ANK2_MOUSE
ID ANK2_MOUSE Reviewed; 3898 AA.
AC Q8C8R3; Q3TM62; Q3V2X0; Q6PCN2; Q80ZZ7; Q8BNC1; Q8C445; Q8CCV0;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 2.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Ankyrin-2 {ECO:0000250|UniProtKB:Q01484};
DE Short=ANK-2;
DE AltName: Full=Ankyrin-B {ECO:0000303|PubMed:19007774, ECO:0000303|PubMed:21745462};
DE AltName: Full=Brain ankyrin {ECO:0000250|UniProtKB:Q01484, ECO:0000312|EMBL:AAH59251.1};
GN Name=Ank2 {ECO:0000312|MGI:MGI:88025};
GN Synonyms=AnkB {ECO:0000303|PubMed:27718357};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1] {ECO:0000305, ECO:0000312|EMBL:BAC32012.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3; 6; 7 AND 8), NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 1-1674 (ISOFORM 5), NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1-1190 (ISOFORM 2), AND NUCLEOTIDE SEQUENCE [LARGE
RP SCALE MRNA] OF 3402-3897 (ISOFORM 4).
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAC32012.1};
RC TISSUE=Cerebellum, Hippocampus {ECO:0000312|EMBL:BAC38764.1},
RC Lung {ECO:0000312|EMBL:BAE38580.1},
RC Medulla oblongata {ECO:0000312|EMBL:BAC27676.1},
RC Retina {ECO:0000312|EMBL:BAC32012.1}, and
RC Spinal ganglion {ECO:0000312|EMBL:BAE43385.1};
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3] {ECO:0000305, ECO:0000312|EMBL:AAH59251.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 2922-3898 (ISOFORM 4).
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:AAH59251.1};
RC TISSUE=Brain {ECO:0000312|EMBL:AAH59251.1};
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4] {ECO:0000305}
RP TISSUE SPECIFICITY.
RX PubMed=8253844; DOI=10.1083/jcb.123.6.1463;
RA Chan W., Kordeli E., Bennett V.;
RT "440-kD ankyrinB: structure of the major developmentally regulated domain
RT and selective localization in unmyelinated axons.";
RL J. Cell Biol. 123:1463-1473(1993).
RN [5]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP AND INTERACTION WITH ATP1A1; ATP1A2; SLC8A1 AND IP3 RECEPTOR.
RX PubMed=12571597; DOI=10.1038/nature01335;
RA Mohler P.J., Schott J.-J., Gramolini A.O., Dilly K.W., Guatimosim S.,
RA duBell W.H., Song L.-S., Haurogne K., Kyndt F., Ali M.E., Rogers T.B.,
RA Lederer W.J., Escande D., Le Marec H., Bennett V.;
RT "Ankyrin-B mutation causes type 4 long-QT cardiac arrhythmia and sudden
RT cardiac death.";
RL Nature 421:634-639(2003).
RN [6] {ECO:0000305}
RP FUNCTION, INTERACTION WITH SPTBN1, SUBCELLULAR LOCATION, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=15262991; DOI=10.1074/jbc.m406018200;
RA Mohler P.J., Yoon W., Bennett V.;
RT "Ankyrin-B targets beta2-spectrin to an intracellular compartment in
RT neonatal cardiomyocytes.";
RL J. Biol. Chem. 279:40185-40193(2004).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30 (ISOFORM 2), AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [8]
RP DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=17940615; DOI=10.1371/journal.pone.0001051;
RA Mohler P.J., Healy J.A., Xue H., Puca A.A., Kline C.F., Allingham R.R.,
RA Kranias E.G., Rockman H.A., Bennett V.;
RT "Ankyrin-B syndrome: enhanced cardiac function balanced by risk of cardiac
RT death and premature senescence.";
RL PLoS ONE 2:E1051-E1051(2007).
RN [9]
RP FUNCTION, INTERACTION WITH DMD AND DCTN4, AND SUBCELLULAR LOCATION.
RX PubMed=19109891; DOI=10.1016/j.cell.2008.10.018;
RA Ayalon G., Davis J.Q., Scotland P.B., Bennett V.;
RT "An ankyrin-based mechanism for functional organization of dystrophin and
RT dystroglycan.";
RL Cell 135:1189-1200(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-378; TYR-531 AND TYR-1349,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=18034455; DOI=10.1021/pr0701254;
RA Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT "Large-scale identification and evolution indexing of tyrosine
RT phosphorylation sites from murine brain.";
RL J. Proteome Res. 7:311-318(2008).
RN [11]
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP INTERACTION WITH NA/K ATPASE; NA/CA EXCHANGER AND SPTBN1.
RX PubMed=19007774; DOI=10.1016/j.exer.2008.09.022;
RA Kizhatil K., Sandhu N.K., Peachey N.S., Bennett V.;
RT "Ankyrin-B is required for coordinated expression of beta-2-spectrin, the
RT Na/K-ATPase and the Na/Ca exchanger in the inner segment of rod
RT photoreceptors.";
RL Exp. Eye Res. 88:57-64(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31; SER-34; SER-846; THR-853;
RP SER-874; SER-1426; SER-1428; SER-1440; SER-1467; SER-1562; SER-1699;
RP SER-1700; SER-1703; SER-1816; SER-1819; SER-1889; SER-2090; THR-2202;
RP SER-2206; THR-2232; SER-2238; THR-2333; SER-2364; SER-2399; SER-2413;
RP SER-2475; SER-2480; THR-2542; SER-2639; SER-2661; SER-2741; SER-2755;
RP SER-2913; SER-3032; THR-3035; SER-3226; SER-3229; SER-3230; SER-3343;
RP SER-3362; SER-3427; SER-3686; SER-3692; THR-3718; THR-3739; THR-3745;
RP THR-3756; THR-3759; SER-3764 AND SER-3850, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-590 (ISOFORM 3), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT
RP SER-44 (ISOFORM 7), AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Pancreas, Spleen,
RC and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [13]
RP TISSUE SPECIFICITY, AND IDENTIFICATION IN A COMPLEX WITH EZR; AHNAK; BFSP1;
RP BFSP2; PRX; PLEC; VIM AND SPECTRIN.
RX PubMed=21745462; DOI=10.1016/j.ydbio.2011.06.036;
RA Maddala R., Skiba N.P., Lalane R. III, Sherman D.L., Brophy P.J., Rao P.V.;
RT "Periaxin is required for hexagonal geometry and membrane organization of
RT mature lens fibers.";
RL Dev. Biol. 357:179-190(2011).
RN [14]
RP FUNCTION, INTERACTION WITH RABGAP1L, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND MUTAGENESIS OF 1318-ASP-ASP-1319; ARG-1194 AND GLU-3575.
RX PubMed=27718357; DOI=10.7554/elife.20417;
RA Qu F., Lorenzo D.N., King S.J., Brooks R., Bear J.E., Bennett V.;
RT "Ankyrin-B is a PI3P effector that promotes polarized alpha5beta1-integrin
RT recycling via recruiting RabGAP1L to early endosomes.";
RL Elife 5:0-0(2016).
CC -!- FUNCTION: Plays an essential role in the localization and membrane
CC stabilization of ion transporters and ion channels in several cell
CC types, including cardiomyocytes, as well as in striated muscle cells.
CC In skeletal muscle, required for proper localization of DMD and DCTN4
CC and for the formation and/or stability of a special subset of
CC microtubules associated with costameres and neuromuscular junctions
CC (PubMed:19109891). In cardiomyocytes, required for coordinate assembly
CC of Na/Ca exchanger, SLC8A1/NCX1, Na/K ATPases ATP1A1 and ATP1A2 and
CC inositol 1,4,5-trisphosphate (InsP3) receptors at sarcoplasmic
CC reticulum/sarcolemma sites (PubMed:12571597). Required for expression
CC and targeting of SPTBN1 in neonatal cardiomyocytes and for the
CC regulation of neonatal cardiomyocyte contraction rate
CC (PubMed:15262991). In the inner segment of rod photoreceptors, required
CC for the coordinated expression of the Na/K ATPase, Na/Ca exchanger and
CC beta-2-spectrin (SPTBN1) (PubMed:19007774). Plays a role in endocytosis
CC and intracellular protein transport. Associates with
CC phosphatidylinositol 3-phosphate (PI3P)-positive organelles and binds
CC dynactin to promote long-range motility of cells. Recruits RABGAP1L to
CC (PI3P)-positive early endosomes, where RABGAP1L inactivates RAB22A, and
CC promotes polarized trafficking to the leading edge of the migrating
CC cells. Part of the ANK2/RABGAP1L complex which is required for the
CC polarized recycling of fibronectin receptor ITGA5 ITGB1 to the plasma
CC membrane that enables continuous directional cell migration
CC (PubMed:27718357). {ECO:0000269|PubMed:12571597,
CC ECO:0000269|PubMed:15262991, ECO:0000269|PubMed:19007774,
CC ECO:0000269|PubMed:19109891, ECO:0000269|PubMed:27718357}.
CC -!- SUBUNIT: Interacts with RHBG (By similarity). Interacts with SPTBN1
CC (PubMed:15262991, PubMed:19007774). Colocalizes with Na/Ca exchanger
CC (PubMed:19007774). Interacts with Na/K ATPases ATP1A1 and ATP1A2
CC (PubMed:19007774, PubMed:12571597). Directly interacts with DMD; this
CC interaction is necessary for DMD localization at the sarcolemma.
CC Interacts with DCTN4; this interaction is required for DCTN4 retention
CC at costameres (PubMed:19109891). Identified in complexes that contain
CC VIM, EZR, AHNAK, BFSP1, BFSP2, ANK2, PLEC, PRX and spectrin
CC (PubMed:21745462). Interacts (via death domain) with RABGAP1L (via Rab-
CC GAP TBC domain) (PubMed:27718357). Interacts with SLC8A1/NCX1
CC (PubMed:12571597). May interact with inositol 1,4,5-trisphosphate
CC receptors (PubMed:12571597). {ECO:0000250|UniProtKB:Q01484,
CC ECO:0000269|PubMed:12571597, ECO:0000269|PubMed:15262991,
CC ECO:0000269|PubMed:19007774, ECO:0000269|PubMed:19109891,
CC ECO:0000269|PubMed:21745462, ECO:0000269|PubMed:27718357}.
CC -!- INTERACTION:
CC Q8C8R3; Q61743: Kcnj11; NbExp=2; IntAct=EBI-774322, EBI-8603527;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q01484}. Cytoplasm, myofibril, sarcomere, M line
CC {ECO:0000269|PubMed:12571597, ECO:0000269|PubMed:19109891}. Cell
CC membrane {ECO:0000269|PubMed:19007774}. Postsynaptic cell membrane
CC {ECO:0000269|PubMed:19109891}. Early endosome
CC {ECO:0000269|PubMed:27718357}. Recycling endosome
CC {ECO:0000269|PubMed:27718357}. Lysosome {ECO:0000269|PubMed:27718357}.
CC Mitochondrion {ECO:0000269|PubMed:27718357}. Cytoplasm, myofibril,
CC sarcomere, Z line {ECO:0000269|PubMed:12571597}. Cell membrane,
CC sarcolemma, T-tubule {ECO:0000269|PubMed:12571597}. Note=Expressed at
CC the apical membrane of airway lung epithelial cells. Localized to the
CC plasma membrane of the inner segments of photoreceptors in retina
CC (PubMed:19007774). Colocalizes with SPTBN1 in a distinct intracellular
CC compartment of neonatal cardiomyocytes (PubMed:15262991). In skeletal
CC muscle, localizes to neuromuscular junctions (PubMed:19109891).
CC Localizes with puncta at mitochondria ends. Colocalizes and
CC cotransports on motile vesicles with RABGAP1L (PubMed:27718357).
CC {ECO:0000269|PubMed:15262991, ECO:0000269|PubMed:19007774,
CC ECO:0000269|PubMed:19109891, ECO:0000269|PubMed:27718357}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=8;
CC Name=1;
CC IsoId=Q8C8R3-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:16141072};
CC IsoId=Q8C8R3-2; Sequence=VSP_053011, VSP_053023, VSP_053025;
CC Name=3 {ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:16141072};
CC IsoId=Q8C8R3-3; Sequence=VSP_053010, VSP_053027, VSP_053029;
CC Name=4 {ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:16141072};
CC IsoId=Q8C8R3-4; Sequence=VSP_053029;
CC Name=5 {ECO:0000269|PubMed:16141072};
CC IsoId=Q8C8R3-5; Sequence=VSP_053013, VSP_053021;
CC Name=6 {ECO:0000269|PubMed:16141072};
CC IsoId=Q8C8R3-6; Sequence=VSP_053012, VSP_053016, VSP_053019,
CC VSP_053020;
CC Name=7 {ECO:0000269|PubMed:16141072};
CC IsoId=Q8C8R3-7; Sequence=VSP_053014, VSP_053017, VSP_053018;
CC Name=8 {ECO:0000269|PubMed:16141072};
CC IsoId=Q8C8R3-8; Sequence=VSP_053015, VSP_053017, VSP_053018;
CC -!- TISSUE SPECIFICITY: Detected in eye lens fiber cells (at protein level)
CC (PubMed:21745462). In the retina, expressed in the inner segments of
CC rod photoreceptors (PubMed:19007774). Expressed in cardiomyocytes, as
CC well as in skeletal muscles (PubMed:17940615, PubMed:27718357,
CC PubMed:12571597). Also detected in brain and pancreas, as well as in
CC kidney and spleen (at protein level) (PubMed:8253844, PubMed:17940615,
CC PubMed:12571597). In the pancreas, highly expressed in islets,
CC predominantly in beta cells, but low expression, if any in acinar cells
CC (at protein level) (PubMed:17940615). In the central nervous system,
CC expressed in the corpus callosum and in cerebellar Purkinje neurons (at
CC protein level) (PubMed:17940615, PubMed:27718357). Expressed in lung
CC and, at low levels, in testes (at protein level) (PubMed:17940615).
CC {ECO:0000269|PubMed:12571597, ECO:0000269|PubMed:17940615,
CC ECO:0000269|PubMed:19007774, ECO:0000269|PubMed:21745462,
CC ECO:0000269|PubMed:27718357, ECO:0000269|PubMed:8253844}.
CC -!- DEVELOPMENTAL STAGE: Expressed in neonatal developing ventricular
CC cardiomyocytes as well as adult cardiomyocytes.
CC {ECO:0000269|PubMed:15262991}.
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 -!- PTM: Phosphorylated at multiple sites by different protein kinases and
CC each phosphorylation event regulates the protein's structure and
CC function. {ECO:0000250|UniProtKB:Q01484, ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Heterozygous knockout mice exhibit bradycardia
CC and show a high degree of heart-rate variability associated with
CC multiple episodes of abrupt sinus slowing and show episodes of
CC intermittent isorhythmic atrioventricular dissociation similar to
CC rhythm disturbances. Over half of the mutant animals die after exercise
CC combined with epinephrine (PubMed:12571597). Mutant animals display
CC premature senescence and reduced longevity (PubMed:17940615).
CC {ECO:0000269|PubMed:12571597, ECO:0000269|PubMed:17940615}.
CC -!- MISCELLANEOUS: [Isoform 2]: Incomplete sequence. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AK036018; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK032060; BAC27676.1; -; mRNA.
DR EMBL; AK036018; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK044634; BAC32012.1; -; mRNA.
DR EMBL; AK083111; BAC38764.1; -; mRNA.
DR EMBL; AK083826; BAE43385.1; -; mRNA.
DR EMBL; AK084070; BAC39111.1; -; mRNA.
DR EMBL; AK166115; BAE38580.1; -; mRNA.
DR EMBL; AC102480; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC102591; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC131744; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC043123; AAH43123.1; -; mRNA.
DR EMBL; BC059251; AAH59251.1; -; mRNA.
DR CCDS; CCDS38625.1; -. [Q8C8R3-3]
DR RefSeq; NP_001029340.1; NM_001034168.1.
DR RefSeq; NP_848770.2; NM_178655.3. [Q8C8R3-3]
DR SMR; Q8C8R3; -.
DR BioGRID; 224951; 14.
DR CORUM; Q8C8R3; -.
DR DIP; DIP-58645N; -.
DR IntAct; Q8C8R3; 26.
DR MINT; Q8C8R3; -.
DR STRING; 10090.ENSMUSP00000043765; -.
DR iPTMnet; Q8C8R3; -.
DR PhosphoSitePlus; Q8C8R3; -.
DR SwissPalm; Q8C8R3; -.
DR jPOST; Q8C8R3; -.
DR MaxQB; Q8C8R3; -.
DR PaxDb; Q8C8R3; -.
DR PeptideAtlas; Q8C8R3; -.
DR PRIDE; Q8C8R3; -.
DR ProteomicsDB; 296232; -. [Q8C8R3-1]
DR ProteomicsDB; 296233; -. [Q8C8R3-2]
DR ProteomicsDB; 296234; -. [Q8C8R3-3]
DR ProteomicsDB; 296235; -. [Q8C8R3-4]
DR ProteomicsDB; 296236; -. [Q8C8R3-5]
DR ProteomicsDB; 296237; -. [Q8C8R3-6]
DR ProteomicsDB; 296238; -. [Q8C8R3-7]
DR ProteomicsDB; 296239; -. [Q8C8R3-8]
DR ABCD; Q8C8R3; 3 sequenced antibodies.
DR Antibodypedia; 26481; 357 antibodies from 25 providers.
DR DNASU; 109676; -.
DR Ensembl; ENSMUST00000044443; ENSMUSP00000043765; ENSMUSG00000032826. [Q8C8R3-3]
DR Ensembl; ENSMUST00000182008; ENSMUSP00000138730; ENSMUSG00000032826. [Q8C8R3-6]
DR Ensembl; ENSMUST00000182994; ENSMUSP00000138089; ENSMUSG00000032826. [Q8C8R3-7]
DR GeneID; 109676; -.
DR KEGG; mmu:109676; -.
DR UCSC; uc008rgu.1; mouse. [Q8C8R3-3]
DR UCSC; uc008rgz.1; mouse. [Q8C8R3-7]
DR UCSC; uc012cxg.1; mouse. [Q8C8R3-6]
DR CTD; 287; -.
DR MGI; MGI:88025; Ank2.
DR VEuPathDB; HostDB:ENSMUSG00000032826; -.
DR eggNOG; KOG4177; Eukaryota.
DR GeneTree; ENSGT00940000155279; -.
DR HOGENOM; CLU_000134_30_0_1; -.
DR InParanoid; Q8C8R3; -.
DR OMA; YLNWGAD; -.
DR OrthoDB; 1011028at2759; -.
DR PhylomeDB; Q8C8R3; -.
DR TreeFam; TF351263; -.
DR BioGRID-ORCS; 109676; 3 hits in 42 CRISPR screens.
DR ChiTaRS; Ank2; mouse.
DR PRO; PR:Q8C8R3; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q8C8R3; protein.
DR Bgee; ENSMUSG00000032826; Expressed in dentate gyrus of hippocampal formation granule cell and 213 other tissues.
DR ExpressionAtlas; Q8C8R3; baseline and differential.
DR Genevisible; Q8C8R3; MM.
DR GO; GO:0031672; C:A band; IDA:BHF-UCL.
DR GO; GO:0016323; C:basolateral plasma membrane; ISO:MGI.
DR GO; GO:0043034; C:costamere; IDA:BHF-UCL.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0014704; C:intercalated disc; IDA:BHF-UCL.
DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR GO; GO:0031430; C:M band; IDA:BHF-UCL.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0033010; C:paranodal junction; IDA:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0014069; C:postsynaptic density; IDA:MGI.
DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0055037; C:recycling endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0042383; C:sarcolemma; IDA:BHF-UCL.
DR GO; GO:0030315; C:T-tubule; IDA:BHF-UCL.
DR GO; GO:0030018; C:Z disc; IDA:BHF-UCL.
DR GO; GO:0051117; F:ATPase binding; IPI:BHF-UCL.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0140031; F:phosphorylation-dependent protein binding; ISO:MGI.
DR GO; GO:0015459; F:potassium channel regulator activity; IMP:MGI.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IDA:BHF-UCL.
DR GO; GO:0030507; F:spectrin binding; ISO:MGI.
DR GO; GO:0044325; F:transmembrane transporter binding; IPI:BHF-UCL.
DR GO; GO:0086014; P:atrial cardiac muscle cell action potential; IMP:BHF-UCL.
DR GO; GO:0086066; P:atrial cardiac muscle cell to AV node cell communication; IMP:BHF-UCL.
DR GO; GO:0003283; P:atrial septum development; ISO:MGI.
DR GO; GO:0060048; P:cardiac muscle contraction; IMP:MGI.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; IMP:BHF-UCL.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR GO; GO:1901021; P:positive regulation of calcium ion transmembrane transporter activity; IMP:BHF-UCL.
DR GO; GO:0051928; P:positive regulation of calcium ion transport; IMP:BHF-UCL.
DR GO; GO:2001259; P:positive regulation of cation channel activity; IMP:BHF-UCL.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:BHF-UCL.
DR GO; GO:1901018; P:positive regulation of potassium ion transmembrane transporter activity; IMP:BHF-UCL.
DR GO; GO:0043268; P:positive regulation of potassium ion transport; IMP:BHF-UCL.
DR GO; GO:0008104; P:protein localization; IMP:BHF-UCL.
DR GO; GO:0034394; P:protein localization to cell surface; IMP:UniProtKB.
DR GO; GO:0070972; P:protein localization to endoplasmic reticulum; IMP:BHF-UCL.
DR GO; GO:0036309; P:protein localization to M-band; IMP:BHF-UCL.
DR GO; GO:0033365; P:protein localization to organelle; ISO:MGI.
DR GO; GO:0072659; P:protein localization to plasma membrane; IMP:BHF-UCL.
DR GO; GO:0036371; P:protein localization to T-tubule; IMP:BHF-UCL.
DR GO; GO:0050821; P:protein stabilization; IMP:BHF-UCL.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0098910; P:regulation of atrial cardiac muscle cell action potential; IMP:BHF-UCL.
DR GO; GO:0098904; P:regulation of AV node cell action potential; IMP:BHF-UCL.
DR GO; GO:1901019; P:regulation of calcium ion transmembrane transporter activity; IMP:BHF-UCL.
DR GO; GO:0051924; P:regulation of calcium ion transport; IMP:BHF-UCL.
DR GO; GO:0086004; P:regulation of cardiac muscle cell contraction; IMP:BHF-UCL.
DR GO; GO:0086036; P:regulation of cardiac muscle cell membrane potential; IMP:MGI.
DR GO; GO:0055117; P:regulation of cardiac muscle contraction; IMP:BHF-UCL.
DR GO; GO:0010882; P:regulation of cardiac muscle contraction by calcium ion signaling; IMP:BHF-UCL.
DR GO; GO:0010881; P:regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion; IMP:BHF-UCL.
DR GO; GO:2001257; P:regulation of cation channel activity; IMP:MGI.
DR GO; GO:0002027; P:regulation of heart rate; IMP:BHF-UCL.
DR GO; GO:0086091; P:regulation of heart rate by cardiac conduction; IMP:BHF-UCL.
DR GO; GO:0031647; P:regulation of protein stability; IC:BHF-UCL.
DR GO; GO:0051279; P:regulation of release of sequestered calcium ion into cytosol; ISO:MGI.
DR GO; GO:0098907; P:regulation of SA node cell action potential; IMP:BHF-UCL.
DR GO; GO:0060307; P:regulation of ventricular cardiac muscle cell membrane repolarization; ISO:MGI.
DR GO; GO:0086015; P:SA node cell action potential; IMP:BHF-UCL.
DR GO; GO:0086070; P:SA node cell to atrial cardiac muscle cell communication; IMP:BHF-UCL.
DR GO; GO:0033292; P:T-tubule organization; IMP:BHF-UCL.
DR GO; GO:0086005; P:ventricular cardiac muscle cell action potential; ISO:MGI.
DR Gene3D; 1.10.533.10; -; 1.
DR Gene3D; 1.25.40.20; -; 3.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR040745; Ankyrin_UPA.
DR InterPro; IPR011029; DEATH-like_dom_sf.
DR InterPro; IPR000488; Death_domain.
DR InterPro; IPR000906; ZU5_dom.
DR Pfam; PF00023; Ank; 1.
DR Pfam; PF12796; Ank_2; 7.
DR Pfam; PF13637; Ank_4; 2.
DR Pfam; PF00531; Death; 1.
DR Pfam; PF17809; UPA_2; 1.
DR Pfam; PF00791; ZU5; 2.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 23.
DR SMART; SM00005; DEATH; 1.
DR SMART; SM00218; ZU5; 1.
DR SUPFAM; SSF47986; SSF47986; 1.
DR SUPFAM; SSF48403; SSF48403; 3.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 20.
DR PROSITE; PS50017; DEATH_DOMAIN; 1.
DR PROSITE; PS51145; ZU5; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; ANK repeat; Cell membrane; Cytoplasm; Cytoskeleton;
KW Endocytosis; Endosome; Lysosome; Membrane; Mitochondrion; Phosphoprotein;
KW Postsynaptic cell membrane; Protein transport; Reference proteome; Repeat;
KW Synapse; Transport.
FT CHAIN 1..3898
FT /note="Ankyrin-2"
FT /id="PRO_0000364087"
FT REPEAT 30..62
FT /note="ANK 1"
FT REPEAT 63..92
FT /note="ANK 2"
FT REPEAT 96..125
FT /note="ANK 3"
FT REPEAT 129..158
FT /note="ANK 4"
FT REPEAT 162..191
FT /note="ANK 5"
FT REPEAT 193..220
FT /note="ANK 6"
FT REPEAT 232..261
FT /note="ANK 7"
FT REPEAT 265..294
FT /note="ANK 8"
FT REPEAT 298..327
FT /note="ANK 9"
FT REPEAT 331..360
FT /note="ANK 10"
FT REPEAT 364..393
FT /note="ANK 11"
FT REPEAT 397..426
FT /note="ANK 12"
FT REPEAT 430..459
FT /note="ANK 13"
FT REPEAT 463..492
FT /note="ANK 14"
FT REPEAT 496..525
FT /note="ANK 15"
FT REPEAT 529..558
FT /note="ANK 16"
FT REPEAT 562..591
FT /note="ANK 17"
FT REPEAT 595..624
FT /note="ANK 18"
FT REPEAT 628..657
FT /note="ANK 19"
FT REPEAT 661..690
FT /note="ANK 20"
FT REPEAT 694..723
FT /note="ANK 21"
FT REPEAT 727..756
FT /note="ANK 22"
FT REPEAT 760..789
FT /note="ANK 23"
FT REPEAT 793..822
FT /note="ANK 24"
FT DOMAIN 968..1123
FT /note="ZU5 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00485"
FT DOMAIN 1125..1271
FT /note="ZU5 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00485"
FT DOMAIN 1417..1502
FT /note="Death 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00064"
FT DOMAIN 3522..3606
FT /note="Death 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00064"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 966..1125
FT /note="Interaction with SPTBN1"
FT /evidence="ECO:0000250"
FT REGION 1256..1390
FT /note="UPA domain"
FT /evidence="ECO:0000250"
FT REGION 1425..1451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1589..2030
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2178..2296
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2319..2441
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2467..2829
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2932..2984
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3026..3063
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3088..3419
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3443..3464
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3643..3796
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3853..3875
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..31
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1435..1451
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1627..1657
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1677..1709
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1731..1769
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1772..1826
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1845..1863
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1966..2013
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2014..2030
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2178..2192
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2218..2244
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2245..2265
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2266..2286
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2319..2340
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2479..2517
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2524..2579
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2614..2638
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2654..2677
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2688..2709
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2721..2752
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2756..2791
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2794..2812
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2941..2955
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3028..3059
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3134..3152
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3157..3197
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3284..3298
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3306..3336
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3358..3387
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3396..3411
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3443..3457
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3643..3662
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3695..3716
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3749..3763
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 31
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 34
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 378
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18034455"
FT MOD_RES 531
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18034455"
FT MOD_RES 846
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 853
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 874
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1349
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18034455"
FT MOD_RES 1426
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1428
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1440
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1467
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1562
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1699
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1700
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1703
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1816
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1819
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1889
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 2090
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 2202
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 2206
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 2232
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 2238
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 2333
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 2364
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 2399
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 2413
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 2475
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 2480
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 2542
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 2639
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 2661
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 2741
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 2755
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 2913
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 3032
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 3035
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 3226
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 3229
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 3230
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 3343
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 3362
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 3427
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 3686
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 3692
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 3718
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 3739
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 3745
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 3756
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 3759
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 3764
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 3850
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..838
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_053010"
FT VAR_SEQ 1..28
FT /note="MMNEDAAQKSDSGEKFNGSSQRRKRPKK -> MASPTSPGPEGGACTPQNPP
FT RIRQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_053011"
FT VAR_SEQ 1..28
FT /note="MMNEDAAQKSDSGEKFNGSSQRRKRPKK -> MTTMLQKSQNKCESQTTCNE
FT VTQSSCIQRKDPNGVHPDDQ (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_053012"
FT VAR_SEQ 1..27
FT /note="MMNEDAAQKSDSGEKFNGSSQRRKRPK -> MTTMLQ (in isoform
FT 5)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_053013"
FT VAR_SEQ 1..27
FT /note="MMNEDAAQKSDSGEKFNGSSQRRKRPK -> MAHAAASIKKVREAELDEKEK
FT NLDRERKKQRKIPRDRMERKR (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_053014"
FT VAR_SEQ 1..27
FT /note="MMNEDAAQKSDSGEKFNGSSQRRKRPK -> MATMLQ (in isoform
FT 8)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_053015"
FT VAR_SEQ 224..231
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_053016"
FT VAR_SEQ 397..439
FT /note="NGFTPLHIACKKNRIKVMELLVKYGASIQAITESGLTPIHVAA -> VNLAQ
FT STFTQCSKTTLLGQRHLHQCKSMDLWLITAKLFPPLNH (in isoform 7 and
FT isoform 8)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_053017"
FT VAR_SEQ 440..3898
FT /note="Missing (in isoform 7 and isoform 8)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_053018"
FT VAR_SEQ 463..477
FT /note="RGETALHMAARAGQV -> MQPKWESMSLSAEPV (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_053019"
FT VAR_SEQ 478..3898
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_053020"
FT VAR_SEQ 597..629
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_053021"
FT VAR_SEQ 899..902
FT /note="LRSF -> TIP (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_053023"
FT VAR_SEQ 1042
FT /note="G -> GKLHLPTAPPPLNEGESLVSRILQLGPPGTKFLG (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_053025"
FT VAR_SEQ 1444..3514
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_053027"
FT VAR_SEQ 3894
FT /note="E -> EVTLSEPSVLSSTSQFQAEPVEGRRVSKVVKTTMVHGERMEKSLGDS
FT SLATDLPSAKDDFEE (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_053029"
FT MUTAGEN 1194
FT /note="R->A: Loss of binding to phosphatidylinositol 3-
FT phosphate (PI3P) lipids and loss of localization to PI3P-
FT positive organelles. Expression of mutant protein does not
FT rescue ITGB1 recycling deficit of ANK2 null mutant
FT fibroblasts."
FT /evidence="ECO:0000269|PubMed:27718357"
FT MUTAGEN 1318..1319
FT /note="DD->AA: Loss of long-range transport of PI3P-
FT positive organelles in embryonic fibroblasts. Expression of
FT mutant protein in ANK2 null mutant fibroblasts partially
FT rescues ITGB1 recycling to about 50% of the wild-type
FT levels."
FT /evidence="ECO:0000269|PubMed:27718357"
FT MUTAGEN 3575
FT /note="E->A: Significantly weaker interaction with
FT RABGAP1L."
FT /evidence="ECO:0000269|PubMed:27718357"
FT MUTAGEN 3575
FT /note="E->K: Loss of interaction with RABGAP1L. Localizes
FT on motile vesicles, but does not cotransport with RABGAP1L.
FT Loss of polarized transport of PI3P-positive organelles to
FT the leading edge of the migrating fibroblasts. Expression
FT of mutant protein does not rescue ITGB1 recycling deficit
FT of ANK2 null mutant fibroblasts nor the impaired
FT haptotactic response of the fibroblasts."
FT /evidence="ECO:0000269|PubMed:27718357"
FT CONFLICT 1026
FT /note="L -> Q (in Ref. 1; BAC27676)"
FT /evidence="ECO:0000305"
FT CONFLICT 1112
FT /note="R -> H (in Ref. 1; BAC27676)"
FT /evidence="ECO:0000305"
FT CONFLICT 3649
FT /note="E -> K (in Ref. 1; BAC27676)"
FT /evidence="ECO:0000305"
FT CONFLICT 3731
FT /note="A -> T (in Ref. 3; AAH43123)"
FT /evidence="ECO:0000305"
FT MOD_RES Q8C8R3-2:30
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16452087"
FT MOD_RES Q8C8R3-3:590
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT Q8C8R3-3:1014
FT /note="V -> A (in Ref. 1; BAC27676)"
FT /evidence="ECO:0000305"
FT MOD_RES Q8C8R3-7:44
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 3898 AA; 426261 MW; A779A20AA489DB34 CRC64;
MMNEDAAQKS DSGEKFNGSS QRRKRPKKSD SNASFLRAAR AGNLDKVVEY LKGGIDINTC
NQNGLNALHL AAKEGHVGLV QELLGRGSSV DSATKKGNTA LHIASLAGQA EVVKVLVKEG
ANINAQSQNG FTPLYMAAQE NHIDVVKYLL ENGANQSTAT EDGFTPLAVA LQQGHNQAVA
ILLENDTKGK VRLPALHIAA RKDDTKSAAL LLQNDHNADV QSKMMVNRTT ESGFTPLHIA
AHYGNVNVAT LLLNRGAAVD FTARNGITPL HVASKRGNTN MVKLLLDRGG QIDAKTRDGL
TPLHCAARSG HDQVVELLLE RKAPLLARTK NGLSPLHMAA QGDHVECVKH LLQYKAPVDD
VTLDYLTALH VAAHCGHYRV TKLLLDKRAN PNARALNGFT PLHIACKKNR IKVMELLVKY
GASIQAITES GLTPIHVAAF MGHLNIVLLL LQNGASPDVT NIRGETALHM AARAGQVEVV
RCLLRNGALV DARAREEQTP LHIASRLGKT EIVQLLLQHM AHPDAATTNG YTPLHISARE
GQVDVASVLL EAGAAHSLAT KKGFTPLHVA AKYGSLDVAK LLLQRRAAAD SAGKNGLTPL
HVAAHYDNQK VALLLLEKGA SPHATAKNGY TPLHIAAKKN QMQIASTLLN YGAETNTVTK
QGVTPLHLAS QEGHTDMVTL LLDKGANIHM STKSGLTSLH LAAQEDKVNV ADILTKHGAD
RDAYTKLGYT PLIVACHYGN VKMVNFLLKQ GANVNAKTKN GYTPLHQAAQ QGHTHIINVL
LQHGAKPNAT TANGNTALAI AKRLGYISVV DTLKVVTEEV TTTTTTITEK HKLNVPETMT
EVLDVSDEEG DDTVTGDGGE YLRPEDLKEL GDDSLPSSQF LDGMNYLRYS LEGGRSDSLR
SFSSDRSHTL SHASYLRDSA MIDDTVVIPS HQVSALAKEA ERNSYRLSWG TENLDNVALS
SSPIHSGFLV SFMVDARGGA MRGCRHNGLR IIIPPRKCTA PTRVTCRLVK RHRLATMPPM
VEGEGLASRL IEVGPSGAQF LGPVIVEIPH FAALRGKERE LVVLRSENGD SWKEHFCDYT
EDELNEILNG MDEVLDSPED LEKKRICRII TRDFPQYFAV VSRIKQDSNL IGPEGGVLSS
TVVSQVQAVF PEGALTKRIR VGLQAQPMHS ELVKKILGNK ATFSPIVTLE PRRRKFHKPI
TMTIPVPKAS SDVMLNGFGG DAPTLRLLCS ITGGTTPAQW EDITGTTPLT FVNECVSFTT
NVSARFWLID CRQIQESVAF ASQVYREIIC VPYMAKFVVF AKSHDPIEAR LRCFCMTDDK
VDKTLEQQEN FSEVARSRDV EVLEGKPIYV DCFGNLVPLT KSGQHHIFSF FAFKENRLPL
FVKVRDTTQE PCGRLSFMKE PKSTRGLVHQ AICNLNITLP IYAKESESDQ EPEEEIGMTS
EKNDETESTE TSVLKSHLVN EVPVLASPDL LSEVSEMKQD LIKMTAILTT DVSDKAGSLK
VKELAKAGEE EPGEPFEIVE RVKEDLEKVN AILRSGTCMR DEGRARSSQS ERELEEEWVI
VSDEEIQEAK QHAPVEIDEH PCIEVRVDRE TKAKVEKDST GLVNYLTDDL NSYTSPHEKK
PHTAPEKSGE TSQASAVGKS SESNKGKATS AEEKQSAQKQ LKPGLAIKKP VRRKLKEKQK
QKEESSQSSE EKTELKKGSS EESVDEDRGL VPEPLPTAKA TSPLIEETPI GSIKDKVKAL
QKRVEDEQKG RSKLPVRVKG KEDVPKRTTP RTHPAVSPSS KSSTSSKAER HSSLSSSAKP
ERHTPVSPSS KNEKLSPVSP SAKTERHSPV FSGKPEKHSP GSPSTKNERH SPVSSLKTER
HTPGSPSGKT DKRPPVPSSG RTEKHPPVSP GKTEKHLPGS PSIRTPEKPA PGSATGKHEK
HLPVSPGKTE KQPPISPTSK TERIEETMSV RELMKAFQSG QDPSKHKTGL FEHKSAKQKQ
PQDKSKSRVE KEKGHTVTQR EVTQRETQRI ESQTAKRGQR FQVSAATESR RFRSTTITVG
LRMEDPVRER FERTPIIKTP EVVPSVAAEE SHRGSEKIVD EQGDMDFQIS PDRKTSTDFS
EVIKQELEDN DKYQQFRLTE DTEKAQVHLD QVITSPFNTA FPLDYMKDEF LPALSLQSGA
LGGSSESLKQ EVIAGSPCSS LMEGTPQISS EESYKHEGLA ETPETSPESL SFSPKKSEEQ
IGEAKETTKV GTPTDIHSEK ELPITNDITD SSQKQGAGVT RGSEPSTEHS QKEVTQDPHK
DVCSKQDGCP ESQSVSLASE VFTEKGSCGE SQLPLVSSAF KTQSESETQE SLTPSEVTKP
FPPSDASVKT AEGTEPKPQG AIRSPQGLEL PLPNRDSEVL SPMADESLAV SHKDSLEASP
VLEDNSSHKT PDSLEPSPLK ESPCRDSLES SPVEPKMKAG ILPSHFPLPA AIAKTDLVAE
VASMRSRLLR DPDGSAEDDS LEQTSLMESS GKSPLSPDTP SSEEVSYEVT PKPSDSSTPK
PAVIHECAEE DDSENGEKKR FTPEEEMFKM VTKIKTFDEL EQEAKQKRDY KKEPRQDGSS
SASDPDADYS AEVNDEKQMA GTEGEGEVPV LVTSENRKVS SSSSESEPEL TQLSKGADSG
LLTEPVIRVQ PPSPLPSSID SNSSPEEATQ FQPIVPKQYT FKMNEEIQEE PATSEDKDCK
SHLAEDSQTH SADAADGSDG DLNRETTQPE TCDGHGCETV SPSNSATPVS LGVQSPEHKD
VDKPLAIDKD SLAHQDTCEN DREEREFDPS GVESTQADLP NESSSLSSRC AIPEGNESAK
EIASPSSPVK VEVTITDQAL ESMPEDCPIQ DSSTTMQTER FAMDVPVSEL AETDENSDPQ
IISPYENVPS SSFFSAEPSK IQTDTCHSTV VHSPEVYSVI IRSSPEDVVV TNSSNRTVSG
EESHCESHDL ETESEQKSAL WAAQSDAPPL AVAPTASDAA SVTGEQASKV IITKTDADAD
SWSEIREDDA AFEARVKEEE QKIFGLMVDR QSQGTTPDTT PARTPTEEGT PTSEQNPFLF
QEGKLFEMTR SGAIDMTKRP YADESLHFFQ IGQESNEEAI SEDLKEGATG AEPPQTETTS
ESLELSEPKE AMDDEGELLP DDVSEEIEDL PASDANIDSQ VIISASTETP TKEAVSTAVE
EPPTTQRSDS LSTVKQTPRP AVPGPVGQLD FSPVTRSVYS GQDDESPESS PEEQKSVIEI
PTAPVDNVPS AESKPQIPIR TLPTLVPAPP SAEDESAFSD DFPSSLDEDS KEGGAKPKSK
IPVKAPTQRT EWQPSPTDIP LQKTAVPQGQ ETLSRAPDGR SKSESDASSL DAKTKCPVKA
RSYIETETES RERAEGFESE SEDGATKPKL FASRLPVKSR STSSSGRPGT SPTRESREHF
FDLYRNSIEF FEEISDEASK LVDRLTQSER EQEPPSDDES SSALEVSVIE SLPPVDIEHS
APEDIFDTRP IWDESIETMI ERIPDENGHD RAEDPQDEQE RMEERLAYIA DHLGFSWTEL
ARELDFTEEQ IHQIRIENPN SLQDQSHALL KYWLERDGKH ATDTILIECL TKINRMDIVH
LLETNTEPLQ ERMGRSYAEI EQTITLDHSE GFSVLPDELC AAKEKKEQEA SKESESSDHP
PMVSEEDISV GYSTFQDCLP KTEGDSPAAA LSPQMHQEPV QQDFSGKTQD QQEYYVTTPG
AEVEDPQKAT AVPDSLCKTP EDISTPPEGT KPCLQTPVTS ERGSPIVQEP EEASEPKEES
SPRKTSLVIV ESTDDQSQVF ERLDGDAAFQ KGDDMPDIPP ETVTEEEYVD ENGHTVVKKV
TRKIIRRYVS SDGTEKEEVT MQGMPQEPVN IEDGDNYSKV IKRVVLKSDT QQSEDNNE
