ANKR2_MOUSE
ID ANKR2_MOUSE Reviewed; 328 AA.
AC Q9WV06; B2RS77; Q8QZX4;
DT 11-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT 22-JAN-2014, sequence version 3.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Ankyrin repeat domain-containing protein 2;
DE AltName: Full=Skeletal muscle ankyrin repeat protein;
DE Short=mArpp;
GN Name=Ankrd2; Synonyms=Arpp;
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]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL
RP STAGE, AND INDUCTION BY MECHANICAL STRETCH.
RC STRAIN=129/Sv, and C57BL/10; TISSUE=Skeletal muscle, and Spleen;
RX PubMed=10873377; DOI=10.1006/geno.2000.6213;
RA Kemp T.J., Sadusky T.J., Saltisi F., Carey N., Moss J., Yang S.Y.,
RA Sassoon D.A., Goldspink G., Coulton G.R.;
RT "Identification of Ankrd2, a novel skeletal muscle gene coding for a
RT stretch-responsive ankyrin-repeat protein.";
RL Genomics 66:229-241(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Diaphragm;
RX PubMed=11444853; DOI=10.1006/bbrc.2001.5131;
RA Pallavicini A., Kojic S., Bean C., Vainzof M., Salamon M., Ievolella C.,
RA Bortoletto G., Pacchioni B., Zatz M., Lanfranchi G., Faulkner G., Valle G.;
RT "Characterization of human skeletal muscle Ankrd2.";
RL Biochem. Biophys. Res. Commun. 285:378-386(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC STRAIN=129/SvJ, and C57BL/6J; TISSUE=Skeletal muscle;
RX PubMed=12004005; DOI=10.1038/labinvest.3780459;
RA Tsukamoto Y., Senda T., Nakano T., Nakada C., Hida T., Ishiguro N.,
RA Kondo G., Baba T., Sato K., Osaki M., Mori S., Ito H., Moriyama M.;
RT "Arpp, a new homolog of carp, is preferentially expressed in type 1
RT skeletal muscle fibers and is markedly induced by denervation.";
RL Lab. Invest. 82:645-655(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Head;
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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 [8]
RP SUBCELLULAR LOCATION.
RX PubMed=18302940; DOI=10.1016/j.bbamcr.2008.01.027;
RA Bean C., Facchinello N., Faulkner G., Lanfranchi G.;
RT "The effects of Ankrd2 alteration indicate its involvement in cell cycle
RT regulation during muscle differentiation.";
RL Biochim. Biophys. Acta 1783:1023-1035(2008).
RN [9]
RP SUBCELLULAR LOCATION.
RX PubMed=17926058; DOI=10.1007/s00418-007-0348-9;
RA Tsukamoto Y., Hijiya N., Yano S., Yokoyama S., Nakada C., Uchida T.,
RA Matsuura K., Moriyama M.;
RT "Arpp/Ankrd2, a member of the muscle ankyrin repeat proteins (MARPs),
RT translocates from the I-band to the nucleus after muscle injury.";
RL Histochem. Cell Biol. 129:55-64(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue;
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 [11]
RP FUNCTION, PHOSPHORYLATION AT SER-68 BY PKB/AKT2, INTERACTION WITH AKT2, AND
RP SUBCELLULAR LOCATION.
RX PubMed=21737686; DOI=10.1091/mbc.e10-11-0928;
RA Cenni V., Bavelloni A., Beretti F., Tagliavini F., Manzoli L., Lattanzi G.,
RA Maraldi N.M., Cocco L., Marmiroli S.;
RT "Ankrd2/ARPP is a novel Akt2 specific substrate and regulates myogenic
RT differentiation upon cellular exposure to H(2)O(2).";
RL Mol. Biol. Cell 22:2946-2956(2011).
RN [12]
RP FUNCTION IN MYOBLAST DIFFERENTIATION, AND INTERACTION WITH ID3.
RX PubMed=23824195; DOI=10.1074/jbc.m112.434423;
RA Mohamed J.S., Lopez M.A., Cox G.A., Boriek A.M.;
RT "Ankyrin repeat domain protein 2 and inhibitor of DNA binding 3
RT cooperatively inhibit myoblast differentiation by physical interaction.";
RL J. Biol. Chem. 288:24560-24568(2013).
CC -!- FUNCTION: Functions as a negative regulator of myocyte differentiation.
CC May interact with both sarcoplasmic structural proteins and nuclear
CC proteins to regulate gene expression during muscle development and in
CC response to muscle stress. {ECO:0000269|PubMed:21737686,
CC ECO:0000269|PubMed:23824195}.
CC -!- SUBUNIT: Interacts with ID3; both proteins cooperate in myoblast
CC differentiation. Interacts with TTN/titin (By similarity). Interacts
CC (via ANK repeats) with TCAP; the interaction is direct (By similarity).
CC Interacts with TJP1 (via PDZ domains) (By similarity). Interacts with
CC PML; the interaction is direct (By similarity). Interacts with p53/TP53
CC (By similarity). Interacts with YBX1 (By similarity). Interacts with
CC AKT2. {ECO:0000250, ECO:0000269|PubMed:21737686,
CC ECO:0000269|PubMed:23824195}.
CC -!- INTERACTION:
CC Q9WV06; P41133: Id3; NbExp=4; IntAct=EBI-8854438, EBI-309448;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere, I band.
CC Cytoplasm, cytosol. Nucleus. Nucleus, PML body {ECO:0000250}. Note=In
CC the sarcoplasm of differentiated striated muscle cells, where it is
CC cytosolic and enriched in the I band. In nucleus and PML bodies of
CC proliferating and undifferentiated myoblasts. Associates with the
CC euchromatin in the nucleus of myocytes upon muscle stress.
CC -!- TISSUE SPECIFICITY: Expressed by myoblasts (at protein level).
CC Expressed in skeletal and cardiac muscles.
CC {ECO:0000269|PubMed:10873377}.
CC -!- DEVELOPMENTAL STAGE: Expressed at 9.5 dpc, with a pattern of expression
CC that shows restricted localization to the myotome of somites. By 13.5
CC dpc, expression is observed within intercostal and back muscles. At
CC 14.5 dpc and 15.5 dpc, expression is observed in tail myotomal muscles,
CC and in intervertebral and back muscles. Hybridization was also detected
CC within limb muscles. This pattern of expression was maintained at least
CC up until 17.5 dpc. No localization within the heart.
CC {ECO:0000269|PubMed:10873377}.
CC -!- INDUCTION: Up-regulated in response to mechanical stretch of skeletal
CC muscle (hypertrophy mechanically-induced).
CC {ECO:0000269|PubMed:10873377}.
CC -!- PTM: Phosphorylation at Ser-68 by PKB/AKT2 in response to oxidative
CC stress induces translocation to the nucleus and negatively regulates
CC myoblast differentiation. {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB88557.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB88558.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAE21246.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AJ249346; CAB99432.1; -; Genomic_DNA.
DR EMBL; AJ245514; CAB99431.1; -; mRNA.
DR EMBL; AJ011118; CAB46646.1; -; mRNA.
DR EMBL; AB076256; BAB88557.1; ALT_INIT; mRNA.
DR EMBL; AB076257; BAB88558.1; ALT_INIT; Genomic_DNA.
DR EMBL; AK132585; BAE21246.1; ALT_INIT; mRNA.
DR EMBL; AC133503; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466534; EDL41876.1; -; Genomic_DNA.
DR EMBL; BC138760; AAI38761.1; -; mRNA.
DR EMBL; BC138761; AAI38762.1; -; mRNA.
DR RefSeq; NP_064417.1; NM_020033.1.
DR AlphaFoldDB; Q9WV06; -.
DR SMR; Q9WV06; -.
DR BioGRID; 208117; 2.
DR IntAct; Q9WV06; 1.
DR STRING; 10090.ENSMUSP00000026172; -.
DR iPTMnet; Q9WV06; -.
DR PhosphoSitePlus; Q9WV06; -.
DR MaxQB; Q9WV06; -.
DR PaxDb; Q9WV06; -.
DR PRIDE; Q9WV06; -.
DR ProteomicsDB; 296043; -.
DR Antibodypedia; 30973; 91 antibodies from 22 providers.
DR DNASU; 56642; -.
DR Ensembl; ENSMUST00000026172; ENSMUSP00000026172; ENSMUSG00000025172.
DR GeneID; 56642; -.
DR KEGG; mmu:56642; -.
DR UCSC; uc008hna.1; mouse.
DR CTD; 26287; -.
DR MGI; MGI:1861447; Ankrd2.
DR VEuPathDB; HostDB:ENSMUSG00000025172; -.
DR eggNOG; KOG0504; Eukaryota.
DR GeneTree; ENSGT00940000153956; -.
DR HOGENOM; CLU_000134_11_0_1; -.
DR InParanoid; Q9WV06; -.
DR OrthoDB; 1514637at2759; -.
DR PhylomeDB; Q9WV06; -.
DR TreeFam; TF331650; -.
DR BioGRID-ORCS; 56642; 3 hits in 71 CRISPR screens.
DR ChiTaRS; Ankrd2; mouse.
DR PRO; PR:Q9WV06; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q9WV06; protein.
DR Bgee; ENSMUSG00000025172; Expressed in soleus muscle and 77 other tissues.
DR ExpressionAtlas; Q9WV06; baseline and differential.
DR Genevisible; Q9WV06; MM.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0000791; C:euchromatin; IDA:UniProtKB.
DR GO; GO:0031674; C:I band; IDA:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0030016; C:myofibril; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0016605; C:PML body; IDA:MGI.
DR GO; GO:0030017; C:sarcomere; IDA:MGI.
DR GO; GO:0016528; C:sarcoplasm; IDA:MGI.
DR GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR GO; GO:0043422; F:protein kinase B binding; IPI:UniProtKB.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; ISO:MGI.
DR GO; GO:0031432; F:titin binding; IPI:UniProtKB.
DR GO; GO:0014902; P:myotube differentiation; IDA:MGI.
DR GO; GO:0045662; P:negative regulation of myoblast differentiation; IMP:UniProtKB.
DR GO; GO:0010832; P:negative regulation of myotube differentiation; IDA:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0001817; P:regulation of cytokine production; IMP:MGI.
DR GO; GO:1902253; P:regulation of intrinsic apoptotic signaling pathway by p53 class mediator; IDA:MGI.
DR GO; GO:2000291; P:regulation of myoblast proliferation; IDA:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0043619; P:regulation of transcription from RNA polymerase II promoter in response to oxidative stress; ISO:MGI.
DR GO; GO:0035994; P:response to muscle stretch; TAS:MGI.
DR GO; GO:0035914; P:skeletal muscle cell differentiation; IMP:MGI.
DR Gene3D; 1.25.40.20; -; 2.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR Pfam; PF12796; Ank_2; 2.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 4.
DR SUPFAM; SSF48403; SSF48403; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 4.
PE 1: Evidence at protein level;
KW ANK repeat; Cytoplasm; Nucleus; Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..328
FT /note="Ankyrin repeat domain-containing protein 2"
FT /id="PRO_0000066898"
FT REPEAT 116..145
FT /note="ANK 1"
FT REPEAT 149..178
FT /note="ANK 2"
FT REPEAT 182..211
FT /note="ANK 3"
FT REPEAT 215..244
FT /note="ANK 4"
FT REPEAT 248..277
FT /note="ANK 5"
FT REGION 96..116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 297..328
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 36
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 68
FT /note="Phosphoserine; by PKB/AKT2"
FT /evidence="ECO:0000269|PubMed:21737686"
SQ SEQUENCE 328 AA; 36707 MW; DB90D955EE9D175E CRC64;
MEGPEAVQRA TELIEQRLAQ EEETEKLRRS APGKLSMDML VLEEEKRLGV QSPALQKVKG
QERVRKTSLD LRREIIDVGG IQNLIELRKK RKQKKRDALA AAQEPPPEPE EITGPVNEET
FLKAAVEGKM KVIDKYLADG GSADTCDEFR RTALHRASLE GHMEILEKLL ENGATVDFQD
RLDCTAMHWA CRGGHLEVVR LLQSRGADTN VRDKLLSTPL HVAVRTGHVE IVEHFLSLGL
DINAKDREGD SALHDAVRLN RYKIIKLLLL HGADMMAKNL AGKTPTDLVQ LWQADTRHAL
EHPEPESEQN GLERPGSGRE TPQPIPAQ
