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 27-MAR-2024, entry version 216.
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), FUNCTION, 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: Membrane-cytoskeleton linker. May participate in the
CC maintenance/targeting of ion channels and cell adhesion molecules at
CC the nodes of Ranvier and axonal initial segments (PubMed:7836469). In
CC skeletal muscle, required for costamere localization of DMD and
CC betaDAG1 (By similarity). Regulates KCNA1 channel activity in function
CC of dietary Mg(2+) levels, and thereby contributes to the regulation of
CC renal Mg(2+) reabsorption (PubMed:23903368). Required for intracellular
CC adhesion and junctional conductance in myocytes, potentially via
CC stabilization of GJA1/CX43 protein abundance and promotion of PKP2,
CC GJA1/CX43, and SCN5A/Nav1.5 localization to cell-cell junctions (By
CC similarity). {ECO:0000250|UniProtKB:G5E8K5,
CC ECO:0000250|UniProtKB:O70511, ECO:0000269|PubMed:23903368,
CC ECO:0000269|PubMed:7836469}.
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). Interacts with PKP2 and GJA1/CX43 (By
CC similarity). {ECO:0000250|UniProtKB:G5E8K5,
CC ECO:0000250|UniProtKB:O70511, ECO:0000269|PubMed:15579534,
CC ECO:0000269|PubMed:15611082, ECO:0000269|PubMed:21223964,
CC ECO:0000269|PubMed:23903368, 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}. Postsynaptic cell membrane
CC {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: Intellectual developmental disorder, autosomal recessive 37
CC (MRT37) [MIM:615493]: A disorder characterized by significantly below
CC average 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 variants 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";
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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 EMDB; EMD-21537; -.
DR EMDB; EMD-21538; -.
DR SMR; Q12955; -.
DR BioGRID; 106785; 155.
DR CORUM; Q12955; -.
DR DIP; DIP-49017N; -.
DR ELM; Q12955; -.
DR IntAct; Q12955; 58.
DR MINT; Q12955; -.
DR STRING; 9606.ENSP00000280772; -.
DR TCDB; 8.A.28.1.9; the ankyrin (ankyrin) family.
DR GlyCosmos; Q12955; 45 sites, 1 glycan.
DR GlyGen; Q12955; 49 sites, 1 O-linked glycan (49 sites).
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; 9606-ENSP00000280772; -.
DR PeptideAtlas; Q12955; -.
DR ProteomicsDB; 19802; -.
DR ProteomicsDB; 3339; -.
DR ProteomicsDB; 59048; -. [Q12955-3]
DR Pumba; Q12955; -.
DR ABCD; Q12955; 6 sequenced antibodies.
DR Antibodypedia; 4197; 352 antibodies from 29 providers.
DR DNASU; 288; -.
DR Ensembl; ENST00000280772.7; ENSP00000280772.1; ENSG00000151150.22. [Q12955-3]
DR Ensembl; ENST00000355288.6; ENSP00000347436.2; ENSG00000151150.22. [Q12955-6]
DR Ensembl; ENST00000373827.6; ENSP00000362933.2; ENSG00000151150.22. [Q12955-5]
DR Ensembl; ENST00000503366.6; ENSP00000425236.1; ENSG00000151150.22. [Q12955-4]
DR GeneID; 288; -.
DR KEGG; hsa:288; -.
DR MANE-Select; ENST00000280772.7; ENSP00000280772.1; NM_020987.5; NP_066267.2.
DR UCSC; uc001jkw.4; human. [Q12955-3]
DR AGR; HGNC:494; -.
DR CTD; 288; -.
DR DisGeNET; 288; -.
DR GeneCards; ANK3; -.
DR HGNC; HGNC:494; ANK3.
DR HPA; ENSG00000151150; Low tissue specificity.
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 VEuPathDB; HostDB:ENSG00000151150; -.
DR eggNOG; KOG4177; Eukaryota.
DR GeneTree; ENSGT00940000154939; -.
DR HOGENOM; CLU_000134_29_1_1; -.
DR InParanoid; Q12955; -.
DR OrthoDB; 5474900at2759; -.
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 SignaLink; Q12955; -.
DR SIGNOR; Q12955; -.
DR BioGRID-ORCS; 288; 13 hits in 1166 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 endothelial cell and 209 other cell types or 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: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:0044325; F:transmembrane transporter binding; ISS: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: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; 2.60.220.30; -; 2.
DR Gene3D; 2.60.40.2660; -; 1.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 3.
DR Gene3D; 1.10.533.10; Death Domain, Fas; 1.
DR InterPro; IPR037971; Ank3_Death.
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 PANTHER; PTHR24123:SF49; ANKYRIN REPEAT AND DEATH DOMAIN-CONTAINING 1B; 1.
DR PANTHER; PTHR24123; ANKYRIN REPEAT-CONTAINING; 1.
DR Pfam; PF00023; Ank; 1.
DR Pfam; PF12796; Ank_2; 7.
DR Pfam; PF13637; Ank_4; 3.
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; SSF48403; Ankyrin repeat; 3.
DR SUPFAM; SSF47986; DEATH domain; 1.
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 membrane; Cell projection; Cytoplasm; Cytoskeleton; Golgi apparatus;
KW Intellectual disability; Lysosome; Membrane; Phosphoprotein;
KW Postsynaptic cell membrane; Reference proteome; Repeat; 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 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1273..1407
FT /note="UPA domain"
FT /evidence="ECO:0000250"
FT REGION 1519..1540
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1968..1987
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2107..2159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2176..2245
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2299..2322
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2383..2433
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2474..2508
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2588..2751
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2795..2824
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3036..3067
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3131..3272
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3298..3516
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3538..3607
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3635..3718
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3868..3897
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 4019..4090
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 4251..4298
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 4323..4377
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..27
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2112..2129
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2130..2146
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2219..2245
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2403..2433
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2588..2618
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2619..2636
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2673..2720
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2724..2748
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3041..3058
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3131..3185
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3224..3242
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3333..3355
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3378..3405
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3462..3495
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3545..3569
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3576..3599
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3650..3716
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3875..3897
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 4019..4034
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 4035..4052
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 4053..4077
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 4256..4278
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 4338..4366
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 39
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|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:0007744|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:0007744|PubMed:21406692"
FT MOD_RES 1459
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|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:0007744|PubMed:24275569"
FT MOD_RES 4290
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 4298
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 4350
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|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; uncertain 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; uncertain
FT 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; uncertain
FT 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; uncertain
FT 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:0007829|PDB:4O6X"
FT HELIX 4102..4104
FT /evidence="ECO:0007829|PDB:4O6X"
FT HELIX 4105..4111
FT /evidence="ECO:0007829|PDB:4O6X"
FT HELIX 4116..4125
FT /evidence="ECO:0007829|PDB:4O6X"
FT HELIX 4130..4145
FT /evidence="ECO:0007829|PDB:4O6X"
FT HELIX 4146..4148
FT /evidence="ECO:0007829|PDB:4O6X"
FT HELIX 4151..4160
FT /evidence="ECO:0007829|PDB:4O6X"
FT HELIX 4164..4171
FT /evidence="ECO:0007829|PDB:4O6X"
FT HELIX 4173..4178
FT /evidence="ECO:0007829|PDB:4O6X"
FT MOD_RES Q12955-4:1632
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES Q12955-4:1658
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES Q12955-5:1625
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES Q12955-5:1651
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES Q12955-6:765
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES Q12955-6:791
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES Q12955-7:468
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|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
//
