RBCC

Full text data of ANK3

ANK3 [Confidence: low (only semi-automatic identification from reviews)]
Ankyrin-3; ANK-3 (Ankyrin-G)

UniProt Q12955
ID ANK3_HUMAN Reviewed; 4377 AA.
AC Q12955; B1AQT2; B4DIL1; E9PE32; Q5CZH9; Q5VXD5; Q7Z3G4; Q9H0P5;
read moreDT 11-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-SEP-2009, sequence version 3.
DT 22-JAN-2014, entry version 132.
DE RecName: Full=Ankyrin-3;
DE Short=ANK-3;
DE AltName: Full=Ankyrin-G;
GN Name=ANK3;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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
RT at the axonal initial segment and node of Ranvier.";
RL J. Biol. Chem. 270:2352-2359(1995).
RN [2]
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.,
RA Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N.,
RA Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D.,
RA Wambutt R., Korn B., Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and
RT analysis of 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [3]
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [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.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=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.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
RA Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
RA Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
RA Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
RA Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
RA Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
RA Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
RA Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
RA Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
RA Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
RA Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
RA Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
RA Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
RA Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
RA Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
RA Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
RA Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
RA 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 [6]
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
RT and ankyrin-G for basolateral targeting and membrane anchorage in
RT polarized kidney epithelial cells.";
RL J. Biol. Chem. 280:8221-8228(2005).
RN [7]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-4338, AND MASS
RP SPECTROMETRY.
RC TISSUE=Mammary cancer;
RX PubMed=17370265; DOI=10.1002/pmic.200600410;
RA Denis N.J., Vasilescu J., Lambert J.-P., Smith J.C., Figeys D.;
RT "Tryptic digestion of ubiquitin standards reveals an improved strategy
RT for identifying ubiquitinated proteins by mass spectrometry.";
RL Proteomics 7:868-874(2007).
RN [8]
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.,
RA Buerckstuemmer T., 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-39; SER-847; SER-1445
RP AND SER-4298, AND MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [10]
RP VARIANTS ALA-1569; MET-3720 AND PRO-4255, AND ASSOCIATION WITH AUTISM
RP SUSCEPTIBILITY.
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.,
RA Jiang Y.H., Sun Z.S.;
RT "Mutations of ANK3 identified by exome sequencing are associated with
RT autism susceptibility.";
RL Hum. Mutat. 33:1635-1638(2012).
CC -!- FUNCTION: In skeletal muscle, required for costamere localization
CC of DMD and betaDAG1 (By similarity). Membrane-cytoskeleton linker.
CC May participate in the maintenance/targeting of ion channels and
CC cell adhesion molecules at the nodes of Ranvier and axonal initial
CC segments.
CC -!- SUBUNIT: Directly interacts with DMD and betaDAG1. This
CC interaction does not interfere with binding between DMD and
CC betaDAG1. It is also required for DMD and betaDAG1 retention at
CC costameres (By similarity). Interacts (via N-terminal ANK repeats)
CC with SCHIP1 isoform 5 (via C-terminus); this interaction is
CC required for the localization at axon initial segments (AISs) and
CC nodes of Ranvier (NRs) (By similarity). May be a constituent of a
CC neurofascin/NRCAM/ankyrin G complex. Interacts with RHBG.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cell junction,
CC synapse, postsynaptic cell membrane (By similarity). Lysosome (By
CC similarity). Note=In skeletal muscle, localized at costameres and
CC neuromuscular junctions (By similarity). In macrophages,
CC associated with lysosomes (By similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
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 Note=Ref.2 (CAB66645) sequence(s) differ(s) from that shown due
CC to (a) frameshift(s) in position(s) 810;
CC -!- TISSUE SPECIFICITY: Expressed in brain, neurons and other tissues.
CC -!- DOMAIN: The tandem configuration of the two ZU5 and the UPA
CC domains forms a structural supramodule termed ZZU. ZU5-1 mediates
CC interaction with beta-spectrin, and the ZU5-1/UPA interface is
CC required for ankyrin's function other than binding to spectrin (By
CC similarity).
CC -!- DISEASE: Note=Genetic variations in ANK3 are associated with
CC autism spectrum disorders susceptibility.
CC -!- SIMILARITY: Contains 23 ANK repeats.
CC -!- SIMILARITY: Contains 1 death domain.
CC -!- SIMILARITY: Contains 2 ZU5 domains.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Ankyrin entry;
CC URL="http://en.wikipedia.org/wiki/Ankyrin";
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DR EMBL; U13616; AAA64834.1; -; 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 PIR; A55575; A55575.
DR RefSeq; NP_001140.2; NM_001149.3.
DR RefSeq; NP_001191332.1; NM_001204403.1.
DR RefSeq; NP_001191333.1; NM_001204404.1.
DR RefSeq; NP_066267.2; NM_020987.3.
DR UniGene; Hs.499725; -.
DR ProteinModelPortal; Q12955; -.
DR SMR; Q12955; 14-871, 982-1442, 4090-4167.
DR DIP; DIP-49017N; -.
DR IntAct; Q12955; 2.
DR STRING; 9606.ENSP00000280772; -.
DR PhosphoSite; Q12955; -.
DR DMDM; 257051061; -.
DR PaxDb; Q12955; -.
DR PRIDE; Q12955; -.
DR ProMEX; Q12955; -.
DR DNASU; 288; -.
DR Ensembl; ENST00000280772; ENSP00000280772; ENSG00000151150.
DR Ensembl; ENST00000355288; ENSP00000347436; ENSG00000151150.
DR Ensembl; ENST00000373827; ENSP00000362933; ENSG00000151150.
DR Ensembl; ENST00000503366; ENSP00000425236; ENSG00000151150.
DR GeneID; 288; -.
DR KEGG; hsa:288; -.
DR UCSC; uc001jkw.3; human.
DR CTD; 288; -.
DR GeneCards; GC10M061788; -.
DR H-InvDB; HIX0008849; -.
DR HGNC; HGNC:494; ANK3.
DR HPA; CAB015179; -.
DR MIM; 600465; gene.
DR neXtProt; NX_Q12955; -.
DR Orphanet; 356996; Intellectual deficiency - hypotonia - spasticity - sleep disorder.
DR PharmGKB; PA24800; -.
DR eggNOG; COG0666; -.
DR HOGENOM; HOG000012873; -.
DR HOVERGEN; HBG024337; -.
DR InParanoid; Q12955; -.
DR KO; K10380; -.
DR OMA; QNGNNDQ; -.
DR OrthoDB; EOG7P02H2; -.
DR PhylomeDB; Q12955; -.
DR Reactome; REACT_111045; Developmental Biology.
DR ChiTaRS; ANK3; human.
DR GeneWiki; ANK3; -.
DR GenomeRNAi; 288; -.
DR NextBio; 1175; -.
DR PRO; PR:Q12955; -.
DR ArrayExpress; Q12955; -.
DR Bgee; Q12955; -.
DR CleanEx; HS_ANK3; -.
DR Genevestigator; Q12955; -.
DR GO; GO:0043194; C:axon initial segment; ISS: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: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:0033268; C:node of Ranvier; ISS:BHF-UCL.
DR GO; GO:0033270; C:paranode region of axon; IEA:Ensembl.
DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0014731; C:spectrin-associated cytoskeleton; ISS:BHF-UCL.
DR GO; GO:0030315; C:T-tubule; ISS:BHF-UCL.
DR GO; GO:0045296; F:cadherin binding; ISS:BHF-UCL.
DR GO; GO:0044325; F:ion channel binding; ISS:BHF-UCL.
DR GO; GO:0030674; F:protein binding, bridging; 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:0007411; P:axon guidance; IEA:Ensembl.
DR GO; GO:0007409; P:axonogenesis; ISS:BHF-UCL.
DR GO; GO:0043001; P:Golgi to plasma membrane protein transport; IMP:BHF-UCL.
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:0010628; P:positive regulation of gene expression; ISS:BHF-UCL.
DR GO; GO:1900827; P:positive regulation of membrane depolarization involved in regulation of cardiac muscle cell action potential; ISS:BHF-UCL.
DR GO; GO:0045838; P:positive regulation of membrane potential; 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:0072661; P:protein targeting to plasma membrane; IMP:BHF-UCL.
DR GO; GO:0019228; P:regulation of action potential in neuron; ISS: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 GO; GO:0050808; P:synapse organization; IEA:Ensembl.
DR Gene3D; 1.10.533.10; -; 1.
DR Gene3D; 1.25.40.20; -; 3.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR020683; Ankyrin_rpt-contain_dom.
DR InterPro; IPR011029; DEATH-like_dom.
DR InterPro; IPR000488; Death_domain.
DR InterPro; IPR000906; ZU5.
DR Pfam; PF00023; Ank; 3.
DR Pfam; PF12796; Ank_2; 6.
DR Pfam; PF00531; Death; 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; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ANK repeat; Cell junction; Cell membrane;
KW Complete proteome; Cytoplasm; Cytoskeleton; Isopeptide bond; Lysosome;
KW Membrane; Phosphoprotein; Polymorphism; Postsynaptic cell membrane;
KW Reference proteome; Repeat; Synapse; Ubl conjugation.
FT CHAIN 1 4377 Ankyrin-3.
FT /FTId=PRO_0000066886.
FT REPEAT 73 102 ANK 1.
FT REPEAT 106 135 ANK 2.
FT REPEAT 139 168 ANK 3.
FT REPEAT 172 201 ANK 4.
FT REPEAT 203 230 ANK 5.
FT REPEAT 234 263 ANK 6.
FT REPEAT 267 296 ANK 7.
FT REPEAT 300 329 ANK 8.
FT REPEAT 333 362 ANK 9.
FT REPEAT 366 395 ANK 10.
FT REPEAT 399 428 ANK 11.
FT REPEAT 432 461 ANK 12.
FT REPEAT 465 494 ANK 13.
FT REPEAT 498 527 ANK 14.
FT REPEAT 531 560 ANK 15.
FT REPEAT 564 593 ANK 16.
FT REPEAT 597 626 ANK 17.
FT REPEAT 630 659 ANK 18.
FT REPEAT 663 692 ANK 19.
FT REPEAT 696 725 ANK 20.
FT REPEAT 729 758 ANK 21.
FT REPEAT 762 791 ANK 22.
FT REPEAT 795 825 ANK 23.
FT DOMAIN 982 1107 ZU5 1.
FT DOMAIN 1108 1272 ZU5 2.
FT DOMAIN 4090 4174 Death.
FT REGION 1273 1407 UPA domain (By similarity).
FT COMPBIAS 1519 1898 Ser-rich.
FT COMPBIAS 2247 2250 Poly-Thr.
FT COMPBIAS 2393 2396 Poly-Glu.
FT COMPBIAS 3205 3211 Poly-Glu.
FT COMPBIAS 3255 3259 Poly-Pro.
FT COMPBIAS 3482 3487 Poly-Ser.
FT COMPBIAS 3785 3791 Poly-Asn.
FT COMPBIAS 3957 3981 Thr-rich.
FT MOD_RES 39 39 Phosphoserine.
FT MOD_RES 847 847 Phosphoserine.
FT MOD_RES 1445 1445 Phosphoserine.
FT MOD_RES 4298 4298 Phosphoserine.
FT CROSSLNK 4338 4338 Glycyl lysine isopeptide (Lys-Gly)
FT (interchain with G-Cter in ubiquitin).
FT VAR_SEQ 1 866 Missing (in isoform 4).
FT /FTId=VSP_046885.
FT VAR_SEQ 1 37 MAHAASQLKKNRDLEINAEEEPEKKRKHRKRSRDRKK ->
FT MASSASSSPAGTEDSAPAQGGFGSDYSRSSR (in
FT isoform 3).
FT /FTId=VSP_044348.
FT VAR_SEQ 1 36 MAHAASQLKKNRDLEINAEEEPEKKRKHRKRSRDRK -> M
FT SEEPKEKNAKPAHRKRKG (in isoform 2).
FT /FTId=VSP_044349.
FT VAR_SEQ 867 872 SDVEEG -> MALPQS (in isoform 4).
FT /FTId=VSP_046886.
FT VAR_SEQ 872 872 G -> GNRCTWYKIPKVQEFTVKS (in isoform 2).
FT /FTId=VSP_044350.
FT VAR_SEQ 1442 1450 Missing (in isoform 2, isoform 3 and
FT isoform 4).
FT /FTId=VSP_044351.
FT VAR_SEQ 1478 4081 Missing (in isoform 2, isoform 3 and
FT isoform 4).
FT /FTId=VSP_044352.
FT VAR_SEQ 4082 4082 G -> S (in isoform 2, isoform 3 and
FT isoform 4).
FT /FTId=VSP_044353.
FT VAR_SEQ 4199 4199 G -> GYPSLQVELETPTGLHYTPPTPFQQDDYFSDISSIE
FT SPLRTPSRLSDGLVPSQGNIEHSADGPPVVTAEDASLEDSK
FT LEDSVPLTEMPEAVDVDESQLENVCLS (in isoform
FT 2, isoform 3 and isoform 4).
FT /FTId=VSP_044354.
FT VARIANT 1569 1569 S -> A (associated with autism
FT susceptibility).
FT /FTId=VAR_068702.
FT VARIANT 2318 2318 K -> R (in dbSNP:rs59021407).
FT /FTId=VAR_061013.
FT VARIANT 2885 2885 H -> Q (in dbSNP:rs11599164).
FT /FTId=VAR_059115.
FT VARIANT 2996 2996 Q -> H (in dbSNP:rs41274672).
FT /FTId=VAR_061014.
FT VARIANT 3117 3117 I -> V (in dbSNP:rs28932171).
FT /FTId=VAR_059116.
FT VARIANT 3123 3123 K -> R (in dbSNP:rs10821668).
FT /FTId=VAR_059117.
FT VARIANT 3720 3720 T -> M (associated with autism
FT susceptibility).
FT /FTId=VAR_068703.
FT VARIANT 4255 4255 T -> P (associated with autism
FT susceptibility).
FT /FTId=VAR_068704.
FT VARIANT 4257 4257 I -> V (in dbSNP:rs12261793).
FT /FTId=VAR_054333.
FT CONFLICT 197 197 T -> A (in Ref. 4; CAI56716).
FT CONFLICT 222 222 L -> P (in Ref. 4; CAD97900).
FT CONFLICT 327 327 I -> V (in Ref. 4; CAD97900).
FT CONFLICT 338 338 L -> W (in Ref. 3; BAG58523).
FT CONFLICT 523 523 A -> T (in Ref. 4; CAD97900).
FT CONFLICT 578 578 L -> P (in Ref. 4; CAI56716).
FT CONFLICT 921 921 R -> G (in Ref. 2; CAB66645).
FT CONFLICT 977 977 S -> P (in Ref. 2; CAB66645).
FT CONFLICT 1036 1043 MVEGEGLA -> HGERRGIS (in Ref. 1;
FT AAA64834).
FT CONFLICT 1237 1237 D -> G (in Ref. 4; CAI56716).
FT CONFLICT 1418 1418 P -> R (in Ref. 1; AAA64834).
FT CONFLICT 1455 1455 D -> E (in Ref. 3; BAG58523).
FT CONFLICT 1574 1574 F -> L (in Ref. 1; AAA64834).
FT CONFLICT 1685 1685 A -> R (in Ref. 1; AAA64834).
FT CONFLICT 1726 1726 P -> A (in Ref. 1; AAA64834).
FT CONFLICT 2062 2063 ER -> GG (in Ref. 1; AAA64834).
FT CONFLICT 2146 2146 S -> T (in Ref. 1; AAA64834).
FT CONFLICT 3919 3919 H -> P (in Ref. 1; AAA64834).
FT CONFLICT 4137 4137 L -> F (in Ref. 2; CAB66645).
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
//

MIM 600465
*RECORD*
*FIELD* NO
600465
*FIELD* TI
*600465 ANKYRIN 3; ANK3
;;ANKYRIN-G
*FIELD* TX

DESCRIPTION

Ankyrins are peripheral membrane proteins thought to interconnect
read moreintegral proteins with the spectrin-based membrane skeleton (summary by
Kordeli and Bennett, 1991).

The ANK3 gene encodes ankyrin-G, which is located mainly at the nodes of
Ranvier and the axon initial segment (AIS), 2 subcompartments of neurons
responsible for the generation of action potentials. It has been shown
to associate with the voltage-dependent sodium channel (summary by Iqbal
et al., 2013).

Erythrocytic ankyrin, also known as ankyrin-R (ANK1; 612641), and brain
ankyrin, also known as ankyrin-B or ankyrin-2 (ANK2; 106410), are
distinct forms.

CLONING

Kordeli and Bennett (1991) concluded that the ankyrin isoform present at
the node of Ranvier was the product of a previously unidentified ankyrin
gene, as ankyrin was still present in the node of Ranvier in
ankyrin-R-deficient mice (carrying the nb mutation) and was not
recognized by antibodies specific for ankyrin-B or ankyrin-R.

Kordeli et al. (1995) described the cDNA sequence of a third ankyrin
gene with alternatively spliced isoforms expressed in brain as well as a
variety of other tissues. The 2 largest protein isoforms, which contain
an unusual serine-rich sequence, are expressed only in nervous tissue.
Specific antibodies raised against this serine-rich sequence stained AIS
and nodes of Ranvier in cryosections from the rat brain. The full-length
polypeptide has a molecular mass of 480 kD and includes a globular head
domain, with membrane- and spectrin-binding activities, as well as an
extended 'tail' domain. Kordeli et al. (1995) termed the gene ankyrin-G,
based on its giant size and general expression. The 2 brain-specific
isoforms were of sizes 480 and 270 kD.

GENE FUNCTION

Using GABAergic cell type-specific promoters and mouse BACs, Ango et al.
(2004) generated BAC transgenic mice with fluorescence-labeled Purkinje
cells and interneurons visible at synaptic resolution during cerebellar
development. They found that basket axons always contacted Purkinje soma
before innervating Purkinje AIS and prior to the formation of elaborate
pinceau synapses. This synapse-targeting process followed the
establishment of a subcellular gradient of neurofascin-186 (NF186), an
alternatively spliced form of neurofascin (609145) (Davis et al., 1996),
along the Purkinje AIS-soma axis. The gradient was dependent on
ankyrin-G, an AIS-restricted membrane adaptor protein that recruits
NF186. In the absence of the NF186 gradient, basket axons lost
directional growth along Purkinje neurons and precisely followed NF186
to ectopic locations. Disruption of NF186-ankyrin-G interactions at AIS
reduced pinceau synapse formation.

Using coimmunoprecipitation experiments, Mohler et al. (2004)
demonstrated that the 190-kD ankyrin-G isoform in adult rat heart
associates with the cardiac sodium channel Na(v)1.5, the gene product of
the SCN5A gene (600163). By confocal microscopy they showed that
ankyrin-G, like Na(v)1.5, is highly expressed at ventricular
intercalated disc and T-tubule membranes in cardiomyocytes. Mohler et
al. (2004) presented evidence that a human mutation in the SCN5A gene
(600163.0033) blocks ankyrin-G binding and disrupts surface expression
of Na(v)1.5 in cardiomyocytes, resulting in Brugada syndrome (601144), a
dominantly inherited cardiac arrhythmia.

Kizhatil et al. (2009) found that targeting of cyclic nucleotide-gated
(CNG) channels to the rod outer segment required their interaction with
ankyrin-G. Ankyrin-G localized exclusively to rod outer segments,
coimmunoprecipitated with the CNG channel, and bound to the C-terminal
domain of the channel beta-1 subunit (CNGB1; 600724). Ankyrin-G
depletion in neonatal mouse retinas markedly reduced CNG channel
expression. Transgenic expression of CNG channel beta-subunit mutants in
Xenopus rods showed that ankyrin-G binding was necessary and sufficient
for targeting of the beta-1 subunit to outer segments. Thus, Kizhatil et
al. (2009) concluded that ankyrin-G is required for transport of CNG
channels to the plasma membrane of rod outer segments.

MAPPING

By fluorescence in situ hybridization, Kapfhamer et al. (1995) mapped
the ANK3 gene to 10q21. By intersubspecific backcross analysis, they
mapped the murine homolog to mouse chromosome 10 between microsatellite
marker D10Mit31 and the Bcr gene. This interval of mouse chromosome 10
is known to comprise a region with homology of synteny to human 10q. The
localization of ANK3 may help identify neurologic disorders associated
with the gene in man or mouse.

CYTOGENETICS

Iqbal et al. (2013) reported a boy with autism, attention
deficit-hyperactivity disorder, cognitive problems, and sleep disorder
associated with a balanced translocation with breakpoints between
chromosomes 2q11.2 and 10q21.2. The breakpoint on 10q21.2 mapped to
intron 30 of the ANK3 gene and interrupted all ANK3 transcript variants;
the breakpoint on 2q11.2 was in a pseudogene. Patient cells showed
significantly decreased expression of the ANK3 gene, about 25% compared
to controls. The patient had mildly delayed development, delayed speech,
and behavioral abnormalities, including aggression. He had a peculiar
facial appearance, with mildly upslanted palpebral fissures, broad nose,
and flat philtrum. He also had 2 sacral dimples and several patches of
depigmented skin.

MOLECULAR GENETICS

In 3 Pakistani sibs, born of consanguineous parents, with autosomal
recessive mental retardation-37 (MRT37; 615493) and behavioral
abnormalities, Iqbal et al. (2013) identified a homozygous frameshift
mutation in the ANK3 gene (600465.0001). The mutation, which was found
by homozygosity mapping and whole-exome sequencing and confirmed by
Sanger sequencing, segregated with the disorder in the family. Iqbal et
al. (2013) concluded that ANK3 mutations and polymorphisms are
associated with a wide spectrum of mental disorders presenting in a
continuum from mental retardation to autism.

ANIMAL MODEL

Sobotzik et al. (2009) demonstrated that targeted depletion of the AnkG
gene in mouse cerebellum caused axons to develop protrusions that
closely resembled dendritic spines. These mutant spines were enriched in
postsynaptic proteins and lacked typical ultrastructural features of the
axon initial segment, such as cytoplasmic bundles of microtubules. These
axonal spines were contacted by presynaptic glutamatergic boutons,
consistent with features of dendrites. The findings indicated that loss
of AnkG causes a disruption in axo-dendritic polarity.

Iqbal et al. (2013) found that targeted knockdown of the Drosophila Ank2
gene, which is the homolog of human ANK3, at the neuromuscular junction
resulted in small synapses and less synaptic boutons compared to
controls. There was a reduction in synapse area and length. Ablation of
Ank2 gene in the mushroom bodies, the learning and memory center of the
fly, caused a reduction in short-term memory despite normal learning and
normal motor function. The findings suggested a specific cognitive
defect.

*FIELD* AV
.0001
MENTAL RETARDATION, AUTOSOMAL RECESSIVE 37 (1 family)
ANK3, 1-BP DEL, 10995C

In 3 Pakistani sibs, born of consanguineous parents, with autosomal
recessive mental retardation-37 (MRT37; 615493) and behavioral
abnormalities, Iqbal et al. (2013) identified a homozygous 1-bp deletion
(c.10995delC) in the ANK3 gene, resulting in a frameshift and premature
termination in exon 42 (Thr3666LeufsTer2). Exon 42 is unique to the
largest isoform of ANK2, and the mutation was predicted to specifically
affect synthesis of the 270/480-kD isoforms, which are brain-specific.
The mutant mRNA was likely targeted for nonsense-mediated mRNA decay,
but no patient cells were available for testing. The mutation, which was
found by homozygosity mapping and whole-exome sequencing and confirmed
by Sanger sequencing, segregated with the disorder in the family. It was
not found in the dbSNP, 1000 Genomes, or Exome Sequencing Project
databases, or in 268 ethnically matched controls or 200 Danish exomes.

.0002
VARIANT OF UNKNOWN SIGNIFICANCE
ANK3, SER1569ALA

This variant is classified as a variant of unknown significance because
its contribution to the development of autism (see 209850) has not been
confirmed.

In a patient with autism, Bi et al. (2012) identified a de novo
heterozygous c.4705T-G transversion in exon 42 of the ANK3 gene,
resulting in a ser1569-to-ala (S1569A) substitution at a highly
conserved residue. The variant was identified by whole-exome sequencing
and confirmed by Sanger sequencing. It was not found in the dbSNP or
1000 Genomes Project databases, or in 2,000 Caucasian exomes. This
patient was ascertained from a cohort of 20 patients with autism
spectrum disorder who underwent whole-exome sequencing. Another patient
with a de novo heterozygous S1569A substitution was subsequently found
in a cohort of 47 patients with autism spectrum disorder who underwent
direct sequencing of the ANK3 gene. Two more patients from the second
cohort carried heterozygous missense variants in the ANK3 gene (T3720M
and T4255P, respectively) that were not present in 2,000 Caucasian
exomes, but each of these variants was also present in an unaffected
parent. Bi et al. (2012) suggested that the role of ANK3 at synapses in
the central nervous system make it a candidate gene for susceptibility
to autism. No functional studies were performed.

*FIELD* RF
1. Ango, F.; di Cristo, G.; Higashiyama, H.; Bennett, V.; Wu, P.;
Huang, Z. J.: Ankyrin-based subcellular gradient of neurofascin,
an immunoglobulin family protein, directs GABAergic innervation at
Purkinje axon initial segment. Cell 119: 257-272, 2004.

2. Bi, C.; Wu, J.; Jiang, T.; Liu, Q.; Cai, W.; Yu, P.; Cai, T.; Zhao,
M.; Jiang, Y.; Sun, Z. S.: Mutations of ANK3 identified by exome
sequencing are associated with autism susceptibility. Hum. Mutat. 33:
1635-1638, 2012.

3. Davis, J. Q.; Lambert, S.; Bennett, V.: Molecular composition
of the node of Ranvier: identification of ankyrin-binding cell adhesion
molecules neurofascin (mucin+/third FNIII domain-) and NrCAM at nodal
axon segments. J. Cell Biol. 135: 1355-1367, 1996.

4. Iqbal, Z.; Vandeweyer, G.; van der Voet, M.; Waryah, A. M.; Zahoor,
M. Y.; Besseling, J. A.; Roca, L. T.; Vulto-van Silfhout, A. T.; Nijhof,
B.; Kramer, J. M.; Van der Aa, N.; Ansar, M.; and 11 others: Homozygous
and heterozygous disruptions of ANK3: at the crossroads of neurodevelopmental
and psychiatric disorders. Hum. Molec. Genet. 22: 1960-1970, 2013.

5. Kapfhamer, D.; Miller, D. E.; Lambert, S.; Bennett, V.; Glover,
T. W.; Burmeister, M.: Chromosomal localization of the ankyrin-G
gene (ANK3/Ank3) to human 10q21 and mouse 10. Genomics 27: 189-191,
1995.

6. Kizhatil, K.; Baker, S. A.; Arshavsky, V. Y.; Bennett, V.: Ankyrin-G
promotes cyclic nucleotide-gated channel transport to rod photoreceptor
sensory cilia. Science 323: 1614-1617, 2009.

7. Kordeli, E.; Bennett, V.: Distinct ankyrin isoforms at neuron
cell bodies and nodes of Ranvier resolved using erythrocyte ankyrin-deficient
mice. J. Cell Biol. 114: 1243-1259, 1991.

8. Kordeli, E.; Lambert, S.; Bennett, V.: Ankyrin-G: a new ankyrin
gene with neural-specific isoforms localized at the axonal initial
segment and node of Ranvier. J. Biol. Chem. 270: 2352-2359, 1995.

9. Mohler, P. J.; Rivolta, I.; Napolitano, C.; LeMaillet, G.; Lambert,
S.; Priori, S. G.; Bennett, V.: Na(v)1.5 E1053K mutation causing
Brugada syndrome blocks binding to ankyrin-G and expression of Na(v)1.5
on the surface of cardiomyocytes. Proc. Nat. Acad. Sci. 101: 17533-17538,
2004.

10. Sobotzik, J.-M.; Sie, J. M.; Politi, C.; Del Turco, D.; Bennett,
V.; Deller, T.; Schultz, C.: AnkyrinG is required to maintain axo-dendritic
polarity in vivo. Proc. Nat. Acad. Sci. 106: 17564-17569, 2009.

*FIELD* CN
Cassandra L. Kniffin - updated: 10/28/2013
Ada Hamosh - updated: 6/18/2009
Victor A. McKusick - updated: 1/27/2005
Patricia A. Hartz - updated: 1/6/2005

*FIELD* CD
Victor A. McKusick: 3/23/1995

*FIELD* ED
carol: 10/31/2013
ckniffin: 10/28/2013
alopez: 6/24/2009
terry: 6/18/2009
carol: 5/1/2009
carol: 2/26/2009
wwang: 2/10/2005
wwang: 2/8/2005
terry: 1/27/2005
mgross: 1/6/2005
dkim: 6/30/1998
mark: 6/2/1995
mark: 3/24/1995
mark: 3/23/1995

RBCC Red Blood Cell Collection

Full text data of ANK3