TANC2_HUMAN
ID TANC2_HUMAN Reviewed; 1990 AA.
AC Q9HCD6; Q9HAC3; Q9NW88; Q9NXY9; Q9ULS2;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 3.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Protein TANC2;
DE AltName: Full=Tetratricopeptide repeat, ankyrin repeat and coiled-coil domain-containing protein 2;
GN Name=TANC2; Synonyms=KIAA1148, KIAA1636;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 127-1990 (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=10997877; DOI=10.1093/dnares/7.4.271;
RA Nagase T., Kikuno R., Nakayama M., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVIII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:273-281(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 676-1990 (ISOFORM 3), AND
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 843-1990 (ISOFORM 4).
RC TISSUE=Embryo;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 869-1990 (ISOFORM 2).
RA Dahllund L., Sjodin J., Wikstrom L.;
RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1448-1990 (ISOFORMS 1/2).
RC TISSUE=Brain;
RX PubMed=10574461; DOI=10.1093/dnares/6.5.329;
RA Hirosawa M., Nagase T., Ishikawa K., Kikuno R., Nomura N., Ohara O.;
RT "Characterization of cDNA clones selected by the GeneMark analysis from
RT size-fractionated cDNA libraries from human brain.";
RL DNA Res. 6:329-336(1999).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1442, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=15144186; DOI=10.1021/ac035352d;
RA Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,
RA Peters E.C.;
RT "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from
RT human T cells using immobilized metal affinity chromatography and tandem
RT mass spectrometry.";
RL Anal. Chem. 76:2763-2772(2004).
RN [7]
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 [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [10]
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 [11]
RP IDENTIFICATION BY 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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-169; SER-238; SER-294;
RP SER-400; SER-1458; SER-1530; SER-1545; SER-1579; SER-1722 AND SER-1827, 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 [13]
RP VARIANT IDDALDS CYS-760.
RX PubMed=23033978; DOI=10.1056/nejmoa1206524;
RA de Ligt J., Willemsen M.H., van Bon B.W., Kleefstra T., Yntema H.G.,
RA Kroes T., Vulto-van Silfhout A.T., Koolen D.A., de Vries P., Gilissen C.,
RA del Rosario M., Hoischen A., Scheffer H., de Vries B.B., Brunner H.G.,
RA Veltman J.A., Vissers L.E.;
RT "Diagnostic exome sequencing in persons with severe intellectual
RT disability.";
RL N. Engl. J. Med. 367:1921-1929(2012).
RN [14]
RP VARIANT VAL-1280.
RX PubMed=28493397; DOI=10.1002/humu.23246;
RG UK10K;
RA Rainger J., Williamson K.A., Soares D.C., Truch J., Kurian D.,
RA Gillessen-Kaesbach G., Seawright A., Prendergast J., Halachev M.,
RA Wheeler A., McTeir L., Gill A.C., van Heyningen V., Davey M.G.,
RA FitzPatrick D.R.;
RT "A recurrent de novo mutation in ACTG1 causes isolated ocular coloboma.";
RL Hum. Mutat. 38:942-946(2017).
RN [15]
RP CHARACTERIZATION OF VARIANTS IDDALDS CYS-760 AND 1066-ARG--VAL-1990 DEL,
RP INTERACTION WITH KIF1A, SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=30021165; DOI=10.1016/j.celrep.2018.06.071;
RA Stucchi R., Plucinska G., Hummel J.J.A., Zahavi E.E., Guerra San Juan I.,
RA Klykov O., Scheltema R.A., Altelaar A.F.M., Hoogenraad C.C.;
RT "Regulation of KIF1A-Driven Dense Core Vesicle Transport: Ca2+/CaM Controls
RT DCV Binding and Liprin-alpha/TANC2 Recruits DCVs to Postsynaptic Sites.";
RL Cell Rep. 24:685-700(2018).
RN [16]
RP INVOLVEMENT IN IDDALDS, AND VARIANTS IDDALDS HIS-755; CYS-760; VAL-794;
RP GLN-961; 1066-ARG--VAL-1990 DEL; 1400-GLN--VAL-1990 DEL; 1483-GLN--VAL-1990
RP DEL AND ARG-1689.
RX PubMed=31616000; DOI=10.1038/s41467-019-12435-8;
RG University of Washington Center for Mendelian Genomics;
RA Guo H., Bettella E., Marcogliese P.C., Zhao R., Andrews J.C.,
RA Nowakowski T.J., Gillentine M.A., Hoekzema K., Wang T., Wu H., Jangam S.,
RA Liu C., Ni H., Willemsen M.H., van Bon B.W., Rinne T., Stevens S.J.C.,
RA Kleefstra T., Brunner H.G., Yntema H.G., Long M., Zhao W., Hu Z.,
RA Colson C., Richard N., Schwartz C.E., Romano C., Castiglia L., Bottitta M.,
RA Dhar S.U., Erwin D.J., Emrick L., Keren B., Afenjar A., Zhu B., Bai B.,
RA Stankiewicz P., Herman K., Mercimek-Andrews S., Juusola J., Wilfert A.B.,
RA Abou Jamra R., Buettner B., Mefford H.C., Muir A.M., Scheffer I.E.,
RA Regan B.M., Malone S., Gecz J., Cobben J., Weiss M.M., Waisfisz Q.,
RA Bijlsma E.K., Hoffer M.J.V., Ruivenkamp C.A.L., Sartori S., Xia F.,
RA Rosenfeld J.A., Bernier R.A., Wangler M.F., Yamamoto S., Xia K.,
RA Stegmann A.P.A., Bellen H.J., Murgia A., Eichler E.E.;
RT "Disruptive mutations in TANC2 define a neurodevelopmental syndrome
RT associated with psychiatric disorders.";
RL Nat. Commun. 10:4679-4679(2019).
CC -!- FUNCTION: Scaffolding protein in the dendritic spines which acts as
CC immobile postsynaptic posts able to recruit KIF1A-driven dense core
CC vesicles to dendritic spines. {ECO:0000269|PubMed:30021165}.
CC -!- SUBUNIT: Interacts with KIF1A; the interaction decreases in presence of
CC calcium. {ECO:0000269|PubMed:30021165}.
CC -!- SUBCELLULAR LOCATION: Cell projection, dendritic spine
CC {ECO:0000269|PubMed:30021165}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q9HCD6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9HCD6-2; Sequence=VSP_033550;
CC Name=3;
CC IsoId=Q9HCD6-3; Sequence=VSP_033546, VSP_033547;
CC Name=4;
CC IsoId=Q9HCD6-4; Sequence=VSP_033548, VSP_033549;
CC -!- DISEASE: Intellectual developmental disorder with autistic features and
CC language delay, with or without seizures (IDDALDS) [MIM:618906]: An
CC autosomal dominant neurodevelopmental disorder characterized by global
CC developmental delay, varying degrees of intellectual disability, autism
CC spectrum disorder, and delayed language. Some patients develop
CC seizures. {ECO:0000269|PubMed:23033978, ECO:0000269|PubMed:30021165,
CC ECO:0000269|PubMed:31616000}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Note=Defects in TANC2 has been found in a patient with
CC isolated coloboma, a defect of the eye characterized by the absence of
CC ocular structures due to abnormal morphogenesis of the optic cup and
CC stalk, and the fusion of the fetal fissure (optic fissure). Isolated
CC colobomas may be associated with an abnormally small eye
CC (microphthalmia) or small cornea. {ECO:0000269|PubMed:28493397}.
CC -!- SIMILARITY: Belongs to the TANC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB92314.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAB92314.1; Type=Frameshift; Evidence={ECO:0000305};
CC -!- SEQUENCE CAUTION: [Isoform 2]:
CC Sequence=CAB92314.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AC005828; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC005972; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC006270; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC015923; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AB046856; BAB13462.2; -; mRNA.
DR EMBL; AK001077; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK021886; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AJ278120; CAB92314.1; ALT_SEQ; mRNA.
DR EMBL; AB032974; BAA86462.2; -; mRNA.
DR CCDS; CCDS45754.1; -. [Q9HCD6-1]
DR RefSeq; NP_079461.2; NM_025185.3. [Q9HCD6-1]
DR RefSeq; XP_005257260.1; XM_005257203.4.
DR AlphaFoldDB; Q9HCD6; -.
DR SMR; Q9HCD6; -.
DR BioGRID; 117559; 76.
DR IntAct; Q9HCD6; 20.
DR MINT; Q9HCD6; -.
DR STRING; 9606.ENSP00000387593; -.
DR GlyGen; Q9HCD6; 6 sites, 1 O-linked glycan (5 sites).
DR iPTMnet; Q9HCD6; -.
DR PhosphoSitePlus; Q9HCD6; -.
DR BioMuta; TANC2; -.
DR DMDM; 189029946; -.
DR EPD; Q9HCD6; -.
DR jPOST; Q9HCD6; -.
DR MassIVE; Q9HCD6; -.
DR MaxQB; Q9HCD6; -.
DR PaxDb; Q9HCD6; -.
DR PeptideAtlas; Q9HCD6; -.
DR PRIDE; Q9HCD6; -.
DR ProteomicsDB; 81677; -. [Q9HCD6-1]
DR ProteomicsDB; 81678; -. [Q9HCD6-2]
DR ProteomicsDB; 81679; -. [Q9HCD6-3]
DR ProteomicsDB; 81680; -. [Q9HCD6-4]
DR Antibodypedia; 9399; 14 antibodies from 9 providers.
DR DNASU; 26115; -.
DR Ensembl; ENST00000389520.8; ENSP00000374171.4; ENSG00000170921.16. [Q9HCD6-2]
DR Ensembl; ENST00000424789.6; ENSP00000387593.2; ENSG00000170921.16. [Q9HCD6-1]
DR GeneID; 26115; -.
DR KEGG; hsa:26115; -.
DR UCSC; uc002jal.5; human. [Q9HCD6-1]
DR CTD; 26115; -.
DR DisGeNET; 26115; -.
DR GeneCards; TANC2; -.
DR HGNC; HGNC:30212; TANC2.
DR HPA; ENSG00000170921; Tissue enhanced (parathyroid).
DR MalaCards; TANC2; -.
DR MIM; 615047; gene.
DR MIM; 618906; phenotype.
DR neXtProt; NX_Q9HCD6; -.
DR OpenTargets; ENSG00000170921; -.
DR Orphanet; 528084; Non-specific syndromic intellectual disability.
DR PharmGKB; PA142670837; -.
DR VEuPathDB; HostDB:ENSG00000170921; -.
DR eggNOG; KOG0504; Eukaryota.
DR GeneTree; ENSGT00940000156447; -.
DR HOGENOM; CLU_001464_0_1_1; -.
DR InParanoid; Q9HCD6; -.
DR OMA; XRKIPDE; -.
DR OrthoDB; 1073736at2759; -.
DR PhylomeDB; Q9HCD6; -.
DR TreeFam; TF323159; -.
DR PathwayCommons; Q9HCD6; -.
DR SignaLink; Q9HCD6; -.
DR SIGNOR; Q9HCD6; -.
DR BioGRID-ORCS; 26115; 13 hits in 1075 CRISPR screens.
DR ChiTaRS; TANC2; human.
DR GenomeRNAi; 26115; -.
DR Pharos; Q9HCD6; Tdark.
DR PRO; PR:Q9HCD6; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q9HCD6; protein.
DR Bgee; ENSG00000170921; Expressed in cortical plate and 165 other tissues.
DR ExpressionAtlas; Q9HCD6; baseline and differential.
DR Genevisible; Q9HCD6; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; IEA:GOC.
DR GO; GO:0043197; C:dendritic spine; IDA:UniProtKB.
DR GO; GO:0099519; P:dense core granule cytoskeletal transport; ISS:UniProtKB.
DR GO; GO:0060998; P:regulation of dendritic spine development; ISS:UniProtKB.
DR GO; GO:0061001; P:regulation of dendritic spine morphogenesis; ISS:UniProtKB.
DR Gene3D; 1.25.40.10; -; 1.
DR Gene3D; 1.25.40.20; -; 2.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR Pfam; PF00023; Ank; 1.
DR Pfam; PF12796; Ank_2; 2.
DR Pfam; PF13637; Ank_4; 1.
DR Pfam; PF13181; TPR_8; 2.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 11.
DR SMART; SM00028; TPR; 3.
DR SUPFAM; SSF48403; SSF48403; 1.
DR SUPFAM; SSF48452; SSF48452; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 6.
DR PROSITE; PS50005; TPR; 3.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ANK repeat; Autism spectrum disorder;
KW Cell projection; Disease variant; Glycoprotein; Intellectual disability;
KW Methylation; Phosphoprotein; Reference proteome; Repeat; Synapse;
KW TPR repeat.
FT CHAIN 1..1990
FT /note="Protein TANC2"
FT /id="PRO_0000333811"
FT REPEAT 846..878
FT /note="ANK 1"
FT REPEAT 884..913
FT /note="ANK 2"
FT REPEAT 917..946
FT /note="ANK 3"
FT REPEAT 950..979
FT /note="ANK 4"
FT REPEAT 990..1019
FT /note="ANK 5"
FT REPEAT 1033..1062
FT /note="ANK 6"
FT REPEAT 1066..1095
FT /note="ANK 7"
FT REPEAT 1099..1128
FT /note="ANK 8"
FT REPEAT 1132..1161
FT /note="ANK 9"
FT REPEAT 1165..1194
FT /note="ANK 10"
FT REPEAT 1198..1227
FT /note="ANK 11"
FT REPEAT 1244..1277
FT /note="TPR 1"
FT REPEAT 1291..1324
FT /note="TPR 2"
FT REPEAT 1325..1358
FT /note="TPR 3"
FT REGION 1..85
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 129..149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 396..442
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1372..1401
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1430..1586
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1692..1718
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1783..1803
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1821..1843
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1968..1990
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..38
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 417..434
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1377..1392
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1446..1512
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1524..1540
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1550..1576
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1823..1842
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 169
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 238
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 294
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 400
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1442
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15144186"
FT MOD_RES 1458
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1530
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1545
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1563
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:A2A690"
FT MOD_RES 1576
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:A2A690"
FT MOD_RES 1579
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1722
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1824
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A2A690"
FT MOD_RES 1827
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CARBOHYD 1928
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:A2A690"
FT VAR_SEQ 944..971
FT /note="VDHLDKNGQCALVHAALRGHLEVVKFLI -> VLAAQLCCFSSLFLYFRCIL
FT FLISSVTS (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_033546"
FT VAR_SEQ 972..1990
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_033547"
FT VAR_SEQ 1006..1010
FT /note="IVSYL -> VRSRQ (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_033548"
FT VAR_SEQ 1011..1990
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_033549"
FT VAR_SEQ 1225
FT /note="I -> IGCQTLPSRPR (in isoform 2)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_033550"
FT VARIANT 755
FT /note="R -> H (in IDDALDS; unknown pathological
FT significance; dbSNP:rs775421108)"
FT /evidence="ECO:0000269|PubMed:31616000"
FT /id="VAR_084328"
FT VARIANT 760
FT /note="R -> C (in IDDALDS; reduced interaction with KIF1A;
FT impaired neuronal dense core vesicles transport; no effect
FT on dendritic spine location; dbSNP:rs1282488329)"
FT /evidence="ECO:0000269|PubMed:23033978,
FT ECO:0000269|PubMed:30021165, ECO:0000269|PubMed:31616000"
FT /id="VAR_069374"
FT VARIANT 794
FT /note="A -> V (in IDDALDS; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:31616000"
FT /id="VAR_084329"
FT VARIANT 961
FT /note="R -> Q (in IDDALDS; unknown pathological
FT significance; dbSNP:rs374131489)"
FT /evidence="ECO:0000269|PubMed:31616000"
FT /id="VAR_084330"
FT VARIANT 1066..1990
FT /note="Missing (in IDDALDS; strongly reduced interaction
FT with KIF1A; strongly reduced localization at the dendritic
FT spine)"
FT /evidence="ECO:0000269|PubMed:30021165,
FT ECO:0000269|PubMed:31616000"
FT /id="VAR_084331"
FT VARIANT 1280
FT /note="G -> V (found in a patient with isolated coloboma;
FT unknown pathological significance)"
FT /evidence="ECO:0000269|PubMed:28493397"
FT /id="VAR_079853"
FT VARIANT 1400..1990
FT /note="Missing (in IDDALDS)"
FT /evidence="ECO:0000269|PubMed:31616000"
FT /id="VAR_084332"
FT VARIANT 1483..1990
FT /note="Missing (in IDDALDS)"
FT /evidence="ECO:0000269|PubMed:31616000"
FT /id="VAR_084333"
FT VARIANT 1689
FT /note="H -> R (in IDDALDS; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:31616000"
FT /id="VAR_084334"
FT CONFLICT 1210
FT /note="R -> P (in Ref. 4; CAB92314)"
FT /evidence="ECO:0000305"
FT CONFLICT 1234
FT /note="T -> P (in Ref. 4; CAB92314)"
FT /evidence="ECO:0000305"
FT CONFLICT 1249
FT /note="E -> K (in Ref. 4; CAB92314)"
FT /evidence="ECO:0000305"
FT CONFLICT 1285
FT /note="T -> P (in Ref. 4; CAB92314)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1990 AA; 219650 MW; E835D98F5C546365 CRC64;
MFRNSLKMLL TGGKSSRKNR SSDGGSEEPP DRRQSSVDSR QSRSGQGGIS TESDCAFEPD
YAVPPLPVSE GDAEQELGPP PSVDEAANTL MTRLGFLLGE KVTEVQPGDQ YSMEVQDENQ
TSAITQRISP CSTLTSSTAS PPASSPCSTL PPISTNATAK DCSYGAVTSP TSTLESRDSG
IIATLTSYSE NVERTKYAGE SSKELGSGGN IKPWQSQKSS MDSCLYRVDE NMTASTYSLN
KIPERNLETV LSQSVQSIPL YLMPRPNSVA ATSSAHLEDL AYLDEQRHTP LRTSLRMPRQ
SMGGARTQQD LRVRFAPYRP PDISLKPLLF EVPSITTESV FVGRDWVFHE IDAQLQSSNA
SVNQGVVIVG NIGFGKTAII SRLVALSCHG TRMRQIASDS PHASPKHVDA NRELPLTQPP
SAHSSITSGS CPGTPEMRRR QEEAMRRLAS QVVAYHYCQA DNAYTCLVPE FVHNVAALLC
RSPQLTAYRE QLLREPHLQS MLSLRSCVQD PMASFRRGVL EPLENLHKER KIPDEDFIIL
IDGLNEAEFH KPDYGDTIVS FLSKMIGKFP SWLKLIVTVR TSLQEITKLL PFHRIFLDRL
EENEAIDQDL QAYILHRIHS SSEIQNNISL NGKMDNTTFG KLSSHLKTLS QGSYLYLKLT
FDLIEKGYLV LKSSSYKVVP VSLSEVYLLQ CNMKFPTQSS FDRVMPLLNV AVASLHPLTD
EHIFQAINAG SIEGTLEWED FQQRMENLSM FLIKRRDMTR MFVHPSFREW LIWREEGEKT
KFLCDPRSGH TLLAFWFSRQ EGKLNRQQTI ELGHHILKAH IFKGLSKKVG VSSSILQGLW
ISYSTEGLSM ALASLRNLYT PNIKVSRLLI LGGANINYRT EVLNNAPILC VQSHLGYTEM
VALLLEFGAN VDASSESGLT PLGYAAAAGY LSIVVLLCKK RAKVDHLDKN GQCALVHAAL
RGHLEVVKFL IQCDWTMAGQ QQGVFKKSHA IQQALIAAAS MGYTEIVSYL LDLPEKDEEE
VERAQINSFD SLWGETALTA AAGRGKLEVC RLLLEQGAAV AQPNRRGAVP LFSTVRQGHW
QIVDLLLTHG ADVNMADKQG RTPLMMAASE GHLGTVDFLL AQGASIALMD KEGLTALSWA
CLKGHLSVVR SLVDNGAATD HADKNGRTPL DLAAFYGDAE VVQFLVDHGA MIEHVDYSGM
RPLDRAVGCR NTSVVVTLLK KGAKIGPATW AMATSKPDIM IILLSKLMEE GDMFYKKGKV
KEAAQRYQYA LKKFPREGFG EDLKTFRELK VSLLLNLSRC RRKMNDFGMA EEFATKALEL
KPKSYEAYYA RARAKRSSRQ FAAALEDLNE AIKLCPNNRE IQRLLLRVEE ECRQMQQPQQ
PPPPPQPQQQ LPEEAEPEPQ HEDIYSVQDI FEEEYLEQDV ENVSIGLQTE ARPSQGLPVI
QSPPSSPPHR DSAYISSSPL GSHQVFDFRS SSSVGSPTRQ TYQSTSPALS PTHQNSHYRP
SPPHTSPAHQ GGSYRFSPPP VGGQGKEYPS PPPSPLRRGP QYRASPPAES MSVYRSQSGS
PVRYQQETSV SQLPGRPKSP LSKMAQRPYQ MPQLPVAVPQ QGLRLQPAKA QIVRSNQPSP
AVHSSTVIPT GAYGQVAHSM ASKYQSSQGD IGVSQSRLVY QGSIGGIVGD GRPVQHVQAS
LSAGAICQHG GLTKEDLPQR PSSAYRGGVR YSQTPQIGRS QSASYYPVCH SKLDLERSSS
QLGSPDVSHL IRRPISVNPN EIKPHPPTPR PLLHSQSVGL RFSPSSNSIS STSNLTPTFR
PSSSIQQMEI PLKPAYERSC DELSPVSPTQ GGYPSEPTRS RTTPFMGIID KTARTQQYPH
LHQQNRTWAV SSVDTVLSPT SPGNLPQPES FSPPSSISNI AFYNKTNNAQ NGHLLEDDYY
SPHGMLANGS RGDLLERVSQ ASSYPDVKVA RTLPVAQAYQ DNLYRQLSRD SRQGQTSPIK
PKRPFVESNV
