ID A0A0U1RPL0_MOUSE Unreviewed; 1096 AA.
AC A0A0U1RPL0;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Ataxin 2-like {ECO:0000313|Ensembl:ENSMUSP00000146023.2};
GN Name=Atxn2l {ECO:0000313|Ensembl:ENSMUSP00000146023.2,
GN ECO:0000313|MGI:MGI:2446242};
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 {ECO:0000313|Ensembl:ENSMUSP00000146023.2, ECO:0000313|Proteomes:UP000000589};
RN [1] {ECO:0007829|PubMed:17114649}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B.,
RA Panse C., Schlapbach R., Mansuy I.M.;
RT "Qualitative and quantitative analyses of protein phosphorylation in naive
RT and stimulated mouse synaptosomal preparations.";
RL Mol. Cell. Proteomics 6:283-293(2007).
RN [2] {ECO:0007829|PubMed:17242355}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [3] {ECO:0007829|PubMed:19144319}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [4] {ECO:0007829|PubMed:19131326}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [5] {ECO:0000313|Ensembl:ENSMUSP00000146023.2, ECO:0000313|Proteomes:UP000000589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000146023.2,
RC ECO:0000313|Proteomes:UP000000589};
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] {ECO:0007829|PubMed:21183079}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 [7] {ECO:0007829|PubMed:23806337}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [8] {ECO:0000313|Ensembl:ENSMUSP00000146023.2}
RP IDENTIFICATION.
RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000146023.2};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the ataxin-2 family.
CC {ECO:0000256|ARBA:ARBA00007503}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_006507784.1; XM_006507721.2.
DR AlphaFoldDB; A0A0U1RPL0; -.
DR SMR; A0A0U1RPL0; -.
DR jPOST; A0A0U1RPL0; -.
DR ProteomicsDB; 355068; -.
DR Antibodypedia; 26552; 140 antibodies from 24 providers.
DR DNASU; 233871; -.
DR Ensembl; ENSMUST00000206577.2; ENSMUSP00000146023.2; ENSMUSG00000032637.16.
DR GeneID; 233871; -.
DR AGR; MGI:2446242; -.
DR CTD; 11273; -.
DR MGI; MGI:2446242; Atxn2l.
DR VEuPathDB; HostDB:ENSMUSG00000032637; -.
DR GeneTree; ENSGT00940000157795; -.
DR OMA; MRVYQDQ; -.
DR OrthoDB; 4269134at2759; -.
DR BioGRID-ORCS; 233871; 15 hits in 81 CRISPR screens.
DR ChiTaRS; Atxn2l; mouse.
DR Proteomes; UP000000589; Chromosome 7.
DR Bgee; ENSMUSG00000032637; Expressed in animal zygote and 226 other cell types or tissues.
DR ExpressionAtlas; A0A0U1RPL0; baseline and differential.
DR GO; GO:0010494; C:cytoplasmic stress granule; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0016020; C:membrane; IEA:Ensembl.
DR GO; GO:0016607; C:nuclear speck; IEA:Ensembl.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0016071; P:mRNA metabolic process; IEA:Ensembl.
DR InterPro; IPR009818; Ataxin-2_C.
DR InterPro; IPR045117; ATXN2-like.
DR InterPro; IPR009604; LsmAD_domain.
DR InterPro; IPR047575; Sm.
DR InterPro; IPR025852; SM_dom_ATX.
DR PANTHER; PTHR12854; ATAXIN 2-RELATED; 1.
DR PANTHER; PTHR12854:SF8; ATAXIN-2-LIKE PROTEIN; 1.
DR Pfam; PF06741; LsmAD; 1.
DR Pfam; PF07145; PAM2; 1.
DR Pfam; PF14438; SM-ATX; 1.
DR SMART; SM01272; LsmAD; 1.
DR PROSITE; PS52002; SM; 1.
PE 1: Evidence at protein level;
KW Proteomics identification {ECO:0007829|EPD:A0A0U1RPL0,
KW ECO:0007829|MaxQB:A0A0U1RPL0};
KW Reference proteome {ECO:0000313|Proteomes:UP000000589}.
FT DOMAIN 120..197
FT /note="Sm"
FT /evidence="ECO:0000259|PROSITE:PS52002"
FT REGION 1..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 314..516
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 548..567
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 573..698
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 730..766
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 818..846
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 862..938
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1023..1042
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 314..330
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 417..432
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 471..497
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 650..698
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 862..916
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 919..933
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1096 AA; 115266 MW; 43A7F0326924B229 CRC64;
MLKPQPPQQT SQPQQPPPTQ QAVARRSPGG TSPPNGGLPG PLTATAAPPG PPAAVSPCLG
PAAAAGSGLR RGAESILAAS APPQHQERPG AVAIGSVRGQ TTGKGPPQSP VFEGVYNNSR
MLHFLTAVVG STCDVKVKNG TTYEGIFKTL SSKFELAVDA VHRKASEPAG GPRREDIVDT
MVFKPSDVLL VHFRNVDFNY ATKDKFTDSA IAMNSKVNGE HKEKVLQRWE GGDSNSDDYD
LESDMSNGWD PNEMFKFNEE NYGVKTTYDS SLSSYTVPLE KDNSEEFRQR ELRAAQLARE
IESSPQYRLR IAMENDDGRT EEEKHSAVQR QGSGRESPSL VSREGKYIPL PQRVREGPRG
GVRCSSSRGG RPGLSSLPPR GPHHLDNSSP GPGSEARGIN GGPSRMSPKA QRPLRGAKTL
SSPSNRPSGE ASVPPTSAVG RMYPPRSPKS AAPAPVSASC PEPPIGSAVA SSASIPVTSS
VVDPGAGSIS PASPKLSLTP TDVKELPTKE PSRNLEAQEL ARIAGKVPGL QNEQKRFQLE
ELRKFGAQFK LQPSSSPETG LDPFPSRILK EEAKGKEKEV DGLLTSDPMG SPVSSKTESI
LDKEDKVPMA GVGGTEGPEQ LPAPCPSQTG SPPVGLIKGD EKEEGPVTEQ VKKSTLNPNA
KEFNPTKPLL SVNKSTSTPT SPGPRTHSTP SIPVLTAGQS GLYSPQYISY IPQIHMGPAV
QAPQMYPYPV SNSVPGQQGK YRGAKGSLPP QRSDQHQPAS APPMMQAAAA AAGPPLVAAT
PYSSYIPYNP QQFPGQPAMM QPMAHYPSQP VFAPMLQSNP RMLTSGSHPQ AIVSSSTPQY
PAAEQPTPQA LYATVHQSYP HHATQLHGHQ PQPATTPTGS QPQSQHAAPS PVQHQAGQAP
HLGSGQPQQN LYHPGALTGT PPSLPPGPSA QSPQSSFPQP AAVYAIHPHQ QLPHGFTNMA
HVTQAHVQTG VTAAPPPHPG APHPPQVMLL HPPQGHGGPP QGAVPPSGVP ALSASTPSPY
PYIGHPQGEQ PGQAPGFPGG ADDRILCRVG RSHSRRRQGL APGSVLCFPP SSLSCDPAAP
LPTASPALSD PDCLLT
//
