SPTB2_MOUSE
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 03-AUG-2022, entry version 210.
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, Pancreas,
RC 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}.
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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; 49.
DR DIP; DIP-31558N; -.
DR IntAct; Q62261; 35.
DR MINT; Q62261; -.
DR STRING; 10090.ENSMUSP00000099902; -.
DR GlyGen; Q62261; 1 site.
DR iPTMnet; Q62261; -.
DR PhosphoSitePlus; Q62261; -.
DR SwissPalm; Q62261; -.
DR EPD; Q62261; -.
DR jPOST; Q62261; -.
DR MaxQB; Q62261; -.
DR PaxDb; Q62261; -.
DR PeptideAtlas; Q62261; -.
DR PRIDE; Q62261; -.
DR ProteomicsDB; 261642; -. [Q62261-1]
DR ProteomicsDB; 261643; -. [Q62261-2]
DR Antibodypedia; 2181; 196 antibodies from 34 providers.
DR DNASU; 20742; -.
DR Ensembl; ENSMUST00000006629; ENSMUSP00000006629; ENSMUSG00000020315. [Q62261-1]
DR Ensembl; ENSMUST00000011877; ENSMUSP00000011877; ENSMUSG00000020315. [Q62261-1]
DR Ensembl; ENSMUST00000102838; ENSMUSP00000099902; ENSMUSG00000020315. [Q62261-2]
DR GeneID; 20742; -.
DR KEGG; mmu:20742; -.
DR UCSC; uc007ihs.1; mouse. [Q62261-1]
DR UCSC; uc007iht.1; mouse. [Q62261-2]
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; FMLNREV; -.
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 72 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 263 other tissues.
DR ExpressionAtlas; Q62261; baseline and differential.
DR Genevisible; Q62261; MM.
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; IEA:Ensembl.
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:0014069; C:postsynaptic density; IDA: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: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:0007182; P:common-partner SMAD protein phosphorylation; IDA:MGI.
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; cd00014; CH; 2.
DR CDD; cd00176; SPEC; 8.
DR Gene3D; 1.10.418.10; -; 2.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR001589; Actinin_actin-bd_CS.
DR InterPro; IPR001715; CH-domain.
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 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; SSF47576; 1.
DR PROSITE; PS00019; ACTININ_1; 1.
DR PROSITE; PS00020; ACTININ_2; 1.
DR PROSITE; PS50021; CH; 2.
DR PROSITE; PS50003; PH_DOMAIN; 1.
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
