEQ 2116..2137 FT /note="VSLWSRLSSSWESLQPEPSHPY -> GEEEGTWPQNLQQPPPPGQHKDGQKS FT TGDERPTTEPLFKVLDTPLSEGDEPATLPAPRDHGQSVQMEGYLGRKHDLEGPNKKASN FT RSWNNLYCVLRNSELTFYKDAKNLALGMPYHGEEPLALRHAICEIAANYKKKKHVFKLR FT LSNGSEWLFHGKDEEEMLSWLQGVSTAINESQSIRVKAQSLPLPSLSGPDASLGKKDKE FT KRFSFFPKKK (in isoform 2)" FT /evidence="ECO:0000303|PubMed:2243099" FT /id="VSP_000719" FT VARIANT 202 FT /note="W -> R (in SPH2; spectrin Kissimmee; FT dbSNP:rs121918646)" FT /evidence="ECO:0000269|PubMed:8102379" FT /id="VAR_001352" FT VARIANT 439 FT /note="S -> N (in dbSNP:rs229587)" FT /evidence="ECO:0000269|PubMed:2195026" FT /id="VAR_001353" FT VARIANT 525 FT /note="E -> K (in dbSNP:rs55752508)" FT /id="VAR_061084" FT VARIANT 613 FT /note="S -> I (in dbSNP:rs3742601)" FT /id="VAR_038514" FT VARIANT 1151 FT /note="N -> D (in dbSNP:rs77806)" FT /evidence="ECO:0000269|PubMed:1976574, FT ECO:0000269|PubMed:2195026, ECO:0000269|PubMed:2243099" FT /id="VAR_001354" FT VARIANT 1374 FT /note="H -> R (in dbSNP:rs10132778)" FT /evidence="ECO:0000269|PubMed:3390609" FT /id="VAR_001355" FT VARIANT 1403 FT /note="R -> Q (in dbSNP:rs17180350)" FT /id="VAR_001356" FT VARIANT 1408 FT /note="G -> R (in dbSNP:rs17245552)" FT /id="VAR_038515" FT VARIANT 2018 FT /note="A -> G (in EL3; Cagliary; dbSNP:rs121918647)" FT /evidence="ECO:0000269|PubMed:8226774" FT /id="VAR_001357" FT VARIANT 2019 FT /note="S -> P (in EL3; Providence; dbSNP:rs121918648)" FT /evidence="ECO:0000269|PubMed:7883966" FT /id="VAR_001358" FT VARIANT 2023 FT /note="A -> V (in EL3; Paris; dbSNP:rs367841692)" FT /evidence="ECO:0000269|PubMed:8018926" FT /id="VAR_001359" FT VARIANT 2024 FT /note="W -> R (in EL3; Linguere; dbSNP:rs1225539653)" FT /evidence="ECO:0000269|PubMed:8018926" FT /id="VAR_001360" FT VARIANT 2025 FT /note="L -> R (in EL3; Buffalo; dbSNP:rs121918649)" FT /evidence="ECO:0000269|PubMed:9005995" FT /id="VAR_001361" FT VARIANT 2053 FT /note="A -> P (in EL3; Kayes; dbSNP:rs121918645)" FT /evidence="ECO:0000269|PubMed:1975598" FT /id="VAR_001362" FT CONFLICT 403 FT /note="E -> G (in Ref. 1; AAA60578/AAA60579)" FT /evidence="ECO:0000305" FT CONFLICT 612 FT /note="I -> M (in Ref. 1; AAA60578/AAA60579)" FT /evidence="ECO:0000305" FT CONFLICT 629..631 FT /note="RKA -> ART (in Ref. 1; AAA60578/AAA60579)" FT /evidence="ECO:0000305" FT CONFLICT 958..959 FT /note="NY -> TL (in Ref. 1; AAA60578/AAA60579)" FT /evidence="ECO:0000305" FT CONFLICT 1031 FT /note="D -> N (in Ref. 1; AAA60578/AAA60579)" FT /evidence="ECO:0000305" FT CONFLICT 1844..1845 FT /note="EL -> DV (in Ref. 1; AAA60578/AAA60579 and 3; FT AAA63259)" FT /evidence="ECO:0000305" FT HELIX 1065..1085 FT /evidence="ECO:0007829|PDB:1S35" FT HELIX 1093..1128 FT /evidence="ECO:0007829|PDB:1S35" FT HELIX 1134..1192 FT /evidence="ECO:0007829|PDB:1S35" FT HELIX 1195..1197 FT /evidence="ECO:0007829|PDB:1S35" FT HELIX 1200..1236 FT /evidence="ECO:0007829|PDB:1S35" FT HELIX 1242..1271 FT /evidence="ECO:0007829|PDB:1S35" FT HELIX 1586..1602 FT /evidence="ECO:0007829|PDB:3KBT" FT HELIX 1603..1607 FT /evidence="ECO:0007829|PDB:3KBT" FT HELIX 1616..1652 FT /evidence="ECO:0007829|PDB:3KBT" FT HELIX 1692..1713 FT /evidence="ECO:0007829|PDB:3EDU" FT HELIX 1722..1759 FT /evidence="ECO:0007829|PDB:3EDU" FT HELIX 1765..1818 FT /evidence="ECO:0007829|PDB:3EDU" FT HELIX 1821..1823 FT /evidence="ECO:0007829|PDB:3KBT" FT HELIX 1838..1863 FT /evidence="ECO:0007829|PDB:3EDU" FT HELIX 1868..1891 FT /evidence="ECO:0007829|PDB:3EDU" FT HELIX 1902..1928 FT /evidence="ECO:0007829|PDB:3LBX" FT STRAND 1936..1938 FT /evidence="ECO:0007829|PDB:3LBX" FT HELIX 1941..1971 FT /evidence="ECO:0007829|PDB:3LBX" FT HELIX 1977..2033 FT /evidence="ECO:0007829|PDB:3LBX" FT HELIX 2041..2060 FT /evidence="ECO:0007829|PDB:3LBX" FT HELIX 2062..2069 FT /evidence="ECO:0007829|PDB:3LBX" FT HELIX 2073..2082 FT /evidence="ECO:0007829|PDB:3LBX" SQ SEQUENCE 2137 AA; 246468 MW; 311AE5CD53237610 CRC64; MTSATEFENV GNQPPYSRIN ARWDAPDDEL DNDNSSARLF ERSRIKALAD EREVVQKKTF TKWVNSHLAR VSCRITDLYK DLRDGRMLIK LLEVLSGEML PKPTKGKMRI HCLENVDKAL QFLKEQRVHL ENMGSHDIVD GNHRLVLGLI WTIILRFQIQ DIVVQTQEGR ETRSAKDALL LWCQMKTAGY PHVNVTNFTS SWKDGLAFNA LIHKHRPDLI DFDKLKDSNA RHNLEHAFNV AERQLGIIPL LDPEDVFTEN PDEKSIITYV VAFYHYFSKM KVLAVEGKRV GKVIDHAIET EKMIEKYSGL ASDLLTWIEQ TITVLNSRKF ANSLTGVQQQ LQAFSTYRTV EKPPKFQEKG NLEVLLFTIQ SRMRANNQKV YTPHDGKLVS DINRAWESLE EAEYRRELAL RNELIRQEKL EQLARRFDRK AAMRETWLSE NQRLVAQDNF GYDLAAVEAA KKKHEAIETD TAAYEERVRA LEDLAQELEK ENYHDQKRIT ARKDNILRLW SYLQELLQSR RQRLETTLAL QKLFQDMLHS IDWMDEIKAH LLSAEFGKHL LEVEDLLQKH KLMEADIAIQ GDKVKAITAA TLKFTEGKGY QPCDPQVIQD RISHLEQCFE ELSNMAAGRK AQLEQSKRLW KFFWEMDEAE SWIKEKEQIY SSLDYGKDLT SVLILQRKHK AFEDELRGLD AHLEQIFQEA HGMVARKQFG HPQIEARIKE VSAQWDQLKD LAAFCKKNLQ DAENFFQFQG DADDLKAWLQ DAHRLLSGED VGQDEGATRA LGKKHKDFLE ELEESRGVME HLEQQAQGFP EEFRDSPDVT HRLQALRELY QQVVAQADLR QQRLQEALDL YTVFGETDAC ELWMGEKEKW LAEMEMPDTL EDLEVVQHRF DILDQEMKTL MTQIDGVNLA ANSLVESGHP RSREVKQYQD HLNTRWQAFQ TLVSERREAV DSALRVHNYC VDCEETSKWI TDKTKVVEST KDLGRDLAGI IAIQRKLSGL ERDVAAIQAR VDALERESQQ LMDSHPEQKE DIGQRQKHLE ELWQGLQQSL QGQEDLLGEV SQLQAFLQDL DDFQAWLSIT QKAVASEDMP ESLPEAEQLL QQHAGIKDEI DGHQDSYQRV KESGEKVIQG QTDPEYLLLG QRLEGLDTGW NALGRMWESR SHTLAQCLGF QEFQKDAKQA EAILSNQEYT LAHLEPPDSL EAAEAGIRKF EDFLGSMENN RDKVLSPVDS GNKLVAEGNL YSDKIKEKVQ LIEDRHRKNN EKAQEASVLL RDNLELQNFL QNCQELTLWI NDKLLTSQDV SYDEARNLHN KWLKHQAFVA ELASHEGWLE NIDAEGKQLM DEKPQFTALV SQKLEALHRL WDELQATTKE KTQHLSAARS SDLRLQTHAD LNKWISAMED QLRSDDPGKD LTSVNRMLAK LKRVEDQVNV RKEELGELFA QVPSMGEEGG DADLSIEKRF LDLLEPLGRR KKQLESSRAK LQISRDLEDE TLWVEERLPL AQSADYGTNL QTVQLFMKKN QTLQNEILGH TPRVEDVLQR GQQLVEAAEI DCQDLEERLG HLQSSWDRLR EAAAGRLQRL RDANEAQQYY LDADEAEAWI GEQELYVISD EIPKDEEGAI VMLKRHLRQQ RAVEDYGRNI KQLASRAQGL LSAGHPEGEQ IIRLQGQVDK HYAGLKDVAE ERKRKLENMY HLFQLKRETD DLEQWISEKE LVASSPEMGQ DFDHVTLLRD KFRDFARETG AIGQERVDNV NAFIERLIDA GHSEAATIAE WKDGLNEMWA DLLELIDTRM QLLAASYDLH RYFYTGAEIL GLIDEKHREL PEDVGLDAST AESFHRVHTA FERELHLLGV QVQQFQDVAT RLQTAYAGEK AEAIQNKEQE VSAAWQALLD ACAGRRTQLV DTADKFRFFS MARDLLSWME SIIRQIETQE RPRDVSSVEL LMKYHQGINA EIETRSKNFS ACLELGESLL QRQHQASEEI REKLQQVMSR RKEMNEKWEA RWERLRMLLE VCQFSRDASV AEAWLIAQEP YLASGDFGHT VDSVEKLIKR HEAFEKSTAS WAERFAALEK PTTLELKERQ IAERPAEETG PQEEEGETAG EAPVSHHAAT ERTSPVSLWS RLSSSWESLQ PEPSHPY //