ID SPTB2_MOUSE Reviewed; 2363 AA. AC Q62261; A2AFU1; Q3TEM7; Q5SQL8; Q5SQL9; Q9QWJ7; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 16-MAY-2006, sequence version 2. DT 27-MAR-2024, entry version 219. DE RecName: Full=Spectrin beta chain, non-erythrocytic 1; DE AltName: Full=Beta-II spectrin; DE AltName: Full=Embryonic liver fodrin; DE AltName: Full=Fodrin beta chain; GN Name=Sptbn1; Synonyms=Elf, Spnb-2, Spnb2, Sptb2; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC STRAIN=BALB/cJ; RX PubMed=8479293; DOI=10.1016/0169-328x(93)90176-p; RA Ma Y., Zimmer W.E., Riederer B.M., Goodman S.R.; RT "The complete amino acid sequence for brain beta spectrin (beta fodrin): RT relationship to globin sequences."; RL Brain Res. Mol. Brain Res. 18:87-99(1993). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY, DEVELOPMENTAL RP STAGE, AND SUBCELLULAR LOCATION. RC STRAIN=C57BL/6J; TISSUE=Liver; RX PubMed=9927192; DOI=10.1038/sj.onc.1202313; RA Mishra L., Cai T., Yu P., Monga S.P., Mishra B.; RT "Elf3 encodes a novel 200-kD beta-spectrin: role in liver development."; RL Oncogene 18:353-364(1999). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S., RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., RA Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of the RT mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-399 (ISOFORM 2). RC STRAIN=C57BL/6J; TISSUE=Thymus; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [5] RP INTERACTION WITH CPNE4. RX PubMed=12522145; DOI=10.1074/jbc.m212632200; RA Tomsig J.L., Snyder S.L., Creutz C.E.; RT "Identification of targets for calcium signaling through the copine family RT of proteins. Characterization of a coiled-coil copine-binding motif."; RL J. Biol. Chem. 278:10048-10054(2003). RN [6] RP INTERACTION WITH ANK2, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION. RX PubMed=15262991; DOI=10.1074/jbc.m406018200; RA Mohler P.J., Yoon W., Bennett V.; RT "Ankyrin-B targets beta2-spectrin to an intracellular compartment in RT neonatal cardiomyocytes."; RL J. Biol. Chem. 279:40185-40193(2004). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2127 AND SER-2137, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic brain; RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200; RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.; RT "Phosphoproteomic analysis of the developing mouse brain."; RL Mol. Cell. Proteomics 3:1093-1101(2004). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2102 AND THR-2194, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain; RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200; RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.; RT "Comprehensive identification of phosphorylation sites in postsynaptic RT density preparations."; RL Mol. Cell. Proteomics 5:914-922(2006). RN [9] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT SER-2323. RC TISSUE=Brain; RX PubMed=16452088; DOI=10.1074/mcp.t500040-mcp200; RA Vosseller K., Trinidad J.C., Chalkley R.J., Specht C.G., Thalhammer A., RA Lynn A.J., Snedecor J.O., Guan S., Medzihradszky K.F., Maltby D.A., RA Schoepfer R., Burlingame A.L.; RT "O-linked N-acetylglucosamine proteomics of postsynaptic density RT preparations using lectin weak affinity chromatography and mass RT spectrometry."; RL Mol. Cell. Proteomics 5:923-934(2006). RN [10] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain cortex; RX PubMed=17114649; DOI=10.1074/mcp.m600046-mcp200; RA Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., RA Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., RA Panse C., Schlapbach R., Mansuy I.M.; RT "Qualitative and quantitative analyses of protein phosphorylation in naive RT and stimulated mouse synaptosomal preparations."; RL Mol. Cell. Proteomics 6:283-293(2007). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2137, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=17242355; DOI=10.1073/pnas.0609836104; RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; RT "Large-scale phosphorylation analysis of mouse liver."; RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1805, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain; RX PubMed=18034455; DOI=10.1021/pr0701254; RA Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.; RT "Large-scale identification and evolution indexing of tyrosine RT phosphorylation sites from murine brain."; RL J. Proteome Res. 7:311-318(2008). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2102, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=18630941; DOI=10.1021/pr800223m; RA Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.; RT "Specific phosphopeptide enrichment with immobilized titanium ion affinity RT chromatography adsorbent for phosphoproteome analysis."; RL J. Proteome Res. 7:3957-3967(2008). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2164 AND SER-2168, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic fibroblast; RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200; RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.; RT "Large scale localization of protein phosphorylation by use of electron RT capture dissociation mass spectrometry."; RL Mol. Cell. Proteomics 8:904-912(2009). RN [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36; SER-228; SER-817; RP SER-903; SER-1076; SER-1079; SER-2102; SER-2127; SER-2137; THR-2146; RP SER-2147; THR-2158; SER-2160; SER-2163; SER-2164; SER-2168; THR-2170; RP SER-2183; THR-2186; THR-2194 AND SER-2340, PHOSPHORYLATION [LARGE SCALE RP ANALYSIS] AT SER-14 (ISOFORM 2), AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, RC Pancreas, Spleen, and Testis; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and expression."; RL Cell 143:1174-1189(2010). RN [16] RP FUNCTION. RX PubMed=34211179; DOI=10.1038/s41588-021-00886-z; RG Undiagnosed Diseases Network; RG Genomics England Research Consortium; RA Cousin M.A., Creighton B.A., Breau K.A., Spillmann R.C., Torti E., RA Dontu S., Tripathi S., Ajit D., Edwards R.J., Afriyie S., Bay J.C., RA Harper K.M., Beltran A.A., Munoz L.J., Falcon Rodriguez L., RA Stankewich M.C., Person R.E., Si Y., Normand E.A., Blevins A., May A.S., RA Bier L., Aggarwal V., Mancini G.M.S., van Slegtenhorst M.A., Cremer K., RA Becker J., Engels H., Aretz S., MacKenzie J.J., Brilstra E., RA van Gassen K.L.I., van Jaarsveld R.H., Oegema R., Parsons G.M., Mark P., RA Helbig I., McKeown S.E., Stratton R., Cogne B., Isidor B., Cacheiro P., RA Smedley D., Firth H.V., Bierhals T., Kloth K., Weiss D., Fairley C., RA Shieh J.T., Kritzer A., Jayakar P., Kurtz-Nelson E., Bernier R.A., Wang T., RA Eichler E.E., van de Laar I.M.B.H., McConkie-Rosell A., McDonald M.T., RA Kemppainen J., Lanpher B.C., Schultz-Rogers L.E., Gunderson L.B., RA Pichurin P.N., Yoon G., Zech M., Jech R., Winkelmann J., Beltran A.S., RA Zimmermann M.T., Temple B., Moy S.S., Klee E.W., Tan Q.K., Lorenzo D.N.; RT "Pathogenic SPTBN1 variants cause an autosomal dominant neurodevelopmental RT syndrome."; RL Nat. Genet. 53:1006-1021(2021). RN [17] RP STRUCTURE BY NMR OF 2199-2304. RX PubMed=8208297; DOI=10.1038/369675a0; RA Macias M.J., Musacchio A., Ponstingl H., Nilges M., Saraste M., RA Oschkinat H.; RT "Structure of the pleckstrin homology domain from beta-spectrin."; RL Nature 369:675-677(1994). RN [18] RP STRUCTURE BY NMR OF 2199-2304. RX PubMed=9199409; DOI=10.1006/jmbi.1997.1044; RA Nilges M., Macias M.J., O'Donoghue S.I., Oschkinat H.; RT "Automated NOESY interpretation with ambiguous distance restraints: the RT refined NMR solution structure of the pleckstrin homology domain from beta- RT spectrin."; RL J. Mol. Biol. 269:408-422(1997). RN [19] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 2199-2304. RX PubMed=7588597; DOI=10.1002/j.1460-2075.1995.tb00149.x; RA Hyvoenen M., Macias M.J., Nilges M., Oschkinat H., Saraste M., Wilmanns M.; RT "Structure of the binding site for inositol phosphates in a PH domain."; RL EMBO J. 14:4676-4685(1995). CC -!- FUNCTION: Fodrin, which seems to be involved in secretion, interacts CC with calmodulin in a calcium-dependent manner and is thus candidate for CC the calcium-dependent movement of the cytoskeleton at the membrane. CC Plays a critical role in central nervous system development and CC function. {ECO:0000269|PubMed:34211179}. CC -!- SUBUNIT: Interacts with ANK2 (PubMed:15262991). Interacts with CPNE4 CC (via VWFA domain) (PubMed:12522145). Like erythrocyte spectrin, the CC spectrin-like proteins are capable to form dimers which can further CC associate to tetramers (By similarity). Interacts with CAMSAP1 (By CC similarity). Can form heterodimers with SPTAN1. CC {ECO:0000250|UniProtKB:P85986, ECO:0000250|UniProtKB:Q01082, CC ECO:0000269|PubMed:12522145, ECO:0000269|PubMed:15262991}. CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}. CC Endomembrane system {ECO:0000269|PubMed:15262991}. Cytoplasm, CC myofibril, sarcomere, M line {ECO:0000269|PubMed:15262991}. Cytoplasm, CC cytosol {ECO:0000250|UniProtKB:Q01082}. Cell membrane CC {ECO:0000250|UniProtKB:Q01082}. Note=Colocalizes with ANK2 in a CC distinct intracellular compartment of neonatal cardiomyocytes. CC {ECO:0000269|PubMed:15262991}. CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm CC {ECO:0000269|PubMed:9927192}. Cell membrane CC {ECO:0000269|PubMed:9927192}; Peripheral membrane protein; Cytoplasmic CC side. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q62261-1; Sequence=Displayed; CC Name=2; Synonyms=Elf3; CC IsoId=Q62261-2; Sequence=VSP_026057, VSP_026058, VSP_026059; CC -!- TISSUE SPECIFICITY: Isoform 2 is present in brain, heart, kidney and CC liver (at protein level). {ECO:0000269|PubMed:15262991, CC ECO:0000269|PubMed:9927192}. CC -!- DEVELOPMENTAL STAGE: Isoform 2 is expressed in brain, heart and liver CC throughout embryonic development. Isoform 1 is mainly expressed in CC neonatal developing ventricular cardiomyocytes. CC {ECO:0000269|PubMed:9927192}. 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; M74773; AAC42040.1; -; mRNA. DR EMBL; AF017112; AAD01616.1; -; mRNA. DR EMBL; AL672225; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL731792; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AK169544; BAE41221.1; -; mRNA. DR CCDS; CCDS24506.1; -. [Q62261-2] DR CCDS; CCDS36123.1; -. [Q62261-1] DR RefSeq; NP_033286.2; NM_009260.2. [Q62261-2] DR RefSeq; NP_787030.2; NM_175836.2. [Q62261-1] DR RefSeq; XP_006514662.1; XM_006514599.3. [Q62261-1] DR RefSeq; XP_006514663.1; XM_006514600.3. [Q62261-1] DR PDB; 1BTN; X-ray; 2.00 A; A=2199-2304. DR PDB; 1MPH; NMR; -; A=2199-2304. DR PDB; 6M3P; X-ray; 3.31 A; A/B=1591-1910. DR PDBsum; 1BTN; -. DR PDBsum; 1MPH; -. DR PDBsum; 6M3P; -. DR AlphaFoldDB; Q62261; -. DR SMR; Q62261; -. DR BioGRID; 203461; 56. DR DIP; DIP-31558N; -. DR IntAct; Q62261; 35. DR MINT; Q62261; -. DR STRING; 10090.ENSMUSP00000006629; -. DR GlyCosmos; Q62261; 1 site, No reported glycans. DR GlyGen; Q62261; 10 sites, 1 O-linked glycan (10 sites). DR iPTMnet; Q62261; -. DR MetOSite; Q62261; -. DR PhosphoSitePlus; Q62261; -. DR SwissPalm; Q62261; -. DR EPD; Q62261; -. DR jPOST; Q62261; -. DR MaxQB; Q62261; -. DR PaxDb; 10090-ENSMUSP00000099902; -. DR PeptideAtlas; Q62261; -. DR ProteomicsDB; 261642; -. [Q62261-1] DR ProteomicsDB; 261643; -. [Q62261-2] DR Pumba; Q62261; -. DR Antibodypedia; 2181; 216 antibodies from 34 providers. DR DNASU; 20742; -. DR Ensembl; ENSMUST00000006629.14; ENSMUSP00000006629.8; ENSMUSG00000020315.19. [Q62261-1] DR Ensembl; ENSMUST00000011877.13; ENSMUSP00000011877.7; ENSMUSG00000020315.19. [Q62261-1] DR Ensembl; ENSMUST00000102838.10; ENSMUSP00000099902.4; ENSMUSG00000020315.19. [Q62261-2] DR GeneID; 20742; -. DR KEGG; mmu:20742; -. DR UCSC; uc007ihs.1; mouse. [Q62261-1] DR UCSC; uc007iht.1; mouse. [Q62261-2] DR AGR; MGI:98388; -. DR CTD; 6711; -. DR MGI; MGI:98388; Sptbn1. DR VEuPathDB; HostDB:ENSMUSG00000020315; -. DR eggNOG; KOG0517; Eukaryota. DR GeneTree; ENSGT00940000154864; -. DR HOGENOM; CLU_000146_0_0_1; -. DR InParanoid; Q62261; -. DR OMA; EGEGMIA; -. DR OrthoDB; 2872403at2759; -. DR PhylomeDB; Q62261; -. DR TreeFam; TF313446; -. DR Reactome; R-MMU-375165; NCAM signaling for neurite out-growth. DR Reactome; R-MMU-445095; Interaction between L1 and Ankyrins. DR Reactome; R-MMU-5673001; RAF/MAP kinase cascade. DR Reactome; R-MMU-6807878; COPI-mediated anterograde transport. DR Reactome; R-MMU-9013420; RHOU GTPase cycle. DR Reactome; R-MMU-9013424; RHOV GTPase cycle. DR BioGRID-ORCS; 20742; 1 hit in 77 CRISPR screens. DR ChiTaRS; Sptbn1; mouse. DR EvolutionaryTrace; Q62261; -. DR PRO; PR:Q62261; -. DR Proteomes; UP000000589; Chromosome 11. DR RNAct; Q62261; Protein. DR Bgee; ENSMUSG00000020315; Expressed in right lung and 267 other cell types or tissues. DR ExpressionAtlas; Q62261; baseline and differential. DR GO; GO:0030673; C:axolemma; IDA: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:0030864; C:cortical actin cytoskeleton; IBA:GO_Central. DR GO; GO:0030863; C:cortical cytoskeleton; IDA:MGI. DR GO; GO:0032437; C:cuticular plate; IDA:MGI. DR GO; GO:0005737; C:cytoplasm; ISO:MGI. DR GO; GO:0005829; C:cytosol; ISS:UniProtKB. DR GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell. DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI. DR GO; GO:0031430; C:M band; IDA:BHF-UCL. DR GO; GO:0016020; C:membrane; IDA:MGI. DR GO; GO:0005730; C:nucleolus; ISO:MGI. DR GO; GO:0005634; C:nucleus; IDA:MGI. DR GO; GO:0005886; C:plasma membrane; IDA:MGI. DR GO; GO:0098794; C:postsynapse; ISO:MGI. DR GO; GO:0014069; C:postsynaptic density; IDA:MGI. DR GO; GO:0032991; C:protein-containing complex; ISO:MGI. DR GO; GO:0008091; C:spectrin; IEA:InterPro. DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central. DR GO; GO:0030506; F:ankyrin binding; ISO:MGI. DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW. DR GO; GO:0051020; F:GTPase binding; ISO:MGI. DR GO; GO:0005543; F:phospholipid binding; IEA:InterPro. DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI. DR GO; GO:0005200; F:structural constituent of cytoskeleton; ISS:UniProtKB. DR GO; GO:0030036; P:actin cytoskeleton organization; ISS:UniProtKB. DR GO; GO:0051693; P:actin filament capping; IEA:UniProtKB-KW. DR GO; GO:0007417; P:central nervous system development; IMP:UniProtKB. DR GO; GO:0021556; P:central nervous system formation; IMP:UniProtKB. DR GO; GO:0043001; P:Golgi to plasma membrane protein transport; ISO:MGI. DR GO; GO:0071709; P:membrane assembly; ISO:MGI. DR GO; GO:0000281; P:mitotic cytokinesis; ISO:MGI. DR GO; GO:0007009; P:plasma membrane organization; ISO:MGI. DR GO; GO:0032743; P:positive regulation of interleukin-2 production; ISO:MGI. DR GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; ISO:MGI. DR GO; GO:0072659; P:protein localization to plasma membrane; IMP:BHF-UCL. DR GO; GO:1903076; P:regulation of protein localization to plasma membrane; ISO:MGI. DR GO; GO:0060390; P:regulation of SMAD protein signal transduction; IDA:MGI. DR CDD; cd21248; CH_SPTB_like_rpt2; 1. DR CDD; cd21316; CH_SPTBN1_rpt1; 1. DR CDD; cd10571; PH_beta_spectrin; 1. DR CDD; cd00176; SPEC; 8. DR Gene3D; 1.20.58.60; -; 12. DR Gene3D; 1.10.418.10; Calponin-like domain; 2. DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1. DR InterPro; IPR001589; Actinin_actin-bd_CS. DR InterPro; IPR001715; CH_dom. DR InterPro; IPR036872; CH_dom_sf. DR InterPro; IPR011993; PH-like_dom_sf. DR InterPro; IPR041681; PH_9. DR InterPro; IPR001605; PH_dom-spectrin-type. DR InterPro; IPR001849; PH_domain. DR InterPro; IPR018159; Spectrin/alpha-actinin. DR InterPro; IPR016343; Spectrin_bsu. DR InterPro; IPR002017; Spectrin_repeat. DR PANTHER; PTHR11915:SF226; SPECTRIN BETA CHAIN, NON-ERYTHROCYTIC 1; 1. DR PANTHER; PTHR11915; SPECTRIN/FILAMIN RELATED CYTOSKELETAL PROTEIN; 1. DR Pfam; PF00307; CH; 2. DR Pfam; PF15410; PH_9; 1. DR Pfam; PF00435; Spectrin; 17. DR PIRSF; PIRSF002297; Spectrin_beta_subunit; 1. DR PRINTS; PR00683; SPECTRINPH. DR SMART; SM00033; CH; 2. DR SMART; SM00233; PH; 1. DR SMART; SM00150; SPEC; 17. DR SUPFAM; SSF47576; Calponin-homology domain, CH-domain; 1. DR SUPFAM; SSF50729; PH domain-like; 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 PROSITE; PS50003; PH_DOMAIN; 1. DR Genevisible; Q62261; MM. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Actin capping; Actin-binding; KW Alternative splicing; Calmodulin-binding; Cell membrane; Cytoplasm; KW Cytoskeleton; Glycoprotein; Membrane; Phosphoprotein; Reference proteome; KW Repeat. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250|UniProtKB:Q01082" FT CHAIN 2..2363 FT /note="Spectrin beta chain, non-erythrocytic 1" FT /id="PRO_0000073462" 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 530..636 FT /note="Spectrin 3" FT /evidence="ECO:0000255" FT REPEAT 639..742 FT /note="Spectrin 4" FT /evidence="ECO:0000255" FT REPEAT 745..847 FT /note="Spectrin 5" FT /evidence="ECO:0000255" FT REPEAT 850..952 FT /note="Spectrin 6" FT /evidence="ECO:0000255" FT REPEAT 957..1060 FT /note="Spectrin 7" FT /evidence="ECO:0000255" FT REPEAT 1063..1166 FT /note="Spectrin 8" FT /evidence="ECO:0000255" FT REPEAT 1170..1259 FT /note="Spectrin 9" FT /evidence="ECO:0000255" FT REPEAT 1276..1376 FT /note="Spectrin 10" FT /evidence="ECO:0000255" FT REPEAT 1381..1482 FT /note="Spectrin 11" FT /evidence="ECO:0000255" FT REPEAT 1486..1590 FT /note="Spectrin 12" FT /evidence="ECO:0000255" FT REPEAT 1592..1696 FT /note="Spectrin 13" FT /evidence="ECO:0000255" FT REPEAT 1698..1801 FT /note="Spectrin 14" FT /evidence="ECO:0000255" FT REPEAT 1805..1907 FT /note="Spectrin 15" FT /evidence="ECO:0000255" FT REPEAT 1914..2014 FT /note="Spectrin 16" FT /evidence="ECO:0000255" FT REPEAT 2018..2097 FT /note="Spectrin 17" FT /evidence="ECO:0000255" FT DOMAIN 2196..2306 FT /note="PH" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145" FT REGION 2..275 FT /note="Actin-binding" FT REGION 1563..2093 FT /note="Interaction with ANK2" FT /evidence="ECO:0000250" FT REGION 2089..2193 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2148..2176 FT /note="Mediates interaction with CAMSAP1" FT /evidence="ECO:0000250" FT REGION 2308..2363 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2089..2105 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2108..2167 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2308..2339 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2340..2356 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 2 FT /note="N-acetylthreonine" FT /evidence="ECO:0000250|UniProtKB:Q01082" FT MOD_RES 36 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 90 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q01082" FT MOD_RES 228 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 817 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 903 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 1057 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q01082" FT MOD_RES 1076 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 1079 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 1237 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q01082" FT MOD_RES 1388 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q01082" FT MOD_RES 1447 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q01082" FT MOD_RES 1557 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q01082" FT MOD_RES 1805 FT /note="Phosphotyrosine" FT /evidence="ECO:0007744|PubMed:18034455" FT MOD_RES 1815 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q01082" FT MOD_RES 1913 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q01082" FT MOD_RES 1989 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q01082" FT MOD_RES 2102 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:16452087, FT ECO:0007744|PubMed:18630941, ECO:0007744|PubMed:21183079" FT MOD_RES 2127 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:15345747, FT ECO:0007744|PubMed:21183079" FT MOD_RES 2137 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:15345747, FT ECO:0007744|PubMed:17242355, ECO:0007744|PubMed:21183079" FT MOD_RES 2146 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 2147 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 2158 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 2159 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q01082" FT MOD_RES 2160 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 2163 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 2164 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19131326, FT ECO:0007744|PubMed:21183079" FT MOD_RES 2168 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19131326, FT ECO:0007744|PubMed:21183079" FT MOD_RES 2170 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 2183 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 2186 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 2194 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:16452087, FT ECO:0007744|PubMed:21183079" FT MOD_RES 2313 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q01082" FT MOD_RES 2318 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q01082" FT MOD_RES 2319 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q01082" FT MOD_RES 2327 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q01082" FT MOD_RES 2339 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q01082" FT MOD_RES 2340 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT CARBOHYD 2323 FT /note="O-linked (GlcNAc) serine" FT /evidence="ECO:0000269|PubMed:16452088" FT VAR_SEQ 1..49 FT /note="MTTTVATDYDNIEIQQQYSDVNNRWDVDDWDNENSSARLFERSRIKALA -> FT MELQRTSSISGPLSPAYTGQVPYNYNQLEGRFKQLQ (in isoform 2)" FT /evidence="ECO:0000303|PubMed:16141072, FT ECO:0000303|PubMed:9927192" FT /id="VSP_026057" FT VAR_SEQ 2140..2246 FT /note="MAGTMETSEMVNGAAEQRTSSKESSPVPSPTLDRKAKSALPAQSAATLPART FT LETPAAQMEGFLNRKHEWEAHNKKASSRSWHNVYCVINNQEMGFYKDAKSAASGI -> FT VSYRSQTYQNYKNFNSRRTASDHSWSGM (in isoform 2)" FT /evidence="ECO:0000303|PubMed:16141072, FT ECO:0000303|PubMed:9927192" FT /id="VSP_026058" FT VAR_SEQ 2247..2363 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:16141072, FT ECO:0000303|PubMed:9927192" FT /id="VSP_026059" FT CONFLICT 252 FT /note="D -> A (in Ref. 4; BAE41221)" FT /evidence="ECO:0000305" FT CONFLICT 309 FT /note="S -> T (in Ref. 2; AAD01616)" FT /evidence="ECO:0000305" FT CONFLICT 368 FT /note="T -> A (in Ref. 2; AAD01616)" FT /evidence="ECO:0000305" FT CONFLICT 737 FT /note="K -> I (in Ref. 1; AAC42040)" FT /evidence="ECO:0000305" FT CONFLICT 796 FT /note="Y -> C (in Ref. 2; AAD01616)" FT /evidence="ECO:0000305" FT CONFLICT 846 FT /note="Q -> R (in Ref. 1; AAC42040)" FT /evidence="ECO:0000305" FT CONFLICT 970 FT /note="W -> C (in Ref. 2; AAD01616)" FT /evidence="ECO:0000305" FT CONFLICT 996 FT /note="R -> C (in Ref. 2; AAD01616)" FT /evidence="ECO:0000305" FT CONFLICT 1401..1403 FT /note="SQI -> KPGF (in Ref. 1; AAC42040)" FT /evidence="ECO:0000305" FT CONFLICT 1414..1455 FT /note="SVNILLKKQQMLENQMEVRKKEIEELQSQAQALSQEGKSTDE -> QSQYSS FT EKGNRRRRIRWKFGRKRSRNCRPSPGSSRGRAQMR (in Ref. 1; AAC42040)" FT /evidence="ECO:0000305" FT CONFLICT 1508 FT /note="A -> R (in Ref. 1; AAC42040)" FT /evidence="ECO:0000305" FT CONFLICT 1619..1624 FT /note="EKAKDE -> KRPRMK (in Ref. 1; AAC42040)" FT /evidence="ECO:0000305" FT CONFLICT 1898 FT /note="D -> G (in Ref. 1; AAC42040)" FT /evidence="ECO:0000305" FT CONFLICT 2171 FT /note="L -> S (in Ref. 1; AAC42040)" FT /evidence="ECO:0000305" FT CONFLICT 2345..2346 FT /note="EK -> AE (in Ref. 1; AAC42040)" FT /evidence="ECO:0000305" FT CONFLICT 2356..2358 FT /note="FSL -> STV (in Ref. 1; AAC42040)" FT /evidence="ECO:0000305" FT HELIX 1602..1615 FT /evidence="ECO:0007829|PDB:6M3P" FT HELIX 1624..1656 FT /evidence="ECO:0007829|PDB:6M3P" FT TURN 1658..1661 FT /evidence="ECO:0007829|PDB:6M3P" FT HELIX 1666..1722 FT /evidence="ECO:0007829|PDB:6M3P" FT HELIX 1730..1768 FT /evidence="ECO:0007829|PDB:6M3P" FT TURN 1771..1774 FT /evidence="ECO:0007829|PDB:6M3P" FT HELIX 1775..1827 FT /evidence="ECO:0007829|PDB:6M3P" FT TURN 1828..1830 FT /evidence="ECO:0007829|PDB:6M3P" FT HELIX 1838..1847 FT /evidence="ECO:0007829|PDB:6M3P" FT HELIX 1849..1873 FT /evidence="ECO:0007829|PDB:6M3P" FT HELIX 1877..1901 FT /evidence="ECO:0007829|PDB:6M3P" FT STRAND 2200..2209 FT /evidence="ECO:0007829|PDB:1BTN" FT STRAND 2211..2213 FT /evidence="ECO:0007829|PDB:1MPH" FT STRAND 2222..2229 FT /evidence="ECO:0007829|PDB:1BTN" FT STRAND 2232..2238 FT /evidence="ECO:0007829|PDB:1BTN" FT HELIX 2239..2244 FT /evidence="ECO:0007829|PDB:1BTN" FT STRAND 2248..2250 FT /evidence="ECO:0007829|PDB:1BTN" FT STRAND 2253..2255 FT /evidence="ECO:0007829|PDB:1MPH" FT STRAND 2260..2263 FT /evidence="ECO:0007829|PDB:1BTN" FT STRAND 2269..2277 FT /evidence="ECO:0007829|PDB:1BTN" FT STRAND 2283..2287 FT /evidence="ECO:0007829|PDB:1BTN" FT HELIX 2291..2303 FT /evidence="ECO:0007829|PDB:1BTN" FT MOD_RES Q62261-2:14 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" SQ SEQUENCE 2363 AA; 274223 MW; 221362054E64BB8C CRC64; MTTTVATDYD NIEIQQQYSD VNNRWDVDDW DNENSSARLF ERSRIKALAD EREAVQKKTF TKWVNSHLAR VSCRITDLYT DLRDGRMLIK LLEVLSGERL PKPTKGRMRI HCLENVDKAL QFLKEQRVHL ENMGSHDIVD GNHRLTLGLI WTIILRFQIQ DISVETEDNK EKKSAKDALL LWCQMKTAGY PNVNIHNFTT SWRDGMAFNA LIHKHRPDLI DFDKLKKSNA HYNLQNAFNL AEQHLGLTKL LDPEDISVDH PDEKSIITYV VTYYHYFSKM KALAVEGKRI GKVLDNAIET EKMIEKYESL ASDLLEWIEQ TIIILNNRKF ANSLVGVQQQ LQAFNTYRTV EKPPKFTEKG NLEVLLFTIQ SKMRANNQKV YMPREGKLIS DINKAWERLE KAEHERELAL RNELIRQEKL EQLARRFDRK AAMRETWLSE NQRLVSQDNF GFDLPAVEAA TKKHEAIETD IAAYEERVQA VVAVARELEA ENYHDIKRIT ARKDNVIRLW EYLLELLRAR RQRLEMNLGL QKIFQEMLYI MDWMDEMKVL LLSQDYGKHL LGVEDLLQKH ALVEADIAIQ AERVRGVNAS AQKFATDGEG YKPCDPQVIR DRVAHMEFCY QELCQLAAER RARLEESRRL WKFFWEMAEE EGWIREKEKI LSSDDYGKDL TSVMRLLSKH RAFEDEMSGR SGHFEQAIKE GEDMIAEEHF GSEKIRERII YIREQWANLE QLSAIRKKRL EEASLLHQFQ ADADDIDAWM LDILKIVSSN DVGHDEYSTQ SLVKKHKDVA EEITNYRPTI DTLHEQASAL PQAHAESPDV KGRLAGIEER CKEMAELTRL RKQALQDTLA LYKMFSEADA CELWIDEKEQ WLNNMQIPEK LEDLEVIQHR FESLEPEMNN QASRVAVVNQ IARQLMHNGH PSEKEIRAQQ DKLNTRWSQF RELVDRKKDA LLSALSIQNY HLECNETKSW IREKTKVIES TQDLGNDLAG VMALQRKLTG MERDLVAIEA KLSDLQKEAE KLESEHPDQA QAILSRLAEI SDVWEEMKTT LKNREASLGE ASKLQQFLRD LDDFQSWLSR TQTAIASEDM PNTLTEAEKL LTQHENIKNE IDNYEEDYQK MRDMGEMVTQ GQTDAQYMFL RQRLQALDTG WNELHKMWEN RQNLLSQSHA YQQFLRDTKQ AEAFLNNQEY VLAHTEMPTT LEGAEAAIKK QEDFMTTMDA NEEKINAVVE TGRRLVSDGN INSDRIQEKV DSIDDRHRKN REAASELLMR LKDNRDLQKF LQDCQELSLW INEKMLTAQD MSYDEARNLH SKWLKHQAFM AELASNKEWL DKIEKEGMQL ISEKPETEAV VKEKLTGLHK MWEVLESTTQ TKAQRLFDAN KAELFTQSCA DLDKWLHGLE SQIQSDDYGK DLTSVNILLK KQQMLENQME VRKKEIEELQ SQAQALSQEG KSTDEVDSKR LTVQTKFMEL LEPLSERKHN LLASKEIHQF NRDVEDEILW VGERMPLATS TDHGHNLQTV QLLIKKNQTL QKEIQGHQPR IDDIFERSQN IITDSSSLNA EAIRQRLADL KQLWGLLIEE TEKRHRRLEE AHKAQQYYFD AAEAEAWMSE QELYMMSEEK AKDEQSAVSM LKKHQILEQA VEDYAETVHQ LSKTSRALVA DSHPESERIS MRQSKVDKLY AGLKDLAEER RGKLDERHRL FQLNREVDDL EQWIAEREVV AGSHELGQDY EHVTMLQERF REFARDTGNI GQERVDTVNN MADELINSGH SDAATIAEWK DGLNEAWADL LELIDTRTQI LAASYELHKF YHDAKEIFGR IQDKHKKLPE ELGRDQNTVE TLQRMHTTFE HDIQALGTQV RQLQEDAARL QAAYAGDKAD DIQKRENEVL EAWKSLLDAC EGRRVRLVDT GDKFRFFSMV RDLMLWMEDV IRQIEAQEKP RDVSSVELLM NNHQGIKAEI DARNDSFTAC IELGKSLLAR KHYASEEIKE KLLQLTEKRK EMIDKWEDRW EWLRLILEVH QFSRDASVAE AWLLGQEPYL SSREIGQSVD EVEKLIKRHE AFEKSAATWD ERFSALERLT TLELLEVRRQ QEEEERKRRP PSPDPNTKVS EEAESQQWDT SKGDQVSQNG LPAEQGSPRM AGTMETSEMV NGAAEQRTSS KESSPVPSPT LDRKAKSALP AQSAATLPAR TLETPAAQME GFLNRKHEWE AHNKKASSRS WHNVYCVINN QEMGFYKDAK SAASGIPYHS EVPVSLKEAI CEVALDYKKK KHVFKLRLSD GNEYLFQAKD DEEMNTWIQA ISSAISSDKH DTSASTQSTP ASSRAQTLPT SVVTITSESS PGKREKDKEK DKEKRFSLFG KKK //