SPTB2_HUMAN
ID SPTB2_HUMAN Reviewed; 2364 AA.
AC Q01082; B2RP63; O60837; Q16057; Q53R99; Q59ER3; Q8IX99;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 223.
DE RecName: Full=Spectrin beta chain, non-erythrocytic 1;
DE AltName: Full=Beta-II spectrin;
DE AltName: Full=Fodrin beta chain;
DE AltName: Full=Spectrin, non-erythroid beta chain 1;
GN Name=SPTBN1; Synonyms=SPTB2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG), AND VARIANT HIS-1411.
RC TISSUE=Brain;
RX PubMed=1527002; DOI=10.1016/s0021-9258(19)37020-6;
RA Hu R.J., Watanabe M., Bennett V.;
RT "Characterization of human brain cDNA encoding the general isoform of beta-
RT spectrin.";
RL J. Biol. Chem. 267:18715-18722(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY, AND VARIANT
RP HIS-1411.
RX PubMed=11665863; DOI=10.1385/jmn:17:1:59;
RA Chen Y., Yu P., Lu D., Tagle D.A., Cai T.;
RT "A novel isoform of beta-spectrin II localizes to cerebellar Purkinje-cell
RT bodies and interacts with neurofibromatosis type 2 gene product
RT schwannomin.";
RL J. Mol. Neurosci. 17:59-70(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
RC TISSUE=Brain;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno R.F.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 293-1544.
RX PubMed=8406479; DOI=10.1006/geno.1993.1323;
RA Chang J.G., Scarpa A., Eddy R.L., Byers M.G., Harris A.S., Morrow J.S.,
RA Watkins P., Shows T.B., Forget B.G.;
RT "Cloning of a portion of the chromosomal gene and cDNA for human beta-
RT fodrin, the nonerythroid form of beta-spectrin.";
RL Genomics 17:287-293(1993).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 2087-2168 (ISOFORM SHORT).
RC TISSUE=Skeletal muscle;
RX PubMed=10806113; DOI=10.1242/jcs.113.11.2023;
RA Hayes N.V.L., Scott C., Heerkens E., Ohanian V., Maggs A.M., Pinder J.C.,
RA Kordeli E., Baines A.J.;
RT "Identification of a novel C-terminal variant of betaII spectrin: two
RT isoforms of betaII spectrin have distinct intracellular locations and
RT activities.";
RL J. Cell Sci. 113:2023-2034(2000).
RN [9]
RP INTERACTION WITH ANK2.
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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2102 AND SER-2138, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2102, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17924679; DOI=10.1021/pr070152u;
RA Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
RT "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells
RT and high confident phosphopeptide identification by cross-validation of
RT MS/MS and MS/MS/MS spectra.";
RL J. Proteome Res. 6:4150-4162(2007).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2102, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2138, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2102; SER-2138; SER-2165;
RP SER-2169; THR-2187; THR-2320; THR-2328 AND SER-2341, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT SER-14 (ISOFORM 2), AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2102, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1447; SER-2138; SER-2169 AND
RP SER-2341, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14 (ISOFORM 2), AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [18]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-90; LYS-1815; LYS-1913 AND
RP LYS-1989, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-817; SER-825; SER-1057;
RP SER-2102; SER-2138; SER-2169; THR-2320 AND SER-2341, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [20]
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 [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2102; SER-2128; SER-2138;
RP SER-2160; SER-2161; SER-2164; SER-2169; SER-2319; THR-2320 AND SER-2340,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [22]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [23]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [24]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2102; SER-2128; SER-2138;
RP SER-2164; SER-2165; SER-2169; THR-2187; THR-2328 AND SER-2341, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and 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 [25]
RP INTERACTION WITH CAMSAP1.
RX PubMed=24117850; DOI=10.1111/jnc.12462;
RA King M.D., Phillips G.W., Bignone P.A., Hayes N.V., Pinder J.C.,
RA Baines A.J.;
RT "A conserved sequence in CAMSAP1 (calmodulin regulated spectrin-associated
RT protein 1) links its interaction with spectrin and calmodulin to neurite
RT outgrowth.";
RL J. Neurochem. 128:391-402(2014).
RN [26]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1237; SER-1388; SER-1557;
RP SER-2102; SER-2165; SER-2169; SER-2172; SER-2314 AND THR-2320, AND
RP IDENTIFICATION BY 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 [27]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [28]
RP INVOLVEMENT IN DDISBA, VARIANTS DDISBA ILE-59; 183-CYS--LYS-2364 DEL;
RP ASP-205; SER-205; HIS-247; ARG-250; GLU-255; ALA-268; ASN-268; SER-268;
RP MET-271; ARG-275; LEU-344; GLN-411; TRP-411; GLN-491; GLY-850;
RP 892-GLU--LYS-2364 DEL; TRP-1003; THR-1086; ASP-1110; SER-1398; PRO-1674;
RP 1787-TRP--LYS-2364 DEL AND GLN-1886, CHARACTERIZATION OF VARIANTS DDISBA
RP ILE-59; 183-CYS--LYS-2364 DEL; ASP-205; SER-205; HIS-247; ARG-250; GLU-255;
RP ALA-268; ASN-268; SER-268; MET-271; ARG-275; LEU-344; GLN-411; TRP-411;
RP GLN-491; GLY-850; 892-GLU--LYS-2364 DEL; TRP-1003; THR-1086; ASP-1110;
RP SER-1398; PRO-1674; 1787-TRP--LYS-2364 DEL AND GLN-1886, FUNCTION,
RP SUBCELLULAR LOCATION, AND INTERACTION WITH ANK2.
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 [29]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 173-280.
RX PubMed=9164454; DOI=10.1038/nsb0397-175;
RA Carugo K.D., Banuelos S., Saraste M.;
RT "Crystal structure of a calponin homology domain.";
RL Nat. Struct. Biol. 4:175-179(1997).
RN [30]
RP X-RAY CRYSTALLOGRAPHY (1.1 ANGSTROMS) OF 173-281.
RX PubMed=9817844; DOI=10.1016/s0969-2126(98)00141-5;
RA Banuelos S., Saraste M., Carugo K.D.;
RT "Structural comparisons of calponin homology domains: implications for
RT actin binding.";
RL Structure 6:1419-1431(1998).
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 CAMSAP1 (PubMed:24117850). Interacts with ANK2
CC (PubMed:15262991, PubMed:34211179). Interacts with CPNE4 (via VWFA
CC domain) (By similarity). Like erythrocyte spectrin, the spectrin-like
CC proteins are capable to form dimers which can further associate to
CC tetramers (By similarity). Can form heterodimers with SPTAN1
CC (PubMed:34211179). Isoform Short cannot bind to the axonal protein
CC fodaxin. {ECO:0000250|UniProtKB:P85986, ECO:0000250|UniProtKB:Q62261,
CC ECO:0000269|PubMed:15262991, ECO:0000269|PubMed:24117850,
CC ECO:0000269|PubMed:34211179}.
CC -!- INTERACTION:
CC Q01082; Q99459: CDC5L; NbExp=3; IntAct=EBI-351561, EBI-374880;
CC Q01082; Q9NRI5: DISC1; NbExp=4; IntAct=EBI-351561, EBI-529989;
CC Q01082; P35240-3: NF2; NbExp=4; IntAct=EBI-351561, EBI-1014509;
CC Q01082; P02549: SPTA1; NbExp=3; IntAct=EBI-351561, EBI-375617;
CC Q01082; Q13813: SPTAN1; NbExp=8; IntAct=EBI-351561, EBI-351450;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q62261}. Cytoplasm, myofibril, sarcomere, M line
CC {ECO:0000250|UniProtKB:Q62261}. Cytoplasm, cytosol
CC {ECO:0000269|PubMed:34211179}. Cell membrane
CC {ECO:0000269|PubMed:34211179}. Note=Colocalizes with ANK2 in a distinct
CC intracellular compartment of neonatal cardiomyocytes.
CC {ECO:0000250|UniProtKB:Q62261}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}; Cytoplasmic side
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=Long;
CC IsoId=Q01082-1; Sequence=Displayed;
CC Name=Short;
CC IsoId=Q01082-2; Sequence=VSP_000720, VSP_000721;
CC Name=2;
CC IsoId=Q01082-3; Sequence=VSP_026054, VSP_026055, VSP_026056;
CC -!- TISSUE SPECIFICITY: Isoform 2 is present in brain, lung and kidney (at
CC protein level). {ECO:0000269|PubMed:11665863}.
CC -!- DISEASE: Developmental delay, impaired speech, and behavioral
CC abnormalities (DDISBA) [MIM:619475]: An autosomal dominant disorder
CC characterized by developmental delay with speech impairment, mild to
CC severe intellectual disability, and behavioral abnormalities including
CC autistic features. Additional variable manifestations may include
CC dysmorphic facial features, seizures, hypotonia, motor abnormalities,
CC and hearing loss. {ECO:0000269|PubMed:34211179}. Note=The disease is
CC caused by variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the spectrin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD92985.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M96803; AAA60580.1; -; mRNA.
DR EMBL; AF327441; AAO15362.1; -; mRNA.
DR EMBL; AB209748; BAD92985.1; ALT_INIT; mRNA.
DR EMBL; AC093110; AAY24229.1; -; Genomic_DNA.
DR EMBL; AC092839; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471053; EAX00147.1; -; Genomic_DNA.
DR EMBL; BC137282; AAI37283.1; -; mRNA.
DR EMBL; BC137283; AAI37284.1; -; mRNA.
DR EMBL; S65762; AAB28324.1; -; mRNA.
DR EMBL; AJ005694; CAA06678.1; -; mRNA.
DR EMBL; AJ238723; CAB91088.1; -; Genomic_DNA.
DR CCDS; CCDS33198.1; -. [Q01082-1]
DR CCDS; CCDS33199.1; -. [Q01082-3]
DR PIR; A44159; A44159.
DR PIR; A47213; A47213.
DR RefSeq; NP_003119.2; NM_003128.2. [Q01082-1]
DR RefSeq; NP_842565.2; NM_178313.2. [Q01082-3]
DR RefSeq; XP_005264574.1; XM_005264517.2. [Q01082-1]
DR RefSeq; XP_006712150.1; XM_006712087.2. [Q01082-1]
DR RefSeq; XP_016860268.1; XM_017004779.1. [Q01082-1]
DR RefSeq; XP_016860269.1; XM_017004780.1. [Q01082-1]
DR RefSeq; XP_016860270.1; XM_017004781.1. [Q01082-1]
DR PDB; 1AA2; X-ray; 2.00 A; A=173-280.
DR PDB; 1BKR; X-ray; 1.10 A; A=172-280.
DR PDB; 3EDV; X-ray; 1.95 A; A/B=1697-2015.
DR PDBsum; 1AA2; -.
DR PDBsum; 1BKR; -.
DR PDBsum; 3EDV; -.
DR AlphaFoldDB; Q01082; -.
DR SMR; Q01082; -.
DR BioGRID; 112589; 290.
DR DIP; DIP-33182N; -.
DR ELM; Q01082; -.
DR IntAct; Q01082; 126.
DR MINT; Q01082; -.
DR STRING; 9606.ENSP00000349259; -.
DR DrugBank; DB03401; 1D-myo-inositol 1,4,5-trisphosphate.
DR DrugBank; DB01373; Calcium.
DR GlyGen; Q01082; 20 sites, 2 O-linked glycans (20 sites).
DR iPTMnet; Q01082; -.
DR MetOSite; Q01082; -.
DR PhosphoSitePlus; Q01082; -.
DR SwissPalm; Q01082; -.
DR BioMuta; SPTBN1; -.
DR DMDM; 116242799; -.
DR CPTAC; CPTAC-590; -.
DR EPD; Q01082; -.
DR jPOST; Q01082; -.
DR MassIVE; Q01082; -.
DR MaxQB; Q01082; -.
DR PaxDb; Q01082; -.
DR PeptideAtlas; Q01082; -.
DR PRIDE; Q01082; -.
DR ProteomicsDB; 57910; -. [Q01082-1]
DR ProteomicsDB; 57911; -. [Q01082-2]
DR ProteomicsDB; 57912; -. [Q01082-3]
DR Antibodypedia; 2181; 196 antibodies from 34 providers.
DR DNASU; 6711; -.
DR Ensembl; ENST00000333896.5; ENSP00000334156.5; ENSG00000115306.16. [Q01082-3]
DR Ensembl; ENST00000356805.9; ENSP00000349259.4; ENSG00000115306.16. [Q01082-1]
DR GeneID; 6711; -.
DR KEGG; hsa:6711; -.
DR MANE-Select; ENST00000356805.9; ENSP00000349259.4; NM_003128.3; NP_003119.2.
DR UCSC; uc002rxu.4; human. [Q01082-1]
DR CTD; 6711; -.
DR DisGeNET; 6711; -.
DR GeneCards; SPTBN1; -.
DR HGNC; HGNC:11275; SPTBN1.
DR HPA; ENSG00000115306; Low tissue specificity.
DR MIM; 182790; gene.
DR MIM; 619475; phenotype.
DR neXtProt; NX_Q01082; -.
DR OpenTargets; ENSG00000115306; -.
DR Orphanet; 528084; Non-specific syndromic intellectual disability.
DR PharmGKB; PA36104; -.
DR VEuPathDB; HostDB:ENSG00000115306; -.
DR eggNOG; KOG0517; Eukaryota.
DR GeneTree; ENSGT00940000154864; -.
DR HOGENOM; CLU_000146_0_0_1; -.
DR InParanoid; Q01082; -.
DR PhylomeDB; Q01082; -.
DR TreeFam; TF313446; -.
DR PathwayCommons; Q01082; -.
DR Reactome; R-HSA-373753; Nephrin family interactions.
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 Reactome; R-HSA-9013420; RHOU GTPase cycle.
DR Reactome; R-HSA-9013424; RHOV GTPase cycle.
DR Reactome; R-HSA-9662360; Sensory processing of sound by inner hair cells of the cochlea.
DR Reactome; R-HSA-9662361; Sensory processing of sound by outer hair cells of the cochlea.
DR Reactome; R-HSA-9703465; Signaling by FLT3 fusion proteins.
DR SignaLink; Q01082; -.
DR SIGNOR; Q01082; -.
DR BioGRID-ORCS; 6711; 20 hits in 1095 CRISPR screens.
DR ChiTaRS; SPTBN1; human.
DR EvolutionaryTrace; Q01082; -.
DR GeneWiki; SPTBN1; -.
DR GenomeRNAi; 6711; -.
DR Pharos; Q01082; Tbio.
DR PRO; PR:Q01082; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q01082; protein.
DR Bgee; ENSG00000115306; Expressed in endothelial cell and 218 other tissues.
DR ExpressionAtlas; Q01082; baseline and differential.
DR Genevisible; Q01082; HS.
DR GO; GO:0030673; C:axolemma; ISS: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:0032437; C:cuticular plate; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IDA:HGNC-UCL.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0031430; C:M band; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; IDA:HGNC-UCL.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0014069; C:postsynaptic density; IEA:Ensembl.
DR GO; GO:0008091; C:spectrin; TAS:ProtInc.
DR GO; GO:0014731; C:spectrin-associated cytoskeleton; NAS:BHF-UCL.
DR GO; GO:0003779; F:actin binding; TAS:ProtInc.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0030506; F:ankyrin binding; IPI:BHF-UCL.
DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0051020; F:GTPase binding; IPI:UniProtKB.
DR GO; GO:0005543; F:phospholipid binding; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; IMP:UniProtKB.
DR GO; GO:0030036; P:actin cytoskeleton organization; IMP: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; IEA:Ensembl.
DR GO; GO:0043001; P:Golgi to plasma membrane protein transport; IMP:BHF-UCL.
DR GO; GO:0071709; P:membrane assembly; IMP:BHF-UCL.
DR GO; GO:0000281; P:mitotic cytokinesis; IMP:BHF-UCL.
DR GO; GO:0007009; P:plasma membrane organization; IMP:BHF-UCL.
DR GO; GO:0032743; P:positive regulation of interleukin-2 production; IMP:UniProtKB.
DR GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; IMP:UniProtKB.
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; IGI:UniProtKB.
DR GO; GO:0060390; P:regulation of SMAD protein signal transduction; IEA:Ensembl.
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; Disease variant; Glycoprotein; Intellectual disability;
KW Membrane; Phosphoprotein; Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378"
FT CHAIN 2..2364
FT /note="Spectrin beta chain, non-erythrocytic 1"
FT /id="PRO_0000073461"
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..1258
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 2197..2307
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:0000269|PubMed:15262991"
FT REGION 2089..2196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2149..2177
FT /note="Mediates interaction with CAMSAP1"
FT /evidence="ECO:0000269|PubMed:24117850"
FT REGION 2309..2364
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..2178
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2309..2340
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2341..2357
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylthreonine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378"
FT MOD_RES 36
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62261"
FT MOD_RES 90
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 228
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62261"
FT MOD_RES 817
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 825
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 903
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62261"
FT MOD_RES 1057
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 1076
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62261"
FT MOD_RES 1079
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62261"
FT MOD_RES 1237
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1388
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1447
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 1557
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1805
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q62261"
FT MOD_RES 1815
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 1913
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 1989
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 2102
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:17924679, ECO:0007744|PubMed:18088087,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19369195,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 2128
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 2138
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 2147
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q62261"
FT MOD_RES 2148
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62261"
FT MOD_RES 2159
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q62261"
FT MOD_RES 2160
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 2161
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 2164
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 2165
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 2169
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 2171
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q62261"
FT MOD_RES 2172
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 2184
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62261"
FT MOD_RES 2187
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 2195
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q62261"
FT MOD_RES 2314
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 2319
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 2320
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 2328
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 2340
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 2341
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT CARBOHYD 2324
FT /note="O-linked (GlcNAc) serine"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..49
FT /note="MTTTVATDYDNIEIQQQYSDVNNRWDVDDWDNENSSARLFERSRIKALA ->
FT MELQRTSSISGPLSPAYTGQVPYNYNQLEGRFKQLQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11665863,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_026054"
FT VAR_SEQ 2141..2225
FT /note="MAETVDTSEMVNGATEQRTSSKESSPIPSPTSDRKAKTALPAQSAATLPART
FT QETPSAQMEGFLNRKHEWEAHNKKASSRSWHNV -> VSYRSQTYQNYKNFNSRRTASD
FT QPWSGL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11665863,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_026055"
FT VAR_SEQ 2141..2168
FT /note="MAETVDTSEMVNGATEQRTSSKESSPIP -> VSYRSQTYQNYKNFNSRRTA
FT SDQPWSGL (in isoform Short)"
FT /evidence="ECO:0000303|PubMed:10806113"
FT /id="VSP_000720"
FT VAR_SEQ 2169..2364
FT /note="Missing (in isoform Short)"
FT /evidence="ECO:0000303|PubMed:10806113"
FT /id="VSP_000721"
FT VAR_SEQ 2226..2364
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11665863,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_026056"
FT VARIANT 59
FT /note="T -> I (in DDISBA; affects function in neuronal
FT axonal growth; reduced F-actin binding; disturbs
FT cytoskeleton organization and dynamics)"
FT /evidence="ECO:0000269|PubMed:34211179"
FT /id="VAR_086305"
FT VARIANT 183..2364
FT /note="Missing (in DDISBA; affects function in neuronal
FT axonal growth; decreased interaction with SPTAN1; disturbs
FT cytoskeleton organization and dynamics)"
FT /evidence="ECO:0000269|PubMed:34211179"
FT /id="VAR_086306"
FT VARIANT 205
FT /note="G -> D (in DDISBA; affects function in neuronal
FT axonal growth; forms cytosolic aggregates; decreased
FT interaction with SPTAN1; disturbs cytoskeleton organization
FT and dynamics)"
FT /evidence="ECO:0000269|PubMed:34211179"
FT /id="VAR_086307"
FT VARIANT 205
FT /note="G -> S (in DDISBA; affects function in neuronal
FT axonal growth; forms cytosolic aggregates; decreased
FT interaction with SPTAN1; disturbs cytoskeleton organization
FT and dynamics)"
FT /evidence="ECO:0000269|PubMed:34211179"
FT /id="VAR_086308"
FT VARIANT 247
FT /note="L -> H (in DDISBA; affects function in neuronal
FT axonal growth; forms cytosolic aggregates; disturbs
FT cytoskeleton organization and dynamics)"
FT /evidence="ECO:0000269|PubMed:34211179"
FT /id="VAR_086309"
FT VARIANT 250
FT /note="L -> R (in DDISBA; affects function in neuronal
FT axonal growth; forms cytosolic aggregates; disturbs
FT cytoskeleton organization and dynamics)"
FT /evidence="ECO:0000269|PubMed:34211179"
FT /id="VAR_086310"
FT VARIANT 255
FT /note="D -> E (in DDISBA; disturbs cytoskeleton
FT organization and dynamics)"
FT /evidence="ECO:0000269|PubMed:34211179"
FT /id="VAR_086311"
FT VARIANT 268
FT /note="T -> A (in DDISBA; affects function in neuronal
FT axonal growth; no effect on F-actin binding; disturbs
FT cytoskeleton organization and dynamics)"
FT /evidence="ECO:0000269|PubMed:34211179"
FT /id="VAR_086312"
FT VARIANT 268
FT /note="T -> N (in DDISBA; affects function in neuronal
FT axonal growth; no effect on F-actin binding; disturbs
FT cytoskeleton organization and dynamics)"
FT /evidence="ECO:0000269|PubMed:34211179"
FT /id="VAR_086313"
FT VARIANT 268
FT /note="T -> S (in DDISBA; affects function in neuronal
FT axonal growth; no effect on F-actin binding; disturbs
FT cytoskeleton organization and dynamics)"
FT /evidence="ECO:0000269|PubMed:34211179"
FT /id="VAR_086314"
FT VARIANT 271
FT /note="V -> M (in DDISBA; affects function in neuronal
FT axonal growth; increased F-actin binding; disturbs
FT cytoskeleton organization and dynamics)"
FT /evidence="ECO:0000269|PubMed:34211179"
FT /id="VAR_086315"
FT VARIANT 275
FT /note="H -> R (in DDISBA; affects function in neuronal
FT axonal growth; increased F-actin binding; disturbs
FT cytoskeleton organization and dynamics)"
FT /evidence="ECO:0000269|PubMed:34211179"
FT /id="VAR_086316"
FT VARIANT 344
FT /note="F -> L (in DDISBA; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:34211179"
FT /id="VAR_086317"
FT VARIANT 411
FT /note="R -> Q (in DDISBA)"
FT /evidence="ECO:0000269|PubMed:34211179"
FT /id="VAR_086318"
FT VARIANT 411
FT /note="R -> W (in DDISBA; disturbs cytoskeleton
FT organization and dynamics)"
FT /evidence="ECO:0000269|PubMed:34211179"
FT /id="VAR_086319"
FT VARIANT 491
FT /note="E -> Q (in DDISBA; disturbs cytoskeleton
FT organization and dynamics)"
FT /evidence="ECO:0000269|PubMed:34211179"
FT /id="VAR_086320"
FT VARIANT 850
FT /note="A -> G (in DDISBA; affects function in neuronal
FT axonal growth; increased F-actin binding; disturbs
FT cytoskeleton organization and dynamics)"
FT /evidence="ECO:0000269|PubMed:34211179"
FT /id="VAR_086321"
FT VARIANT 892..2364
FT /note="Missing (in DDISBA; affects function in neuronal
FT axonal growth; decreased ankyrin binding; disturbs
FT cytoskeleton organization and dynamics)"
FT /evidence="ECO:0000269|PubMed:34211179"
FT /id="VAR_086322"
FT VARIANT 1003
FT /note="R -> W (in DDISBA; affects function in neuronal
FT axonal growth; decreased interaction with SPTAN1; disturbs
FT cytoskeleton organization and dynamics)"
FT /evidence="ECO:0000269|PubMed:34211179"
FT /id="VAR_086323"
FT VARIANT 1086
FT /note="A -> T (in DDISBA)"
FT /evidence="ECO:0000269|PubMed:34211179"
FT /id="VAR_086324"
FT VARIANT 1110
FT /note="E -> D (in DDISBA; distursb cytoskeleton
FT organization and dynamics)"
FT /evidence="ECO:0000269|PubMed:34211179"
FT /id="VAR_086325"
FT VARIANT 1398
FT /note="G -> S (in DDISBA; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:34211179"
FT /id="VAR_086326"
FT VARIANT 1411
FT /note="D -> H (in dbSNP:rs1052790)"
FT /evidence="ECO:0000269|PubMed:11665863,
FT ECO:0000269|PubMed:1527002"
FT /id="VAR_032641"
FT VARIANT 1674
FT /note="S -> P (in DDISBA)"
FT /evidence="ECO:0000269|PubMed:34211179"
FT /id="VAR_086327"
FT VARIANT 1787..2364
FT /note="Missing (in DDISBA; affects function in neuronal
FT axonal growth; decreased ankyrin binding; disturbs
FT cytoskeleton organization and dynamics)"
FT /evidence="ECO:0000269|PubMed:34211179"
FT /id="VAR_086328"
FT VARIANT 1886
FT /note="E -> Q (in DDISBA; disturbs cytoskeleton
FT organization and dynamics)"
FT /evidence="ECO:0000269|PubMed:34211179"
FT /id="VAR_086329"
FT CONFLICT 583
FT /note="R -> W (in Ref. 3; BAD92985)"
FT /evidence="ECO:0000305"
FT HELIX 174..186
FT /evidence="ECO:0007829|PDB:1BKR"
FT TURN 187..189
FT /evidence="ECO:0007829|PDB:1BKR"
FT STRAND 196..199
FT /evidence="ECO:0007829|PDB:1BKR"
FT HELIX 200..202
FT /evidence="ECO:0007829|PDB:1BKR"
FT HELIX 206..215
FT /evidence="ECO:0007829|PDB:1BKR"
FT HELIX 217..219
FT /evidence="ECO:0007829|PDB:1BKR"
FT HELIX 222..224
FT /evidence="ECO:0007829|PDB:1BKR"
FT HELIX 230..245
FT /evidence="ECO:0007829|PDB:1BKR"
FT HELIX 253..256
FT /evidence="ECO:0007829|PDB:1BKR"
FT STRAND 257..260
FT /evidence="ECO:0007829|PDB:1BKR"
FT HELIX 263..277
FT /evidence="ECO:0007829|PDB:1BKR"
FT HELIX 1697..1721
FT /evidence="ECO:0007829|PDB:3EDV"
FT HELIX 1730..1767
FT /evidence="ECO:0007829|PDB:3EDV"
FT HELIX 1773..1826
FT /evidence="ECO:0007829|PDB:3EDV"
FT HELIX 1836..1852
FT /evidence="ECO:0007829|PDB:3EDV"
FT HELIX 1854..1873
FT /evidence="ECO:0007829|PDB:3EDV"
FT HELIX 1877..1935
FT /evidence="ECO:0007829|PDB:3EDV"
FT HELIX 1943..1962
FT /evidence="ECO:0007829|PDB:3EDV"
FT HELIX 1964..1979
FT /evidence="ECO:0007829|PDB:3EDV"
FT HELIX 1985..2014
FT /evidence="ECO:0007829|PDB:3EDV"
FT MOD_RES Q01082-3:14
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332"
SQ SEQUENCE 2364 AA; 274609 MW; 1770C3B0EB07B892 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 VLSQDYGKHL LGVEDLLQKH TLVEADIGIQ AERVRGVNAS AQKFATDGEG
YKPCDPQVIR DRVAHMEFCY QELCQLAAER RARLEESRRL WKFFWEMAEE EGWIREKEKI
LSSDDYGKDL TSVMRLLSKH RAFEDEMSGR SGHFEQAIKE GEDMIAEEHF GSEKIRERII
YIREQWANLE QLSAIRKKRL EEASLLHQFQ ADADDIDAWM LDILKIVSSS DVGHDEYSTQ
SLVKKHKDVA EEIANYRPTL DTLHEQASAL PQEHAESPDV RGRLSGIEER YKEVAELTRL
RKQALQDTLA LYKMFSEADA CELWIDEKEQ WLNNMQIPEK LEDLEVIQHR FESLEPEMNN
QASRVAVVNQ IARQLMHSGH PSEKEIKAQQ 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
RETASELLMR LKDNRDLQKF LQDCQELSLW INEKMLTAQD MSYDEARNLH SKWLKHQAFM
AELASNKEWL DKIEKEGMQL ISEKPETEAV VKEKLTGLHK MWEVLESTTQ TKAQRLFDAN
KAELFTQSCA DLDKWLHGLE SQIQSDDYGK DLTSVNILLK KQQMLENQME VRKKEIEELQ
SQAQALSQEG KSTDEVDSKR LTVQTKFMEL LEPLNERKHN LLASKEIHQF NRDVEDEILW
VGERMPLATS TDHGHNLQTV QLLIKKNQTL QKEIQGHQPR IDDIFERSQN IVTDSSSLSA
EAIRQRLADL KQLWGLLIEE TEKRHRRLEE AHRAQQYYFD AAEAEAWMSE QELYMMSEEK
AKDEQSAVSM LKKHQILEQA VEDYAETVHQ LSKTSRALVA DSHPESERIS MRQSKVDKLY
AGLKDLAEER RGKLDERHRL FQLNREVDDL EQWIAEREVV AGSHELGQDY EHVTMLQERF
REFARDTGNI GQERVDTVNH LADELINSGH SDAATIAEWK DGLNEAWADL LELIDTRTQI
LAASYELHKF YHDAKEIFGR IQDKHKKLPE ELGRDQNTVE TLQRMHTTFE HDIQALGTQV
RQLQEDAARL QAAYAGDKAD DIQKRENEVL EAWKSLLDAC ESRRVRLVDT GDKFRFFSMV
RDLMLWMEDV IRQIEAQEKP RDVSSVELLM NNHQGIKAEI DARNDSFTTC IELGKSLLAR
KHYASEEIKE KLLQLTEKRK EMIDKWEDRW EWLRLILEVH QFSRDASVAE AWLLGQEPYL
SSREIGQSVD EVEKLIKRHE AFEKSAATWD ERFSALERLT TLELLEVRRQ QEEEERKRRP
PSPEPSTKVS EEAESQQQWD TSKGEQVSQN GLPAEQGSPR MAETVDTSEM VNGATEQRTS
SKESSPIPSP TSDRKAKTAL PAQSAATLPA RTQETPSAQM EGFLNRKHEW EAHNKKASSR
SWHNVYCVIN NQEMGFYKDA KTAASGIPYH SEVPVSLKEA VCEVALDYKK KKHVFKLRLN
DGNEYLFQAK DDEEMNTWIQ AISSAISSDK HEVSASTQST PASSRAQTLP TSVVTITSES
SPGKREKDKE KDKEKRFSLF GKKK
