ANK2_HUMAN
ID ANK2_HUMAN Reviewed; 3957 AA.
AC Q01484; Q01485; Q08AC7; Q08AC8; Q7Z3L5;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2012, sequence version 4.
DT 03-AUG-2022, entry version 223.
DE RecName: Full=Ankyrin-2;
DE Short=ANK-2;
DE AltName: Full=Ankyrin-B;
DE AltName: Full=Brain ankyrin;
DE AltName: Full=Non-erythroid ankyrin;
GN Name=ANK2; Synonyms=ANKB {ECO:0000303|PubMed:27718357};
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 2), NUCLEOTIDE SEQUENCE [MRNA] OF
RP 1477-2110 (ISOFORM 3), AND TISSUE SPECIFICITY.
RC TISSUE=Brain stem;
RX PubMed=1830053; DOI=10.1083/jcb.114.2.241;
RA Otto E., Kunimoto M., McLaughlin T., Bennett V.;
RT "Isolation and characterization of cDNAs encoding human brain ankyrins
RT reveal a family of alternatively spliced genes.";
RL J. Cell Biol. 114:241-253(1991).
RN [2]
RP SEQUENCE REVISION.
RA Carpenter S.;
RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RC TISSUE=Brain stem;
RX PubMed=8253844; DOI=10.1083/jcb.123.6.1463;
RA Chan W., Kordeli E., Bennett V.;
RT "440-kD ankyrinB: structure of the major developmentally regulated domain
RT and selective localization in unmyelinated axons.";
RL J. Cell Biol. 123:1463-1473(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Retina;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
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 [GENOMIC DNA] OF 463-495, AND TISSUE SPECIFICITY.
RX PubMed=1833308; DOI=10.1016/0888-7543(91)90173-c;
RA Tse W.T., Menninger J.C., Yang-Feng T.L., Francke U., Sahr K.E., Lux S.E.,
RA Ward D.C., Forget B.G.;
RT "Isolation and chromosomal localization of a novel nonerythroid ankyrin
RT gene.";
RL Genomics 10:858-866(1991).
RN [8]
RP INVOLVEMENT IN LQT4, VARIANT LQT4 GLY-1458, CHARACTERIZATION OF VARIANT
RP LQT4 GLY-1458, AND FUNCTION.
RX PubMed=12571597; DOI=10.1038/nature01335;
RA Mohler P.J., Schott J.-J., Gramolini A.O., Dilly K.W., Guatimosim S.,
RA duBell W.H., Song L.-S., Haurogne K., Kyndt F., Ali M.E., Rogers T.B.,
RA Lederer W.J., Escande D., Le Marec H., Bennett V.;
RT "Ankyrin-B mutation causes type 4 long-QT cardiac arrhythmia and sudden
RT cardiac death.";
RL Nature 421:634-639(2003).
RN [9]
RP INTERACTION WITH SPTBN1, AND MUTAGENESIS OF 975-ASP--ARG-977; ALA-1000 AND
RP 1100-GLU--ASP-1103.
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 INTERACTION WITH RHBG.
RX PubMed=15611082; DOI=10.1074/jbc.m413351200;
RA Lopez C., Metral S., Eladari D., Drevensek S., Gane P., Chambrey R.,
RA Bennett V., Cartron J.-P., Le Van Kim C., Colin Y.;
RT "The ammonium transporter RhBG: requirement of a tyrosine-based signal and
RT ankyrin-G for basolateral targeting and membrane anchorage in polarized
RT kidney epithelial cells.";
RL J. Biol. Chem. 280:8221-8228(2005).
RN [11]
RP SUBUNIT, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=19007774; DOI=10.1016/j.exer.2008.09.022;
RA Kizhatil K., Sandhu N.K., Peachey N.S., Bennett V.;
RT "Ankyrin-B is required for coordinated expression of beta-2-spectrin, the
RT Na/K-ATPase and the Na/Ca exchanger in the inner segment of rod
RT photoreceptors.";
RL Exp. Eye Res. 88:57-64(2009).
RN [12]
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 [13]
RP 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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-846, AND IDENTIFICATION BY
RP 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 [15]
RP INTERACTION WITH RABGAP1L.
RX PubMed=27718357; DOI=10.7554/elife.20417;
RA Qu F., Lorenzo D.N., King S.J., Brooks R., Bear J.E., Bennett V.;
RT "Ankyrin-B is a PI3P effector that promotes polarized alpha5beta1-integrin
RT recycling via recruiting RabGAP1L to early endosomes.";
RL Elife 5:0-0(2016).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 966-3620, DOMAIN DEATH 1, DOMAIN
RP UPA, AND DOMAINS ZU5.
RX PubMed=22411828; DOI=10.1073/pnas.1200613109;
RA Wang C., Yu C., Ye F., Wei Z., Zhang M.;
RT "Structure of the ZU5-ZU5-UPA-DD tandem of ankyrin-B reveals interaction
RT surfaces necessary for ankyrin function.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:4822-4827(2012).
RN [17]
RP VARIANTS LQT4 GLY-1458; ILE-3740; ASN-3744; TRP-3906 AND LYS-3931, AND
RP CHARACTERIZATION OF VARIANTS LQT4.
RX PubMed=15178757; DOI=10.1073/pnas.0402546101;
RA Mohler P.J., Splawski I., Napolitano C., Bottelli G., Sharpe L.,
RA Timothy K., Priori S.G., Keating M.T., Bennett V.;
RT "A cardiac arrhythmia syndrome caused by loss of ankyrin-B function.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:9137-9142(2004).
RN [18]
RP VARIANTS [LARGE SCALE ANALYSIS] GLU-685; ARG-1267 AND LYS-3653.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
RN [19]
RP VARIANTS LQT4 GLY-1458; ILE-3740; ASN-3744; TRP-3906 AND LYS-3931, AND
RP VARIANT ASP-1555.
RX PubMed=17940615; DOI=10.1371/journal.pone.0001051;
RA Mohler P.J., Healy J.A., Xue H., Puca A.A., Kline C.F., Allingham R.R.,
RA Kranias E.G., Rockman H.A., Bennett V.;
RT "Ankyrin-B syndrome: enhanced cardiac function balanced by risk of cardiac
RT death and premature senescence.";
RL PLoS ONE 2:E1051-E1051(2007).
CC -!- FUNCTION: Plays an essential role in the localization and membrane
CC stabilization of ion transporters and ion channels in several cell
CC types, including cardiomyocytes, as well as in striated muscle cells.
CC In skeletal muscle, required for proper localization of DMD and DCTN4
CC and for the formation and/or stability of a special subset of
CC microtubules associated with costameres and neuromuscular junctions. In
CC cardiomyocytes, required for coordinate assembly of Na/Ca exchanger,
CC SLC8A1/NCX1, Na/K ATPases ATP1A1 and ATP1A2 and inositol 1,4,5-
CC trisphosphate (InsP3) receptors at sarcoplasmic reticulum/sarcolemma
CC sites. Required for expression and targeting of SPTBN1 in neonatal
CC cardiomyocytes and for the regulation of neonatal cardiomyocyte
CC contraction rate (PubMed:12571597). In the inner segment of rod
CC photoreceptors, required for the coordinated expression of the Na/K
CC ATPase, Na/Ca exchanger and beta-2-spectrin (SPTBN1) (By similarity).
CC Plays a role in endocytosis and intracellular protein transport.
CC Associates with phosphatidylinositol 3-phosphate (PI3P)-positive
CC organelles and binds dynactin to promote long-range motility of cells.
CC Recruits RABGAP1L to (PI3P)-positive early endosomes, where RABGAP1L
CC inactivates RAB22A, and promotes polarized trafficking to the leading
CC edge of the migrating cells. Part of the ANK2/RABGAP1L complex which is
CC required for the polarized recycling of fibronectin receptor ITGA5
CC ITGB1 to the plasma membrane that enables continuous directional cell
CC migration (By similarity). {ECO:0000250|UniProtKB:Q8C8R3,
CC ECO:0000269|PubMed:12571597}.
CC -!- SUBUNIT: Interacts with RHBG and SPTBN1 (PubMed:15262991,
CC PubMed:15611082). Colocalizes with Na/K ATPase, Na/Ca exchanger and
CC SPTBN1 (PubMed:19007774). Directly interacts with DMD; this interaction
CC is necessary for DMD localization at the sarcolemma. Interacts with
CC DCTN4; this interaction is required for DCTN4 retention at costameres.
CC Identified in complexes that contain VIM, EZR, AHNAK, BFSP1, BFSP2,
CC ANK2, PLEC, PRX and spectrin (By similarity). Interacts (via death
CC domain) with RABGAP1L (via Rab-GAP TBC domain) (PubMed:27718357).
CC {ECO:0000250|UniProtKB:Q8C8R3, ECO:0000269|PubMed:15262991,
CC ECO:0000269|PubMed:15611082, ECO:0000269|PubMed:19007774,
CC ECO:0000269|PubMed:27718357}.
CC -!- INTERACTION:
CC Q01484; O00154: ACOT7; NbExp=2; IntAct=EBI-941975, EBI-948905;
CC Q01484; P11532-5: DMD; NbExp=2; IntAct=EBI-941975, EBI-1018651;
CC Q01484; Q9NZN3: EHD3; NbExp=2; IntAct=EBI-941975, EBI-2870749;
CC Q01484; P62993: GRB2; NbExp=2; IntAct=EBI-941975, EBI-401755;
CC Q01484; Q14654: KCNJ11; NbExp=6; IntAct=EBI-941975, EBI-2866553;
CC Q01484-2; P32418: SLC8A1; NbExp=2; IntAct=EBI-941994, EBI-2682189;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:19007774}. Membrane {ECO:0000269|PubMed:19007774}.
CC Cytoplasm, myofibril, sarcomere, M line {ECO:0000250|UniProtKB:Q8C8R3}.
CC Apical cell membrane {ECO:0000250|UniProtKB:Q8C8R3}. Cell membrane
CC {ECO:0000269|PubMed:19007774}. Postsynaptic cell membrane
CC {ECO:0000250|UniProtKB:Q8C8R3}. Early endosome
CC {ECO:0000250|UniProtKB:Q8C8R3}. Recycling endosome
CC {ECO:0000250|UniProtKB:Q8C8R3}. Lysosome
CC {ECO:0000250|UniProtKB:Q8C8R3}. Mitochondrion
CC {ECO:0000250|UniProtKB:Q8C8R3}. Cytoplasm, myofibril, sarcomere, Z line
CC {ECO:0000250|UniProtKB:Q8C8R3}. Cell membrane, sarcolemma, T-tubule
CC {ECO:0000250|UniProtKB:Q8C8R3}. Note=Expressed at the apical membrane
CC of airway lung epithelial cells (By similarity). Localized to the
CC plasma membrane of the inner segments of photoreceptors in retina.
CC Colocalizes with SPTBN1 in a distinct intracellular compartment of
CC neonatal cardiomyocytes (PubMed:19007774). In skeletal muscle,
CC localizes to neuromuscular junctions (By similarity). Localizes with
CC puncta at mitochondria ends. Colocalizes and cotransports on motile
CC vesicles with RABGAP1L (By similarity). {ECO:0000250|UniProtKB:Q8C8R3,
CC ECO:0000269|PubMed:19007774}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=3;
CC IsoId=Q01484-4; Sequence=Displayed;
CC Name=2;
CC IsoId=Q01484-2; Sequence=VSP_000268;
CC Name=4;
CC IsoId=Q01484-5; Sequence=VSP_037058, VSP_037059, VSP_000268;
CC Name=5;
CC IsoId=Q01484-7; Sequence=VSP_037057, VSP_000268, VSP_037060;
CC -!- TISSUE SPECIFICITY: Present in plasma membrane of neurons as well as
CC glial cells throughout the brain. Expressed in fetal brain and in
CC temporal cortex of adult brain. Also expressed in the inner segments of
CC rod photoreceptors in retina. {ECO:0000269|PubMed:1830053,
CC ECO:0000269|PubMed:1833308, ECO:0000269|PubMed:19007774}.
CC -!- DOMAIN: The tandem configuration of the two ZU5 and the UPA domains
CC forms a structural supramodule termed ZZU. ZU5-1 mediates interaction
CC with beta-spectrin, and the ZU5-1/UPA interface is required for
CC ankyrin's function other than binding to spectrin.
CC {ECO:0000269|PubMed:22411828}.
CC -!- PTM: Phosphorylated at multiple sites by different protein kinases and
CC each phosphorylation event regulates the protein's structure and
CC function. {ECO:0000305}.
CC -!- DISEASE: Long QT syndrome 4 (LQT4) [MIM:600919]: A heart disorder
CC characterized by a prolonged QT interval on the ECG and polymorphic
CC ventricular arrhythmias. They cause syncope and sudden death in
CC response to exercise or emotional stress, and can present with a
CC sentinel event of sudden cardiac death in infancy. Long QT syndrome
CC type 4 shows many atypical features compared to classical long QT
CC syndromes, including pronounced sinus bradycardia, polyphasic T waves
CC and atrial fibrillation. Cardiac repolarization defects may be not as
CC severe as in classical LQT syndromes and prolonged QT interval on EKG
CC is not a consistent feature. {ECO:0000269|PubMed:12571597,
CC ECO:0000269|PubMed:15178757, ECO:0000269|PubMed:17940615}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI25237.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAB42644.1; Type=Miscellaneous discrepancy; Note=CDS lacks C-terminal region which is nevertheless present in the underlying cDNA.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Ankyrin entry;
CC URL="https://en.wikipedia.org/wiki/Ankyrin";
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DR EMBL; X56957; CAA40278.1; -; mRNA.
DR EMBL; X56958; CAA40279.2; -; mRNA.
DR EMBL; Z26634; CAB42644.1; ALT_SEQ; mRNA.
DR EMBL; BX537758; CAD97827.1; -; mRNA.
DR EMBL; AC004057; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC093617; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC093879; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC093900; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC125235; AAI25236.1; -; mRNA.
DR EMBL; BC125236; AAI25237.1; ALT_FRAME; mRNA.
DR EMBL; M37123; AAA62828.1; -; Genomic_DNA.
DR CCDS; CCDS3702.1; -. [Q01484-4]
DR CCDS; CCDS43261.1; -. [Q01484-2]
DR CCDS; CCDS54796.1; -. [Q01484-5]
DR PIR; S37431; S37431.
DR RefSeq; NP_001120965.1; NM_001127493.1. [Q01484-5]
DR RefSeq; NP_001139.3; NM_001148.4. [Q01484-4]
DR RefSeq; NP_066187.2; NM_020977.3. [Q01484-2]
DR PDB; 4D8O; X-ray; 2.20 A; A=966-1039, A=1073-1476, A=3562-3653.
DR PDB; 4RLV; X-ray; 3.49 A; A=28-873.
DR PDB; 4RLY; X-ray; 2.50 A; A=28-318.
DR PDB; 5Y4D; X-ray; 3.30 A; A=28-693.
DR PDB; 5Y4E; X-ray; 2.34 A; A/B=264-483, A/B=857-896.
DR PDB; 5Y4F; X-ray; 1.95 A; A/B=430-873.
DR PDB; 5YIR; X-ray; 2.75 A; C/G/H=1588-1614.
DR PDB; 5YIS; X-ray; 2.20 A; C/D=1588-1614.
DR PDB; 6KZJ; X-ray; 1.50 A; A=1499-1570.
DR PDB; 6M3Q; X-ray; 3.44 A; E=951-1458.
DR PDBsum; 4D8O; -.
DR PDBsum; 4RLV; -.
DR PDBsum; 4RLY; -.
DR PDBsum; 5Y4D; -.
DR PDBsum; 5Y4E; -.
DR PDBsum; 5Y4F; -.
DR PDBsum; 5YIR; -.
DR PDBsum; 5YIS; -.
DR PDBsum; 6KZJ; -.
DR PDBsum; 6M3Q; -.
DR SMR; Q01484; -.
DR BioGRID; 106784; 66.
DR DIP; DIP-37425N; -.
DR IntAct; Q01484; 51.
DR MINT; Q01484; -.
DR STRING; 9606.ENSP00000349588; -.
DR TCDB; 8.A.28.1.1; the ankyrin (ankyrin) family.
DR GlyGen; Q01484; 4 sites, 1 O-linked glycan (4 sites).
DR iPTMnet; Q01484; -.
DR PhosphoSitePlus; Q01484; -.
DR SwissPalm; Q01484; -.
DR BioMuta; ANK2; -.
DR DMDM; 387912917; -.
DR EPD; Q01484; -.
DR jPOST; Q01484; -.
DR MassIVE; Q01484; -.
DR MaxQB; Q01484; -.
DR PaxDb; Q01484; -.
DR PeptideAtlas; Q01484; -.
DR PRIDE; Q01484; -.
DR ProteomicsDB; 57958; -. [Q01484-4]
DR ProteomicsDB; 57959; -. [Q01484-2]
DR ProteomicsDB; 57960; -. [Q01484-5]
DR ProteomicsDB; 57961; -. [Q01484-7]
DR ABCD; Q01484; 3 sequenced antibodies.
DR Antibodypedia; 26481; 357 antibodies from 25 providers.
DR DNASU; 287; -.
DR Ensembl; ENST00000357077.9; ENSP00000349588.4; ENSG00000145362.21. [Q01484-4]
DR Ensembl; ENST00000394537.7; ENSP00000378044.3; ENSG00000145362.21. [Q01484-2]
DR Ensembl; ENST00000506722.5; ENSP00000421067.1; ENSG00000145362.21. [Q01484-5]
DR GeneID; 287; -.
DR KEGG; hsa:287; -.
DR MANE-Select; ENST00000357077.9; ENSP00000349588.4; NM_001148.6; NP_001139.3.
DR UCSC; uc003ibd.5; human. [Q01484-4]
DR CTD; 287; -.
DR DisGeNET; 287; -.
DR GeneCards; ANK2; -.
DR GeneReviews; ANK2; -.
DR HGNC; HGNC:493; ANK2.
DR HPA; ENSG00000145362; Tissue enhanced (brain, retina, skeletal muscle, tongue).
DR MalaCards; ANK2; -.
DR MIM; 106410; gene.
DR MIM; 600919; phenotype.
DR neXtProt; NX_Q01484; -.
DR OpenTargets; ENSG00000145362; -.
DR Orphanet; 101016; Romano-Ward syndrome.
DR PharmGKB; PA24799; -.
DR VEuPathDB; HostDB:ENSG00000145362; -.
DR eggNOG; KOG4177; Eukaryota.
DR GeneTree; ENSGT00940000155279; -.
DR HOGENOM; CLU_000134_7_2_1; -.
DR InParanoid; Q01484; -.
DR OrthoDB; 1011028at2759; -.
DR PhylomeDB; Q01484; -.
DR TreeFam; TF351263; -.
DR PathwayCommons; Q01484; -.
DR Reactome; R-HSA-445095; Interaction between L1 and Ankyrins.
DR Reactome; R-HSA-6807878; COPI-mediated anterograde transport.
DR SignaLink; Q01484; -.
DR SIGNOR; Q01484; -.
DR BioGRID-ORCS; 287; 13 hits in 1073 CRISPR screens.
DR ChiTaRS; ANK2; human.
DR GenomeRNAi; 287; -.
DR Pharos; Q01484; Tbio.
DR PRO; PR:Q01484; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q01484; protein.
DR Bgee; ENSG00000145362; Expressed in lateral nuclear group of thalamus and 195 other tissues.
DR ExpressionAtlas; Q01484; baseline and differential.
DR Genevisible; Q01484; HS.
DR GO; GO:0031672; C:A band; ISS:BHF-UCL.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:UniProtKB.
DR GO; GO:0043034; C:costamere; ISS:BHF-UCL.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0014704; C:intercalated disc; ISS:BHF-UCL.
DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR GO; GO:0031430; C:M band; ISS:BHF-UCL.
DR GO; GO:0045121; C:membrane raft; IEA:Ensembl.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0055037; C:recycling endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0042383; C:sarcolemma; ISS:BHF-UCL.
DR GO; GO:0030315; C:T-tubule; ISS:BHF-UCL.
DR GO; GO:0030018; C:Z disc; ISS:BHF-UCL.
DR GO; GO:0051117; F:ATPase binding; ISS:BHF-UCL.
DR GO; GO:0008093; F:cytoskeletal anchor activity; IBA:GO_Central.
DR GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
DR GO; GO:0140031; F:phosphorylation-dependent protein binding; IPI:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; IPI:BHF-UCL.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; ISS:BHF-UCL.
DR GO; GO:0030507; F:spectrin binding; IPI:BHF-UCL.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; IEA:Ensembl.
DR GO; GO:0044325; F:transmembrane transporter binding; IPI:BHF-UCL.
DR GO; GO:0086014; P:atrial cardiac muscle cell action potential; IMP:BHF-UCL.
DR GO; GO:0086066; P:atrial cardiac muscle cell to AV node cell communication; ISS:BHF-UCL.
DR GO; GO:0003283; P:atrial septum development; IMP:BHF-UCL.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; ISS:BHF-UCL.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR GO; GO:0086046; P:membrane depolarization during SA node cell action potential; TAS:BHF-UCL.
DR GO; GO:0030913; P:paranodal junction assembly; IEA:Ensembl.
DR GO; GO:1901021; P:positive regulation of calcium ion transmembrane transporter activity; ISS:BHF-UCL.
DR GO; GO:0051928; P:positive regulation of calcium ion transport; ISS:BHF-UCL.
DR GO; GO:2001259; P:positive regulation of cation channel activity; ISS:BHF-UCL.
DR GO; GO:0010628; P:positive regulation of gene expression; IGI:BHF-UCL.
DR GO; GO:1901018; P:positive regulation of potassium ion transmembrane transporter activity; ISS:BHF-UCL.
DR GO; GO:0043268; P:positive regulation of potassium ion transport; ISS:BHF-UCL.
DR GO; GO:0008104; P:protein localization; IGI:BHF-UCL.
DR GO; GO:0034394; P:protein localization to cell surface; ISS:BHF-UCL.
DR GO; GO:0070972; P:protein localization to endoplasmic reticulum; IGI:BHF-UCL.
DR GO; GO:0036309; P:protein localization to M-band; ISS:BHF-UCL.
DR GO; GO:0033365; P:protein localization to organelle; IGI:BHF-UCL.
DR GO; GO:0072659; P:protein localization to plasma membrane; IGI:BHF-UCL.
DR GO; GO:0036371; P:protein localization to T-tubule; ISS:BHF-UCL.
DR GO; GO:0050821; P:protein stabilization; ISS:BHF-UCL.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0098910; P:regulation of atrial cardiac muscle cell action potential; IMP:BHF-UCL.
DR GO; GO:1901019; P:regulation of calcium ion transmembrane transporter activity; ISS:BHF-UCL.
DR GO; GO:0051924; P:regulation of calcium ion transport; IGI:BHF-UCL.
DR GO; GO:0086004; P:regulation of cardiac muscle cell contraction; IGI:BHF-UCL.
DR GO; GO:0055117; P:regulation of cardiac muscle contraction; IMP:BHF-UCL.
DR GO; GO:0010882; P:regulation of cardiac muscle contraction by calcium ion signaling; IMP:BHF-UCL.
DR GO; GO:0010881; P:regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion; IGI:BHF-UCL.
DR GO; GO:0002027; P:regulation of heart rate; IMP:BHF-UCL.
DR GO; GO:0086091; P:regulation of heart rate by cardiac conduction; IMP:BHF-UCL.
DR GO; GO:0031647; P:regulation of protein stability; IC:BHF-UCL.
DR GO; GO:0051279; P:regulation of release of sequestered calcium ion into cytosol; IGI:BHF-UCL.
DR GO; GO:0098907; P:regulation of SA node cell action potential; IMP:BHF-UCL.
DR GO; GO:0060307; P:regulation of ventricular cardiac muscle cell membrane repolarization; IMP:BHF-UCL.
DR GO; GO:0051597; P:response to methylmercury; IEA:Ensembl.
DR GO; GO:0086015; P:SA node cell action potential; ISS:BHF-UCL.
DR GO; GO:0086070; P:SA node cell to atrial cardiac muscle cell communication; IMP:BHF-UCL.
DR GO; GO:0070296; P:sarcoplasmic reticulum calcium ion transport; TAS:BHF-UCL.
DR GO; GO:0033292; P:T-tubule organization; ISS:BHF-UCL.
DR GO; GO:0086005; P:ventricular cardiac muscle cell action potential; IMP:BHF-UCL.
DR Gene3D; 1.10.533.10; -; 1.
DR Gene3D; 1.25.40.20; -; 3.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR040745; Ankyrin_UPA.
DR InterPro; IPR011029; DEATH-like_dom_sf.
DR InterPro; IPR000488; Death_domain.
DR InterPro; IPR000906; ZU5_dom.
DR Pfam; PF00023; Ank; 1.
DR Pfam; PF12796; Ank_2; 7.
DR Pfam; PF13637; Ank_4; 2.
DR Pfam; PF00531; Death; 1.
DR Pfam; PF17809; UPA_2; 1.
DR Pfam; PF00791; ZU5; 2.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 23.
DR SMART; SM00005; DEATH; 1.
DR SMART; SM00218; ZU5; 1.
DR SUPFAM; SSF47986; SSF47986; 1.
DR SUPFAM; SSF48403; SSF48403; 3.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 20.
DR PROSITE; PS50017; DEATH_DOMAIN; 1.
DR PROSITE; PS51145; ZU5; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; ANK repeat; Cell membrane; Cytoplasm;
KW Cytoskeleton; Disease variant; Endocytosis; Endosome; Long QT syndrome;
KW Lysosome; Membrane; Mitochondrion; Phosphoprotein;
KW Postsynaptic cell membrane; Protein transport; Reference proteome; Repeat;
KW Synapse; Transport.
FT CHAIN 1..3957
FT /note="Ankyrin-2"
FT /id="PRO_0000066885"
FT REPEAT 30..62
FT /note="ANK 1"
FT REPEAT 63..92
FT /note="ANK 2"
FT REPEAT 96..125
FT /note="ANK 3"
FT REPEAT 129..158
FT /note="ANK 4"
FT REPEAT 162..191
FT /note="ANK 5"
FT REPEAT 193..220
FT /note="ANK 6"
FT REPEAT 232..261
FT /note="ANK 7"
FT REPEAT 265..294
FT /note="ANK 8"
FT REPEAT 298..327
FT /note="ANK 9"
FT REPEAT 331..360
FT /note="ANK 10"
FT REPEAT 364..393
FT /note="ANK 11"
FT REPEAT 397..426
FT /note="ANK 12"
FT REPEAT 430..459
FT /note="ANK 13"
FT REPEAT 463..492
FT /note="ANK 14"
FT REPEAT 496..525
FT /note="ANK 15"
FT REPEAT 529..558
FT /note="ANK 16"
FT REPEAT 562..591
FT /note="ANK 17"
FT REPEAT 595..624
FT /note="ANK 18"
FT REPEAT 628..657
FT /note="ANK 19"
FT REPEAT 661..690
FT /note="ANK 20"
FT REPEAT 694..723
FT /note="ANK 21"
FT REPEAT 727..756
FT /note="ANK 22"
FT REPEAT 760..789
FT /note="ANK 23"
FT REPEAT 793..822
FT /note="ANK 24"
FT DOMAIN 968..1156
FT /note="ZU5 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00485"
FT DOMAIN 1158..1304
FT /note="ZU5 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00485"
FT DOMAIN 1450..1535
FT /note="Death 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00064"
FT REPEAT 1806..1817
FT /note="Repeat A"
FT REPEAT 1818..1829
FT /note="Repeat A"
FT REPEAT 1830..1841
FT /note="Repeat A"
FT REPEAT 1842..1853
FT /note="Repeat A"
FT REPEAT 1854..1865
FT /note="Repeat A"
FT REPEAT 1866..1877
FT /note="Repeat A"
FT REPEAT 1878..1889
FT /note="Repeat A"
FT REPEAT 1890..1900
FT /note="Repeat A; approximate"
FT REPEAT 1901..1912
FT /note="Repeat A"
FT REPEAT 1913..1924
FT /note="Repeat A"
FT REPEAT 1925..1935
FT /note="Repeat A; approximate"
FT REPEAT 1936..1947
FT /note="Repeat A"
FT REPEAT 1948..1959
FT /note="Repeat A"
FT REPEAT 1960..1971
FT /note="Repeat A"
FT REPEAT 1972..1983
FT /note="Repeat A"
FT DOMAIN 3569..3653
FT /note="Death 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00064"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 966..1125
FT /note="Interaction with SPTBN1"
FT /evidence="ECO:0000269|PubMed:15262991"
FT REGION 1289..1423
FT /note="UPA domain"
FT REGION 1457..1486
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1670..2137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1806..1983
FT /note="Repeat-rich region"
FT REGION 2197..2411
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2430..2484
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2507..2586
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2604..2852
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2864..2904
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2923..2951
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2987..3016
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3069..3099
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3136..3462
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3777..3858
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..31
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1670..1688
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1710..1736
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1764..1803
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1825..1903
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1969..1983
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2006..2039
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2040..2055
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2070..2125
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2255..2286
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2299..2318
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2356..2379
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2520..2558
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2565..2586
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2604..2623
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2654..2669
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2694..2721
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2722..2772
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2783..2798
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2814..2832
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2836..2852
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2888..2904
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2926..2951
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3071..3099
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3177..3192
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3196..3217
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3241..3267
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3304..3330
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3331..3347
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3359..3390
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3405..3434
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3442..3458
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3777..3800
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3809..3823
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3829..3843
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 31
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8C8R3"
FT MOD_RES 34
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8C8R3"
FT MOD_RES 378
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q8C8R3"
FT MOD_RES 531
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q8C8R3"
FT MOD_RES 846
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 853
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8C8R3"
FT MOD_RES 874
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8C8R3"
FT MOD_RES 1382
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q8C8R3"
FT MOD_RES 1459
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8C8R3"
FT MOD_RES 1461
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8C8R3"
FT MOD_RES 1473
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8C8R3"
FT MOD_RES 1500
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8C8R3"
FT MOD_RES 1596
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8C8R3"
FT MOD_RES 1732
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8C8R3"
FT MOD_RES 1733
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8C8R3"
FT MOD_RES 1736
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8C8R3"
FT MOD_RES 1855
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8C8R3"
FT MOD_RES 1858
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8C8R3"
FT MOD_RES 1929
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8C8R3"
FT MOD_RES 2127
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8C8R3"
FT MOD_RES 2239
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8C8R3"
FT MOD_RES 2243
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8C8R3"
FT MOD_RES 2269
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8C8R3"
FT MOD_RES 2275
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8C8R3"
FT MOD_RES 2405
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8C8R3"
FT MOD_RES 2440
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8C8R3"
FT MOD_RES 2454
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8C8R3"
FT MOD_RES 2516
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8C8R3"
FT MOD_RES 2521
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8C8R3"
FT MOD_RES 2583
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8C8R3"
FT MOD_RES 2679
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8C8R3"
FT MOD_RES 2701
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8C8R3"
FT MOD_RES 2781
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8C8R3"
FT MOD_RES 2795
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8C8R3"
FT MOD_RES 2956
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8C8R3"
FT MOD_RES 3075
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8C8R3"
FT MOD_RES 3078
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8C8R3"
FT MOD_RES 3273
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8C8R3"
FT MOD_RES 3276
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8C8R3"
FT MOD_RES 3277
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8C8R3"
FT MOD_RES 3390
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8C8R3"
FT MOD_RES 3409
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8C8R3"
FT MOD_RES 3474
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8C8R3"
FT MOD_RES 3735
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8C8R3"
FT MOD_RES 3776
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8C8R3"
FT MOD_RES 3797
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8C8R3"
FT MOD_RES 3803
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8C8R3"
FT MOD_RES 3814
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8C8R3"
FT MOD_RES 3823
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8C8R3"
FT MOD_RES 3909
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8C8R3"
FT VAR_SEQ 1..1348
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_037057"
FT VAR_SEQ 1..27
FT /note="MMNEDAAQKSDSGEKFNGSSQRRKRPK -> MTTMLQ (in isoform
FT 4)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_037058"
FT VAR_SEQ 967
FT /note="G -> GRASPCLERDNSS (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_037059"
FT VAR_SEQ 1477..3561
FT /note="Missing (in isoform 2, isoform 4 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:17974005, ECO:0000303|PubMed:1830053"
FT /id="VSP_000268"
FT VAR_SEQ 3870
FT /note="K -> KELTEELGELEASSDEEAMVTTRVVRRRVIIQ (in isoform
FT 5)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_037060"
FT VARIANT 685
FT /note="G -> E (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035606"
FT VARIANT 687
FT /note="N -> S (in dbSNP:rs29372)"
FT /id="VAR_055504"
FT VARIANT 1267
FT /note="G -> R (in a colorectal cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035607"
FT VARIANT 1458
FT /note="E -> G (in LQT4; unknown pathological significance;
FT abnormal calcium ion homeostasis, when tested in a
FT heterologous system; dbSNP:rs72544141)"
FT /evidence="ECO:0000269|PubMed:12571597,
FT ECO:0000269|PubMed:15178757, ECO:0000269|PubMed:17940615"
FT /id="VAR_022934"
FT VARIANT 1555
FT /note="V -> D"
FT /evidence="ECO:0000269|PubMed:17940615"
FT /id="VAR_081135"
FT VARIANT 2369
FT /note="V -> A (in dbSNP:rs28377576)"
FT /id="VAR_055505"
FT VARIANT 3653
FT /note="T -> K (in a colorectal cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035608"
FT VARIANT 3740
FT /note="L -> I (in LQT4; loss of function;
FT dbSNP:rs35530544)"
FT /evidence="ECO:0000269|PubMed:15178757,
FT ECO:0000269|PubMed:17940615"
FT /id="VAR_022935"
FT VARIANT 3744
FT /note="T -> N (in LQT4; loss of function;
FT dbSNP:rs121912705)"
FT /evidence="ECO:0000269|PubMed:15178757,
FT ECO:0000269|PubMed:17940615"
FT /id="VAR_022936"
FT VARIANT 3906
FT /note="R -> W (in LQT4; loss of function;
FT dbSNP:rs121912706)"
FT /evidence="ECO:0000269|PubMed:15178757,
FT ECO:0000269|PubMed:17940615"
FT /id="VAR_022937"
FT VARIANT 3931
FT /note="E -> K (in LQT4; loss of function;
FT dbSNP:rs45454496)"
FT /evidence="ECO:0000269|PubMed:15178757,
FT ECO:0000269|PubMed:17940615"
FT /id="VAR_022938"
FT MUTAGEN 975..977
FT /note="DAR->AAA: Prevents binding to SPTBN1."
FT /evidence="ECO:0000269|PubMed:15262991"
FT MUTAGEN 1000
FT /note="A->P: Prevents binding to SPTBN1."
FT /evidence="ECO:0000269|PubMed:15262991"
FT MUTAGEN 1100..1103
FT /note="ENGD->AAGA: Weak binding to SPTBN1."
FT /evidence="ECO:0000269|PubMed:15262991"
FT CONFLICT 220
FT /note="V -> I (in Ref. 4; CAD97827)"
FT /evidence="ECO:0000305"
FT CONFLICT 475..476
FT /note="GQ -> PE (in Ref. 7; AAA62828)"
FT /evidence="ECO:0000305"
FT CONFLICT 2787
FT /note="A -> R (in Ref. 3; CAB42644)"
FT /evidence="ECO:0000305"
FT CONFLICT 2999
FT /note="Q -> L (in Ref. 3; CAB42644)"
FT /evidence="ECO:0000305"
FT CONFLICT 3140..3141
FT /note="EE -> RY (in Ref. 5; AC093879)"
FT /evidence="ECO:0000305"
FT CONFLICT 3185
FT /note="D -> S (in Ref. 3; CAB42644)"
FT /evidence="ECO:0000305"
FT CONFLICT 3699
FT /note="V -> A (in Ref. 4; CAD97827)"
FT /evidence="ECO:0000305"
FT CONFLICT 3737
FT /note="A -> S (in Ref. 1; CAA40279 and 3; CAB42644)"
FT /evidence="ECO:0000305"
FT CONFLICT 3955..3956
FT /note="NN -> SM (in Ref. 5; AC093879)"
FT /evidence="ECO:0000305"
FT HELIX 30..41
FT /evidence="ECO:0007829|PDB:4RLY"
FT HELIX 44..52
FT /evidence="ECO:0007829|PDB:4RLY"
FT HELIX 67..74
FT /evidence="ECO:0007829|PDB:4RLY"
FT HELIX 77..86
FT /evidence="ECO:0007829|PDB:4RLY"
FT HELIX 100..106
FT /evidence="ECO:0007829|PDB:4RLY"
FT HELIX 110..118
FT /evidence="ECO:0007829|PDB:4RLY"
FT HELIX 133..139
FT /evidence="ECO:0007829|PDB:4RLY"
FT HELIX 143..150
FT /evidence="ECO:0007829|PDB:4RLY"
FT TURN 151..153
FT /evidence="ECO:0007829|PDB:4RLY"
FT HELIX 166..172
FT /evidence="ECO:0007829|PDB:4RLY"
FT HELIX 176..183
FT /evidence="ECO:0007829|PDB:4RLY"
FT TURN 184..186
FT /evidence="ECO:0007829|PDB:4RLY"
FT HELIX 195..202
FT /evidence="ECO:0007829|PDB:4RLY"
FT HELIX 205..211
FT /evidence="ECO:0007829|PDB:4RLY"
FT HELIX 212..214
FT /evidence="ECO:0007829|PDB:4RLY"
FT TURN 221..223
FT /evidence="ECO:0007829|PDB:5Y4D"
FT HELIX 225..227
FT /evidence="ECO:0007829|PDB:4RLY"
FT HELIX 236..243
FT /evidence="ECO:0007829|PDB:4RLY"
FT HELIX 246..254
FT /evidence="ECO:0007829|PDB:4RLY"
FT HELIX 264..266
FT /evidence="ECO:0007829|PDB:4RLY"
FT HELIX 269..275
FT /evidence="ECO:0007829|PDB:5Y4E"
FT HELIX 279..287
FT /evidence="ECO:0007829|PDB:5Y4E"
FT HELIX 302..308
FT /evidence="ECO:0007829|PDB:5Y4E"
FT HELIX 312..320
FT /evidence="ECO:0007829|PDB:5Y4E"
FT HELIX 335..341
FT /evidence="ECO:0007829|PDB:5Y4E"
FT HELIX 345..353
FT /evidence="ECO:0007829|PDB:5Y4E"
FT HELIX 368..375
FT /evidence="ECO:0007829|PDB:5Y4E"
FT HELIX 378..386
FT /evidence="ECO:0007829|PDB:5Y4E"
FT HELIX 396..398
FT /evidence="ECO:0007829|PDB:5Y4E"
FT HELIX 401..407
FT /evidence="ECO:0007829|PDB:5Y4E"
FT HELIX 411..419
FT /evidence="ECO:0007829|PDB:5Y4E"
FT HELIX 434..441
FT /evidence="ECO:0007829|PDB:5Y4F"
FT HELIX 444..452
FT /evidence="ECO:0007829|PDB:5Y4F"
FT HELIX 467..473
FT /evidence="ECO:0007829|PDB:5Y4F"
FT HELIX 477..485
FT /evidence="ECO:0007829|PDB:5Y4F"
FT HELIX 495..497
FT /evidence="ECO:0007829|PDB:5Y4F"
FT HELIX 500..506
FT /evidence="ECO:0007829|PDB:5Y4F"
FT HELIX 510..518
FT /evidence="ECO:0007829|PDB:5Y4F"
FT HELIX 533..540
FT /evidence="ECO:0007829|PDB:5Y4F"
FT HELIX 543..551
FT /evidence="ECO:0007829|PDB:5Y4F"
FT HELIX 566..573
FT /evidence="ECO:0007829|PDB:5Y4F"
FT HELIX 576..584
FT /evidence="ECO:0007829|PDB:5Y4F"
FT HELIX 599..605
FT /evidence="ECO:0007829|PDB:5Y4F"
FT HELIX 609..617
FT /evidence="ECO:0007829|PDB:5Y4F"
FT HELIX 632..639
FT /evidence="ECO:0007829|PDB:5Y4F"
FT HELIX 642..650
FT /evidence="ECO:0007829|PDB:5Y4F"
FT HELIX 665..672
FT /evidence="ECO:0007829|PDB:5Y4F"
FT HELIX 675..683
FT /evidence="ECO:0007829|PDB:5Y4F"
FT STRAND 693..695
FT /evidence="ECO:0007829|PDB:4RLV"
FT HELIX 698..705
FT /evidence="ECO:0007829|PDB:5Y4F"
FT HELIX 708..716
FT /evidence="ECO:0007829|PDB:5Y4F"
FT HELIX 731..738
FT /evidence="ECO:0007829|PDB:5Y4F"
FT HELIX 741..749
FT /evidence="ECO:0007829|PDB:5Y4F"
FT STRAND 759..761
FT /evidence="ECO:0007829|PDB:4RLV"
FT HELIX 764..770
FT /evidence="ECO:0007829|PDB:5Y4F"
FT HELIX 774..782
FT /evidence="ECO:0007829|PDB:5Y4F"
FT HELIX 797..803
FT /evidence="ECO:0007829|PDB:5Y4F"
FT HELIX 807..814
FT /evidence="ECO:0007829|PDB:5Y4F"
FT TURN 831..833
FT /evidence="ECO:0007829|PDB:5Y4F"
FT STRAND 960..962
FT /evidence="ECO:0007829|PDB:6M3Q"
FT STRAND 969..974
FT /evidence="ECO:0007829|PDB:4D8O"
FT STRAND 979..982
FT /evidence="ECO:0007829|PDB:4D8O"
FT STRAND 984..986
FT /evidence="ECO:0007829|PDB:4D8O"
FT STRAND 990..993
FT /evidence="ECO:0007829|PDB:4D8O"
FT STRAND 998..1000
FT /evidence="ECO:0007829|PDB:6M3Q"
FT STRAND 1002..1009
FT /evidence="ECO:0007829|PDB:4D8O"
FT STRAND 1025..1028
FT /evidence="ECO:0007829|PDB:4D8O"
FT STRAND 1031..1035
FT /evidence="ECO:0007829|PDB:4D8O"
FT STRAND 1039..1042
FT /evidence="ECO:0007829|PDB:4D8O"
FT STRAND 1076..1082
FT /evidence="ECO:0007829|PDB:4D8O"
FT TURN 1088..1091
FT /evidence="ECO:0007829|PDB:4D8O"
FT STRAND 1092..1103
FT /evidence="ECO:0007829|PDB:4D8O"
FT HELIX 1114..1121
FT /evidence="ECO:0007829|PDB:6M3Q"
FT HELIX 1131..1137
FT /evidence="ECO:0007829|PDB:4D8O"
FT STRAND 1139..1146
FT /evidence="ECO:0007829|PDB:4D8O"
FT STRAND 1149..1157
FT /evidence="ECO:0007829|PDB:4D8O"
FT STRAND 1159..1165
FT /evidence="ECO:0007829|PDB:4D8O"
FT STRAND 1168..1172
FT /evidence="ECO:0007829|PDB:4D8O"
FT STRAND 1174..1176
FT /evidence="ECO:0007829|PDB:4D8O"
FT STRAND 1180..1183
FT /evidence="ECO:0007829|PDB:4D8O"
FT STRAND 1192..1199
FT /evidence="ECO:0007829|PDB:4D8O"
FT HELIX 1203..1210
FT /evidence="ECO:0007829|PDB:4D8O"
FT STRAND 1213..1216
FT /evidence="ECO:0007829|PDB:4D8O"
FT STRAND 1219..1226
FT /evidence="ECO:0007829|PDB:4D8O"
FT STRAND 1228..1238
FT /evidence="ECO:0007829|PDB:4D8O"
FT STRAND 1258..1263
FT /evidence="ECO:0007829|PDB:4D8O"
FT HELIX 1277..1279
FT /evidence="ECO:0007829|PDB:4D8O"
FT STRAND 1283..1285
FT /evidence="ECO:0007829|PDB:4D8O"
FT STRAND 1288..1295
FT /evidence="ECO:0007829|PDB:4D8O"
FT STRAND 1298..1305
FT /evidence="ECO:0007829|PDB:4D8O"
FT HELIX 1307..1309
FT /evidence="ECO:0007829|PDB:4D8O"
FT HELIX 1310..1321
FT /evidence="ECO:0007829|PDB:4D8O"
FT STRAND 1325..1335
FT /evidence="ECO:0007829|PDB:4D8O"
FT STRAND 1338..1349
FT /evidence="ECO:0007829|PDB:4D8O"
FT HELIX 1357..1359
FT /evidence="ECO:0007829|PDB:4D8O"
FT STRAND 1365..1369
FT /evidence="ECO:0007829|PDB:4D8O"
FT STRAND 1373..1376
FT /evidence="ECO:0007829|PDB:4D8O"
FT STRAND 1380..1391
FT /evidence="ECO:0007829|PDB:4D8O"
FT STRAND 1399..1402
FT /evidence="ECO:0007829|PDB:4D8O"
FT STRAND 1410..1418
FT /evidence="ECO:0007829|PDB:4D8O"
FT STRAND 1420..1422
FT /evidence="ECO:0007829|PDB:6M3Q"
FT STRAND 1424..1432
FT /evidence="ECO:0007829|PDB:4D8O"
FT STRAND 1445..1451
FT /evidence="ECO:0007829|PDB:4D8O"
FT HELIX 1484..1491
FT /evidence="ECO:0007829|PDB:4D8O"
FT HELIX 1501..1521
FT /evidence="ECO:0007829|PDB:6KZJ"
FT HELIX 1534..1543
FT /evidence="ECO:0007829|PDB:6KZJ"
FT HELIX 1548..1568
FT /evidence="ECO:0007829|PDB:6KZJ"
FT STRAND 1592..1594
FT /evidence="ECO:0007829|PDB:5YIS"
FT HELIX 1597..1601
FT /evidence="ECO:0007829|PDB:5YIS"
FT STRAND 1606..1609
FT /evidence="ECO:0007829|PDB:5YIS"
SQ SEQUENCE 3957 AA; 433715 MW; 41C1A240CC5A3B72 CRC64;
MMNEDAAQKS DSGEKFNGSS QRRKRPKKSD SNASFLRAAR AGNLDKVVEY LKGGIDINTC
NQNGLNALHL AAKEGHVGLV QELLGRGSSV DSATKKGNTA LHIASLAGQA EVVKVLVKEG
ANINAQSQNG FTPLYMAAQE NHIDVVKYLL ENGANQSTAT EDGFTPLAVA LQQGHNQAVA
ILLENDTKGK VRLPALHIAA RKDDTKSAAL LLQNDHNADV QSKMMVNRTT ESGFTPLHIA
AHYGNVNVAT LLLNRGAAVD FTARNGITPL HVASKRGNTN MVKLLLDRGG QIDAKTRDGL
TPLHCAARSG HDQVVELLLE RGAPLLARTK NGLSPLHMAA QGDHVECVKH LLQHKAPVDD
VTLDYLTALH VAAHCGHYRV TKLLLDKRAN PNARALNGFT PLHIACKKNR IKVMELLVKY
GASIQAITES GLTPIHVAAF MGHLNIVLLL LQNGASPDVT NIRGETALHM AARAGQVEVV
RCLLRNGALV DARAREEQTP LHIASRLGKT EIVQLLLQHM AHPDAATTNG YTPLHISARE
GQVDVASVLL EAGAAHSLAT KKGFTPLHVA AKYGSLDVAK LLLQRRAAAD SAGKNGLTPL
HVAAHYDNQK VALLLLEKGA SPHATAKNGY TPLHIAAKKN QMQIASTLLN YGAETNIVTK
QGVTPLHLAS QEGHTDMVTL LLDKGANIHM STKSGLTSLH LAAQEDKVNV ADILTKHGAD
QDAHTKLGYT PLIVACHYGN VKMVNFLLKQ GANVNAKTKN GYTPLHQAAQ QGHTHIINVL
LQHGAKPNAT TANGNTALAI AKRLGYISVV DTLKVVTEEV TTTTTTITEK HKLNVPETMT
EVLDVSDEEG DDTMTGDGGE YLRPEDLKEL GDDSLPSSQF LDGMNYLRYS LEGGRSDSLR
SFSSDRSHTL SHASYLRDSA VMDDSVVIPS HQVSTLAKEA ERNSYRLSWG TENLDNVALS
SSPIHSGFLV SFMVDARGGA MRGCRHNGLR IIIPPRKCTA PTRVTCRLVK RHRLATMPPM
VEGEGLASRL IEVGPSGAQF LGKLHLPTAP PPLNEGESLV SRILQLGPPG TKFLGPVIVE
IPHFAALRGK ERELVVLRSE NGDSWKEHFC DYTEDELNEI LNGMDEVLDS PEDLEKKRIC
RIITRDFPQY FAVVSRIKQD SNLIGPEGGV LSSTVVPQVQ AVFPEGALTK RIRVGLQAQP
MHSELVKKIL GNKATFSPIV TLEPRRRKFH KPITMTIPVP KASSDVMLNG FGGDAPTLRL
LCSITGGTTP AQWEDITGTT PLTFVNECVS FTTNVSARFW LIDCRQIQES VTFASQVYRE
IICVPYMAKF VVFAKSHDPI EARLRCFCMT DDKVDKTLEQ QENFAEVARS RDVEVLEGKP
IYVDCFGNLV PLTKSGQHHI FSFFAFKENR LPLFVKVRDT TQEPCGRLSF MKEPKSTRGL
VHQAICNLNI TLPIYTKESE SDQEQEEEID MTSEKNDETE STETSVLKSH LVNEVPVLAS
PDLLSEVSEM KQDLIKMTAI LTTDVSDKAG SIKVKELVKA AEEEPGEPFE IVERVKEDLE
KVNEILRSGT CTRDESSVQS SRSERGLVEE EWVIVSDEEI EEARQKAPLE ITEYPCVEVR
IDKEIKGKVE KDSTGLVNYL TDDLNTCVPL PKEQLQTVQD KAGKKCEALA VGRSSEKEGK
DIPPDETQST QKQHKPSLGI KKPVRRKLKE KQKQKEEGLQ ASAEKAELKK GSSEESLGED
PGLAPEPLPT VKATSPLIEE TPIGSIKDKV KALQKRVEDE QKGRSKLPIR VKGKEDVPKK
TTHRPHPAAS PSLKSERHAP GSPSPKTERH STLSSSAKTE RHPPVSPSSK TEKHSPVSPS
AKTERHSPAS SSSKTEKHSP VSPSTKTERH SPVSSTKTER HPPVSPSGKT DKRPPVSPSG
RTEKHPPVSP GRTEKRLPVS PSGRTDKHQP VSTAGKTEKH LPVSPSGKTE KQPPVSPTSK
TERIEETMSV RELMKAFQSG QDPSKHKTGL FEHKSAKQKQ PQEKGKVRVE KEKGPILTQR
EAQKTENQTI KRGQRLPVTG TAESKRGVRV SSIGVKKEDA AGGKEKVLSH KIPEPVQSVP
EEESHRESEV PKEKMADEQG DMDLQISPDR KTSTDFSEVI KQELEDNDKY QQFRLSEETE
KAQLHLDQVL TSPFNTTFPL DYMKDEFLPA LSLQSGALDG SSESLKNEGV AGSPCGSLME
GTPQISSEES YKHEGLAETP ETSPESLSFS PKKSEEQTGE TKESTKTETT TEIRSEKEHP
TTKDITGGSE ERGATVTEDS ETSTESFQKE ATLGSPKDTS PKRQDDCTGS CSVALAKETP
TGLTEEAACD EGQRTFGSSA HKTQTDSEVQ ESTATSDETK ALPLPEASVK TDTGTESKPQ
GVIRSPQGLE LALPSRDSEV LSAVADDSLA VSHKDSLEAS PVLEDNSSHK TPDSLEPSPL
KESPCRDSLE SSPVEPKMKA GIFPSHFPLP AAVAKTELLT EVASVRSRLL RDPDGSAEDD
SLEQTSLMES SGKSPLSPDT PSSEEVSYEV TPKTTDVSTP KPAVIHECAE EDDSENGEKK
RFTPEEEMFK MVTKIKMFDE LEQEAKQKRD YKKEPKQEES SSSSDPDADC SVDVDEPKHT
GSGEDESGVP VLVTSESRKV SSSSESEPEL AQLKKGADSG LLPEPVIRVQ PPSPLPSSMD
SNSSPEEVQF QPVVSKQYTF KMNEDTQEEP GKSEEEKDSE SHLAEDRHAV STEAEDRSYD
KLNRDTDQPK ICDGHGCEAM SPSSSAAPVS SGLQSPTGDD VDEQPVIYKE SLALQGTHEK
DTEGEELDVS RAESPQADCP SESFSSSSSL PHCLVSEGKE LDEDISATSS IQKTEVTKTD
ETFENLPKDC PSQDSSITTQ TDRFSMDVPV SDLAENDEIY DPQITSPYEN VPSQSFFSSE
ESKTQTDANH TTSFHSSEVY SVTITSPVED VVVASSSSGT VLSKESNFEG QDIKMESQQE
STLWEMQSDS VSSSFEPTMS ATTTVVGEQI SKVIITKTDV DSDSWSEIRE DDEAFEARVK
EEEQKIFGLM VDRQSQGTTP DTTPARTPTE EGTPTSEQNP FLFQEGKLFE MTRSGAIDMT
KRSYADESFH FFQIGQESRE ETLSEDVKEG ATGADPLPLE TSAESLALSE SKETVDDEAD
LLPDDVSEEV EEIPASDAQL NSQMGISAST ETPTKEAVSV GTKDLPTVQT GDIPPLSGVK
QISCPDSSEP AVQVQLDFST LTRSVYSDRG DDSPDSSPEE QKSVIEIPTA PMENVPFTES
KSKIPVRTMP TSTPAPPSAE YESSVSEDFL SSVDEENKAD EAKPKSKLPV KVPLQRVEQQ
LSDLDTSVQK TVAPQGQDMA SIAPDNRSKS ESDASSLDSK TKCPVKTRSY TETETESRER
AEELELESEE GATRPKILTS RLPVKSRSTT SSCRGGTSPT KESKEHFFDL YRNSIEFFEE
ISDEASKLVD RLTQSEREQE IVSDDESSSA LEVSVIENLP PVETEHSVPE DIFDTRPIWD
ESIETLIERI PDENGHDHAE DPQDEQERIE ERLAYIADHL GFSWTELARE LDFTEEQIHQ
IRIENPNSLQ DQSHALLKYW LERDGKHATD TNLVECLTKI NRMDIVHLME TNTEPLQERI
SHSYAEIEQT ITLDHSEGFS VLQEELCTAQ HKQKEEQAVS KESETCDHPP IVSEEDISVG
YSTFQDGVPK TEGDSSATAL FPQTHKEQVQ QDFSGKMQDL PEESSLEYQQ EYFVTTPGTE
TSETQKAMIV PSSPSKTPEE VSTPAEEEKL YLQTPTSSER GGSPIIQEPE EPSEHREESS
PRKTSLVIVE SADNQPETCE RLDEDAAFEK GDDMPEIPPE TVTEEEYIDE HGHTVVKKVT
RKIIRRYVSS EGTEKEEIMV QGMPQEPVNI EEGDGYSKVI KRVVLKSDTE QSEDNNE
