SPTN2_HUMAN
ID SPTN2_HUMAN Reviewed; 2390 AA.
AC O15020; O14872; O14873;
DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 3.
DT 03-AUG-2022, entry version 206.
DE RecName: Full=Spectrin beta chain, non-erythrocytic 2;
DE AltName: Full=Beta-III spectrin;
DE AltName: Full=Spinocerebellar ataxia 5 protein;
GN Name=SPTBN2; Synonyms=KIAA0302, SCA5;
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 [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT GLY-825.
RC TISSUE=Brain;
RX PubMed=9205841; DOI=10.1093/dnares/4.2.141;
RA Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. VII. The
RT complete sequences of 100 new cDNA clones from brain which can code for
RT large proteins in vitro.";
RL DNA Res. 4:141-150(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-34.
RC TISSUE=Brain;
RX PubMed=9826670; DOI=10.1073/pnas.95.24.14158;
RA Stankewich M.C., Tse W.T., Peters L.L., Ch'ng Y., John K.M., Stabach P.R.,
RA Devarajan P., Morrow J.S., Lux S.E.;
RT "A widely expressed betaIII spectrin associated with Golgi and cytoplasmic
RT vesicles.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:14158-14163(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1900-2390 (ISOFORMS 1 AND 2).
RC TISSUE=Brain;
RA Tse W.T., Peters L.L., John K.M., Lux S.E.;
RT "SPTBN2, a new, widely expressed beta III spectrin gene located on human
RT chromosome 11q13 and mouse chromosome 19.";
RL Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2171, AND IDENTIFICATION BY
RP 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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2171 AND SER-2359, AND
RP IDENTIFICATION BY MASS 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 [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-2171 AND SER-2359, CLEAVAGE OF INITIATOR METHIONINE [LARGE
RP SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [8]
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2171, AND IDENTIFICATION BY
RP 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 [10]
RP INVOLVEMENT IN SCAR14.
RX PubMed=23236289; DOI=10.1371/journal.pgen.1003074;
RA Lise S., Clarkson Y., Perkins E., Kwasniewska A., Sadighi Akha E.,
RA Schnekenberg R.P., Suminaite D., Hope J., Baker I., Gregory L., Green A.,
RA Allan C., Lamble S., Jayawant S., Quaghebeur G., Cader M.Z., Hughes S.,
RA Armstrong R.J., Kanapin A., Rimmer A., Lunter G., Mathieson I.,
RA Cazier J.B., Buck D., Taylor J.C., Bentley D., McVean G., Donnelly P.,
RA Knight S.J., Jackson M., Ragoussis J., Nemeth A.H.;
RT "Recessive mutations in SPTBN2 implicate beta-III spectrin in both
RT cognitive and motor development.";
RL PLoS Genet. 8:E1003074-E1003074(2012).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2171; THR-2354 AND SER-2359,
RP AND 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 [12]
RP INVOLVEMENT IN SCAR14.
RX PubMed=23838597; DOI=10.1038/ejhg.2013.150;
RA Elsayed S.M., Heller R., Thoenes M., Zaki M.S., Swan D., Elsobky E.,
RA Zuehlke C., Ebermann I., Nuernberg G., Nuernberg P., Bolz H.J.;
RT "Autosomal dominant SCA5 and autosomal recessive infantile SCA are allelic
RT conditions resulting from SPTBN2 mutations.";
RL Eur. J. Hum. Genet. 22:286-288(2014).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31; SER-959; SER-1073;
RP THR-2354 AND SER-2359, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [14]
RP STRUCTURE BY NMR OF 2219-2328.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of pleckstrin homology domain of human beta III
RT spectrin.";
RL Submitted (NOV-2004) to the PDB data bank.
RN [15]
RP STRUCTURE BY NMR OF 178-291.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the second CH domain of human spectrin beta chain,
RT brain 2.";
RL Submitted (AUG-2005) to the PDB data bank.
RN [16]
RP VARIANTS SCA5 PRO-253; 532-GLU--MET-544 DEL AND 629-LEU--ARG-634 DELINS
RP TRP.
RX PubMed=16429157; DOI=10.1038/ng1728;
RA Ikeda Y., Dick K.A., Weatherspoon M.R., Gincel D., Armbrust K.R.,
RA Dalton J.C., Stevanin G., Duerr A., Zuehlke C., Buerk K., Clark H.B.,
RA Brice A., Rothstein J.D., Schut L.J., Day J.W., Ranum L.P.W.;
RT "Spectrin mutations cause spinocerebellar ataxia type 5.";
RL Nat. Genet. 38:184-190(2006).
RN [17]
RP VARIANT [LARGE SCALE ANALYSIS] LYS-774.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
RN [18]
RP VARIANT SCA5 TRP-480.
RX PubMed=22914369; DOI=10.1177/0883073812454331;
RA Jacob F.D., Ho E.S., Martinez-Ojeda M., Darras B.T., Khwaja O.S.;
RT "Case of infantile onset spinocerebellar ataxia type 5.";
RL J. Child Neurol. 28:1292-1295(2013).
CC -!- FUNCTION: Probably plays an important role in neuronal membrane
CC skeleton.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cytoplasm, cell cortex.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O15020-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O15020-2; Sequence=VSP_000722;
CC -!- TISSUE SPECIFICITY: Highly expressed in brain, kidney, pancreas, and
CC liver, and at lower levels in lung and placenta.
CC -!- DISEASE: Spinocerebellar ataxia 5 (SCA5) [MIM:600224]: Spinocerebellar
CC ataxia is a clinically and genetically heterogeneous group of
CC cerebellar disorders. Patients show progressive incoordination of gait
CC and often poor coordination of hands, speech and eye movements, due to
CC degeneration of the cerebellum with variable involvement of the
CC brainstem and spinal cord. SCA5 is an autosomal dominant cerebellar
CC ataxia (ADCA). It is a slowly progressive disorder with variable age at
CC onset, ranging between 10 and 50 years. {ECO:0000269|PubMed:16429157,
CC ECO:0000269|PubMed:22914369}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Spinocerebellar ataxia, autosomal recessive, 14 (SCAR14)
CC [MIM:615386]: A form of spinocerebellar ataxia, a clinically and
CC genetically heterogeneous group of cerebellar disorders. Patients show
CC progressive incoordination of gait and often poor coordination of
CC hands, speech and eye movements, due to degeneration of the cerebellum
CC with variable involvement of the brainstem and spinal cord. SCAR14 is
CC characterized by delayed psychomotor development, severe early onset
CC gait ataxia, eye movement abnormalities, cerebellar atrophy on brain
CC imaging, and intellectual disability. {ECO:0000269|PubMed:23236289,
CC ECO:0000269|PubMed:23838597}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the spectrin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA32700.2; 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; AB008567; BAA32700.2; ALT_INIT; mRNA.
DR EMBL; AP001157; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AF079569; AAC80006.1; -; mRNA.
DR EMBL; AF026487; AAC79502.1; -; mRNA.
DR EMBL; AF026488; AAC79503.1; -; mRNA.
DR EMBL; AF026488; AAC79504.1; -; mRNA.
DR CCDS; CCDS8150.1; -. [O15020-1]
DR RefSeq; NP_008877.1; NM_006946.2. [O15020-1]
DR RefSeq; XP_005274249.1; XM_005274192.4.
DR RefSeq; XP_005274250.1; XM_005274193.3. [O15020-1]
DR RefSeq; XP_006718734.1; XM_006718671.3. [O15020-1]
DR RefSeq; XP_016873663.1; XM_017018174.1. [O15020-1]
DR RefSeq; XP_016873664.1; XM_017018175.1. [O15020-1]
DR RefSeq; XP_016873665.1; XM_017018176.1. [O15020-1]
DR RefSeq; XP_016873666.1; XM_017018177.1. [O15020-1]
DR RefSeq; XP_016873667.1; XM_017018178.1. [O15020-1]
DR PDB; 1WJM; NMR; -; A=2219-2328.
DR PDB; 1WYQ; NMR; -; A=178-291.
DR PDB; 6ANU; EM; 7.00 A; a/b/c/d/e/f=1-284.
DR PDBsum; 1WJM; -.
DR PDBsum; 1WYQ; -.
DR PDBsum; 6ANU; -.
DR AlphaFoldDB; O15020; -.
DR BMRB; O15020; -.
DR SMR; O15020; -.
DR BioGRID; 112590; 142.
DR DIP; DIP-47270N; -.
DR IntAct; O15020; 43.
DR MINT; O15020; -.
DR STRING; 9606.ENSP00000432568; -.
DR CarbonylDB; O15020; -.
DR iPTMnet; O15020; -.
DR MetOSite; O15020; -.
DR PhosphoSitePlus; O15020; -.
DR SwissPalm; O15020; -.
DR BioMuta; SPTBN2; -.
DR EPD; O15020; -.
DR jPOST; O15020; -.
DR MassIVE; O15020; -.
DR MaxQB; O15020; -.
DR PaxDb; O15020; -.
DR PeptideAtlas; O15020; -.
DR PRIDE; O15020; -.
DR ProteomicsDB; 48376; -. [O15020-1]
DR ProteomicsDB; 48377; -. [O15020-2]
DR Antibodypedia; 4075; 724 antibodies from 25 providers.
DR DNASU; 6712; -.
DR Ensembl; ENST00000309996.7; ENSP00000311489.2; ENSG00000173898.15. [O15020-1]
DR Ensembl; ENST00000529997.5; ENSP00000433593.1; ENSG00000173898.15. [O15020-2]
DR Ensembl; ENST00000533211.6; ENSP00000432568.1; ENSG00000173898.15. [O15020-1]
DR Ensembl; ENST00000611817.5; ENSP00000480692.2; ENSG00000173898.15. [O15020-1]
DR Ensembl; ENST00000647510.2; ENSP00000508362.1; ENSG00000173898.15. [O15020-1]
DR GeneID; 6712; -.
DR KEGG; hsa:6712; -.
DR MANE-Select; ENST00000533211.6; ENSP00000432568.1; NM_006946.4; NP_008877.2.
DR UCSC; uc001ojc.2; human. [O15020-1]
DR CTD; 6712; -.
DR DisGeNET; 6712; -.
DR GeneCards; SPTBN2; -.
DR HGNC; HGNC:11276; SPTBN2.
DR HPA; ENSG00000173898; Tissue enhanced (brain, skin).
DR MalaCards; SPTBN2; -.
DR MIM; 600224; phenotype.
DR MIM; 604985; gene.
DR MIM; 615386; phenotype.
DR neXtProt; NX_O15020; -.
DR OpenTargets; ENSG00000173898; -.
DR Orphanet; 352403; Spectrin-associated autosomal recessive cerebellar ataxia.
DR Orphanet; 98766; Spinocerebellar ataxia type 5.
DR PharmGKB; PA36105; -.
DR VEuPathDB; HostDB:ENSG00000173898; -.
DR eggNOG; KOG0517; Eukaryota.
DR GeneTree; ENSGT00940000158847; -.
DR HOGENOM; CLU_000146_0_0_1; -.
DR InParanoid; O15020; -.
DR OMA; DNHEPWI; -.
DR OrthoDB; 543832at2759; -.
DR PhylomeDB; O15020; -.
DR TreeFam; TF313446; -.
DR PathwayCommons; O15020; -.
DR Reactome; R-HSA-2132295; MHC class II antigen presentation.
DR Reactome; R-HSA-375165; NCAM signaling for neurite out-growth.
DR Reactome; R-HSA-445095; Interaction between L1 and Ankyrins.
DR Reactome; R-HSA-5673001; RAF/MAP kinase cascade.
DR Reactome; R-HSA-6807878; COPI-mediated anterograde transport.
DR SignaLink; O15020; -.
DR BioGRID-ORCS; 6712; 25 hits in 1075 CRISPR screens.
DR ChiTaRS; SPTBN2; human.
DR EvolutionaryTrace; O15020; -.
DR GeneWiki; SPTBN2; -.
DR GenomeRNAi; 6712; -.
DR Pharos; O15020; Tbio.
DR PRO; PR:O15020; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; O15020; protein.
DR Bgee; ENSG00000173898; Expressed in right hemisphere of cerebellum and 157 other tissues.
DR ExpressionAtlas; O15020; baseline and differential.
DR Genevisible; O15020; HS.
DR GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl.
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:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR GO; GO:0098688; C:parallel fiber to Purkinje cell synapse; IEA:Ensembl.
DR GO; GO:0033010; C:paranodal junction; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0099189; C:postsynaptic spectrin-associated cytoskeleton; IEA:Ensembl.
DR GO; GO:0098793; C:presynapse; IEA:Ensembl.
DR GO; GO:0008091; C:spectrin; IDA:UniProtKB.
DR GO; GO:0003779; F:actin binding; TAS:ProtInc.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR GO; GO:0005543; F:phospholipid binding; IEA:InterPro.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; TAS:UniProtKB.
DR GO; GO:0098918; F:structural constituent of synapse; IBA:GO_Central.
DR GO; GO:0030036; P:actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0051693; P:actin filament capping; IEA:UniProtKB-KW.
DR GO; GO:0030534; P:adult behavior; IEA:Ensembl.
DR GO; GO:0021692; P:cerebellar Purkinje cell layer morphogenesis; IEA:Ensembl.
DR GO; GO:0035264; P:multicellular organism growth; IEA:Ensembl.
DR GO; GO:0099173; P:postsynapse organization; IEA:Ensembl.
DR GO; GO:0007416; P:synapse assembly; IEA:Ensembl.
DR GO; GO:0016192; P:vesicle-mediated transport; IDA:UniProtKB.
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; Cytoplasm; Cytoskeleton; Disease variant;
KW Neurodegeneration; Phosphoprotein; Reference proteome; Repeat;
KW Spinocerebellar ataxia.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:20068231"
FT CHAIN 2..2390
FT /note="Spectrin beta chain, non-erythrocytic 2"
FT /id="PRO_0000073463"
FT DOMAIN 57..161
FT /note="Calponin-homology (CH) 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 176..281
FT /note="Calponin-homology (CH) 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT REPEAT 306..414
FT /note="Spectrin 1"
FT /evidence="ECO:0000255"
FT REPEAT 427..527
FT /note="Spectrin 2"
FT /evidence="ECO:0000255"
FT REPEAT 532..639
FT /note="Spectrin 3"
FT /evidence="ECO:0000255"
FT REPEAT 642..744
FT /note="Spectrin 4"
FT /evidence="ECO:0000255"
FT REPEAT 749..849
FT /note="Spectrin 5"
FT /evidence="ECO:0000255"
FT REPEAT 855..954
FT /note="Spectrin 6"
FT /evidence="ECO:0000255"
FT REPEAT 960..1063
FT /note="Spectrin 7"
FT /evidence="ECO:0000255"
FT REPEAT 1066..1169
FT /note="Spectrin 8"
FT /evidence="ECO:0000255"
FT REPEAT 1174..1262
FT /note="Spectrin 9"
FT /evidence="ECO:0000255"
FT REPEAT 1279..1379
FT /note="Spectrin 10"
FT /evidence="ECO:0000255"
FT REPEAT 1384..1485
FT /note="Spectrin 11"
FT /evidence="ECO:0000255"
FT REPEAT 1489..1586
FT /note="Spectrin 12"
FT /evidence="ECO:0000255"
FT REPEAT 1589..1692
FT /note="Spectrin 13"
FT /evidence="ECO:0000255"
FT REPEAT 1696..1797
FT /note="Spectrin 14"
FT /evidence="ECO:0000255"
FT REPEAT 1801..1904
FT /note="Spectrin 15"
FT /evidence="ECO:0000255"
FT REPEAT 1910..2010
FT /note="Spectrin 16"
FT /evidence="ECO:0000255"
FT REPEAT 2017..2076
FT /note="Spectrin 17"
FT /evidence="ECO:0000255"
FT DOMAIN 2218..2328
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT REGION 2..278
FT /note="Actin-binding"
FT REGION 2081..2222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2331..2390
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2081..2099
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2115..2129
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2136..2157
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2189..2204
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2369..2390
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 6
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QWN8"
FT MOD_RES 31
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 959
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1073
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 2171
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 2199
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QWN8"
FT MOD_RES 2354
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 2359
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT VAR_SEQ 2314..2390
FT /note="AEMSSWLRVVNAAIATASSASGEPEEPVVPSTTRGMTRAMTMPPVSPVGAEG
FT PVVLRSKDGREREREKRFSFFKKNK -> VSCPSCSSLSVPFQKLPAADSPSFPVLPLF
FT PGLVLCGKTGCVRRPHQAALPV (in isoform 2)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_000722"
FT VARIANT 253
FT /note="L -> P (in SCA5; dbSNP:rs121918306)"
FT /evidence="ECO:0000269|PubMed:16429157"
FT /id="VAR_026767"
FT VARIANT 480
FT /note="R -> W (in SCA5; dbSNP:rs397514749)"
FT /evidence="ECO:0000269|PubMed:22914369"
FT /id="VAR_070232"
FT VARIANT 532..544
FT /note="Missing (in SCA5)"
FT /evidence="ECO:0000269|PubMed:16429157"
FT /id="VAR_026768"
FT VARIANT 629..634
FT /note="LAAARR -> W (in SCA5)"
FT /evidence="ECO:0000269|PubMed:16429157"
FT /id="VAR_026769"
FT VARIANT 774
FT /note="E -> K (in a colorectal cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035458"
FT VARIANT 825
FT /note="S -> G (in dbSNP:rs4930388)"
FT /evidence="ECO:0000269|PubMed:9205841"
FT /id="VAR_026770"
FT VARIANT 835
FT /note="E -> K (in dbSNP:rs36054877)"
FT /id="VAR_048631"
FT VARIANT 1034
FT /note="V -> A (in dbSNP:rs506028)"
FT /id="VAR_026771"
FT HELIX 180..191
FT /evidence="ECO:0007829|PDB:1WYQ"
FT STRAND 193..195
FT /evidence="ECO:0007829|PDB:1WYQ"
FT STRAND 205..208
FT /evidence="ECO:0007829|PDB:1WYQ"
FT HELIX 209..218
FT /evidence="ECO:0007829|PDB:1WYQ"
FT TURN 220..222
FT /evidence="ECO:0007829|PDB:1WYQ"
FT TURN 225..227
FT /evidence="ECO:0007829|PDB:1WYQ"
FT HELIX 234..246
FT /evidence="ECO:0007829|PDB:1WYQ"
FT TURN 256..258
FT /evidence="ECO:0007829|PDB:1WYQ"
FT STRAND 261..263
FT /evidence="ECO:0007829|PDB:1WYQ"
FT HELIX 266..282
FT /evidence="ECO:0007829|PDB:1WYQ"
FT STRAND 283..285
FT /evidence="ECO:0007829|PDB:1WYQ"
FT STRAND 2221..2233
FT /evidence="ECO:0007829|PDB:1WJM"
FT STRAND 2244..2251
FT /evidence="ECO:0007829|PDB:1WJM"
FT STRAND 2254..2260
FT /evidence="ECO:0007829|PDB:1WJM"
FT HELIX 2261..2264
FT /evidence="ECO:0007829|PDB:1WJM"
FT TURN 2265..2267
FT /evidence="ECO:0007829|PDB:1WJM"
FT STRAND 2269..2272
FT /evidence="ECO:0007829|PDB:1WJM"
FT STRAND 2282..2285
FT /evidence="ECO:0007829|PDB:1WJM"
FT STRAND 2293..2299
FT /evidence="ECO:0007829|PDB:1WJM"
FT STRAND 2301..2303
FT /evidence="ECO:0007829|PDB:1WJM"
FT STRAND 2305..2309
FT /evidence="ECO:0007829|PDB:1WJM"
FT HELIX 2313..2328
FT /evidence="ECO:0007829|PDB:1WJM"
SQ SEQUENCE 2390 AA; 271325 MW; 1CC523CC6493DBFE CRC64;
MSSTLSPTDF DSLEIQGQYS DINNRWDLPD SDWDNDSSSA RLFERSRIKA LADEREAVQK
KTFTKWVNSH LARVTCRVGD LYSDLRDGRN LLRLLEVLSG EILPKPTKGR MRIHCLENVD
KALQFLKEQK VHLENMGSHD IVDGNHRLTL GLVWTIILRF QIQDISVETE DNKEKKSAKD
ALLLWCQMKT AGYPNVNVHN FTTSWRDGLA FNAIVHKHRP DLLDFESLKK CNAHYNLQNA
FNLAEKELGL TKLLDPEDVN VDQPDEKSII TYVATYYHYF SKMKALAVEG KRIGKVLDHA
MEAERLVEKY ESLASELLQW IEQTIVTLND RQLANSLSGV QNQLQSFNSY RTVEKPPKFT
EKGNLEVLLF TIQSKLRANN QKVYTPREGR LISDINKAWE RLEKAEHERE LALRTELIRQ
EKLEQLAARF DRKAAMRETW LSENQRLVSQ DNFGLELAAV EAAVRKHEAI ETDIVAYSGR
VQAVDAVAAE LAAERYHDIK RIAARQHNVA RLWDFLRQMV AARRERLLLN LELQKVFQDL
LYLMDWMEEM KGRLQSQDLG RHLAGVEDLL QLHELVEADI AVQAERVRAV SASALRFCNP
GKEYRPCDPQ LVSERVAKLE QSYEALCELA AARRARLEES RRLWRFLWEV GEAEAWVREQ
QHLLASADTG RDLTGALRLL NKHTALRGEM SGRLGPLKLT LEQGQQLVAE GHPGASQASA
RAAELQAQWE RLEALAEERA QRLAQAASLY QFQADANDME AWLVDALRLV SSPELGHDEF
STQALARQHR ALEEEIRSHR PTLDALREQA AALPPTLSRT PEVQSRVPTL ERHYEELQAR
AGERARALEA ALALYTMLSE AGACGLWVEE KEQWLNGLAL PERLEDLEVV QQRFETLEPE
MNTLAAQITA VNDIAEQLLK ANPPGKDRIV NTQEQLNHRW QQFRRLADGK KAALTSALSI
QNYHLECTET QAWMREKTKV IESTQGLGND LAGVLALQRK LAGTERDLEA IAARVGELTR
EANALAAGHP AQAVAINARL REVQTGWEDL RATMRRREES LGEARRLQDF LRSLDDFQAW
LGRTQTAVAS EEGPATLPEA EALLAQHAAL RGEVERAQSE YSRLRALGEE VTRDQADPQC
LFLRQRLEAL GTGWEELGRM WESRQGRLAQ AHGFQGFLRD ARQAEGVLSS QEYVLSHTEM
PGTLQAADAA IKKLEDFMST MDANGERIHG LLEAGRQLVS EGNIHADKIR EKADSIERRH
KKNQDAAQQF LGRLRDNREQ QHFLQDCHEL KLWIDEKMLT AQDVSYDEAR NLHTKWQKHQ
AFMAELAANK DWLDKVDKEG RELTLEKPEL KALVSEKLRD LHRRWDELET TTQAKARSLF
DANRAELFAQ SCCALESWLE SLQAQLHSDD YGKDLTSVNI LLKKQQMLEW EMAVREKEVE
AIQAQAKALA QEDQGAGEVE RTSRAVEEKF RALCQPMRER CRRLQASREQ HQFHRDVEDE
ILWVTERLPM ASSMEHGKDL PSVQLLMKKN QTLQKEIQGH EPRIADLRER QRALGAAAAG
PELAELQEMW KRLGHELELR GKRLEDALRA QQFYRDAAEA EAWMGEQELH MMGQEKAKDE
LSAQAEVKKH QVLEQALADY AQTIHQLAAS SQDMIDHEHP ESTRISIRQA QVDKLYAGLK
ELAGERRERL QEHLRLCQLR RELDDLEQWI QEREVVAASH ELGQDYEHVT MLRDKFREFS
RDTSTIGQER VDSANALANG LIAGGHAARA TVAEWKDSLN EAWADLLELL DTRGQVLAAA
YELQRFLHGA RQALARVQHK QQQLPDGTGR DLNAAEALQR RHCAYEHDIQ ALSPQVQQVQ
DDGHRLQKAY AGDKAEEIGR HMQAVAEAWA QLQGSSAARR QLLLDTTDKF RFFKAVRELM
LWMDEVNLQM DAQERPRDVS SADLVIKNQQ GIKAEIEARA DRFSSCIDMG KELLARSHYA
AEEISEKLSQ LQARRQETAE KWQEKMDWLQ LVLEVLVFGR DAGMAEAWLC SQEPLVRSAE
LGCTVDEVES LIKRHEAFQK SAVAWEERFC ALEKLTALEE REKERKRKRE EEERRKQPPA
PEPTASVPPG DLVGGQTASD TTWDGTQPRP PPSTQAPSVN GVCTDGEPSQ PLLGQQRLEH
SSFPEGPGPG SGDEANGPRG ERQTRTRGPA PSAMPQSRST ESAHAATLPP RGPEPSAQEQ
MEGMLCRKQE MEAFGKKAAN RSWQNVYCVL RRGSLGFYKD AKAASAGVPY HGEVPVSLAR
AQGSVAFDYR KRKHVFKLGL QDGKEYLFQA KDEAEMSSWL RVVNAAIATA SSASGEPEEP
VVPSTTRGMT RAMTMPPVSP VGAEGPVVLR SKDGRERERE KRFSFFKKNK
