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Database: UniProt
Entry: Q12955
LinkDB: Q12955
Original site: Q12955 
ID   ANK3_HUMAN              Reviewed;        4377 AA.
AC   Q12955; B1AQT2; B4DIL1; E9PE32; Q13484; Q5CZH9; Q5VXD5; Q7Z3G4; Q9H0P5;
DT   11-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-SEP-2009, sequence version 3.
DT   12-AUG-2020, entry version 198.
DE   RecName: Full=Ankyrin-3 {ECO:0000303|PubMed:7836469};
DE            Short=ANK-3 {ECO:0000303|PubMed:7836469};
DE   AltName: Full=Ankyrin-G {ECO:0000303|PubMed:7836469};
GN   Name=ANK3 {ECO:0000312|HGNC:HGNC:494};
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 1), AND TISSUE SPECIFICITY.
RC   TISSUE=Brain stem;
RX   PubMed=7836469; DOI=10.1074/jbc.270.5.2352;
RA   Kordeli E., Lambert S., Bennett V.;
RT   "AnkyrinG. A new ankyrin gene with neural-specific isoforms localized at
RT   the axonal initial segment and node of Ranvier.";
RL   J. Biol. Chem. 270:2352-2359(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), FUNCTION (ISOFORM 5), AND
RP   SUBCELLULAR LOCATION (ISOFORM 5).
RC   TISSUE=Kidney;
RX   PubMed=8666667; DOI=10.1083/jcb.133.4.819;
RA   Devarajan P., Stabach P.R., Mann A.S., Ardito T., Kashgarian M.,
RA   Morrow J.S.;
RT   "Identification of a small cytoplasmic ankyrin (AnkG119) in the kidney and
RT   muscle that binds beta I sigma spectrin and associates with the Golgi
RT   apparatus.";
RL   J. Cell Biol. 133:819-830(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC   TISSUE=Kidney;
RX   PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA   Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA   Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA   Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA   Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA   Klein M., Poustka A.;
RT   "Towards a catalog of human genes and proteins: sequencing and analysis of
RT   500 novel complete protein coding human cDNAs.";
RL   Genome Res. 11:422-435(2001).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Hippocampus;
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   TISSUE=Cervix, and Fetal kidney;
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   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15164054; DOI=10.1038/nature02462;
RA   Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA   Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA   Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA   Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA   Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA   Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA   Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA   Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA   Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA   Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA   Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA   Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA   Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA   Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA   McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA   Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA   Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA   Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA   Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA   Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA   Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA   Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA   Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT   "The DNA sequence and comparative analysis of human chromosome 10.";
RL   Nature 429:375-381(2004).
RN   [7]
RP   INTERACTION WITH SCN5A.
RX   PubMed=15579534; DOI=10.1073/pnas.0403711101;
RA   Mohler P.J., Rivolta I., Napolitano C., LeMaillet G., Lambert S.,
RA   Priori S.G., Bennett V.;
RT   "Nav1.5 E1053K mutation causing Brugada syndrome blocks binding to ankyrin-
RT   G and expression of Nav1.5 on the surface of cardiomyocytes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:17533-17538(2004).
RN   [8]
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   [9]
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   [10]
RP   INTERACTION WITH PLEC AND FLNC, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP   AND DEVELOPMENTAL STAGE.
RX   PubMed=21223964; DOI=10.1016/j.yexcr.2011.01.002;
RA   Maiweilidan Y., Klauza I., Kordeli E.;
RT   "Novel interactions of ankyrins-G at the costameres: the muscle-specific
RT   Obscurin/Titin-Binding-related Domain (OTBD) binds plectin and filamin C.";
RL   Exp. Cell Res. 317:724-736(2011).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-39; SER-847; SER-1445 AND
RP   SER-4298, 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   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1459; SER-4298 AND SER-4350,
RP   AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma, and Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4229; SER-4290 AND SER-4298,
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1632 AND SER-1658 (ISOFORM
RP   2), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1625 AND SER-1651
RP   (ISOFORM 3), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-765 AND SER-791
RP   (ISOFORM 4), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-468 (ISOFORM 5),
RP   AND 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   [14]
RP   INTERACTION WITH KCNA1.
RX   PubMed=23903368; DOI=10.1038/ki.2013.280;
RA   San-Cristobal P., Lainez S., Dimke H., de Graaf M.J., Hoenderop J.G.,
RA   Bindels R.J.;
RT   "Ankyrin-3 is a novel binding partner of the voltage-gated potassium
RT   channel Kv1.1 implicated in renal magnesium handling.";
RL   Kidney Int. 85:94-102(2014).
RN   [15]
RP   INTERACTION WITH IQCJ-SCHIP1 AND SCHIP1.
RX   PubMed=25950943; DOI=10.1111/jnc.13158;
RA   Papandreou M.J., Vacher H., Fache M.P., Klingler E., Rueda-Boroni F.,
RA   Ferracci G., Debarnot C., Piperoglou C., Garcia Del Cano G., Goutebroze L.,
RA   Dargent B.;
RT   "CK2-regulated schwannomin-interacting protein IQCJ-SCHIP-1 association
RT   with AnkG contributes to the maintenance of the axon initial segment.";
RL   J. Neurochem. 134:527-537(2015).
RN   [16]
RP   VARIANT HIS-968.
RX   PubMed=25966638; DOI=10.1038/ejhg.2015.91;
RA   Tham E., Eklund E.A., Hammarsjoe A., Bengtson P., Geiberger S.,
RA   Lagerstedt-Robinson K., Malmgren H., Nilsson D., Grigelionis G., Conner P.,
RA   Lindgren P., Lindstrand A., Wedell A., Albaage M., Zielinska K.,
RA   Nordgren A., Papadogiannakis N., Nishimura G., Grigelioniene G.;
RT   "A novel phenotype in N-glycosylation disorders: Gillessen-Kaesbach-
RT   Nishimura skeletal dysplasia due to pathogenic variants in ALG9.";
RL   Eur. J. Hum. Genet. 24:198-207(2016).
RN   [17]
RP   X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 4088-4199.
RX   PubMed=25307106; DOI=10.1002/prot.24702;
RA   Liu Y., Zhang Y., Wang J.H.;
RT   "Crystal structure of human Ankyrin G death domain.";
RL   Proteins 82:3476-3482(2014).
RN   [18]
RP   VARIANTS ALA-1569; MET-3720 AND PRO-4255, AND POSSIBLE INVOLVEMENT IN
RP   SUSCEPTIBILITY TO AUTISM.
RX   PubMed=22865819; DOI=10.1002/humu.22174;
RA   Bi C., Wu J., Jiang T., Liu Q., Cai W., Yu P., Cai T., Zhao M., Jiang Y.H.,
RA   Sun Z.S.;
RT   "Mutations of ANK3 identified by exome sequencing are associated with
RT   autism susceptibility.";
RL   Hum. Mutat. 33:1635-1638(2012).
RN   [19]
RP   INVOLVEMENT IN MRT37.
RX   PubMed=23390136; DOI=10.1093/hmg/ddt043;
RA   Iqbal Z., Vandeweyer G., van der Voet M., Waryah A.M., Zahoor M.Y.,
RA   Besseling J.A., Roca L.T., Vulto-van Silfhout A.T., Nijhof B., Kramer J.M.,
RA   Van der Aa N., Ansar M., Peeters H., Helsmoortel C., Gilissen C.,
RA   Vissers L.E., Veltman J.A., de Brouwer A.P., Frank Kooy R., Riazuddin S.,
RA   Schenck A., van Bokhoven H., Rooms L.;
RT   "Homozygous and heterozygous disruptions of ANK3: at the crossroads of
RT   neurodevelopmental and psychiatric disorders.";
RL   Hum. Mol. Genet. 22:1960-1970(2013).
CC   -!- FUNCTION: In skeletal muscle, required for costamere localization of
CC       DMD and betaDAG1 (By similarity). Membrane-cytoskeleton linker. May
CC       participate in the maintenance/targeting of ion channels and cell
CC       adhesion molecules at the nodes of Ranvier and axonal initial segments.
CC       Regulates KCNA1 channel activity in function of dietary Mg(2+) levels,
CC       and thereby contributes to the regulation of renal Mg(2+) reabsorption
CC       (PubMed:23903368). {ECO:0000250, ECO:0000269|PubMed:17974005}.
CC   -!- FUNCTION: [Isoform 5]: May be part of a Golgi-specific membrane
CC       cytoskeleton in association with beta-spectrin.
CC       {ECO:0000305|PubMed:17974005}.
CC   -!- SUBUNIT: Directly interacts with DMD and betaDAG1. This interaction
CC       does not interfere with binding between DMD and betaDAG1. It is also
CC       required for DMD and betaDAG1 retention at costameres (By similarity).
CC       Interacts (via N-terminal ANK repeats) with SCHIP1 isoform 5 (via C-
CC       terminus); this interaction is required for the localization at axon
CC       initial segments (AISs) and nodes of Ranvier (NRs) (By similarity). May
CC       be a constituent of a NFASC/NRCAM/ankyrin G complex. Interacts with
CC       RHBG (PubMed:15611082). Interacts with PLEC and FLNC (PubMed:21223964).
CC       Interacts with KCNA1; this inhibits channel activity (PubMed:23903368).
CC       Interacts (via ANK repeats) with IQCJ-SCHIP1; required for IQCJ-SCHIP1
CC       localization at axon initial segments (AIS) and nodes of Ranvier
CC       (PubMed:25950943). Interacts with SCHIP1 (PubMed:25950943). Interacts
CC       with SCN5A (PubMed:15579534). {ECO:0000250|UniProtKB:G5E8K5,
CC       ECO:0000269|PubMed:15579534, ECO:0000269|PubMed:15611082,
CC       ECO:0000269|PubMed:21223964, ECO:0000269|PubMed:23903368,
CC       ECO:0000269|PubMed:25950943}.
CC   -!- INTERACTION:
CC       Q12955; O00203-1: AP3B1; NbExp=2; IntAct=EBI-2691178, EBI-15816315;
CC       Q12955; Q15796: SMAD2; NbExp=2; IntAct=EBI-2691178, EBI-1040141;
CC       Q12955-5; Q15742: NAB2; NbExp=3; IntAct=EBI-12154305, EBI-8641936;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC       {ECO:0000269|PubMed:21223964}. Cell projection, axon
CC       {ECO:0000250|UniProtKB:O70511}. Cell membrane, sarcolemma
CC       {ECO:0000269|PubMed:21223964}. Cell junction, synapse, postsynaptic
CC       cell membrane {ECO:0000250|UniProtKB:O70511}. Lysosome
CC       {ECO:0000250|UniProtKB:G5E8K5}. Cell membrane, sarcolemma, T-tubule
CC       {ECO:0000250|UniProtKB:O70511}. Note=In skeletal muscle, localized at
CC       costameres and neuromuscular junctions. In macrophages, associated with
CC       lysosomes. {ECO:0000250|UniProtKB:G5E8K5,
CC       ECO:0000250|UniProtKB:O70511}.
CC   -!- SUBCELLULAR LOCATION: [Isoform 5]: Cytoplasm, cytoskeleton
CC       {ECO:0000269|PubMed:8666667}. Golgi apparatus
CC       {ECO:0000269|PubMed:8666667}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=5;
CC       Name=1;
CC         IsoId=Q12955-3; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q12955-4; Sequence=VSP_044349, VSP_044350, VSP_044351,
CC                                  VSP_044352, VSP_044353, VSP_044354;
CC       Name=3;
CC         IsoId=Q12955-5; Sequence=VSP_044348, VSP_044351, VSP_044352,
CC                                  VSP_044353, VSP_044354;
CC       Name=4;
CC         IsoId=Q12955-6; Sequence=VSP_046885, VSP_046886, VSP_044351,
CC                                  VSP_044352, VSP_044353, VSP_044354;
CC       Name=5; Synonyms=AnkG119, Golgi ankyrin;
CC         IsoId=Q12955-7; Sequence=VSP_053753, VSP_053754, VSP_053755,
CC                                  VSP_053756, VSP_053757, VSP_044351,
CC                                  VSP_053758, VSP_053759;
CC   -!- TISSUE SPECIFICITY: Expressed in brain, neurons, muscles and other
CC       tissues. {ECO:0000269|PubMed:21223964, ECO:0000269|PubMed:7836469}.
CC   -!- DEVELOPMENTAL STAGE: Up-regulated during muscle cell differentiation.
CC       {ECO:0000269|PubMed:21223964}.
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 (By similarity).
CC       {ECO:0000250}.
CC   -!- DISEASE: Note=Genetic variations in ANK3 may be associated with autism
CC       spectrum disorders susceptibility. {ECO:0000269|PubMed:22865819}.
CC   -!- DISEASE: Mental retardation, autosomal recessive 37 (MRT37)
CC       [MIM:615493]: A disorder characterized by significantly below average
CC       general intellectual functioning associated with impairments in
CC       adaptive behavior and manifested during the developmental period. MRT37
CC       patients manifest delayed global development with speech delay,
CC       hypotonia, spasticity, and a sleep disorder. Severe behavioral
CC       abnormalities include aggression, hyperactivity, and grinding of the
CC       teeth. Note=The disease is caused by mutations affecting the gene
CC       represented in this entry. A homozygous deletion in ANK3 predicted to
CC       result in frameshift and premature truncation, has been shown to be the
CC       cause of moderate intellectual disability, an ADHD-like phenotype and
CC       behavioral problems in a consanguineous family (PubMed:23390136).
CC       {ECO:0000269|PubMed:23390136}.
CC   -!- MISCELLANEOUS: [Isoform 5]: Avidly binds beta spectrin. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION: [Isoform 4]:
CC       Sequence=CAB66645.1; Type=Frameshift; Evidence={ECO:0000305};
CC   -!- WEB RESOURCE: Name=Wikipedia; Note=Ankyrin entry;
CC       URL="https://en.wikipedia.org/wiki/Ankyrin";
DR   EMBL; U13616; AAA64834.1; -; mRNA.
DR   EMBL; U43965; AAB08437.1; -; mRNA.
DR   EMBL; AL136710; CAB66645.1; ALT_FRAME; mRNA.
DR   EMBL; AK295661; BAG58523.1; -; mRNA.
DR   EMBL; BX537917; CAD97900.2; -; mRNA.
DR   EMBL; BX648574; CAI56716.1; -; mRNA.
DR   EMBL; AC022390; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC023904; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL359267; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL359377; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL391707; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL592430; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL607065; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   CCDS; CCDS55711.1; -. [Q12955-4]
DR   CCDS; CCDS55712.1; -. [Q12955-5]
DR   CCDS; CCDS7258.1; -. [Q12955-3]
DR   CCDS; CCDS7259.1; -. [Q12955-6]
DR   PIR; A55575; A55575.
DR   RefSeq; NP_001140.2; NM_001149.3. [Q12955-6]
DR   RefSeq; NP_001191332.1; NM_001204403.1. [Q12955-5]
DR   RefSeq; NP_001191333.1; NM_001204404.1. [Q12955-4]
DR   RefSeq; NP_066267.2; NM_020987.4. [Q12955-3]
DR   PDB; 4O6X; X-ray; 2.10 A; A/B=4088-4199.
DR   PDBsum; 4O6X; -.
DR   SMR; Q12955; -.
DR   BioGRID; 106785; 54.
DR   CORUM; Q12955; -.
DR   DIP; DIP-49017N; -.
DR   ELM; Q12955; -.
DR   IntAct; Q12955; 41.
DR   MINT; Q12955; -.
DR   STRING; 9606.ENSP00000280772; -.
DR   iPTMnet; Q12955; -.
DR   PhosphoSitePlus; Q12955; -.
DR   SwissPalm; Q12955; -.
DR   BioMuta; ANK3; -.
DR   DMDM; 257051061; -.
DR   EPD; Q12955; -.
DR   jPOST; Q12955; -.
DR   MassIVE; Q12955; -.
DR   MaxQB; Q12955; -.
DR   PaxDb; Q12955; -.
DR   PeptideAtlas; Q12955; -.
DR   PRIDE; Q12955; -.
DR   ProteomicsDB; 19802; -.
DR   ProteomicsDB; 3339; -.
DR   ProteomicsDB; 59048; -. [Q12955-3]
DR   Antibodypedia; 4197; 266 antibodies.
DR   DNASU; 288; -.
DR   Ensembl; ENST00000280772; ENSP00000280772; ENSG00000151150. [Q12955-3]
DR   Ensembl; ENST00000355288; ENSP00000347436; ENSG00000151150. [Q12955-6]
DR   Ensembl; ENST00000373827; ENSP00000362933; ENSG00000151150. [Q12955-5]
DR   Ensembl; ENST00000503366; ENSP00000425236; ENSG00000151150. [Q12955-4]
DR   GeneID; 288; -.
DR   KEGG; hsa:288; -.
DR   UCSC; uc001jkw.4; human. [Q12955-3]
DR   CTD; 288; -.
DR   DisGeNET; 288; -.
DR   EuPathDB; HostDB:ENSG00000151150.20; -.
DR   GeneCards; ANK3; -.
DR   HGNC; HGNC:494; ANK3.
DR   HPA; ENSG00000151150; Tissue enhanced (brain, parathyroid gland).
DR   MalaCards; ANK3; -.
DR   MIM; 600465; gene.
DR   MIM; 615493; phenotype.
DR   neXtProt; NX_Q12955; -.
DR   OpenTargets; ENSG00000151150; -.
DR   Orphanet; 356996; ANK3-related intellectual disability-sleep disturbance syndrome.
DR   PharmGKB; PA24800; -.
DR   eggNOG; KOG4177; Eukaryota.
DR   GeneTree; ENSGT00940000154939; -.
DR   HOGENOM; CLU_000134_29_1_1; -.
DR   InParanoid; Q12955; -.
DR   KO; K10380; -.
DR   OMA; MPDYFSE; -.
DR   OrthoDB; 1011028at2759; -.
DR   PhylomeDB; Q12955; -.
DR   TreeFam; TF351263; -.
DR   PathwayCommons; Q12955; -.
DR   Reactome; R-HSA-445095; Interaction between L1 and Ankyrins.
DR   Reactome; R-HSA-6807878; COPI-mediated anterograde transport.
DR   BioGRID-ORCS; 288; 4 hits in 883 CRISPR screens.
DR   ChiTaRS; ANK3; human.
DR   GeneWiki; ANK3; -.
DR   GenomeRNAi; 288; -.
DR   Pharos; Q12955; Tbio.
DR   PRO; PR:Q12955; -.
DR   Proteomes; UP000005640; Chromosome 10.
DR   RNAct; Q12955; protein.
DR   Bgee; ENSG00000151150; Expressed in substantia nigra and 246 other tissues.
DR   ExpressionAtlas; Q12955; baseline and differential.
DR   Genevisible; Q12955; HS.
DR   GO; GO:0043194; C:axon initial segment; IDA:CAFA.
DR   GO; GO:0009925; C:basal plasma membrane; IDA:BHF-UCL.
DR   GO; GO:0016323; C:basolateral plasma membrane; IDA:UniProtKB.
DR   GO; GO:0009986; C:cell surface; ISS:BHF-UCL.
DR   GO; GO:0043034; C:costamere; TAS:BHF-UCL.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0030425; C:dendrite; ISS:BHF-UCL.
DR   GO; GO:0005783; C:endoplasmic reticulum; TAS:ProtInc.
DR   GO; GO:0005794; C:Golgi apparatus; TAS:ProtInc.
DR   GO; GO:0014704; C:intercalated disc; ISS:BHF-UCL.
DR   GO; GO:0016328; C:lateral plasma membrane; IDA:BHF-UCL.
DR   GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0031594; C:neuromuscular junction; ISS:BHF-UCL.
DR   GO; GO:0043005; C:neuron projection; ISS:BHF-UCL.
DR   GO; GO:0033268; C:node of Ranvier; ISS:ARUK-UCL.
DR   GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR   GO; GO:0045211; C:postsynaptic membrane; ISS:BHF-UCL.
DR   GO; GO:0042383; C:sarcolemma; IDA:BHF-UCL.
DR   GO; GO:0016529; C:sarcoplasmic reticulum; ISS:BHF-UCL.
DR   GO; GO:0014731; C:spectrin-associated cytoskeleton; 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:0045296; F:cadherin binding; ISS:BHF-UCL.
DR   GO; GO:0008093; F:cytoskeletal anchor activity; IBA:GO_Central.
DR   GO; GO:0008092; F:cytoskeletal protein binding; ISS:BHF-UCL.
DR   GO; GO:0044325; F:ion channel binding; ISS:BHF-UCL.
DR   GO; GO:0030674; F:protein-macromolecule adaptor activity; ISS:BHF-UCL.
DR   GO; GO:0030507; F:spectrin binding; ISS:BHF-UCL.
DR   GO; GO:0005200; F:structural constituent of cytoskeleton; IMP:BHF-UCL.
DR   GO; GO:0007409; P:axonogenesis; ISS:BHF-UCL.
DR   GO; GO:0071286; P:cellular response to magnesium ion; ISS:UniProtKB.
DR   GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; TAS:Reactome.
DR   GO; GO:0045184; P:establishment of protein localization; IMP:UniProtKB.
DR   GO; GO:0043001; P:Golgi to plasma membrane protein transport; IMP:BHF-UCL.
DR   GO; GO:0010960; P:magnesium ion homeostasis; ISS:UniProtKB.
DR   GO; GO:0072660; P:maintenance of protein location in plasma membrane; IGI:BHF-UCL.
DR   GO; GO:0071709; P:membrane assembly; IMP:BHF-UCL.
DR   GO; GO:0000281; P:mitotic cytokinesis; IMP:BHF-UCL.
DR   GO; GO:1902260; P:negative regulation of delayed rectifier potassium channel activity; ISS:UniProtKB.
DR   GO; GO:0007528; P:neuromuscular junction development; ISS:BHF-UCL.
DR   GO; GO:0019228; P:neuronal action potential; ISS:BHF-UCL.
DR   GO; GO:0007009; P:plasma membrane organization; IMP:BHF-UCL.
DR   GO; GO:2001259; P:positive regulation of cation channel activity; ISS:BHF-UCL.
DR   GO; GO:0010650; P:positive regulation of cell communication by electrical coupling; ISS:BHF-UCL.
DR   GO; GO:0010628; P:positive regulation of gene expression; ISS:BHF-UCL.
DR   GO; GO:0034112; P:positive regulation of homotypic cell-cell adhesion; ISS:BHF-UCL.
DR   GO; GO:1900827; P:positive regulation of membrane depolarization during cardiac muscle cell action potential; ISS:BHF-UCL.
DR   GO; GO:0045838; P:positive regulation of membrane potential; ISS:BHF-UCL.
DR   GO; GO:0090314; P:positive regulation of protein targeting to membrane; ISS:BHF-UCL.
DR   GO; GO:2000651; P:positive regulation of sodium ion transmembrane transporter activity; ISS:BHF-UCL.
DR   GO; GO:0010765; P:positive regulation of sodium ion transport; ISS:BHF-UCL.
DR   GO; GO:0099612; P:protein localization to axon; ISS:UniProtKB.
DR   GO; GO:0072659; P:protein localization to plasma membrane; IMP:BHF-UCL.
DR   GO; GO:0043266; P:regulation of potassium ion transport; ISS:BHF-UCL.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   CDD; cd08803; Death_ank3; 1.
DR   Gene3D; 1.25.40.20; -; 3.
DR   InterPro; IPR037971; Ank3_Death.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR020683; Ankyrin_rpt-contain_dom.
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; 6.
DR   Pfam; PF13606; Ank_3; 1.
DR   Pfam; PF00531; Death; 1.
DR   Pfam; PF17809; UPA_2; 1.
DR   Pfam; PF00791; ZU5; 1.
DR   PRINTS; PR01415; ANKYRIN.
DR   SMART; SM00248; ANK; 22.
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; 21.
DR   PROSITE; PS50017; DEATH_DOMAIN; 1.
DR   PROSITE; PS51145; ZU5; 2.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; ANK repeat; Autism spectrum disorder;
KW   Cell junction; Cell membrane; Cell projection; Cytoplasm; Cytoskeleton;
KW   Golgi apparatus; Lysosome; Membrane; Mental retardation; Phosphoprotein;
KW   Polymorphism; Postsynaptic cell membrane; Reference proteome; Repeat;
KW   Synapse.
FT   CHAIN           1..4377
FT                   /note="Ankyrin-3"
FT                   /id="PRO_0000066886"
FT   REPEAT          73..102
FT                   /note="ANK 1"
FT   REPEAT          106..135
FT                   /note="ANK 2"
FT   REPEAT          139..168
FT                   /note="ANK 3"
FT   REPEAT          172..201
FT                   /note="ANK 4"
FT   REPEAT          203..230
FT                   /note="ANK 5"
FT   REPEAT          234..263
FT                   /note="ANK 6"
FT   REPEAT          267..296
FT                   /note="ANK 7"
FT   REPEAT          300..329
FT                   /note="ANK 8"
FT   REPEAT          333..362
FT                   /note="ANK 9"
FT   REPEAT          366..395
FT                   /note="ANK 10"
FT   REPEAT          399..428
FT                   /note="ANK 11"
FT   REPEAT          432..461
FT                   /note="ANK 12"
FT   REPEAT          465..494
FT                   /note="ANK 13"
FT   REPEAT          498..527
FT                   /note="ANK 14"
FT   REPEAT          531..560
FT                   /note="ANK 15"
FT   REPEAT          564..593
FT                   /note="ANK 16"
FT   REPEAT          597..626
FT                   /note="ANK 17"
FT   REPEAT          630..659
FT                   /note="ANK 18"
FT   REPEAT          663..692
FT                   /note="ANK 19"
FT   REPEAT          696..725
FT                   /note="ANK 20"
FT   REPEAT          729..758
FT                   /note="ANK 21"
FT   REPEAT          762..791
FT                   /note="ANK 22"
FT   REPEAT          795..825
FT                   /note="ANK 23"
FT   DOMAIN          984..1139
FT                   /note="ZU5 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00485"
FT   DOMAIN          1141..1288
FT                   /note="ZU5 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00485"
FT   DOMAIN          4090..4174
FT                   /note="Death"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00064"
FT   REGION          1273..1407
FT                   /note="UPA domain"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        1519..1898
FT                   /note="Ser-rich"
FT   COMPBIAS        2247..2250
FT                   /note="Poly-Thr"
FT   COMPBIAS        2393..2396
FT                   /note="Poly-Glu"
FT   COMPBIAS        3205..3211
FT                   /note="Poly-Glu"
FT   COMPBIAS        3255..3259
FT                   /note="Poly-Pro"
FT   COMPBIAS        3482..3487
FT                   /note="Poly-Ser"
FT   COMPBIAS        3785..3791
FT                   /note="Poly-Asn"
FT   COMPBIAS        3957..3981
FT                   /note="Thr-rich"
FT   MOD_RES         39
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:21406692"
FT   MOD_RES         623
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O70511"
FT   MOD_RES         847
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:21406692"
FT   MOD_RES         861
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O70511"
FT   MOD_RES         867
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:G5E8K5"
FT   MOD_RES         913
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O70511"
FT   MOD_RES         916
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O70511"
FT   MOD_RES         922
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:G5E8K5"
FT   MOD_RES         957
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O70511"
FT   MOD_RES         959
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O70511"
FT   MOD_RES         1113
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:G5E8K5"
FT   MOD_RES         1445
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:21406692"
FT   MOD_RES         1459
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:23186163"
FT   MOD_RES         1470
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:G5E8K5"
FT   MOD_RES         1622
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:G5E8K5"
FT   MOD_RES         1625
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:G5E8K5"
FT   MOD_RES         1984
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O70511"
FT   MOD_RES         2111
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O70511"
FT   MOD_RES         2123
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O70511"
FT   MOD_RES         2126
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O70511"
FT   MOD_RES         4211
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:G5E8K5"
FT   MOD_RES         4229
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:24275569"
FT   MOD_RES         4290
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:24275569"
FT   MOD_RES         4298
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:21406692,
FT                   ECO:0000244|PubMed:23186163, ECO:0000244|PubMed:24275569"
FT   MOD_RES         4350
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:23186163"
FT   VAR_SEQ         1..866
FT                   /note="Missing (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:11230166"
FT                   /id="VSP_046885"
FT   VAR_SEQ         1..37
FT                   /note="MAHAASQLKKNRDLEINAEEEPEKKRKHRKRSRDRKK -> MASSASSSPAG
FT                   TEDSAPAQGGFGSDYSRSSR (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:17974005"
FT                   /id="VSP_044348"
FT   VAR_SEQ         1..36
FT                   /note="MAHAASQLKKNRDLEINAEEEPEKKRKHRKRSRDRK -> MSEEPKEKNAKP
FT                   AHRKRKG (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_044349"
FT   VAR_SEQ         1..6
FT                   /note="MAHAAS -> MNLRCD (in isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:8666667"
FT                   /id="VSP_053753"
FT   VAR_SEQ         7..385
FT                   /note="Missing (in isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:8666667"
FT                   /id="VSP_053754"
FT   VAR_SEQ         850..870
FT                   /note="Missing (in isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:8666667"
FT                   /id="VSP_053755"
FT   VAR_SEQ         867..872
FT                   /note="SDVEEG -> MALPQS (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:11230166"
FT                   /id="VSP_046886"
FT   VAR_SEQ         872
FT                   /note="G -> GNRCTWYKIPKVQEFTVKS (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_044350"
FT   VAR_SEQ         913..918
FT                   /note="Missing (in isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:8666667"
FT                   /id="VSP_053756"
FT   VAR_SEQ         1036..1043
FT                   /note="MVEGEGLA -> HGERRGIS (in isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:8666667"
FT                   /id="VSP_053757"
FT   VAR_SEQ         1442..1450
FT                   /note="Missing (in isoform 2, isoform 3, isoform 4 and
FT                   isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:11230166,
FT                   ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:17974005,
FT                   ECO:0000303|PubMed:8666667"
FT                   /id="VSP_044351"
FT   VAR_SEQ         1478..4081
FT                   /note="Missing (in isoform 2, isoform 3 and isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:11230166,
FT                   ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:17974005"
FT                   /id="VSP_044352"
FT   VAR_SEQ         1478..1880
FT                   /note="IERSTGATRSLPTTYSYKPFFSTRPYQSWTTAPITVPGPAKSGFTSLSSSSS
FT                   NTPSASPLKSIWSVSTPSPIKSTLGASTTSSVKSISDVASPIRSFRTMSSPIKTVVSQS
FT                   PYNIQVSSGTLARAPAVTEATPLKGLASNSTFSSRTSPVTTAGSLLERSSITMTPPASP
FT                   KSNINMYSSSLPFKSIITSAAPLISSPLKSVVSPVKSAVDVISSAKITMASSLSSPVKQ
FT                   MPGHAEVALVNGSISPLKYPSSSTLINGCKATATLQEKISSATNSVSSVVSAATDTVEK
FT                   VFSTTTAMPFSPLRSYVSAAPSAFQSLRTPSASALYTSLGSSISATTSSVTSSIITVPV
FT                   YSVVNVLPEPALKKLPDSNSFTKSAAALLSPIKTLTTETHPQPHFSRTSSPVKSSL ->
FT                   TSCTVKVRKSQLKEVCKHSIEYFKGISGETLKLVDRLSEEEKKMQSELSDEEESTSRNT
FT                   SLSETSRGGQPSVTTKSARDKKTEAAPLKSKSEKAGSEKRSSRRTGPQSPCERTDIRMA
FT                   IVADHLGLSWTELARELNFSVDEINQIRVENPNSLISQSFMLLKKWVTRDGKNATTDAL
FT                   TSVLTKINRIDIVTLLEGPIFDYGNISGTRSFADENNVFHDPVDGWQNETSSGNLESCA
FT                   QARRVTGGLLDRLDDSPDQCRDSITSYLKGEAGKFEANGSHTEITPEAKTKSYFPESQN
FT                   DVGKQSTKETLKPKIHGSGHVEEPASPLAAYQKSLEETSKLSKLIIEETKPCVPVSMKK
FT                   MSRTSPADGKPRLSLHEEEGSSGSEQKQGEGFKVKTKKEIRHVEKKSHS (in
FT                   isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:8666667"
FT                   /id="VSP_053758"
FT   VAR_SEQ         1881..4377
FT                   /note="Missing (in isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:8666667"
FT                   /id="VSP_053759"
FT   VAR_SEQ         4082
FT                   /note="G -> S (in isoform 2, isoform 3 and isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:11230166,
FT                   ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:17974005"
FT                   /id="VSP_044353"
FT   VAR_SEQ         4199
FT                   /note="G -> GYPSLQVELETPTGLHYTPPTPFQQDDYFSDISSIESPLRTPSRLSD
FT                   GLVPSQGNIEHSADGPPVVTAEDASLEDSKLEDSVPLTEMPEAVDVDESQLENVCLS
FT                   (in isoform 2, isoform 3 and isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:11230166,
FT                   ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:17974005"
FT                   /id="VSP_044354"
FT   VARIANT         968
FT                   /note="D -> H (found in a patient with Gillessen-Kaesbach-
FT                   Nishimura syndrome; unknown pathological significance;
FT                   dbSNP:rs730882195)"
FT                   /evidence="ECO:0000269|PubMed:25966638"
FT                   /id="VAR_077912"
FT   VARIANT         1569
FT                   /note="S -> A (found in a patient with autism; unknown
FT                   pathological significance; dbSNP:rs375050420)"
FT                   /evidence="ECO:0000269|PubMed:22865819"
FT                   /id="VAR_068702"
FT   VARIANT         2318
FT                   /note="K -> R (in dbSNP:rs59021407)"
FT                   /id="VAR_061013"
FT   VARIANT         2885
FT                   /note="H -> Q (in dbSNP:rs11599164)"
FT                   /id="VAR_059115"
FT   VARIANT         2996
FT                   /note="Q -> H (in dbSNP:rs41274672)"
FT                   /id="VAR_061014"
FT   VARIANT         3117
FT                   /note="I -> V (in dbSNP:rs28932171)"
FT                   /id="VAR_059116"
FT   VARIANT         3123
FT                   /note="K -> R (in dbSNP:rs10821668)"
FT                   /id="VAR_059117"
FT   VARIANT         3720
FT                   /note="T -> M (found in a patient with autism; unknown
FT                   pathological significance; dbSNP:rs201547988)"
FT                   /evidence="ECO:0000269|PubMed:22865819"
FT                   /id="VAR_068703"
FT   VARIANT         4255
FT                   /note="T -> P (found in a patient with autism; unknown
FT                   pathological significance; dbSNP:rs769573528)"
FT                   /evidence="ECO:0000269|PubMed:22865819"
FT                   /id="VAR_068704"
FT   VARIANT         4257
FT                   /note="I -> V (in dbSNP:rs12261793)"
FT                   /id="VAR_054333"
FT   CONFLICT        197
FT                   /note="T -> A (in Ref. 5; CAI56716)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        222
FT                   /note="L -> P (in Ref. 5; CAD97900)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        327
FT                   /note="I -> V (in Ref. 5; CAD97900)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        338
FT                   /note="L -> W (in Ref. 4; BAG58523)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        523
FT                   /note="A -> T (in Ref. 5; CAD97900)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        578
FT                   /note="L -> P (in Ref. 5; CAI56716)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        921
FT                   /note="R -> G (in Ref. 3; CAB66645)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        977
FT                   /note="S -> P (in Ref. 3; CAB66645)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1237
FT                   /note="D -> G (in Ref. 5; CAI56716)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1418
FT                   /note="P -> R (in Ref. 1; AAA64834)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1455
FT                   /note="D -> E (in Ref. 4; BAG58523)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1574
FT                   /note="F -> L (in Ref. 1; AAA64834)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1685
FT                   /note="A -> R (in Ref. 1; AAA64834)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1726
FT                   /note="P -> A (in Ref. 1; AAA64834)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2062..2063
FT                   /note="ER -> GG (in Ref. 1; AAA64834)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2146
FT                   /note="S -> T (in Ref. 1; AAA64834)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        3919
FT                   /note="H -> P (in Ref. 1; AAA64834)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        4137
FT                   /note="L -> F (in Ref. 3; CAB66645)"
FT                   /evidence="ECO:0000305"
FT   HELIX           4089..4101
FT                   /evidence="ECO:0000244|PDB:4O6X"
FT   HELIX           4102..4104
FT                   /evidence="ECO:0000244|PDB:4O6X"
FT   HELIX           4105..4111
FT                   /evidence="ECO:0000244|PDB:4O6X"
FT   HELIX           4116..4125
FT                   /evidence="ECO:0000244|PDB:4O6X"
FT   HELIX           4130..4145
FT                   /evidence="ECO:0000244|PDB:4O6X"
FT   HELIX           4146..4148
FT                   /evidence="ECO:0000244|PDB:4O6X"
FT   HELIX           4151..4160
FT                   /evidence="ECO:0000244|PDB:4O6X"
FT   HELIX           4164..4171
FT                   /evidence="ECO:0000244|PDB:4O6X"
FT   HELIX           4173..4178
FT                   /evidence="ECO:0000244|PDB:4O6X"
FT   MOD_RES         Q12955-4:1632
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:24275569"
FT   MOD_RES         Q12955-4:1658
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:24275569"
FT   MOD_RES         Q12955-5:1625
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:24275569"
FT   MOD_RES         Q12955-5:1651
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:24275569"
FT   MOD_RES         Q12955-6:765
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:24275569"
FT   MOD_RES         Q12955-6:791
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:24275569"
FT   MOD_RES         Q12955-7:468
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:24275569"
SQ   SEQUENCE   4377 AA;  480410 MW;  F6F9FABD09F15C13 CRC64;
     MAHAASQLKK NRDLEINAEE EPEKKRKHRK RSRDRKKKSD ANASYLRAAR AGHLEKALDY
     IKNGVDINIC NQNGLNALHL ASKEGHVEVV SELLQREANV DAATKKGNTA LHIASLAGQA
     EVVKVLVTNG ANVNAQSQNG FTPLYMAAQE NHLEVVKFLL DNGASQSLAT EDGFTPLAVA
     LQQGHDQVVS LLLENDTKGK VRLPALHIAA RKDDTKAAAL LLQNDNNADV ESKSGFTPLH
     IAAHYGNINV ATLLLNRAAA VDFTARNDIT PLHVASKRGN ANMVKLLLDR GAKIDAKTRD
     GLTPLHCGAR SGHEQVVEML LDRAAPILSK TKNGLSPLHM ATQGDHLNCV QLLLQHNVPV
     DDVTNDYLTA LHVAAHCGHY KVAKVLLDKK ANPNAKALNG FTPLHIACKK NRIKVMELLL
     KHGASIQAVT ESGLTPIHVA AFMGHVNIVS QLMHHGASPN TTNVRGETAL HMAARSGQAE
     VVRYLVQDGA QVEAKAKDDQ TPLHISARLG KADIVQQLLQ QGASPNAATT SGYTPLHLSA
     REGHEDVAAF LLDHGASLSI TTKKGFTPLH VAAKYGKLEV ANLLLQKSAS PDAAGKSGLT
     PLHVAAHYDN QKVALLLLDQ GASPHAAAKN GYTPLHIAAK KNQMDIATTL LEYGADANAV
     TRQGIASVHL AAQEGHVDMV SLLLGRNANV NLSNKSGLTP LHLAAQEDRV NVAEVLVNQG
     AHVDAQTKMG YTPLHVGCHY GNIKIVNFLL QHSAKVNAKT KNGYTPLHQA AQQGHTHIIN
     VLLQNNASPN ELTVNGNTAL GIARRLGYIS VVDTLKIVTE ETMTTTTVTE KHKMNVPETM
     NEVLDMSDDE VRKANAPEML SDGEYISDVE EGEDAMTGDT DKYLGPQDLK ELGDDSLPAE
     GYMGFSLGAR SASLRSFSSD RSYTLNRSSY ARDSMMIEEL LVPSKEQHLT FTREFDSDSL
     RHYSWAADTL DNVNLVSSPI HSGFLVSFMV DARGGSMRGS RHHGMRIIIP PRKCTAPTRI
     TCRLVKRHKL ANPPPMVEGE GLASRLVEMG PAGAQFLGPV IVEIPHFGSM RGKERELIVL
     RSENGETWKE HQFDSKNEDL TELLNGMDEE LDSPEELGKK RICRIITKDF PQYFAVVSRI
     KQESNQIGPE GGILSSTTVP LVQASFPEGA LTKRIRVGLQ AQPVPDEIVK KILGNKATFS
     PIVTVEPRRR KFHKPITMTI PVPPPSGEGV SNGYKGDTTP NLRLLCSITG GTSPAQWEDI
     TGTTPLTFIK DCVSFTTNVS ARFWLADCHQ VLETVGLATQ LYRELICVPY MAKFVVFAKM
     NDPVESSLRC FCMTDDKVDK TLEQQENFEE VARSKDIEVL EGKPIYVDCY GNLAPLTKGG
     QQLVFNFYSF KENRLPFSIK IRDTSQEPCG RLSFLKEPKT TKGLPQTAVC NLNITLPAHK
     KETESDQDDE IEKTDRRQSF ASLALRKRYS YLTEPGMIER STGATRSLPT TYSYKPFFST
     RPYQSWTTAP ITVPGPAKSG FTSLSSSSSN TPSASPLKSI WSVSTPSPIK STLGASTTSS
     VKSISDVASP IRSFRTMSSP IKTVVSQSPY NIQVSSGTLA RAPAVTEATP LKGLASNSTF
     SSRTSPVTTA GSLLERSSIT MTPPASPKSN INMYSSSLPF KSIITSAAPL ISSPLKSVVS
     PVKSAVDVIS SAKITMASSL SSPVKQMPGH AEVALVNGSI SPLKYPSSST LINGCKATAT
     LQEKISSATN SVSSVVSAAT DTVEKVFSTT TAMPFSPLRS YVSAAPSAFQ SLRTPSASAL
     YTSLGSSISA TTSSVTSSII TVPVYSVVNV LPEPALKKLP DSNSFTKSAA ALLSPIKTLT
     TETHPQPHFS RTSSPVKSSL FLAPSALKLS TPSSLSSSQE ILKDVAEMKE DLMRMTAILQ
     TDVPEEKPFQ PELPKEGRID DEEPFKIVEK VKEDLVKVSE ILKKDVCVDN KGSPKSPKSD
     KGHSPEDDWI EFSSEEIREA RQQAAASQSP SLPERVQVKA KAASEKDYNL TKVIDYLTND
     IGSSSLTNLK YKFEDAKKDG EERQKRVLKP AIALQEHKLK MPPASMRTST SEKELCKMAD
     SFFGTDTILE SPDDFSQHDQ DKSPLSDSGF ETRSEKTPSA PQSAESTGPK PLFHEVPIPP
     VITETRTEVV HVIRSYDPSA GDVPQTQPEE PVSPKPSPTF MELEPKPTTS SIKEKVKAFQ
     MKASSEEDDH NRVLSKGMRV KEETHITTTT RMVYHSPPGG EGASERIEET MSVHDIMKAF
     QSGRDPSKEL AGLFEHKSAV SPDVHKSAAE TSAQHAEKDN QMKPKLERII EVHIEKGNQA
     EPTEVIIRET KKHPEKEMYV YQKDLSRGDI NLKDFLPEKH DAFPCSEEQG QQEEEELTAE
     ESLPSYLESS RVNTPVSQEE DSRPSSAQLI SDDSYKTLKL LSQHSIEYHD DELSELRGES
     YRFAEKMLLS EKLDVSHSDT EESVTDHAGP PSSELQGSDK RSREKIATAP KKEILSKIYK
     DVSENGVGKV SKDEHFDKVT VLHYSGNVSS PKHAMWMRFT EDRLDRGREK LIYEDRVDRT
     VKEAEEKLTE VSQFFRDKTE KLNDELQSPE KKARPKNGKE YSSQSPTSSS PEKVLLTELL
     ASNDEWVKAR QHGPDGQGFP KAEEKAPSLP SSPEKMVLSQ QTEDSKSTVE AKGSISQSKA
     PDGPQSGFQL KQSKLSSIRL KFEQGTHAKS KDMSQEDRKS DGQSRIPVKK IQESKLPVYQ
     VFAREKQQKA IDLPDESVSV QKDFMVLKTK DEHAQSNEIV VNDSGSDNVK KQRTEMSSKA
     MPDSFSEQQA KDLACHITSD LATRGPWDKK VFRTWESSGA TNNKSQKEKL SHVLVHDVRE
     NHIGHPESKS VDQKNEFMSV TERERKLLTN GSLSEIKEMT VKSPSKKVLY REYVVKEGDH
     PGGLLDQPSR RSESSAVSHI PVRVADERRM LSSNIPDGFC EQSAFPKHEL SQKLSQSSMS
     KETVETQHFN SIEDEKVTYS EISKVSKHQS YVGLCPPLEE TETSPTKSPD SLEFSPGKES
     PSSDVFDHSP IDGLEKLAPL AQTEGGKEIK TLPVYVSFVQ VGKQYEKEIQ QGGVKKIISQ
     ECKTVQETRG TFYTTRQQKQ PPSPQGSPED DTLEQVSFLD SSGKSPLTPE TPSSEEVSYE
     FTSKTPDSLI AYIPGKPSPI PEVSEESEEE EQAKSTSLKQ TTVEETAVER EMPNDVSKDS
     NQRPKNNRVA YIEFPPPPPL DADQIESDKK HHYLPEKEVD MIEVNLQDEH DKYQLAEPVI
     RVQPPSPVPP GADVSDSSDD ESIYQPVPVK KYTFKLKEVD DEQKEKPKAS AEKASNQKEL
     ESNGSGKDNE FGLGLDSPQN EIAQNGNNDQ SITECSIATT AEFSHDTDAT EIDSLDGYDL
     QDEDDGLTES DSKLPIQAME IKKDIWNTEG ILKPADRSFS QSKLEVIEEE GKVGPDEDKP
     PSKSSSSEKT PDKTDQKSGA QFFTLEGRHP DRSVFPDTYF SYKVDEEFAT PFKTVATKGL
     DFDPWSNNRG DDEVFDSKSR EDETKPFGLA VEDRSPATTP DTTPARTPTD ESTPTSEPNP
     FPFHEGKMFE MTRSGAIDMS KRDFVEERLQ FFQIGEHTSE GKSGDQGEGD KSMVTATPQP
     QSGDTTVETN LERNVETPTV EPNPSIPTSG ECQEGTSSSG SLEKSAAATN TSKVDPKLRT
     PIKMGISAST MTMKKEGPGE ITDKIEAVMT SCQGLENETI TMISNTANSQ MGVRPHEKHD
     FQKDNFNNNN NLDSSTIQTD NIMSNIVLTE HSAPTCTTEK DNPVKVSSGK KTGVLQGHCV
     RDKQKVLGEQ QKTKELIGIR QKSKLPIKAT SPKDTFPPNH MSNTKASKMK QVSQSEKTKA
     LTTSSCVDVK SRIPVKNTHR DNIIAVRKAC ATQKQGQPEK GKAKQLPSKL PVKVRSTCVT
     TTTTTATTTT TTTTTTTTSC TVKVRKSQLK EVCKHSIEYF KGISGETLKL VDRLSEEEKK
     MQSELSDEEE STSRNTSLSE TSRGGQPSVT TKSARDKKTE AAPLKSKSEK AGSEKRSSRR
     TGPQSPCERT DIRMAIVADH LGLSWTELAR ELNFSVDEIN QIRVENPNSL ISQSFMLLKK
     WVTRDGKNAT TDALTSVLTK INRIDIVTLL EGPIFDYGNI SGTRSFADEN NVFHDPVDGW
     QNETSSGNLE SCAQARRVTG GLLDRLDDSP DQCRDSITSY LKGEAGKFEA NGSHTEITPE
     AKTKSYFPES QNDVGKQSTK ETLKPKIHGS GHVEEPASPL AAYQKSLEET SKLIIEETKP
     CVPVSMKKMS RTSPADGKPR LSLHEEEGSS GSEQKQGEGF KVKTKKEIRH VEKKSHS
//
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