Full text data of SPTBN1
SPTBN1
(SPTB2)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Spectrin beta chain, non-erythrocytic 1 (Beta-II spectrin; Fodrin beta chain; Spectrin, non-erythroid beta chain 1)
Spectrin beta chain, non-erythrocytic 1 (Beta-II spectrin; Fodrin beta chain; Spectrin, non-erythroid beta chain 1)
hRBCD
IPI00005614
IPI00005614 Splice isoform Long of Q01082 Spectrin beta chain, brain 1 Splice isoform Long of Q01082 Spectrin beta chain, brain 1 membrane 1 2 2 2 2 1 2 2 n/a n/a n/a 1 n/a 5 4 n/a n/a n/a 7 7 cytoskeleton n/a found at its expected molecular weight found at molecular weight
IPI00005614 Splice isoform Long of Q01082 Spectrin beta chain, brain 1 Splice isoform Long of Q01082 Spectrin beta chain, brain 1 membrane 1 2 2 2 2 1 2 2 n/a n/a n/a 1 n/a 5 4 n/a n/a n/a 7 7 cytoskeleton n/a found at its expected molecular weight found at molecular weight
UniProt
Q01082
ID SPTB2_HUMAN Reviewed; 2364 AA.
AC Q01082; B2RP63; O60837; Q16057; Q53R99; Q59ER3; Q8IX99;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
read moreDT 17-OCT-2006, sequence version 2.
DT 22-JAN-2014, entry version 149.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG), AND VARIANT HIS-1411.
RC TISSUE=Brain;
RX PubMed=1527002;
RA Hu R.J., Watanabe M., Bennett V.;
RT "Characterization of human brain cDNA encoding the general isoform of
RT beta-spectrin.";
RL J. Biol. Chem. 267:18715-18722(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY, AND
RP VARIANT 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-
RT cell 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.,
RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA 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.,
RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA 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.,
RA Waterston R.H., Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2
RT and 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: 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.,
RA Morrow J.S., 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;
RA Hayes N.V.L., Scott C., Heerkens E., Ohanian V., Maggs A.M.,
RA Pinder J.C., 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 MASS SPECTROMETRY.
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.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2102, AND MASS
RP SPECTROMETRY.
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
RT cells and high confident phosphopeptide identification by cross-
RT validation of 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 MASS
RP SPECTROMETRY.
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 MASS
RP SPECTROMETRY.
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
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2102; SER-2138;
RP SER-2165; SER-2169; THR-2187; THR-2320; THR-2328 AND SER-2341,
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14 (ISOFORM 2), AND MASS
RP SPECTROMETRY.
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, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2102, AND MASS
RP SPECTROMETRY.
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
RP AND SER-2341, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14
RP (ISOFORM 2), AND MASS SPECTROMETRY.
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 MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., 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 MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation 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.,
RA Buerckstuemmer T., 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;
RP SER-2138; SER-2160; SER-2161; SER-2164; SER-2169; SER-2319; THR-2320
RP AND SER-2340, AND MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [22]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, AND MASS SPECTROMETRY.
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.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [23]
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-
RT associated protein 1) links its interaction with spectrin and
RT calmodulin to neurite outgrowth.";
RL J. Neurochem. 0:0-0(2013).
RN [24]
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 [25]
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,
CC interacts with calmodulin in a calcium-dependent manner and is
CC thus candidate for the calcium-dependent movement of the
CC cytoskeleton at the membrane.
CC -!- SUBUNIT: Like erythrocyte spectrin, the spectrin-like proteins are
CC capable to form dimers which can further associate to tetramers.
CC Interacts with CAMSAP1. Interacts with ANK2. Isoform Short cannot
CC bind to the axonal protein fodaxin.
CC -!- INTERACTION:
CC Q9NRI5:DISC1; NbExp=3; IntAct=EBI-351561, EBI-529989;
CC P02549:SPTA1; NbExp=3; IntAct=EBI-351561, EBI-375617;
CC Q13813:SPTAN1; NbExp=7; IntAct=EBI-351561, EBI-351450;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton (By similarity).
CC Cytoplasm, myofibril, sarcomere, M line (By similarity).
CC Note=Colocalizes with ANK2 in a distinct intracellular compartment
CC of neonatal cardiomyocytes (By similarity).
CC -!- SUBCELLULAR LOCATION: Isoform 2: Cell membrane; Peripheral
CC membrane protein; Cytoplasmic side (By similarity).
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 Note=Contains a phosphoserine at position 8 (By similarity).
CC Contains a phosphoserine at position 10. Contains a
CC phosphoserine at position 14;
CC -!- TISSUE SPECIFICITY: Isoform 2 is present in brain, lung and kidney
CC (at protein level).
CC -!- PTM: Isoform 2 is phosphorylated on Ser-8 and Ser-10 (By
CC similarity).
CC -!- SIMILARITY: Belongs to the spectrin family.
CC -!- SIMILARITY: Contains 2 CH (calponin-homology) domains.
CC -!- SIMILARITY: Contains 1 PH domain.
CC -!- SIMILARITY: Contains 17 spectrin repeats.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD92985.1; Type=Erroneous initiation;
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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 PIR; A44159; A44159.
DR PIR; A47213; A47213.
DR RefSeq; NP_003119.2; NM_003128.2.
DR RefSeq; NP_842565.2; NM_178313.2.
DR RefSeq; XP_005264574.1; XM_005264517.1.
DR UniGene; Hs.503178; -.
DR UniGene; Hs.705692; -.
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 ProteinModelPortal; Q01082; -.
DR SMR; Q01082; 48-280, 299-2086, 2200-2305.
DR DIP; DIP-33182N; -.
DR IntAct; Q01082; 40.
DR MINT; MINT-1136298; -.
DR STRING; 9606.ENSP00000349259; -.
DR PhosphoSite; Q01082; -.
DR DMDM; 116242799; -.
DR PaxDb; Q01082; -.
DR PRIDE; Q01082; -.
DR Ensembl; ENST00000333896; ENSP00000334156; ENSG00000115306.
DR Ensembl; ENST00000356805; ENSP00000349259; ENSG00000115306.
DR GeneID; 6711; -.
DR KEGG; hsa:6711; -.
DR UCSC; uc002rxu.3; human.
DR CTD; 6711; -.
DR GeneCards; GC02P054665; -.
DR H-InvDB; HIX0002055; -.
DR HGNC; HGNC:11275; SPTBN1.
DR HPA; HPA012685; -.
DR HPA; HPA013149; -.
DR MIM; 182790; gene.
DR neXtProt; NX_Q01082; -.
DR PharmGKB; PA36104; -.
DR eggNOG; COG5069; -.
DR HOVERGEN; HBG057912; -.
DR InParanoid; Q01082; -.
DR KO; K06115; -.
DR OMA; LWQFYWD; -.
DR OrthoDB; EOG73RB9J; -.
DR Reactome; REACT_111045; Developmental Biology.
DR Reactome; REACT_111155; Cell-Cell communication.
DR Reactome; REACT_127416; Developmental Biology.
DR SignaLink; Q01082; -.
DR ChiTaRS; SPTBN1; human.
DR EvolutionaryTrace; Q01082; -.
DR GeneWiki; SPTBN1; -.
DR GenomeRNAi; 6711; -.
DR NextBio; 26172; -.
DR PRO; PR:Q01082; -.
DR ArrayExpress; Q01082; -.
DR Bgee; Q01082; -.
DR CleanEx; HS_SPTBN1; -.
DR Genevestigator; Q01082; -.
DR GO; GO:0030673; C:axolemma; ISS:BHF-UCL.
DR GO; GO:0032437; C:cuticular plate; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0031430; C:M band; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; IDA:HGNC.
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:0030506; F:ankyrin binding; NAS:BHF-UCL.
DR GO; GO:0005543; F:phospholipid binding; IEA:InterPro.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; IMP:BHF-UCL.
DR GO; GO:0051693; P:actin filament capping; IEA:UniProtKB-KW.
DR GO; GO:0007411; P:axon guidance; TAS:Reactome.
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:0072661; P:protein targeting to plasma membrane; IMP:BHF-UCL.
DR GO; GO:0007184; P:SMAD protein import into nucleus; IEA:Ensembl.
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; IPR001605; PH_dom-spectrin-type.
DR InterPro; IPR011993; PH_like_dom.
DR InterPro; IPR001849; Pleckstrin_homology.
DR InterPro; IPR018159; Spectrin/alpha-actinin.
DR InterPro; IPR016343; Spectrin_bsu.
DR InterPro; IPR002017; Spectrin_repeat.
DR Pfam; PF00307; CH; 2.
DR Pfam; PF00169; PH; 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;
KW Complete proteome; Cytoplasm; Cytoskeleton; Glycoprotein; Membrane;
KW Phosphoprotein; Polymorphism; Reference proteome; Repeat.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 2364 Spectrin beta chain, non-erythrocytic 1.
FT /FTId=PRO_0000073461.
FT DOMAIN 1 275 Actin-binding.
FT DOMAIN 54 158 CH 1.
FT DOMAIN 173 275 CH 2.
FT REPEAT 303 411 Spectrin 1.
FT REPEAT 423 525 Spectrin 2.
FT REPEAT 530 636 Spectrin 3.
FT REPEAT 639 742 Spectrin 4.
FT REPEAT 745 847 Spectrin 5.
FT REPEAT 851 952 Spectrin 6.
FT REPEAT 957 1060 Spectrin 7.
FT REPEAT 1063 1166 Spectrin 8.
FT REPEAT 1169 1257 Spectrin 9.
FT REPEAT 1276 1376 Spectrin 10.
FT REPEAT 1381 1482 Spectrin 11.
FT REPEAT 1486 1590 Spectrin 12.
FT REPEAT 1592 1696 Spectrin 13.
FT REPEAT 1698 1801 Spectrin 14.
FT REPEAT 1805 1907 Spectrin 15.
FT REPEAT 1914 2014 Spectrin 16.
FT REPEAT 2018 2097 Spectrin 17.
FT DOMAIN 2197 2307 PH.
FT REGION 1563 2093 Interaction with ANK2.
FT REGION 2149 2177 Mediates interaction with CAMSAP1.
FT MOD_RES 2 2 N-acetylthreonine.
FT MOD_RES 90 90 N6-acetyllysine.
FT MOD_RES 817 817 Phosphoserine.
FT MOD_RES 825 825 Phosphoserine.
FT MOD_RES 1057 1057 Phosphoserine.
FT MOD_RES 1447 1447 Phosphoserine.
FT MOD_RES 1805 1805 Phosphotyrosine (By similarity).
FT MOD_RES 1815 1815 N6-acetyllysine.
FT MOD_RES 1913 1913 N6-acetyllysine.
FT MOD_RES 1989 1989 N6-acetyllysine.
FT MOD_RES 2102 2102 Phosphoserine.
FT MOD_RES 2128 2128 Phosphoserine.
FT MOD_RES 2138 2138 Phosphoserine.
FT MOD_RES 2160 2160 Phosphoserine.
FT MOD_RES 2161 2161 Phosphoserine.
FT MOD_RES 2164 2164 Phosphoserine.
FT MOD_RES 2165 2165 Phosphoserine.
FT MOD_RES 2169 2169 Phosphoserine.
FT MOD_RES 2187 2187 Phosphothreonine.
FT MOD_RES 2195 2195 Phosphothreonine (By similarity).
FT MOD_RES 2319 2319 Phosphoserine.
FT MOD_RES 2320 2320 Phosphothreonine.
FT MOD_RES 2328 2328 Phosphothreonine.
FT MOD_RES 2340 2340 Phosphoserine.
FT MOD_RES 2341 2341 Phosphoserine.
FT CARBOHYD 2324 2324 O-linked (GlcNAc) (By similarity).
FT VAR_SEQ 1 49 MTTTVATDYDNIEIQQQYSDVNNRWDVDDWDNENSSARLFE
FT RSRIKALA -> MELQRTSSISGPLSPAYTGQVPYNYNQLE
FT GRFKQLQ (in isoform 2).
FT /FTId=VSP_026054.
FT VAR_SEQ 2141 2225 MAETVDTSEMVNGATEQRTSSKESSPIPSPTSDRKAKTALP
FT AQSAATLPARTQETPSAQMEGFLNRKHEWEAHNKKASSRSW
FT HNV -> VSYRSQTYQNYKNFNSRRTASDQPWSGL (in
FT isoform 2).
FT /FTId=VSP_026055.
FT VAR_SEQ 2141 2168 MAETVDTSEMVNGATEQRTSSKESSPIP -> VSYRSQTYQ
FT NYKNFNSRRTASDQPWSGL (in isoform Short).
FT /FTId=VSP_000720.
FT VAR_SEQ 2169 2364 Missing (in isoform Short).
FT /FTId=VSP_000721.
FT VAR_SEQ 2226 2364 Missing (in isoform 2).
FT /FTId=VSP_026056.
FT VARIANT 1411 1411 D -> H (in dbSNP:rs1052790).
FT /FTId=VAR_032641.
FT CONFLICT 583 583 R -> W (in Ref. 3; BAD92985).
FT HELIX 174 186
FT TURN 187 189
FT STRAND 196 199
FT HELIX 200 202
FT HELIX 206 215
FT HELIX 217 219
FT HELIX 222 224
FT HELIX 230 245
FT HELIX 253 256
FT STRAND 257 260
FT HELIX 263 277
FT HELIX 1697 1721
FT HELIX 1730 1767
FT HELIX 1773 1826
FT HELIX 1836 1852
FT HELIX 1854 1873
FT HELIX 1877 1935
FT HELIX 1943 1962
FT HELIX 1964 1979
FT HELIX 1985 2014
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
//
ID SPTB2_HUMAN Reviewed; 2364 AA.
AC Q01082; B2RP63; O60837; Q16057; Q53R99; Q59ER3; Q8IX99;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
read moreDT 17-OCT-2006, sequence version 2.
DT 22-JAN-2014, entry version 149.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG), AND VARIANT HIS-1411.
RC TISSUE=Brain;
RX PubMed=1527002;
RA Hu R.J., Watanabe M., Bennett V.;
RT "Characterization of human brain cDNA encoding the general isoform of
RT beta-spectrin.";
RL J. Biol. Chem. 267:18715-18722(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY, AND
RP VARIANT 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-
RT cell 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.,
RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA 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.,
RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA 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.,
RA Waterston R.H., Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2
RT and 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: 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.,
RA Morrow J.S., 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;
RA Hayes N.V.L., Scott C., Heerkens E., Ohanian V., Maggs A.M.,
RA Pinder J.C., 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 MASS SPECTROMETRY.
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.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2102, AND MASS
RP SPECTROMETRY.
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
RT cells and high confident phosphopeptide identification by cross-
RT validation of 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 MASS
RP SPECTROMETRY.
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 MASS
RP SPECTROMETRY.
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
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2102; SER-2138;
RP SER-2165; SER-2169; THR-2187; THR-2320; THR-2328 AND SER-2341,
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14 (ISOFORM 2), AND MASS
RP SPECTROMETRY.
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, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2102, AND MASS
RP SPECTROMETRY.
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
RP AND SER-2341, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14
RP (ISOFORM 2), AND MASS SPECTROMETRY.
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 MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., 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 MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation 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.,
RA Buerckstuemmer T., 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;
RP SER-2138; SER-2160; SER-2161; SER-2164; SER-2169; SER-2319; THR-2320
RP AND SER-2340, AND MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [22]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, AND MASS SPECTROMETRY.
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.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [23]
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-
RT associated protein 1) links its interaction with spectrin and
RT calmodulin to neurite outgrowth.";
RL J. Neurochem. 0:0-0(2013).
RN [24]
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 [25]
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,
CC interacts with calmodulin in a calcium-dependent manner and is
CC thus candidate for the calcium-dependent movement of the
CC cytoskeleton at the membrane.
CC -!- SUBUNIT: Like erythrocyte spectrin, the spectrin-like proteins are
CC capable to form dimers which can further associate to tetramers.
CC Interacts with CAMSAP1. Interacts with ANK2. Isoform Short cannot
CC bind to the axonal protein fodaxin.
CC -!- INTERACTION:
CC Q9NRI5:DISC1; NbExp=3; IntAct=EBI-351561, EBI-529989;
CC P02549:SPTA1; NbExp=3; IntAct=EBI-351561, EBI-375617;
CC Q13813:SPTAN1; NbExp=7; IntAct=EBI-351561, EBI-351450;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton (By similarity).
CC Cytoplasm, myofibril, sarcomere, M line (By similarity).
CC Note=Colocalizes with ANK2 in a distinct intracellular compartment
CC of neonatal cardiomyocytes (By similarity).
CC -!- SUBCELLULAR LOCATION: Isoform 2: Cell membrane; Peripheral
CC membrane protein; Cytoplasmic side (By similarity).
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 Note=Contains a phosphoserine at position 8 (By similarity).
CC Contains a phosphoserine at position 10. Contains a
CC phosphoserine at position 14;
CC -!- TISSUE SPECIFICITY: Isoform 2 is present in brain, lung and kidney
CC (at protein level).
CC -!- PTM: Isoform 2 is phosphorylated on Ser-8 and Ser-10 (By
CC similarity).
CC -!- SIMILARITY: Belongs to the spectrin family.
CC -!- SIMILARITY: Contains 2 CH (calponin-homology) domains.
CC -!- SIMILARITY: Contains 1 PH domain.
CC -!- SIMILARITY: Contains 17 spectrin repeats.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD92985.1; Type=Erroneous initiation;
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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 PIR; A44159; A44159.
DR PIR; A47213; A47213.
DR RefSeq; NP_003119.2; NM_003128.2.
DR RefSeq; NP_842565.2; NM_178313.2.
DR RefSeq; XP_005264574.1; XM_005264517.1.
DR UniGene; Hs.503178; -.
DR UniGene; Hs.705692; -.
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 ProteinModelPortal; Q01082; -.
DR SMR; Q01082; 48-280, 299-2086, 2200-2305.
DR DIP; DIP-33182N; -.
DR IntAct; Q01082; 40.
DR MINT; MINT-1136298; -.
DR STRING; 9606.ENSP00000349259; -.
DR PhosphoSite; Q01082; -.
DR DMDM; 116242799; -.
DR PaxDb; Q01082; -.
DR PRIDE; Q01082; -.
DR Ensembl; ENST00000333896; ENSP00000334156; ENSG00000115306.
DR Ensembl; ENST00000356805; ENSP00000349259; ENSG00000115306.
DR GeneID; 6711; -.
DR KEGG; hsa:6711; -.
DR UCSC; uc002rxu.3; human.
DR CTD; 6711; -.
DR GeneCards; GC02P054665; -.
DR H-InvDB; HIX0002055; -.
DR HGNC; HGNC:11275; SPTBN1.
DR HPA; HPA012685; -.
DR HPA; HPA013149; -.
DR MIM; 182790; gene.
DR neXtProt; NX_Q01082; -.
DR PharmGKB; PA36104; -.
DR eggNOG; COG5069; -.
DR HOVERGEN; HBG057912; -.
DR InParanoid; Q01082; -.
DR KO; K06115; -.
DR OMA; LWQFYWD; -.
DR OrthoDB; EOG73RB9J; -.
DR Reactome; REACT_111045; Developmental Biology.
DR Reactome; REACT_111155; Cell-Cell communication.
DR Reactome; REACT_127416; Developmental Biology.
DR SignaLink; Q01082; -.
DR ChiTaRS; SPTBN1; human.
DR EvolutionaryTrace; Q01082; -.
DR GeneWiki; SPTBN1; -.
DR GenomeRNAi; 6711; -.
DR NextBio; 26172; -.
DR PRO; PR:Q01082; -.
DR ArrayExpress; Q01082; -.
DR Bgee; Q01082; -.
DR CleanEx; HS_SPTBN1; -.
DR Genevestigator; Q01082; -.
DR GO; GO:0030673; C:axolemma; ISS:BHF-UCL.
DR GO; GO:0032437; C:cuticular plate; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0031430; C:M band; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; IDA:HGNC.
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:0030506; F:ankyrin binding; NAS:BHF-UCL.
DR GO; GO:0005543; F:phospholipid binding; IEA:InterPro.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; IMP:BHF-UCL.
DR GO; GO:0051693; P:actin filament capping; IEA:UniProtKB-KW.
DR GO; GO:0007411; P:axon guidance; TAS:Reactome.
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:0072661; P:protein targeting to plasma membrane; IMP:BHF-UCL.
DR GO; GO:0007184; P:SMAD protein import into nucleus; IEA:Ensembl.
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; IPR001605; PH_dom-spectrin-type.
DR InterPro; IPR011993; PH_like_dom.
DR InterPro; IPR001849; Pleckstrin_homology.
DR InterPro; IPR018159; Spectrin/alpha-actinin.
DR InterPro; IPR016343; Spectrin_bsu.
DR InterPro; IPR002017; Spectrin_repeat.
DR Pfam; PF00307; CH; 2.
DR Pfam; PF00169; PH; 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;
KW Complete proteome; Cytoplasm; Cytoskeleton; Glycoprotein; Membrane;
KW Phosphoprotein; Polymorphism; Reference proteome; Repeat.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 2364 Spectrin beta chain, non-erythrocytic 1.
FT /FTId=PRO_0000073461.
FT DOMAIN 1 275 Actin-binding.
FT DOMAIN 54 158 CH 1.
FT DOMAIN 173 275 CH 2.
FT REPEAT 303 411 Spectrin 1.
FT REPEAT 423 525 Spectrin 2.
FT REPEAT 530 636 Spectrin 3.
FT REPEAT 639 742 Spectrin 4.
FT REPEAT 745 847 Spectrin 5.
FT REPEAT 851 952 Spectrin 6.
FT REPEAT 957 1060 Spectrin 7.
FT REPEAT 1063 1166 Spectrin 8.
FT REPEAT 1169 1257 Spectrin 9.
FT REPEAT 1276 1376 Spectrin 10.
FT REPEAT 1381 1482 Spectrin 11.
FT REPEAT 1486 1590 Spectrin 12.
FT REPEAT 1592 1696 Spectrin 13.
FT REPEAT 1698 1801 Spectrin 14.
FT REPEAT 1805 1907 Spectrin 15.
FT REPEAT 1914 2014 Spectrin 16.
FT REPEAT 2018 2097 Spectrin 17.
FT DOMAIN 2197 2307 PH.
FT REGION 1563 2093 Interaction with ANK2.
FT REGION 2149 2177 Mediates interaction with CAMSAP1.
FT MOD_RES 2 2 N-acetylthreonine.
FT MOD_RES 90 90 N6-acetyllysine.
FT MOD_RES 817 817 Phosphoserine.
FT MOD_RES 825 825 Phosphoserine.
FT MOD_RES 1057 1057 Phosphoserine.
FT MOD_RES 1447 1447 Phosphoserine.
FT MOD_RES 1805 1805 Phosphotyrosine (By similarity).
FT MOD_RES 1815 1815 N6-acetyllysine.
FT MOD_RES 1913 1913 N6-acetyllysine.
FT MOD_RES 1989 1989 N6-acetyllysine.
FT MOD_RES 2102 2102 Phosphoserine.
FT MOD_RES 2128 2128 Phosphoserine.
FT MOD_RES 2138 2138 Phosphoserine.
FT MOD_RES 2160 2160 Phosphoserine.
FT MOD_RES 2161 2161 Phosphoserine.
FT MOD_RES 2164 2164 Phosphoserine.
FT MOD_RES 2165 2165 Phosphoserine.
FT MOD_RES 2169 2169 Phosphoserine.
FT MOD_RES 2187 2187 Phosphothreonine.
FT MOD_RES 2195 2195 Phosphothreonine (By similarity).
FT MOD_RES 2319 2319 Phosphoserine.
FT MOD_RES 2320 2320 Phosphothreonine.
FT MOD_RES 2328 2328 Phosphothreonine.
FT MOD_RES 2340 2340 Phosphoserine.
FT MOD_RES 2341 2341 Phosphoserine.
FT CARBOHYD 2324 2324 O-linked (GlcNAc) (By similarity).
FT VAR_SEQ 1 49 MTTTVATDYDNIEIQQQYSDVNNRWDVDDWDNENSSARLFE
FT RSRIKALA -> MELQRTSSISGPLSPAYTGQVPYNYNQLE
FT GRFKQLQ (in isoform 2).
FT /FTId=VSP_026054.
FT VAR_SEQ 2141 2225 MAETVDTSEMVNGATEQRTSSKESSPIPSPTSDRKAKTALP
FT AQSAATLPARTQETPSAQMEGFLNRKHEWEAHNKKASSRSW
FT HNV -> VSYRSQTYQNYKNFNSRRTASDQPWSGL (in
FT isoform 2).
FT /FTId=VSP_026055.
FT VAR_SEQ 2141 2168 MAETVDTSEMVNGATEQRTSSKESSPIP -> VSYRSQTYQ
FT NYKNFNSRRTASDQPWSGL (in isoform Short).
FT /FTId=VSP_000720.
FT VAR_SEQ 2169 2364 Missing (in isoform Short).
FT /FTId=VSP_000721.
FT VAR_SEQ 2226 2364 Missing (in isoform 2).
FT /FTId=VSP_026056.
FT VARIANT 1411 1411 D -> H (in dbSNP:rs1052790).
FT /FTId=VAR_032641.
FT CONFLICT 583 583 R -> W (in Ref. 3; BAD92985).
FT HELIX 174 186
FT TURN 187 189
FT STRAND 196 199
FT HELIX 200 202
FT HELIX 206 215
FT HELIX 217 219
FT HELIX 222 224
FT HELIX 230 245
FT HELIX 253 256
FT STRAND 257 260
FT HELIX 263 277
FT HELIX 1697 1721
FT HELIX 1730 1767
FT HELIX 1773 1826
FT HELIX 1836 1852
FT HELIX 1854 1873
FT HELIX 1877 1935
FT HELIX 1943 1962
FT HELIX 1964 1979
FT HELIX 1985 2014
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
//
MIM
182790
*RECORD*
*FIELD* NO
182790
*FIELD* TI
*182790 SPECTRIN, BETA, NONERYTHROCYTIC, 1; SPTBN1
;;SPECTRIN, NONERYTHROID, BETA SUBUNIT; SPTB2;;
read moreBETA-SPECTRIN, GENERAL FORM;;
BETA-G SPECTRIN;;
FODRIN, BETA;;
EMBRYONIC LIVER BETA-FODRIN; ELF;;
SPECTRIN, BETA-II
*FIELD* TX
DESCRIPTION
Spectrin is a tetrameric cytoskeletal protein essential for
determination of cell shape, resilience of membranes to mechanical
stress, positioning of transmembrane proteins, and organization of
organelles and molecular traffic. Alpha- and beta-spectrin subunits form
antiparallel dimers that self associate to give the spectrin tetramer.
Beta subunits, such as SPTBN1, contain most of the spectrin binding
activity (Hayes et al., 2000).
CLONING
Immunochemical studies demonstrate the existence of beta-spectrin-like
polypeptides in nonerythroid tissues. Watkins et al. (1988) obtained a
genomic clone for nonerythroid beta-spectrin by screening a DNA library
with a synthetic oligonucleotide probe corresponding to human erythroid
beta-spectrin (182870) cDNA. The genomic clone showed 76% homology to
the erythroid beta-spectrin cDNA when translated to amino acid sequence.
By screening a human brainstem expression library with bovine
alpha-spectrin, followed by screening a human hippocampus cDNA library,
Hu et al. (1992) cloned SPTBN1, which they designated 'general form of
beta-spectrin,' or beta-G spectrin, to distinguish it from erythrocyte
beta-spectrin, or beta-R spectrin (SPTB). The deduced 2,364-amino acid
SPTBN1 protein has a calculated molecular mass of 274.5 kD. Like SPTB,
SPTBN1 has a putative N-terminal actin-binding domain, a central tandem
series of 17 repeats of a 106-amino acid motif, and a C-terminal domain.
Northern blot analysis of several rat tissues detected highest
expression in lung, followed by kidney, brain, thymus, heart, and liver.
Western blot analysis of cytosolic and membrane fractions of rat tissues
revealed Sptbn1 proteins of 275 to 285 kD that were enriched in membrane
fractions of brain, kidney, and lung.
Chang et al. (1993) found that the genomic DNA for human brain
beta-fodrin contained regions that cross-hybridized with an erythroid
beta-spectrin cDNA probe and that the DNA sequence of these regions
showed a high degree of identity and a similar exon/intron organization.
Mishra et al. (1999) cloned 3 isoforms of mouse beta-spectrin, which
they called Elf for 'embryonic liver beta-fodrin.' The longest isoform,
Elf3, comprises 2,154 residues and is characterized by an actin-binding
domain, a long repeat domain, and a short regulatory domain remarkable
for the absence of a PH domain. Northern blot analysis demonstrated an
abundant 9.0-kb Elf3 transcript in brain, liver, and heart tissues.
Immunohistochemical studies demonstrated Elf labeling of the basolateral
or sinusoidal membrane surface, as well as a granular cytoplasmic
pattern in hepatocytes. Mishra et al. (1999) demonstrated that Elf3
plays a vital role in hepatocyte differentiation and intrahepatic bile
duct formation.
By database analysis and PCR of a skeletal muscle cDNA library, Hayes et
al. (2000) cloned 2 partial SPTBN1 3-prime splice variants, which they
designated sigma-1 and sigma-2. The sigma-1 variant is identical to the
3-prime sequence of the SPTBN1 cDNA cloned by Hu et al. (1992). The
sigma-2 variant encodes a protein with a shorter C terminus that lacks
the pleckstrin homology domain of the longer isoform and has 28 unique
C-terminal residues. Antibodies raised to the short C terminus detected
240-kD proteins in rat cardiac and skeletal muscle and in rat nervous
tissue; in cerebellum and forebrain, additional 270-kD proteins were
detected. In rat heart and skeletal muscle, both long and short
C-terminal forms localized in the region of the Z line. The central
region of the sarcomere, coincident with the M line, was selectively
labeled with antibodies to the short C-terminal isoform. In cerebellum,
parallel fibers showed the long form, but not the short form. In
cultured cerebellar granule neurons, the long form was dominant in
neurites, while the short form was more abundant in cell bodies. The
long form was also readily detected in postsynaptic density preparations
of fractionated rat brain, but the short form was only weakly
represented.
By database analysis and PCR of a brain cDNA library, Chen et al. (2001)
cloned a full-length cDNA encoding the short SPTBN1 isoform. The deduced
2,155-amino acid protein has a calculated molecular mass of 251 kD. In
addition to the variation found by Hayes et al. (2000) in the C-terminal
domain, Chen et al. (2001) found that the first 36 N-terminal amino
acids differ from those in the long isoform, and the actin-binding
domain is 13 amino acids shorter. Northern blot analysis of several
human tissues detected a 7.5-kb transcript expressed abundantly in
brain, kidney, and lung, and more weakly in liver. A 9.5-kb transcript
was also detected in lung. Western blot analysis detected the short
SPTBN1 isoform at an apparent molecular mass of 225 kD in brain, lung,
kidney, and liver. The longer isoform was found at an apparent molecular
mass of 240 kD in the same tissues.
GENE FUNCTION
Hayes et al. (2000) found that the C terminus of the long SPTBN1 isoform
bound fodaxin partially purified from rat brain, but the short isoform
did not.
GENE STRUCTURE
Chen et al. (2001) determined that the SPTBN1 gene spans more than 180
kb and contains a total of 38 exons. Alternative splicing results in
transcripts with unique 5-prime and 3-prime ends. The first exon and
part of the second exon in each transcript is noncoding.
MAPPING
Watkins et al. (1988) used a genomic clone to map the nonerythroid
beta-spectrin gene to human chromosome 2 by study of DNA from somatic
cell hybrids.
By hybridization to DNA of a panel of somatic hybrid cell lines, Chang
et al. (1993) mapped the gene to chromosome 2 and localized the gene to
2p21 by isotopic in situ hybridization.
ANIMAL MODEL
Disruption of ELF leads to the disruption of TGF-beta (190180) signaling
by Smad proteins in mice. Elf -/- mice exhibit a phenotype similar to
Smad2/Smad3 double heterozygous mice, with midgestational death due to
gastrointestinal, liver, neural, and heart defects. Tang et al. (2003)
showed that TGF-beta triggers phosphorylation and association of Elf
with Smad3 and Smad4, followed by nuclear translocation. Elf deficiency
results in mislocalization of Smad3 and Smad4 and loss of
TGF-beta-dependent transcriptional response, which could be rescued by
overexpression of the carboxy-terminal region of Elf. Tang et al. (2003)
concluded that their study revealed an unexpected molecular link between
a major dynamic scaffolding protein and a key signaling pathway.
*FIELD* RF
1. Chang, J. G.; Scarpa, A.; Eddy, R. L.; Byers, M. G.; Harris, A.
S.; Morrow, J. S.; Watkins, P.; Shows, T. B.; Forget, B. G.: Cloning
of a portion of the chromosomal gene and cDNA for human beta-fodrin,
the nonerythroid form of beta-spectrin. Genomics 17: 287-293, 1993.
2. Chen, Y.; Yu, P.; Lu, D.; Tagle, D. A.; Cai, T.: A novel isoform
of beta-spectrin II localizes to cerebellar-Purkinje-cell bodies and
interacts with neurofibromatosis type 2 gene product schwannomin. J.
Molec. Neurosci. 17: 59-70, 2001.
3. Hayes, N. V. L.; Scott, C.; Heerkens, E.; Ohanian, V.; Maggs, A.
M.; Pinder, J. C.; Kordeli, E.; Baines, A. J.: Identification of
a novel C-terminal variant of beta-II spectrin: two isoforms of beta-II
spectrin have distinct intracellular locations and activities. J.
Cell Sci. 113: 2023-2034, 2000.
4. Hu, R.-J.; Watanabe, M.; Bennett, V.: Characterization of human
brain cDNA encoding the general isoform of beta-spectrin. J. Biol.
Chem. 267: 18715-18722, 1992.
5. Mishra, L.; Cai, T.; Yu, P.; Monga, S. P.; Mishra, B.: Elf3 encodes
a novel 200-kD beta-spectrin: role in liver development. Oncogene 18:
353-364, 1999.
6. Tang, Y.; Katuri, V.; Dillner, A.; Mishra, B.; Deng, C.-X.; Mishra,
L.: Disruption of transforming growth factor-beta signaling in ELF
beta-spectrin-deficient mice. Science 299: 574-577, 2003.
7. Watkins, P. C.; Eddy, R.; Forget, B. G.; Chang, J. G.; Rochelle,
R.; Shows, T. B.: Assignment of a non-erythroid spectrin gene to
human chromosome 2. (Abstract) Am. J. Hum. Genet. 43: A161, 1988.
*FIELD* CN
Patricia A. Hartz - updated: 2/2/2005
Ada Hamosh - updated: 2/3/2003
*FIELD* CD
Victor A. McKusick: 10/7/1988
*FIELD* ED
terry: 02/22/2005
mgross: 2/2/2005
alopez: 2/5/2003
terry: 2/3/2003
mcapotos: 6/7/2000
psherman: 5/22/2000
carol: 4/28/1999
terry: 4/9/1998
terry: 5/22/1996
carol: 8/19/1993
supermim: 3/16/1992
supermim: 3/20/1990
supermim: 2/28/1990
ddp: 10/27/1989
carol: 6/8/1989
*RECORD*
*FIELD* NO
182790
*FIELD* TI
*182790 SPECTRIN, BETA, NONERYTHROCYTIC, 1; SPTBN1
;;SPECTRIN, NONERYTHROID, BETA SUBUNIT; SPTB2;;
read moreBETA-SPECTRIN, GENERAL FORM;;
BETA-G SPECTRIN;;
FODRIN, BETA;;
EMBRYONIC LIVER BETA-FODRIN; ELF;;
SPECTRIN, BETA-II
*FIELD* TX
DESCRIPTION
Spectrin is a tetrameric cytoskeletal protein essential for
determination of cell shape, resilience of membranes to mechanical
stress, positioning of transmembrane proteins, and organization of
organelles and molecular traffic. Alpha- and beta-spectrin subunits form
antiparallel dimers that self associate to give the spectrin tetramer.
Beta subunits, such as SPTBN1, contain most of the spectrin binding
activity (Hayes et al., 2000).
CLONING
Immunochemical studies demonstrate the existence of beta-spectrin-like
polypeptides in nonerythroid tissues. Watkins et al. (1988) obtained a
genomic clone for nonerythroid beta-spectrin by screening a DNA library
with a synthetic oligonucleotide probe corresponding to human erythroid
beta-spectrin (182870) cDNA. The genomic clone showed 76% homology to
the erythroid beta-spectrin cDNA when translated to amino acid sequence.
By screening a human brainstem expression library with bovine
alpha-spectrin, followed by screening a human hippocampus cDNA library,
Hu et al. (1992) cloned SPTBN1, which they designated 'general form of
beta-spectrin,' or beta-G spectrin, to distinguish it from erythrocyte
beta-spectrin, or beta-R spectrin (SPTB). The deduced 2,364-amino acid
SPTBN1 protein has a calculated molecular mass of 274.5 kD. Like SPTB,
SPTBN1 has a putative N-terminal actin-binding domain, a central tandem
series of 17 repeats of a 106-amino acid motif, and a C-terminal domain.
Northern blot analysis of several rat tissues detected highest
expression in lung, followed by kidney, brain, thymus, heart, and liver.
Western blot analysis of cytosolic and membrane fractions of rat tissues
revealed Sptbn1 proteins of 275 to 285 kD that were enriched in membrane
fractions of brain, kidney, and lung.
Chang et al. (1993) found that the genomic DNA for human brain
beta-fodrin contained regions that cross-hybridized with an erythroid
beta-spectrin cDNA probe and that the DNA sequence of these regions
showed a high degree of identity and a similar exon/intron organization.
Mishra et al. (1999) cloned 3 isoforms of mouse beta-spectrin, which
they called Elf for 'embryonic liver beta-fodrin.' The longest isoform,
Elf3, comprises 2,154 residues and is characterized by an actin-binding
domain, a long repeat domain, and a short regulatory domain remarkable
for the absence of a PH domain. Northern blot analysis demonstrated an
abundant 9.0-kb Elf3 transcript in brain, liver, and heart tissues.
Immunohistochemical studies demonstrated Elf labeling of the basolateral
or sinusoidal membrane surface, as well as a granular cytoplasmic
pattern in hepatocytes. Mishra et al. (1999) demonstrated that Elf3
plays a vital role in hepatocyte differentiation and intrahepatic bile
duct formation.
By database analysis and PCR of a skeletal muscle cDNA library, Hayes et
al. (2000) cloned 2 partial SPTBN1 3-prime splice variants, which they
designated sigma-1 and sigma-2. The sigma-1 variant is identical to the
3-prime sequence of the SPTBN1 cDNA cloned by Hu et al. (1992). The
sigma-2 variant encodes a protein with a shorter C terminus that lacks
the pleckstrin homology domain of the longer isoform and has 28 unique
C-terminal residues. Antibodies raised to the short C terminus detected
240-kD proteins in rat cardiac and skeletal muscle and in rat nervous
tissue; in cerebellum and forebrain, additional 270-kD proteins were
detected. In rat heart and skeletal muscle, both long and short
C-terminal forms localized in the region of the Z line. The central
region of the sarcomere, coincident with the M line, was selectively
labeled with antibodies to the short C-terminal isoform. In cerebellum,
parallel fibers showed the long form, but not the short form. In
cultured cerebellar granule neurons, the long form was dominant in
neurites, while the short form was more abundant in cell bodies. The
long form was also readily detected in postsynaptic density preparations
of fractionated rat brain, but the short form was only weakly
represented.
By database analysis and PCR of a brain cDNA library, Chen et al. (2001)
cloned a full-length cDNA encoding the short SPTBN1 isoform. The deduced
2,155-amino acid protein has a calculated molecular mass of 251 kD. In
addition to the variation found by Hayes et al. (2000) in the C-terminal
domain, Chen et al. (2001) found that the first 36 N-terminal amino
acids differ from those in the long isoform, and the actin-binding
domain is 13 amino acids shorter. Northern blot analysis of several
human tissues detected a 7.5-kb transcript expressed abundantly in
brain, kidney, and lung, and more weakly in liver. A 9.5-kb transcript
was also detected in lung. Western blot analysis detected the short
SPTBN1 isoform at an apparent molecular mass of 225 kD in brain, lung,
kidney, and liver. The longer isoform was found at an apparent molecular
mass of 240 kD in the same tissues.
GENE FUNCTION
Hayes et al. (2000) found that the C terminus of the long SPTBN1 isoform
bound fodaxin partially purified from rat brain, but the short isoform
did not.
GENE STRUCTURE
Chen et al. (2001) determined that the SPTBN1 gene spans more than 180
kb and contains a total of 38 exons. Alternative splicing results in
transcripts with unique 5-prime and 3-prime ends. The first exon and
part of the second exon in each transcript is noncoding.
MAPPING
Watkins et al. (1988) used a genomic clone to map the nonerythroid
beta-spectrin gene to human chromosome 2 by study of DNA from somatic
cell hybrids.
By hybridization to DNA of a panel of somatic hybrid cell lines, Chang
et al. (1993) mapped the gene to chromosome 2 and localized the gene to
2p21 by isotopic in situ hybridization.
ANIMAL MODEL
Disruption of ELF leads to the disruption of TGF-beta (190180) signaling
by Smad proteins in mice. Elf -/- mice exhibit a phenotype similar to
Smad2/Smad3 double heterozygous mice, with midgestational death due to
gastrointestinal, liver, neural, and heart defects. Tang et al. (2003)
showed that TGF-beta triggers phosphorylation and association of Elf
with Smad3 and Smad4, followed by nuclear translocation. Elf deficiency
results in mislocalization of Smad3 and Smad4 and loss of
TGF-beta-dependent transcriptional response, which could be rescued by
overexpression of the carboxy-terminal region of Elf. Tang et al. (2003)
concluded that their study revealed an unexpected molecular link between
a major dynamic scaffolding protein and a key signaling pathway.
*FIELD* RF
1. Chang, J. G.; Scarpa, A.; Eddy, R. L.; Byers, M. G.; Harris, A.
S.; Morrow, J. S.; Watkins, P.; Shows, T. B.; Forget, B. G.: Cloning
of a portion of the chromosomal gene and cDNA for human beta-fodrin,
the nonerythroid form of beta-spectrin. Genomics 17: 287-293, 1993.
2. Chen, Y.; Yu, P.; Lu, D.; Tagle, D. A.; Cai, T.: A novel isoform
of beta-spectrin II localizes to cerebellar-Purkinje-cell bodies and
interacts with neurofibromatosis type 2 gene product schwannomin. J.
Molec. Neurosci. 17: 59-70, 2001.
3. Hayes, N. V. L.; Scott, C.; Heerkens, E.; Ohanian, V.; Maggs, A.
M.; Pinder, J. C.; Kordeli, E.; Baines, A. J.: Identification of
a novel C-terminal variant of beta-II spectrin: two isoforms of beta-II
spectrin have distinct intracellular locations and activities. J.
Cell Sci. 113: 2023-2034, 2000.
4. Hu, R.-J.; Watanabe, M.; Bennett, V.: Characterization of human
brain cDNA encoding the general isoform of beta-spectrin. J. Biol.
Chem. 267: 18715-18722, 1992.
5. Mishra, L.; Cai, T.; Yu, P.; Monga, S. P.; Mishra, B.: Elf3 encodes
a novel 200-kD beta-spectrin: role in liver development. Oncogene 18:
353-364, 1999.
6. Tang, Y.; Katuri, V.; Dillner, A.; Mishra, B.; Deng, C.-X.; Mishra,
L.: Disruption of transforming growth factor-beta signaling in ELF
beta-spectrin-deficient mice. Science 299: 574-577, 2003.
7. Watkins, P. C.; Eddy, R.; Forget, B. G.; Chang, J. G.; Rochelle,
R.; Shows, T. B.: Assignment of a non-erythroid spectrin gene to
human chromosome 2. (Abstract) Am. J. Hum. Genet. 43: A161, 1988.
*FIELD* CN
Patricia A. Hartz - updated: 2/2/2005
Ada Hamosh - updated: 2/3/2003
*FIELD* CD
Victor A. McKusick: 10/7/1988
*FIELD* ED
terry: 02/22/2005
mgross: 2/2/2005
alopez: 2/5/2003
terry: 2/3/2003
mcapotos: 6/7/2000
psherman: 5/22/2000
carol: 4/28/1999
terry: 4/9/1998
terry: 5/22/1996
carol: 8/19/1993
supermim: 3/16/1992
supermim: 3/20/1990
supermim: 2/28/1990
ddp: 10/27/1989
carol: 6/8/1989