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Ankyrin repeat domain-containing protein 2 (Skeletal muscle ankyrin repeat protein) (hArpp)

 ANKR2_HUMAN             Reviewed;         360 AA.
Q9GZV1; Q3B778; Q5T456; Q70EZ9; Q8WUD7; Q96MG0; Q9NQC9;
11-JUL-2002, integrated into UniProtKB/Swiss-Prot.
08-APR-2008, sequence version 3.
28-MAR-2018, entry version 149.
RecName: Full=Ankyrin repeat domain-containing protein 2;
AltName: Full=Skeletal muscle ankyrin repeat protein;
Short=hArpp;
Name=ANKRD2; Synonyms=ARPP;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE
[MRNA] OF 25-360 (ISOFORM 1), VARIANT THR-62, AND TISSUE SPECIFICITY.
TISSUE=Skeletal muscle;
PubMed=11444853; DOI=10.1006/bbrc.2001.5131;
Pallavicini A., Kojic S., Bean C., Vainzof M., Salamon M.,
Ievolella C., Bortoletto G., Pacchioni B., Zatz M., Lanfranchi G.,
Faulkner G., Valle G.;
"Characterization of human skeletal muscle Ankrd2.";
Biochem. Biophys. Res. Commun. 285:378-386(2001).
[2]
NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH TTN, AND VARIANT THR-62.
TISSUE=Heart;
PubMed=14583192; DOI=10.1016/j.jmb.2003.09.012;
Miller M.K., Bang M.-L., Witt C.C., Labeit D., Trombitas C.,
Watanabe K., Granzier H., McElhinny A.S., Gregorio C.C., Labeit S.;
"The muscle ankyrin repeat proteins: CARP, ankrd2/Arpp and DARP as a
family of titin filament-based stress response molecules.";
J. Mol. Biol. 333:951-964(2003).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
THR-62.
TISSUE=Skeletal muscle;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164054; DOI=10.1038/nature02462;
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J.,
Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 10.";
Nature 429:375-381(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 25-360 (ISOFORM 2).
TISSUE=Skeletal muscle;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 25-360 (ISOFORM 1), TISSUE SPECIFICITY,
AND VARIANT THR-62.
PubMed=11453652; DOI=10.1006/bbrc.2001.5216;
Moriyama M., Tsukamoto Y., Fujiwara M., Kondo G., Nakada C., Baba T.,
Ishiguro N., Miyazaki A., Nakamura K., Hori N., Sato K., Shomori K.,
Takeuchi K., Satoh H., Mori S., Ito H.;
"Identification of a novel human ankyrin-repeated protein homologous
to CARP.";
Biochem. Biophys. Res. Commun. 285:715-723(2001).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 49-150.
TISSUE=Skeletal muscle;
PubMed=10873377; DOI=10.1006/geno.2000.6213;
Kemp T.J., Sadusky T.J., Saltisi F., Carey N., Moss J., Yang S.Y.,
Sassoon D.A., Goldspink G., Coulton G.R.;
"Identification of Ankrd2, a novel skeletal muscle gene coding for a
stretch-responsive ankyrin-repeat protein.";
Genomics 66:229-241(2000).
[8]
INTERACTION WITH PML; TCAP; TP53/P53 AND YBX1, AND SUBCELLULAR
LOCATION.
PubMed=15136035; DOI=10.1016/j.jmb.2004.03.071;
Kojic S., Medeot E., Guccione E., Krmac H., Zara I., Martinelli V.,
Valle G., Faulkner G.;
"The Ankrd2 protein, a link between the sarcomere and the nucleus in
skeletal muscle.";
J. Mol. Biol. 339:313-325(2004).
[9]
FUNCTION, PHOSPHORYLATION AT SER-99 BY PKB/AKT2, MUTAGENESIS OF
SER-99, INTERACTION WITH AKT2, AND SUBCELLULAR LOCATION.
PubMed=21737686; DOI=10.1091/mbc.E10-11-0928;
Cenni V., Bavelloni A., Beretti F., Tagliavini F., Manzoli L.,
Lattanzi G., Maraldi N.M., Cocco L., Marmiroli S.;
"Ankrd2/ARPP is a novel Akt2 specific substrate and regulates myogenic
differentiation upon cellular exposure to H(2)O(2).";
Mol. Biol. Cell 22:2946-2956(2011).
[10]
FUNCTION, AND INTERACTION WITH TJP1.
PubMed=22016770; DOI=10.1371/journal.pone.0025519;
Belgrano A., Rakicevic L., Mittempergher L., Campanaro S.,
Martinelli V.C., Mouly V., Valle G., Kojic S., Faulkner G.;
"Multi-tasking role of the mechanosensing protein Ankrd2 in the
signaling network of striated muscle.";
PLoS ONE 6:E25519-E25519(2011).
-!- FUNCTION: Functions as a negative regulator of myocyte
differentiation. May interact with both sarcoplasmic structural
proteins and nuclear proteins to regulate gene expression during
muscle development and in response to muscle stress.
{ECO:0000269|PubMed:21737686, ECO:0000269|PubMed:22016770}.
-!- SUBUNIT: Interacts with ID3; both proteins cooperate in myoblast
differentiation (By similarity). Interacts with TTN/titin.
Interacts (via ANK repeats) with TCAP; the interaction is direct.
Interacts with TJP1 (via PDZ domains). Interacts with PML; the
interaction is direct. Interacts with p53/TP53. Interacts with
YBX1. Interacts with AKT2. {ECO:0000250,
ECO:0000269|PubMed:14583192, ECO:0000269|PubMed:15136035,
ECO:0000269|PubMed:21737686, ECO:0000269|PubMed:22016770}.
-!- SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere, I band
{ECO:0000250}. Cytoplasm, cytosol. Nucleus. Nucleus, PML body.
Note=In the sarcoplasm of differentiated striated muscle cells,
where it is cytosolic and enriched in the I band. In nucleus and
PML bodies of proliferating and undifferentiated myoblasts.
Associates with the euchromatin in the nucleus of myocytes upon
muscle stress.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9GZV1-1; Sequence=Displayed;
Name=2;
IsoId=Q9GZV1-2; Sequence=VSP_000269;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Mostly expressed in skeletal and cardiac
muscles. Found in slow fibers. Also expressed in kidney, but to a
lower extent (at protein level). {ECO:0000269|PubMed:11444853,
ECO:0000269|PubMed:11453652}.
-!- PTM: Phosphorylation at Ser-99 by PKB/AKT2 in response to
oxidative stress induces translocation to the nucleus and
negatively regulates myoblast differentiation.
{ECO:0000269|PubMed:21737686}.
-!- SEQUENCE CAUTION:
Sequence=AK056990; Type=Erroneous termination; Positions=210; Note=Translated as Gln.; Evidence={ECO:0000305};
Sequence=BAB60958.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=CAC19411.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=CAC19412.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=CAE47432.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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EMBL; AJ304804; CAC19411.1; ALT_INIT; Genomic_DNA.
EMBL; AJ304805; CAC19412.1; ALT_INIT; mRNA.
EMBL; AJ583444; CAE47432.1; ALT_INIT; mRNA.
EMBL; AK056990; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; AL355315; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL359388; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC020817; AAH20817.2; -; mRNA.
EMBL; BC107759; AAI07760.1; -; mRNA.
EMBL; AB058599; BAB60958.1; ALT_INIT; mRNA.
EMBL; AJ249975; CAB99416.1; -; mRNA.
CCDS; CCDS44468.1; -. [Q9GZV1-2]
CCDS; CCDS7466.1; -. [Q9GZV1-1]
PIR; JC7713; JC7713.
RefSeq; NP_001123453.1; NM_001129981.2. [Q9GZV1-2]
RefSeq; NP_001278147.1; NM_001291218.1.
RefSeq; NP_001278148.2; NM_001291219.2.
RefSeq; NP_001333726.1; NM_001346797.1.
RefSeq; NP_065082.2; NM_020349.3. [Q9GZV1-1]
UniGene; Hs.73708; -.
ProteinModelPortal; Q9GZV1; -.
SMR; Q9GZV1; -.
BioGrid; 117669; 9.
IntAct; Q9GZV1; 1.
STRING; 9606.ENSP00000306163; -.
iPTMnet; Q9GZV1; -.
PhosphoSitePlus; Q9GZV1; -.
BioMuta; ANKRD2; -.
DMDM; 182676433; -.
MaxQB; Q9GZV1; -.
PaxDb; Q9GZV1; -.
PeptideAtlas; Q9GZV1; -.
PRIDE; Q9GZV1; -.
Ensembl; ENST00000298808; ENSP00000298808; ENSG00000165887. [Q9GZV1-2]
Ensembl; ENST00000307518; ENSP00000306163; ENSG00000165887. [Q9GZV1-1]
GeneID; 26287; -.
KEGG; hsa:26287; -.
UCSC; uc001knw.5; human. [Q9GZV1-1]
CTD; 26287; -.
DisGeNET; 26287; -.
EuPathDB; HostDB:ENSG00000165887.11; -.
GeneCards; ANKRD2; -.
HGNC; HGNC:495; ANKRD2.
HPA; HPA040842; -.
HPA; HPA040884; -.
MIM; 610734; gene.
neXtProt; NX_Q9GZV1; -.
OpenTargets; ENSG00000165887; -.
PharmGKB; PA24804; -.
eggNOG; KOG0504; Eukaryota.
eggNOG; COG0666; LUCA.
GeneTree; ENSGT00910000144039; -.
HOVERGEN; HBG071561; -.
InParanoid; Q9GZV1; -.
KO; K21434; -.
OMA; DTCDQFR; -.
OrthoDB; EOG091G0DCN; -.
PhylomeDB; Q9GZV1; -.
TreeFam; TF331650; -.
SIGNOR; Q9GZV1; -.
GeneWiki; ANKRD2; -.
GenomeRNAi; 26287; -.
PRO; PR:Q9GZV1; -.
Proteomes; UP000005640; Chromosome 10.
Bgee; ENSG00000165887; -.
CleanEx; HS_ANKRD2; -.
ExpressionAtlas; Q9GZV1; baseline and differential.
Genevisible; Q9GZV1; HS.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0000791; C:euchromatin; ISS:UniProtKB.
GO; GO:0031674; C:I band; IBA:GO_Central.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0016605; C:PML body; IEA:UniProtKB-SubCell.
GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
GO; GO:0043422; F:protein kinase B binding; IPI:UniProtKB.
GO; GO:0061629; F:RNA polymerase II sequence-specific DNA binding transcription factor binding; IDA:MGI.
GO; GO:0008307; F:structural constituent of muscle; NAS:UniProtKB.
GO; GO:0031432; F:titin binding; IBA:GO_Central.
GO; GO:0003712; F:transcription cofactor activity; IBA:GO_Central.
GO; GO:0006936; P:muscle contraction; NAS:UniProtKB.
GO; GO:0007517; P:muscle organ development; NAS:UniProtKB.
GO; GO:0045662; P:negative regulation of myoblast differentiation; IMP:UniProtKB.
GO; GO:0010832; P:negative regulation of myotube differentiation; IEA:Ensembl.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IGI:MGI.
GO; GO:0001817; P:regulation of cytokine production; IEA:Ensembl.
GO; GO:1902253; P:regulation of intrinsic apoptotic signaling pathway by p53 class mediator; IEA:Ensembl.
GO; GO:2000291; P:regulation of myoblast proliferation; IEA:Ensembl.
GO; GO:0043619; P:regulation of transcription from RNA polymerase II promoter in response to oxidative stress; IDA:MGI.
GO; GO:0035914; P:skeletal muscle cell differentiation; IBA:GO_Central.
CDD; cd00204; ANK; 1.
Gene3D; 1.25.40.20; -; 2.
InterPro; IPR002110; Ankyrin_rpt.
InterPro; IPR020683; Ankyrin_rpt-contain_dom.
InterPro; IPR036770; Ankyrin_rpt-contain_sf.
Pfam; PF12796; Ank_2; 2.
PRINTS; PR01415; ANKYRIN.
SMART; SM00248; ANK; 5.
SUPFAM; SSF48403; SSF48403; 1.
PROSITE; PS50297; ANK_REP_REGION; 1.
PROSITE; PS50088; ANK_REPEAT; 4.
1: Evidence at protein level;
Alternative splicing; ANK repeat; Complete proteome; Cytoplasm;
Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repeat.
CHAIN 1 360 Ankyrin repeat domain-containing protein
2.
/FTId=PRO_0000066897.
REPEAT 147 176 ANK 1.
REPEAT 180 209 ANK 2.
REPEAT 213 242 ANK 3.
REPEAT 246 275 ANK 4.
REPEAT 279 308 ANK 5.
REGION 5 120 May mediate interaction with PML,
p53/TP53 and YBX1.
{ECO:0000269|PubMed:15136035}.
MOD_RES 99 99 Phosphoserine; by PKB/AKT2.
{ECO:0000269|PubMed:21737686}.
VAR_SEQ 246 278 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_000269.
VARIANT 62 62 A -> T (in dbSNP:rs7094973).
{ECO:0000269|PubMed:11444853,
ECO:0000269|PubMed:11453652,
ECO:0000269|PubMed:14583192,
ECO:0000269|PubMed:14702039}.
/FTId=VAR_042498.
MUTAGEN 99 99 S->A: Loss of interaction and
phosphorylation by PKB/AKT2, loss of
translocation to the nucleus and loss of
function in myocyte differentiation.
{ECO:0000269|PubMed:21737686}.
CONFLICT 49 49 L -> S (in Ref. 7; CAB99416).
{ECO:0000305}.
SEQUENCE 360 AA; 39859 MW; E88FC3FA242D0739 CRC64;
MAKAPSWAGV GALAYKAPEA LWPAEAVMDG TMEDSEAVQR ATALIEQRLA QEEENEKLRG
DARQKLPMDL LVLEDEKHHG AQSAALQKVK GQERVRKTSL DLRREIIDVG GIQNLIELRK
KRKQKKRDAL AASHEPPPEP EEITGPVDEE TFLKAAVEGK MKVIEKFLAD GGSADTCDQF
RRTALHRASL EGHMEILEKL LDNGATVDFQ DRLDCTAMHW ACRGGHLEVV KLLQSHGADT
NVRDKLLSTP LHVAVRTGQV EIVEHFLSLG LEINARDREG DTALHDAVRL NRYKIIKLLL
LHGADMMTKN LAGKTPTDLV QLWQADTRHA LEHPEPGAEH NGLEGPNDSG RETPQPVPAQ


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