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ANKR1_MOUSE
ID   ANKR1_MOUSE             Reviewed;         319 AA.
AC   Q9CR42; O55014; Q3UIF7; Q3UJ39; Q792Q9;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 161.
DE   RecName: Full=Ankyrin repeat domain-containing protein 1;
DE   AltName: Full=Cardiac ankyrin repeat protein;
GN   Name=Ankrd1; Synonyms=Carp;
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 [MRNA], DEVELOPMENTAL STAGE, TISSUE SPECIFICITY, AND
RP   FUNCTION.
RC   TISSUE=Heart;
RX   PubMed=9043061; DOI=10.1242/dev.124.4.793;
RA   Zou Y., Evans S., Chen J., Kuo H.-C., Harvey R.P., Chien K.R.;
RT   "CARP, a cardiac ankyrin repeat protein, is downstream in the Nkx2-5
RT   homeobox gene pathway.";
RL   Development 124:793-804(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Heart;
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
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]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 103-176.
RA   Schoenfeld J.R., Lowe D.G., Zou Y., Chen J.;
RL   Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   DEVELOPMENTAL STAGE.
RX   PubMed=9278441; DOI=10.1074/jbc.272.36.22800;
RA   Jeyaseelan R., Poizat C., Baker R.K., Abdishoo S., Isterabadi L.B.,
RA   Lyons G.E., Kedes L.;
RT   "A novel cardiac-restricted target for doxorubicin. CARP, a nuclear
RT   modulator of gene expression in cardiac progenitor cells and
RT   cardiomyocytes.";
RL   J. Biol. Chem. 272:22800-22808(1997).
CC   -!- FUNCTION: May play an important role in endothelial cell activation.
CC       May act as a nuclear transcription factor that negatively regulates the
CC       expression of cardiac genes. {ECO:0000269|PubMed:9043061}.
CC   -!- SUBUNIT: Interacts with TTN/titin and YBX1. {ECO:0000250}.
CC   -!- INTERACTION:
CC       Q9CR42; P09405: Ncl; NbExp=5; IntAct=EBI-8308696, EBI-641864;
CC       Q9CR42; P19338: NCL; Xeno; NbExp=2; IntAct=EBI-8308696, EBI-346967;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed in heart, cardiac muscle.
CC       {ECO:0000269|PubMed:9043061}.
CC   -!- DEVELOPMENTAL STAGE: Expression was first clearly detected as early as
CC       8.5 dpc specifically in heart and is regulated temporally and spatially
CC       in the myocardium. Transcripts are present in uniformly high levels in
CC       the myocardium. Throughout cardiac development, expression is specific
CC       for the myocardium; endocardial cushions and valves exhibit only
CC       background levels of signal. Transcript levels persist but gradually
CC       decrease in neonatal, 2-week-old, and adult hearts.
CC       {ECO:0000269|PubMed:9043061, ECO:0000269|PubMed:9278441}.
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DR   EMBL; AF041847; AAC03533.1; -; mRNA.
DR   EMBL; AK009655; BAB26419.1; -; mRNA.
DR   EMBL; AK009959; BAB26611.1; -; mRNA.
DR   EMBL; AK145944; BAE26773.1; -; mRNA.
DR   EMBL; AK146471; BAE27197.1; -; mRNA.
DR   EMBL; AK146627; BAE27316.1; -; mRNA.
DR   EMBL; AK146940; BAE27549.1; -; mRNA.
DR   EMBL; BC037138; AAH37138.1; -; mRNA.
DR   EMBL; AF041849; AAB97080.1; -; mRNA.
DR   CCDS; CCDS29771.1; -.
DR   RefSeq; NP_038496.2; NM_013468.3.
DR   AlphaFoldDB; Q9CR42; -.
DR   SMR; Q9CR42; -.
DR   BioGRID; 223553; 2.
DR   IntAct; Q9CR42; 29.
DR   MINT; Q9CR42; -.
DR   STRING; 10090.ENSMUSP00000025718; -.
DR   MoonDB; Q9CR42; Predicted.
DR   iPTMnet; Q9CR42; -.
DR   PhosphoSitePlus; Q9CR42; -.
DR   MaxQB; Q9CR42; -.
DR   PaxDb; Q9CR42; -.
DR   PRIDE; Q9CR42; -.
DR   ProteomicsDB; 281984; -.
DR   Antibodypedia; 30337; 264 antibodies from 28 providers.
DR   DNASU; 107765; -.
DR   Ensembl; ENSMUST00000237142; ENSMUSP00000157960; ENSMUSG00000024803.
DR   GeneID; 107765; -.
DR   KEGG; mmu:107765; -.
DR   UCSC; uc008hhh.1; mouse.
DR   CTD; 27063; -.
DR   MGI; MGI:1097717; Ankrd1.
DR   VEuPathDB; HostDB:ENSMUSG00000024803; -.
DR   eggNOG; KOG0504; Eukaryota.
DR   GeneTree; ENSGT00940000153956; -.
DR   HOGENOM; CLU_000134_11_1_1; -.
DR   InParanoid; Q9CR42; -.
DR   OMA; HSTALHW; -.
DR   OrthoDB; 1514637at2759; -.
DR   PhylomeDB; Q9CR42; -.
DR   TreeFam; TF331650; -.
DR   BioGRID-ORCS; 107765; 0 hits in 73 CRISPR screens.
DR   ChiTaRS; Car8; mouse.
DR   PRO; PR:Q9CR42; -.
DR   Proteomes; UP000000589; Chromosome 19.
DR   RNAct; Q9CR42; protein.
DR   Bgee; ENSMUSG00000024803; Expressed in cardiac muscle of left ventricle and 101 other tissues.
DR   ExpressionAtlas; Q9CR42; baseline and differential.
DR   Genevisible; Q9CR42; MM.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0001650; C:fibrillar center; ISO:MGI.
DR   GO; GO:0031674; C:I band; IDA:BHF-UCL.
DR   GO; GO:0030016; C:myofibril; IDA:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0032991; C:protein-containing complex; IDA:MGI.
DR   GO; GO:0005667; C:transcription regulator complex; IDA:MGI.
DR   GO; GO:0003677; F:DNA binding; ISO:MGI.
DR   GO; GO:0042826; F:histone deacetylase binding; ISO:MGI.
DR   GO; GO:0002039; F:p53 binding; ISO:MGI.
DR   GO; GO:0070412; F:R-SMAD binding; ISO:MGI.
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:0003713; F:transcription coactivator activity; ISO:MGI.
DR   GO; GO:0003714; F:transcription corepressor activity; IDA:MGI.
DR   GO; GO:0055008; P:cardiac muscle tissue morphogenesis; ISO:MGI.
DR   GO; GO:0071347; P:cellular response to interleukin-1; ISO:MGI.
DR   GO; GO:0071222; P:cellular response to lipopolysaccharide; IDA:UniProtKB.
DR   GO; GO:0071260; P:cellular response to mechanical stimulus; ISO:MGI.
DR   GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; ISO:MGI.
DR   GO; GO:0071356; P:cellular response to tumor necrosis factor; ISO:MGI.
DR   GO; GO:0071466; P:cellular response to xenobiotic stimulus; IDA:UniProtKB.
DR   GO; GO:2000279; P:negative regulation of DNA biosynthetic process; ISO:MGI.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
DR   GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI.
DR   GO; GO:0043517; P:positive regulation of DNA damage response, signal transduction by p53 class mediator; ISO:MGI.
DR   GO; GO:0010976; P:positive regulation of neuron projection development; ISO:MGI.
DR   GO; GO:0050714; P:positive regulation of protein secretion; ISO:MGI.
DR   GO; GO:0070528; P:protein kinase C signaling; IGI:MGI.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:MGI.
DR   GO; GO:0035994; P:response to muscle stretch; ISO: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; PF00023; Ank; 1.
DR   Pfam; PF12796; Ank_2; 1.
DR   Pfam; PF13637; Ank_4; 1.
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; Coiled coil; Nucleus; Reference proteome; Repeat.
FT   CHAIN           1..319
FT                   /note="Ankyrin repeat domain-containing protein 1"
FT                   /id="PRO_0000240480"
FT   REPEAT          152..181
FT                   /note="ANK 1"
FT   REPEAT          185..214
FT                   /note="ANK 2"
FT   REPEAT          218..247
FT                   /note="ANK 3"
FT   REPEAT          251..280
FT                   /note="ANK 4"
FT   REPEAT          284..315
FT                   /note="ANK 5"
FT   REGION          46..65
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          53..89
FT                   /evidence="ECO:0000255"
FT   CONFLICT        48
FT                   /note="L -> F (in Ref. 2; BAE27549)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        139..140
FT                   /note="FL -> LV (in Ref. 1; AAC03533 and 4; AAB97080)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        299
FT                   /note="T -> N (in Ref. 2; BAE27316)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        306
FT                   /note="L -> P (in Ref. 1; AAC03533)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   319 AA;  36004 MW;  26A3C4062CF0E7D0 CRC64;
     MMVLRVEELV TGKKNSNGAA GEFLPGEFRN GEYEAAVALE KQEDLKTLPA NSVKQGEEQR
     KSEKLREAEL KKKKLEQRSK LENLEDLEII VQLKKRKKYK KTKVPVVKEP EPEIMTEPVD
     VPRFLKAALE NKLPVVEKFL SDKNSPDVCD EYKRTALHRA CLEGHLAIVE KLMEAGAQIE
     FRDMLESTAI HWACRGGNAD VLKLLLNKGA KISARDKLLS TALHVAVRTG HYECAEHLIA
     CEADLNAKDR EGDTPLHDAV RLNRYKMIRL LMTFGADLKV KNCAGKTPMD LVLHWQSGTK
     AIFDSLKENA YKNSRIATF
 
 
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