(data stored in SCRATCH zone)

SWISSPROT: SPTB2_HUMAN

ID   SPTB2_HUMAN             Reviewed;        2364 AA.
AC   Q01082; B2RP63; O60837; Q16057; Q53R99; Q59ER3; Q8IX99;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 2.
DT   11-DEC-2019, entry version 210.
DE   RecName: Full=Spectrin beta chain, non-erythrocytic 1;
DE   AltName: Full=Beta-II spectrin;
DE   AltName: Full=Fodrin beta chain;
DE   AltName: Full=Spectrin, non-erythroid beta chain 1;
GN   Name=SPTBN1; Synonyms=SPTB2;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG), AND VARIANT HIS-1411.
RC   TISSUE=Brain;
RX   PubMed=1527002;
RA   Hu R.J., Watanabe M., Bennett V.;
RT   "Characterization of human brain cDNA encoding the general isoform of beta-
RT   spectrin.";
RL   J. Biol. Chem. 267:18715-18722(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY, AND VARIANT
RP   HIS-1411.
RX   PubMed=11665863; DOI=10.1385/jmn:17:1:59;
RA   Chen Y., Yu P., Lu D., Tagle D.A., Cai T.;
RT   "A novel isoform of beta-spectrin II localizes to cerebellar Purkinje-cell
RT   bodies and interacts with neurofibromatosis type 2 gene product
RT   schwannomin.";
RL   J. Mol. Neurosci. 17:59-70(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
RC   TISSUE=Brain;
RA   Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA   Ohara O., Nagase T., Kikuno R.F.;
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15815621; DOI=10.1038/nature03466;
RA   Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA   Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA   Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA   Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA   Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA   Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA   Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA   Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA   Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA   McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA   Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA   Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA   Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA   Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA   Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA   Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA   Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA   Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA   Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA   Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA   Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA   Wilson R.K.;
RT   "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT   4.";
RL   Nature 434:724-731(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 293-1544.
RX   PubMed=8406479; DOI=10.1006/geno.1993.1323;
RA   Chang J.G., Scarpa A., Eddy R.L., Byers M.G., Harris A.S., Morrow J.S.,
RA   Watkins P., Shows T.B., Forget B.G.;
RT   "Cloning of a portion of the chromosomal gene and cDNA for human beta-
RT   fodrin, the nonerythroid form of beta-spectrin.";
RL   Genomics 17:287-293(1993).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 2087-2168 (ISOFORM SHORT).
RC   TISSUE=Skeletal muscle;
RX   PubMed=10806113;
RA   Hayes N.V.L., Scott C., Heerkens E., Ohanian V., Maggs A.M., Pinder J.C.,
RA   Kordeli E., Baines A.J.;
RT   "Identification of a novel C-terminal variant of betaII spectrin: two
RT   isoforms of betaII spectrin have distinct intracellular locations and
RT   activities.";
RL   J. Cell Sci. 113:2023-2034(2000).
RN   [9]
RP   INTERACTION WITH ANK2.
RX   PubMed=15262991; DOI=10.1074/jbc.m406018200;
RA   Mohler P.J., Yoon W., Bennett V.;
RT   "Ankyrin-B targets beta2-spectrin to an intracellular compartment in
RT   neonatal cardiomyocytes.";
RL   J. Biol. Chem. 279:40185-40193(2004).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2102 AND SER-2138, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA   Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT   "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT   networks.";
RL   Cell 127:635-648(2006).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2102, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=17924679; DOI=10.1021/pr070152u;
RA   Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
RT   "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells
RT   and high confident phosphopeptide identification by cross-validation of
RT   MS/MS and MS/MS/MS spectra.";
RL   J. Proteome Res. 6:4150-4162(2007).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2102, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Platelet;
RX   PubMed=18088087; DOI=10.1021/pr0704130;
RA   Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA   Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT   "Phosphoproteome of resting human platelets.";
RL   J. Proteome Res. 7:526-534(2008).
RN   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2138, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA   Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA   Greff Z., Keri G., Stemmann O., Mann M.;
RT   "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT   kinome across the cell cycle.";
RL   Mol. Cell 31:438-448(2008).
RN   [14]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2102; SER-2138; SER-2165;
RP   SER-2169; THR-2187; THR-2320; THR-2328 AND SER-2341, PHOSPHORYLATION [LARGE
RP   SCALE ANALYSIS] AT SER-14 (ISOFORM 2), AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [15]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT   refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [16]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2102, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA   Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA   Mann M., Daub H.;
RT   "Large-scale proteomics analysis of the human kinome.";
RL   Mol. Cell. Proteomics 8:1751-1764(2009).
RN   [17]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1447; SER-2138; SER-2169 AND
RP   SER-2341, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14 (ISOFORM 2), AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA   Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA   Rodionov V., Han D.K.;
RT   "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT   reveals system-wide modulation of protein-protein interactions.";
RL   Sci. Signal. 2:RA46-RA46(2009).
RN   [18]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-90; LYS-1815; LYS-1913 AND
RP   LYS-1989, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA   Olsen J.V., Mann M.;
RT   "Lysine acetylation targets protein complexes and co-regulates major
RT   cellular functions.";
RL   Science 325:834-840(2009).
RN   [19]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-817; SER-825; SER-1057;
RP   SER-2102; SER-2138; SER-2169; THR-2320 AND SER-2341, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT   site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [20]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [21]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2102; SER-2128; SER-2138;
RP   SER-2160; SER-2161; SER-2164; SER-2169; SER-2319; THR-2320 AND SER-2340,
RP   AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA   Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT   "System-wide temporal characterization of the proteome and phosphoproteome
RT   of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [22]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA   Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA   Giglione C.;
RT   "Comparative large-scale characterisation of plant vs. mammal proteins
RT   reveals similar and idiosyncratic N-alpha acetylation features.";
RL   Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN   [23]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [24]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2102; SER-2128; SER-2138;
RP   SER-2164; SER-2165; SER-2169; THR-2187; THR-2328 AND SER-2341, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma, and Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [25]
RP   INTERACTION WITH CAMSAP1.
RX   PubMed=24117850; DOI=10.1111/jnc.12462;
RA   King M.D., Phillips G.W., Bignone P.A., Hayes N.V., Pinder J.C.,
RA   Baines A.J.;
RT   "A conserved sequence in CAMSAP1 (calmodulin regulated spectrin-associated
RT   protein 1) links its interaction with spectrin and calmodulin to neurite
RT   outgrowth.";
RL   J. Neurochem. 128:391-402(2014).
RN   [26]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1237; SER-1388; SER-1557;
RP   SER-2102; SER-2165; SER-2169; SER-2172; SER-2314 AND THR-2320, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [27]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25944712; DOI=10.1002/pmic.201400617;
RA   Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA   Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT   "N-terminome analysis of the human mitochondrial proteome.";
RL   Proteomics 15:2519-2524(2015).
RN   [28]
RP   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   [29]
RP   X-RAY CRYSTALLOGRAPHY (1.1 ANGSTROMS) OF 173-281.
RX   PubMed=9817844; DOI=10.1016/s0969-2126(98)00141-5;
RA   Banuelos S., Saraste M., Carugo K.D.;
RT   "Structural comparisons of calponin homology domains: implications for
RT   actin binding.";
RL   Structure 6:1419-1431(1998).
CC   -!- FUNCTION: Fodrin, which seems to be involved in secretion, interacts
CC       with calmodulin in a calcium-dependent manner and is thus candidate for
CC       the calcium-dependent movement of the cytoskeleton at the membrane.
CC   -!- SUBUNIT: Interacts with CAMSAP1 (PubMed:24117850). Interacts with ANK2
CC       (PubMed:15262991). Interacts with CPNE4 (via VWFA domain) (By
CC       similarity). Like erythrocyte spectrin, the spectrin-like proteins are
CC       capable to form dimers which can further associate to tetramers (By
CC       similarity). Isoform Short cannot bind to the axonal protein fodaxin.
CC       {ECO:0000250|UniProtKB:P85986, ECO:0000250|UniProtKB:Q62261,
CC       ECO:0000269|PubMed:15262991, ECO:0000269|PubMed:24117850}.
CC   -!- INTERACTION:
CC       Q99459:CDC5L; NbExp=3; IntAct=EBI-351561, EBI-374880;
CC       Q9NRI5:DISC1; NbExp=4; IntAct=EBI-351561, EBI-529989;
CC       P02549:SPTA1; NbExp=3; IntAct=EBI-351561, EBI-375617;
CC       Q13813:SPTAN1; NbExp=8; IntAct=EBI-351561, EBI-351450;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasm,
CC       myofibril, sarcomere, M line {ECO:0000250}. Note=Colocalizes with ANK2
CC       in a distinct intracellular compartment of neonatal cardiomyocytes.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane {ECO:0000250};
CC       Peripheral membrane protein {ECO:0000250}; Cytoplasmic side
CC       {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=Long;
CC         IsoId=Q01082-1; Sequence=Displayed;
CC       Name=Short;
CC         IsoId=Q01082-2; Sequence=VSP_000720, VSP_000721;
CC       Name=2;
CC         IsoId=Q01082-3; Sequence=VSP_026054, VSP_026055, VSP_026056;
CC   -!- TISSUE SPECIFICITY: Isoform 2 is present in brain, lung and kidney (at
CC       protein level). {ECO:0000269|PubMed:11665863}.
CC   -!- SIMILARITY: Belongs to the spectrin family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD92985.1; Type=Erroneous initiation; Evidence={ECO:0000305};
DR   EMBL; M96803; AAA60580.1; -; mRNA.
DR   EMBL; AF327441; AAO15362.1; -; mRNA.
DR   EMBL; AB209748; BAD92985.1; ALT_INIT; mRNA.
DR   EMBL; AC093110; AAY24229.1; -; Genomic_DNA.
DR   EMBL; AC092839; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471053; EAX00147.1; -; Genomic_DNA.
DR   EMBL; BC137282; AAI37283.1; -; mRNA.
DR   EMBL; BC137283; AAI37284.1; -; mRNA.
DR   EMBL; S65762; AAB28324.1; -; mRNA.
DR   EMBL; AJ005694; CAA06678.1; -; mRNA.
DR   EMBL; AJ238723; CAB91088.1; -; Genomic_DNA.
DR   CCDS; CCDS33198.1; -. [Q01082-1]
DR   CCDS; CCDS33199.1; -. [Q01082-3]
DR   PIR; A44159; A44159.
DR   PIR; A47213; A47213.
DR   RefSeq; NP_003119.2; NM_003128.2. [Q01082-1]
DR   RefSeq; NP_842565.2; NM_178313.2. [Q01082-3]
DR   RefSeq; XP_005264574.1; XM_005264517.2. [Q01082-1]
DR   RefSeq; XP_006712150.1; XM_006712087.2. [Q01082-1]
DR   RefSeq; XP_016860268.1; XM_017004779.1. [Q01082-1]
DR   RefSeq; XP_016860269.1; XM_017004780.1. [Q01082-1]
DR   RefSeq; XP_016860270.1; XM_017004781.1. [Q01082-1]
DR   PDB; 1AA2; X-ray; 2.00 A; A=173-280.
DR   PDB; 1BKR; X-ray; 1.10 A; A=172-280.
DR   PDB; 3EDV; X-ray; 1.95 A; A/B=1697-2015.
DR   PDBsum; 1AA2; -.
DR   PDBsum; 1BKR; -.
DR   PDBsum; 3EDV; -.
DR   SMR; Q01082; -.
DR   BioGrid; 112589; 178.
DR   DIP; DIP-33182N; -.
DR   ELM; Q01082; -.
DR   IntAct; Q01082; 100.
DR   MINT; Q01082; -.
DR   STRING; 9606.ENSP00000349259; -.
DR   DrugBank; DB03401; 1D-myo-inositol 1,4,5-trisphosphate.
DR   DrugBank; DB01373; Calcium.
DR   iPTMnet; Q01082; -.
DR   PhosphoSitePlus; Q01082; -.
DR   SwissPalm; Q01082; -.
DR   BioMuta; SPTBN1; -.
DR   DMDM; 116242799; -.
DR   CPTAC; CPTAC-590; -.
DR   EPD; Q01082; -.
DR   jPOST; Q01082; -.
DR   MassIVE; Q01082; -.
DR   MaxQB; Q01082; -.
DR   PaxDb; Q01082; -.
DR   PeptideAtlas; Q01082; -.
DR   PRIDE; Q01082; -.
DR   ProteomicsDB; 57910; -. [Q01082-1]
DR   ProteomicsDB; 57911; -. [Q01082-2]
DR   ProteomicsDB; 57912; -. [Q01082-3]
DR   Ensembl; ENST00000333896; ENSP00000334156; ENSG00000115306. [Q01082-3]
DR   Ensembl; ENST00000356805; ENSP00000349259; ENSG00000115306. [Q01082-1]
DR   GeneID; 6711; -.
DR   KEGG; hsa:6711; -.
DR   UCSC; uc002rxu.4; human. [Q01082-1]
DR   CTD; 6711; -.
DR   DisGeNET; 6711; -.
DR   EuPathDB; HostDB:ENSG00000115306.15; -.
DR   GeneCards; SPTBN1; -.
DR   HGNC; HGNC:11275; SPTBN1.
DR   HPA; HPA012685; -.
DR   HPA; HPA013149; -.
DR   MIM; 182790; gene.
DR   neXtProt; NX_Q01082; -.
DR   OpenTargets; ENSG00000115306; -.
DR   PharmGKB; PA36104; -.
DR   eggNOG; KOG0035; Eukaryota.
DR   eggNOG; COG5069; LUCA.
DR   GeneTree; ENSGT00940000154864; -.
DR   InParanoid; Q01082; -.
DR   KO; K06115; -.
DR   OrthoDB; 543832at2759; -.
DR   PhylomeDB; Q01082; -.
DR   TreeFam; TF313446; -.
DR   Reactome; R-HSA-373753; Nephrin family interactions.
DR   Reactome; R-HSA-375165; NCAM signaling for neurite out-growth.
DR   Reactome; R-HSA-445095; Interaction between L1 and Ankyrins.
DR   Reactome; R-HSA-5673001; RAF/MAP kinase cascade.
DR   Reactome; R-HSA-6807878; COPI-mediated anterograde transport.
DR   SignaLink; Q01082; -.
DR   SIGNOR; Q01082; -.
DR   ChiTaRS; SPTBN1; human.
DR   EvolutionaryTrace; Q01082; -.
DR   GeneWiki; SPTBN1; -.
DR   GenomeRNAi; 6711; -.
DR   Pharos; Q01082; Tbio.
DR   PRO; PR:Q01082; -.
DR   Proteomes; UP000005640; Chromosome 2.
DR   RNAct; Q01082; protein.
DR   Bgee; ENSG00000115306; Expressed in 256 organ(s), highest expression level in forebrain.
DR   ExpressionAtlas; Q01082; baseline and differential.
DR   Genevisible; Q01082; HS.
DR   GO; GO:0030673; C:axolemma; ISS:BHF-UCL.
DR   GO; GO:0032437; C:cuticular plate; IEA:Ensembl.
DR   GO; GO:0005737; C:cytoplasm; IDA:HGNC-UCL.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR   GO; GO:0031430; C:M band; IEA:UniProtKB-SubCell.
DR   GO; GO:0005730; C:nucleolus; IDA:HGNC-UCL.
DR   GO; GO:0014069; C:postsynaptic density; IEA:Ensembl.
DR   GO; GO:0008091; C:spectrin; TAS:ProtInc.
DR   GO; GO:0014731; C:spectrin-associated cytoskeleton; NAS:BHF-UCL.
DR   GO; GO:0003779; F:actin binding; TAS:ProtInc.
DR   GO; GO:0030506; F:ankyrin binding; IPI:BHF-UCL.
DR   GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR   GO; GO:0051020; F:GTPase binding; IPI:UniProtKB.
DR   GO; GO:0005543; F:phospholipid binding; IEA:InterPro.
DR   GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
DR   GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
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:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; TAS:Reactome.
DR   GO; GO:0043001; P:Golgi to plasma membrane protein transport; IMP:BHF-UCL.
DR   GO; GO:0000165; P:MAPK cascade; TAS:Reactome.
DR   GO; GO:0071709; P:membrane assembly; IMP:BHF-UCL.
DR   GO; GO:0000281; P:mitotic cytokinesis; IMP:BHF-UCL.
DR   GO; GO:0007009; P:plasma membrane organization; IMP:BHF-UCL.
DR   GO; GO:1900042; P:positive regulation of interleukin-2 secretion; IMP:UniProtKB.
DR   GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; IMP:UniProtKB.
DR   GO; GO:0072659; P:protein localization to plasma membrane; IMP:BHF-UCL.
DR   GO; GO:1903076; P:regulation of protein localization to plasma membrane; IGI:UniProtKB.
DR   GO; GO:0060390; P:regulation of SMAD protein signal transduction; IEA:Ensembl.
DR   CDD; cd00014; CH; 2.
DR   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; Q01082.
DR   SWISS-2DPAGE; Q01082.
KW   3D-structure; Acetylation; Actin capping; Actin-binding;
KW   Alternative splicing; Calmodulin-binding; Cell membrane; Cytoplasm;
KW   Cytoskeleton; Glycoprotein; Membrane; Phosphoprotein; Polymorphism;
KW   Reference proteome; Repeat.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000244|PubMed:19413330,
FT                   ECO:0000244|PubMed:22223895, ECO:0000244|PubMed:22814378"
FT   CHAIN           2..2364
FT                   /note="Spectrin beta chain, non-erythrocytic 1"
FT                   /id="PRO_0000073461"
FT   DOMAIN          54..158
FT                   /note="Calponin-homology (CH) 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT   DOMAIN          173..278
FT                   /note="Calponin-homology (CH) 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT   REPEAT          303..411
FT                   /note="Spectrin 1"
FT                   /evidence="ECO:0000255"
FT   REPEAT          423..525
FT                   /note="Spectrin 2"
FT                   /evidence="ECO:0000255"
FT   REPEAT          530..636
FT                   /note="Spectrin 3"
FT                   /evidence="ECO:0000255"
FT   REPEAT          639..742
FT                   /note="Spectrin 4"
FT                   /evidence="ECO:0000255"
FT   REPEAT          745..847
FT                   /note="Spectrin 5"
FT                   /evidence="ECO:0000255"
FT   REPEAT          850..952
FT                   /note="Spectrin 6"
FT                   /evidence="ECO:0000255"
FT   REPEAT          957..1060
FT                   /note="Spectrin 7"
FT                   /evidence="ECO:0000255"
FT   REPEAT          1063..1166
FT                   /note="Spectrin 8"
FT                   /evidence="ECO:0000255"
FT   REPEAT          1170..1258
FT                   /note="Spectrin 9"
FT                   /evidence="ECO:0000255"
FT   REPEAT          1276..1376
FT                   /note="Spectrin 10"
FT                   /evidence="ECO:0000255"
FT   REPEAT          1381..1482
FT                   /note="Spectrin 11"
FT                   /evidence="ECO:0000255"
FT   REPEAT          1486..1590
FT                   /note="Spectrin 12"
FT                   /evidence="ECO:0000255"
FT   REPEAT          1592..1696
FT                   /note="Spectrin 13"
FT                   /evidence="ECO:0000255"
FT   REPEAT          1698..1801
FT                   /note="Spectrin 14"
FT                   /evidence="ECO:0000255"
FT   REPEAT          1805..1907
FT                   /note="Spectrin 15"
FT                   /evidence="ECO:0000255"
FT   REPEAT          1914..2014
FT                   /note="Spectrin 16"
FT                   /evidence="ECO:0000255"
FT   REPEAT          2018..2097
FT                   /note="Spectrin 17"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          2197..2307
FT                   /note="PH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT   REGION          2..275
FT                   /note="Actin-binding"
FT   REGION          1563..2093
FT                   /note="Interaction with ANK2"
FT                   /evidence="ECO:0000269|PubMed:15262991"
FT   REGION          2149..2177
FT                   /note="Mediates interaction with CAMSAP1"
FT                   /evidence="ECO:0000269|PubMed:24117850"
FT   MOD_RES         2
FT                   /note="N-acetylthreonine"
FT                   /evidence="ECO:0000244|PubMed:19413330,
FT                   ECO:0000244|PubMed:22223895, ECO:0000244|PubMed:22814378"
FT   MOD_RES         36
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q62261"
FT   MOD_RES         90
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000244|PubMed:19608861"
FT   MOD_RES         228
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q62261"
FT   MOD_RES         817
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:20068231"
FT   MOD_RES         825
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:20068231"
FT   MOD_RES         903
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q62261"
FT   MOD_RES         1057
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:20068231"
FT   MOD_RES         1076
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q62261"
FT   MOD_RES         1079
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q62261"
FT   MOD_RES         1237
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:24275569"
FT   MOD_RES         1388
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:24275569"
FT   MOD_RES         1447
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:19690332"
FT   MOD_RES         1557
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:24275569"
FT   MOD_RES         1805
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q62261"
FT   MOD_RES         1815
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000244|PubMed:19608861"
FT   MOD_RES         1913
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000244|PubMed:19608861"
FT   MOD_RES         1989
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000244|PubMed:19608861"
FT   MOD_RES         2102
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:17081983,
FT                   ECO:0000244|PubMed:17924679, ECO:0000244|PubMed:18088087,
FT                   ECO:0000244|PubMed:18669648, ECO:0000244|PubMed:19369195,
FT                   ECO:0000244|PubMed:20068231, ECO:0000244|PubMed:21406692,
FT                   ECO:0000244|PubMed:23186163, ECO:0000244|PubMed:24275569"
FT   MOD_RES         2128
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:21406692,
FT                   ECO:0000244|PubMed:23186163"
FT   MOD_RES         2138
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:17081983,
FT                   ECO:0000244|PubMed:18669648, ECO:0000244|PubMed:18691976,
FT                   ECO:0000244|PubMed:19690332, ECO:0000244|PubMed:20068231,
FT                   ECO:0000244|PubMed:21406692, ECO:0000244|PubMed:23186163"
FT   MOD_RES         2147
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q62261"
FT   MOD_RES         2148
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q62261"
FT   MOD_RES         2159
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q62261"
FT   MOD_RES         2160
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:21406692"
FT   MOD_RES         2161
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:21406692"
FT   MOD_RES         2164
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:21406692,
FT                   ECO:0000244|PubMed:23186163"
FT   MOD_RES         2165
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:18669648,
FT                   ECO:0000244|PubMed:23186163, ECO:0000244|PubMed:24275569"
FT   MOD_RES         2169
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:18669648,
FT                   ECO:0000244|PubMed:19690332, ECO:0000244|PubMed:20068231,
FT                   ECO:0000244|PubMed:21406692, ECO:0000244|PubMed:23186163,
FT                   ECO:0000244|PubMed:24275569"
FT   MOD_RES         2171
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q62261"
FT   MOD_RES         2172
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:24275569"
FT   MOD_RES         2184
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q62261"
FT   MOD_RES         2187
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000244|PubMed:18669648,
FT                   ECO:0000244|PubMed:23186163"
FT   MOD_RES         2195
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q62261"
FT   MOD_RES         2314
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:24275569"
FT   MOD_RES         2319
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:21406692"
FT   MOD_RES         2320
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000244|PubMed:18669648,
FT                   ECO:0000244|PubMed:20068231, ECO:0000244|PubMed:21406692,
FT                   ECO:0000244|PubMed:24275569"
FT   MOD_RES         2328
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000244|PubMed:18669648,
FT                   ECO:0000244|PubMed:23186163"
FT   MOD_RES         2340
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:21406692"
FT   MOD_RES         2341
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:18669648,
FT                   ECO:0000244|PubMed:19690332, ECO:0000244|PubMed:20068231,
FT                   ECO:0000244|PubMed:23186163"
FT   CARBOHYD        2324
FT                   /note="O-linked (GlcNAc) serine"
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         1..49
FT                   /note="MTTTVATDYDNIEIQQQYSDVNNRWDVDDWDNENSSARLFERSRIKALA ->
FT                   MELQRTSSISGPLSPAYTGQVPYNYNQLEGRFKQLQ (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:11665863,
FT                   ECO:0000303|PubMed:15489334"
FT                   /id="VSP_026054"
FT   VAR_SEQ         2141..2225
FT                   /note="MAETVDTSEMVNGATEQRTSSKESSPIPSPTSDRKAKTALPAQSAATLPART
FT                   QETPSAQMEGFLNRKHEWEAHNKKASSRSWHNV -> VSYRSQTYQNYKNFNSRRTASD
FT                   QPWSGL (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:11665863,
FT                   ECO:0000303|PubMed:15489334"
FT                   /id="VSP_026055"
FT   VAR_SEQ         2141..2168
FT                   /note="MAETVDTSEMVNGATEQRTSSKESSPIP -> VSYRSQTYQNYKNFNSRRTA
FT                   SDQPWSGL (in isoform Short)"
FT                   /evidence="ECO:0000303|PubMed:10806113"
FT                   /id="VSP_000720"
FT   VAR_SEQ         2169..2364
FT                   /note="Missing (in isoform Short)"
FT                   /evidence="ECO:0000303|PubMed:10806113"
FT                   /id="VSP_000721"
FT   VAR_SEQ         2226..2364
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:11665863,
FT                   ECO:0000303|PubMed:15489334"
FT                   /id="VSP_026056"
FT   VARIANT         1411
FT                   /note="D -> H (in dbSNP:rs1052790)"
FT                   /evidence="ECO:0000269|PubMed:11665863,
FT                   ECO:0000269|PubMed:1527002"
FT                   /id="VAR_032641"
FT   CONFLICT        583
FT                   /note="R -> W (in Ref. 3; BAD92985)"
FT                   /evidence="ECO:0000305"
FT   HELIX           174..186
FT                   /evidence="ECO:0000244|PDB:1BKR"
FT   TURN            187..189
FT                   /evidence="ECO:0000244|PDB:1BKR"
FT   STRAND          196..199
FT                   /evidence="ECO:0000244|PDB:1BKR"
FT   HELIX           200..202
FT                   /evidence="ECO:0000244|PDB:1BKR"
FT   HELIX           206..215
FT                   /evidence="ECO:0000244|PDB:1BKR"
FT   HELIX           217..219
FT                   /evidence="ECO:0000244|PDB:1BKR"
FT   HELIX           222..224
FT                   /evidence="ECO:0000244|PDB:1BKR"
FT   HELIX           230..245
FT                   /evidence="ECO:0000244|PDB:1BKR"
FT   HELIX           253..256
FT                   /evidence="ECO:0000244|PDB:1BKR"
FT   STRAND          257..260
FT                   /evidence="ECO:0000244|PDB:1BKR"
FT   HELIX           263..277
FT                   /evidence="ECO:0000244|PDB:1BKR"
FT   HELIX           1697..1721
FT                   /evidence="ECO:0000244|PDB:3EDV"
FT   HELIX           1730..1767
FT                   /evidence="ECO:0000244|PDB:3EDV"
FT   HELIX           1773..1826
FT                   /evidence="ECO:0000244|PDB:3EDV"
FT   HELIX           1836..1852
FT                   /evidence="ECO:0000244|PDB:3EDV"
FT   HELIX           1854..1873
FT                   /evidence="ECO:0000244|PDB:3EDV"
FT   HELIX           1877..1935
FT                   /evidence="ECO:0000244|PDB:3EDV"
FT   HELIX           1943..1962
FT                   /evidence="ECO:0000244|PDB:3EDV"
FT   HELIX           1964..1979
FT                   /evidence="ECO:0000244|PDB:3EDV"
FT   HELIX           1985..2014
FT                   /evidence="ECO:0000244|PDB:3EDV"
FT   MOD_RES         Q01082-3:14
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:18669648,
FT                   ECO:0000244|PubMed:19690332"
SQ   SEQUENCE   2364 AA;  274609 MW;  1770C3B0EB07B892 CRC64;
     MTTTVATDYD NIEIQQQYSD VNNRWDVDDW DNENSSARLF ERSRIKALAD EREAVQKKTF
     TKWVNSHLAR VSCRITDLYT DLRDGRMLIK LLEVLSGERL PKPTKGRMRI HCLENVDKAL
     QFLKEQRVHL ENMGSHDIVD GNHRLTLGLI WTIILRFQIQ DISVETEDNK EKKSAKDALL
     LWCQMKTAGY PNVNIHNFTT SWRDGMAFNA LIHKHRPDLI DFDKLKKSNA HYNLQNAFNL
     AEQHLGLTKL LDPEDISVDH PDEKSIITYV VTYYHYFSKM KALAVEGKRI GKVLDNAIET
     EKMIEKYESL ASDLLEWIEQ TIIILNNRKF ANSLVGVQQQ LQAFNTYRTV EKPPKFTEKG
     NLEVLLFTIQ SKMRANNQKV YMPREGKLIS DINKAWERLE KAEHERELAL RNELIRQEKL
     EQLARRFDRK AAMRETWLSE NQRLVSQDNF GFDLPAVEAA TKKHEAIETD IAAYEERVQA
     VVAVARELEA ENYHDIKRIT ARKDNVIRLW EYLLELLRAR RQRLEMNLGL QKIFQEMLYI
     MDWMDEMKVL VLSQDYGKHL LGVEDLLQKH TLVEADIGIQ AERVRGVNAS AQKFATDGEG
     YKPCDPQVIR DRVAHMEFCY QELCQLAAER RARLEESRRL WKFFWEMAEE EGWIREKEKI
     LSSDDYGKDL TSVMRLLSKH RAFEDEMSGR SGHFEQAIKE GEDMIAEEHF GSEKIRERII
     YIREQWANLE QLSAIRKKRL EEASLLHQFQ ADADDIDAWM LDILKIVSSS DVGHDEYSTQ
     SLVKKHKDVA EEIANYRPTL DTLHEQASAL PQEHAESPDV RGRLSGIEER YKEVAELTRL
     RKQALQDTLA LYKMFSEADA CELWIDEKEQ WLNNMQIPEK LEDLEVIQHR FESLEPEMNN
     QASRVAVVNQ IARQLMHSGH PSEKEIKAQQ DKLNTRWSQF RELVDRKKDA LLSALSIQNY
     HLECNETKSW IREKTKVIES TQDLGNDLAG VMALQRKLTG MERDLVAIEA KLSDLQKEAE
     KLESEHPDQA QAILSRLAEI SDVWEEMKTT LKNREASLGE ASKLQQFLRD LDDFQSWLSR
     TQTAIASEDM PNTLTEAEKL LTQHENIKNE IDNYEEDYQK MRDMGEMVTQ GQTDAQYMFL
     RQRLQALDTG WNELHKMWEN RQNLLSQSHA YQQFLRDTKQ AEAFLNNQEY VLAHTEMPTT
     LEGAEAAIKK QEDFMTTMDA NEEKINAVVE TGRRLVSDGN INSDRIQEKV DSIDDRHRKN
     RETASELLMR LKDNRDLQKF LQDCQELSLW INEKMLTAQD MSYDEARNLH SKWLKHQAFM
     AELASNKEWL DKIEKEGMQL ISEKPETEAV VKEKLTGLHK MWEVLESTTQ TKAQRLFDAN
     KAELFTQSCA DLDKWLHGLE SQIQSDDYGK DLTSVNILLK KQQMLENQME VRKKEIEELQ
     SQAQALSQEG KSTDEVDSKR LTVQTKFMEL LEPLNERKHN LLASKEIHQF NRDVEDEILW
     VGERMPLATS TDHGHNLQTV QLLIKKNQTL QKEIQGHQPR IDDIFERSQN IVTDSSSLSA
     EAIRQRLADL KQLWGLLIEE TEKRHRRLEE AHRAQQYYFD AAEAEAWMSE QELYMMSEEK
     AKDEQSAVSM LKKHQILEQA VEDYAETVHQ LSKTSRALVA DSHPESERIS MRQSKVDKLY
     AGLKDLAEER RGKLDERHRL FQLNREVDDL EQWIAEREVV AGSHELGQDY EHVTMLQERF
     REFARDTGNI GQERVDTVNH LADELINSGH SDAATIAEWK DGLNEAWADL LELIDTRTQI
     LAASYELHKF YHDAKEIFGR IQDKHKKLPE ELGRDQNTVE TLQRMHTTFE HDIQALGTQV
     RQLQEDAARL QAAYAGDKAD DIQKRENEVL EAWKSLLDAC ESRRVRLVDT GDKFRFFSMV
     RDLMLWMEDV IRQIEAQEKP RDVSSVELLM NNHQGIKAEI DARNDSFTTC IELGKSLLAR
     KHYASEEIKE KLLQLTEKRK EMIDKWEDRW EWLRLILEVH QFSRDASVAE AWLLGQEPYL
     SSREIGQSVD EVEKLIKRHE AFEKSAATWD ERFSALERLT TLELLEVRRQ QEEEERKRRP
     PSPEPSTKVS EEAESQQQWD TSKGEQVSQN GLPAEQGSPR MAETVDTSEM VNGATEQRTS
     SKESSPIPSP TSDRKAKTAL PAQSAATLPA RTQETPSAQM EGFLNRKHEW EAHNKKASSR
     SWHNVYCVIN NQEMGFYKDA KTAASGIPYH SEVPVSLKEA VCEVALDYKK KKHVFKLRLN
     DGNEYLFQAK DDEEMNTWIQ AISSAISSDK HEVSASTQST PASSRAQTLP TSVVTITSES
     SPGKREKDKE KDKEKRFSLF GKKK
//

If you have problems or comments...

PBIL Back to PBIL home page