SPTB1_HUMAN
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 03-AUG-2022, entry version 220.
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;
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 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 [13]
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 [14]
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 [15]
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 [16]
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 [17]
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 [18]
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 [19]
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 [20]
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 [21]
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 [22]
RP VARIANTS EL3 VAL-2023 AND ARG-2024.
RX PubMed=8018926;
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 [23]
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).
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.
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=4; 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}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC 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}.
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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_000338.3; NM_000347.5.
DR RefSeq; NP_001020029.1; NM_001024858.2. [P11277-2]
DR RefSeq; XP_005268080.1; XM_005268023.4.
DR RefSeq; XP_016877101.1; XM_017021612.1. [P11277-2]
DR RefSeq; XP_016877103.1; XM_017021614.1.
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 PDBsum; 1S35; -.
DR PDBsum; 3EDU; -.
DR PDBsum; 3F57; -.
DR PDBsum; 3KBT; -.
DR PDBsum; 3KBU; -.
DR PDBsum; 3LBX; -.
DR AlphaFoldDB; P11277; -.
DR SMR; P11277; -.
DR BioGRID; 112588; 89.
DR DIP; DIP-1021N; -.
DR IntAct; P11277; 24.
DR STRING; 9606.ENSP00000451752; -.
DR CarbonylDB; P11277; -.
DR GlyConnect; 2860; 1 O-Linked glycan (5 sites).
DR GlyGen; P11277; 5 sites, 1 O-linked glycan (5 sites).
DR iPTMnet; P11277; -.
DR MetOSite; P11277; -.
DR PhosphoSitePlus; P11277; -.
DR BioMuta; SPTB; -.
DR DMDM; 215274269; -.
DR SWISS-2DPAGE; P11277; -.
DR EPD; P11277; -.
DR jPOST; P11277; -.
DR MassIVE; P11277; -.
DR MaxQB; P11277; -.
DR PaxDb; P11277; -.
DR PeptideAtlas; P11277; -.
DR PRIDE; P11277; -.
DR ProteomicsDB; 52731; -. [P11277-1]
DR ProteomicsDB; 52732; -. [P11277-2]
DR ProteomicsDB; 52733; -. [P11277-3]
DR ABCD; P11277; 1 sequenced antibody.
DR Antibodypedia; 183; 111 antibodies from 22 providers.
DR DNASU; 6710; -.
DR Ensembl; ENST00000389720.4; ENSP00000374370.4; ENSG00000070182.21. [P11277-1]
DR Ensembl; ENST00000389722.7; ENSP00000374372.3; ENSG00000070182.21. [P11277-2]
DR Ensembl; ENST00000644917.1; ENSP00000495909.1; ENSG00000070182.21. [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 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 neXtProt; NX_P11277; -.
DR OpenTargets; ENSG00000070182; -.
DR Orphanet; 288; Hereditary elliptocytosis.
DR Orphanet; 822; Hereditary spherocytosis.
DR PharmGKB; PA36103; -.
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; 543832at2759; -.
DR PhylomeDB; P11277; -.
DR TreeFam; TF313446; -.
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 BioGRID-ORCS; 6710; 16 hits in 1077 CRISPR screens.
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 152 other tissues.
DR ExpressionAtlas; P11277; baseline and differential.
DR Genevisible; P11277; HS.
DR GO; GO:0015629; C:actin cytoskeleton; TAS:BHF-UCL.
DR GO; GO:0030054; C:cell junction; IBA:GO_Central.
DR GO; GO:0042995; C:cell projection; 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:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0031235; C:intrinsic component of the cytoplasmic side of the plasma membrane; TAS:BHF-UCL.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0008091; C:spectrin; TAS:ProtInc.
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:0051693; P:actin filament capping; IEA:UniProtKB-KW.
DR CDD; cd00014; CH; 2.
DR CDD; cd00176; SPEC; 8.
DR Gene3D; 1.10.418.10; -; 2.
DR InterPro; IPR001589; Actinin_actin-bd_CS.
DR InterPro; IPR001715; CH-domain.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR018159; Spectrin/alpha-actinin.
DR InterPro; IPR016343; Spectrin_bsu.
DR InterPro; IPR002017; Spectrin_repeat.
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; SSF47576; 1.
DR PROSITE; PS00019; ACTININ_1; 1.
DR PROSITE; PS00020; ACTININ_2; 1.
DR PROSITE; PS50021; CH; 2.
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 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..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2074..2091
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 /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 1200..1236
FT /evidence="ECO:0007829|PDB:1S35"
FT HELIX 1242..1271
FT /evidence="ECO:0007829|PDB:1S35"
FT HELIX 1586..1605
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 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
