(data stored in ACNUC32233 zone)

SWISSPROT: 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   11-DEC-2019, entry version 193.
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 mutations
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 mutations
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};
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.
DR   RefSeq; XP_005274249.1; XM_005274192.4. [O15020-1]
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   SMR; O15020; -.
DR   BioGrid; 112590; 42.
DR   DIP; DIP-47270N; -.
DR   IntAct; O15020; 32.
DR   MINT; O15020; -.
DR   STRING; 9606.ENSP00000432568; -.
DR   CarbonylDB; O15020; -.
DR   iPTMnet; 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   DNASU; 6712; -.
DR   Ensembl; ENST00000309996; ENSP00000311489; ENSG00000173898. [O15020-1]
DR   Ensembl; ENST00000529997; ENSP00000433593; ENSG00000173898. [O15020-2]
DR   Ensembl; ENST00000533211; ENSP00000432568; ENSG00000173898. [O15020-1]
DR   GeneID; 6712; -.
DR   KEGG; hsa:6712; -.
DR   UCSC; uc001ojc.2; human. [O15020-1]
DR   CTD; 6712; -.
DR   DisGeNET; 6712; -.
DR   EuPathDB; HostDB:ENSG00000173898.11; -.
DR   GeneCards; SPTBN2; -.
DR   HGNC; HGNC:11276; SPTBN2.
DR   HPA; CAB009844; -.
DR   HPA; HPA039293; -.
DR   HPA; HPA043529; -.
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   eggNOG; KOG0035; Eukaryota.
DR   eggNOG; COG5069; LUCA.
DR   GeneTree; ENSGT00940000158847; -.
DR   HOGENOM; HOG000007281; -.
DR   InParanoid; O15020; -.
DR   KO; K06115; -.
DR   OMA; SKWDHLL; -.
DR   OrthoDB; 543832at2759; -.
DR   PhylomeDB; O15020; -.
DR   TreeFam; TF313446; -.
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   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 157 organ(s), highest expression level in frontal cortex.
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; IDA:HPA.
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:0043025; C:neuronal cell body; IEA:Ensembl.
DR   GO; GO:0098688; C:parallel fiber to Purkinje cell synapse; IEA:Ensembl.
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: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; IEA:Ensembl.
DR   GO; GO:0051693; P:actin filament capping; IEA:UniProtKB-KW.
DR   GO; GO:0030534; P:adult behavior; IEA:Ensembl.
DR   GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; TAS:Reactome.
DR   GO; GO:0007411; P:axon guidance; TAS:Reactome.
DR   GO; GO:0021692; P:cerebellar Purkinje cell layer morphogenesis; IEA:Ensembl.
DR   GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; TAS:Reactome.
DR   GO; GO:0000165; P:MAPK cascade; TAS:Reactome.
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   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;
DR   PRODOM; O15020.
DR   SWISS-2DPAGE; O15020.
KW   3D-structure; Acetylation; Actin capping; Actin-binding;
KW   Alternative splicing; Cytoplasm; Cytoskeleton; Disease mutation;
KW   Neurodegeneration; Phosphoprotein; Polymorphism; Reference proteome;
KW   Repeat; Spinocerebellar ataxia.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000244|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   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000244|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:0000244|PubMed:24275569"
FT   MOD_RES         959
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:24275569"
FT   MOD_RES         1073
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:24275569"
FT   MOD_RES         2171
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:17081983,
FT                   ECO:0000244|PubMed:18669648, ECO:0000244|PubMed:20068231,
FT                   ECO:0000244|PubMed:21406692, ECO:0000244|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:0000244|PubMed:23186163,
FT                   ECO:0000244|PubMed:24275569"
FT   MOD_RES         2359
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:18669648,
FT                   ECO:0000244|PubMed:20068231, ECO:0000244|PubMed:23186163,
FT                   ECO:0000244|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:0000244|PDB:1WYQ"
FT   STRAND          193..195
FT                   /evidence="ECO:0000244|PDB:1WYQ"
FT   STRAND          205..208
FT                   /evidence="ECO:0000244|PDB:1WYQ"
FT   HELIX           209..218
FT                   /evidence="ECO:0000244|PDB:1WYQ"
FT   TURN            220..222
FT                   /evidence="ECO:0000244|PDB:1WYQ"
FT   TURN            225..227
FT                   /evidence="ECO:0000244|PDB:1WYQ"
FT   HELIX           234..246
FT                   /evidence="ECO:0000244|PDB:1WYQ"
FT   TURN            256..258
FT                   /evidence="ECO:0000244|PDB:1WYQ"
FT   STRAND          261..263
FT                   /evidence="ECO:0000244|PDB:1WYQ"
FT   HELIX           266..282
FT                   /evidence="ECO:0000244|PDB:1WYQ"
FT   STRAND          283..285
FT                   /evidence="ECO:0000244|PDB:1WYQ"
FT   STRAND          2221..2233
FT                   /evidence="ECO:0000244|PDB:1WJM"
FT   STRAND          2244..2251
FT                   /evidence="ECO:0000244|PDB:1WJM"
FT   STRAND          2254..2260
FT                   /evidence="ECO:0000244|PDB:1WJM"
FT   HELIX           2261..2264
FT                   /evidence="ECO:0000244|PDB:1WJM"
FT   TURN            2265..2267
FT                   /evidence="ECO:0000244|PDB:1WJM"
FT   STRAND          2269..2272
FT                   /evidence="ECO:0000244|PDB:1WJM"
FT   STRAND          2282..2285
FT                   /evidence="ECO:0000244|PDB:1WJM"
FT   STRAND          2293..2299
FT                   /evidence="ECO:0000244|PDB:1WJM"
FT   STRAND          2301..2303
FT                   /evidence="ECO:0000244|PDB:1WJM"
FT   STRAND          2305..2309
FT                   /evidence="ECO:0000244|PDB:1WJM"
FT   HELIX           2313..2328
FT                   /evidence="ECO:0000244|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
//

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