ATX2L_MOUSE
ID ATX2L_MOUSE Reviewed; 1049 AA.
AC Q7TQH0; Q80XN9; Q8K059;
DT 13-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Ataxin-2-like protein;
GN Name=Atxn2l; Synonyms=A2lp;
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 [LARGE SCALE MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 239-1049 (ISOFORM 2), AND NUCLEOTIDE SEQUENCE [LARGE
RP SCALE MRNA] OF 266-1049 (ISOFORM 3).
RC TISSUE=Colon, Kidney, and Olfactory epithelium;
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 [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain cortex;
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 [3]
RP INTERACTION WITH CIC AND ATXN1, AND TISSUE SPECIFICITY.
RX PubMed=17322884; DOI=10.1038/ng1977;
RA Bowman A.B., Lam Y.C., Jafar-Nejad P., Chen H.-K., Richman R., Samaco R.C.,
RA Fryer J.D., Kahle J.J., Orr H.T., Zoghbi H.Y.;
RT "Duplication of Atxn1l suppresses SCA1 neuropathology by decreasing
RT incorporation of polyglutamine-expanded ataxin-1 into native complexes.";
RL Nat. Genet. 39:373-379(2007).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-109; SER-496 AND SER-499, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-109 AND SER-597, AND
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-109, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27; THR-45; SER-109; SER-236;
RP SER-407; SER-496; SER-499; SER-560; SER-597 AND SER-637, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, 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 [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-205, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
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).
CC -!- FUNCTION: Involved in the regulation of stress granule and P-body
CC formation. {ECO:0000250|UniProtKB:Q8WWM7}.
CC -!- SUBUNIT: Interacts with MPL/TPOR and EPOR and dissociates after ligand
CC stimulation. Interacts with DDX6, G3BP, and ATXN2. Interacts with PRMT1
CC (By similarity). Interacts with CIC and ATXN1 (PubMed:17322884).
CC {ECO:0000250|UniProtKB:Q8WWM7, ECO:0000269|PubMed:17322884}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Peripheral membrane
CC protein {ECO:0000250}. Cytoplasm {ECO:0000250|UniProtKB:Q8WWM7}.
CC Nucleus speckle {ECO:0000250|UniProtKB:Q8WWM7}. Cytoplasmic granule
CC {ECO:0000250|UniProtKB:Q8WWM7}. Note=Predominantly cytoplasmic but is
CC also detected in nuclear speckles. Component of cytoplasmic stress
CC granules. Inhibition of methylation alters nuclear localization.
CC Methylation does not seem to be required for localization to stress
CC granules under stress conditions. {ECO:0000250|UniProtKB:Q8WWM7}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q7TQH0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q7TQH0-2; Sequence=VSP_011595, VSP_011596;
CC Name=3;
CC IsoId=Q7TQH0-3; Sequence=VSP_011595;
CC -!- TISSUE SPECIFICITY: Expressed in cerebellum.
CC {ECO:0000269|PubMed:17322884}.
CC -!- PTM: Thrombopoietin triggers the phosphorylation on tyrosine residues
CC in a way that is dependent on MPL C-terminal domain. {ECO:0000250}.
CC -!- PTM: Asymmetrically dimethylated. Probably methylated by PRMT1.
CC {ECO:0000250|UniProtKB:Q8WWM7}.
CC -!- SIMILARITY: Belongs to the ataxin-2 family. {ECO:0000305}.
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DR EMBL; BC034083; AAH34083.1; -; mRNA.
DR EMBL; BC043451; AAH43451.1; -; mRNA.
DR EMBL; BC054483; AAH54483.1; -; mRNA.
DR CCDS; CCDS21831.1; -. [Q7TQH0-1]
DR RefSeq; NP_898841.1; NM_183020.1. [Q7TQH0-1]
DR RefSeq; XP_006507788.1; XM_006507725.2. [Q7TQH0-3]
DR AlphaFoldDB; Q7TQH0; -.
DR SMR; Q7TQH0; -.
DR BioGRID; 231460; 21.
DR IntAct; Q7TQH0; 8.
DR MINT; Q7TQH0; -.
DR STRING; 10090.ENSMUSP00000035415; -.
DR iPTMnet; Q7TQH0; -.
DR PhosphoSitePlus; Q7TQH0; -.
DR SwissPalm; Q7TQH0; -.
DR EPD; Q7TQH0; -.
DR jPOST; Q7TQH0; -.
DR MaxQB; Q7TQH0; -.
DR PaxDb; Q7TQH0; -.
DR PeptideAtlas; Q7TQH0; -.
DR PRIDE; Q7TQH0; -.
DR ProteomicsDB; 273628; -. [Q7TQH0-1]
DR ProteomicsDB; 273629; -. [Q7TQH0-2]
DR ProteomicsDB; 273630; -. [Q7TQH0-3]
DR Antibodypedia; 26552; 126 antibodies from 24 providers.
DR DNASU; 233871; -.
DR Ensembl; ENSMUST00000040202; ENSMUSP00000035415; ENSMUSG00000032637. [Q7TQH0-1]
DR GeneID; 233871; -.
DR KEGG; mmu:233871; -.
DR UCSC; uc009jrr.1; mouse. [Q7TQH0-3]
DR UCSC; uc009jrs.1; mouse. [Q7TQH0-1]
DR UCSC; uc009jru.1; mouse. [Q7TQH0-2]
DR CTD; 11273; -.
DR MGI; MGI:2446242; Atxn2l.
DR VEuPathDB; HostDB:ENSMUSG00000032637; -.
DR eggNOG; KOG2375; Eukaryota.
DR GeneTree; ENSGT00940000157795; -.
DR InParanoid; Q7TQH0; -.
DR OrthoDB; 282700at2759; -.
DR PhylomeDB; Q7TQH0; -.
DR TreeFam; TF326591; -.
DR BioGRID-ORCS; 233871; 14 hits in 76 CRISPR screens.
DR ChiTaRS; Atxn2l; mouse.
DR PRO; PR:Q7TQH0; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q7TQH0; protein.
DR Bgee; ENSMUSG00000032637; Expressed in animal zygote and 223 other tissues.
DR ExpressionAtlas; Q7TQH0; baseline and differential.
DR Genevisible; Q7TQH0; MM.
DR GO; GO:0010494; C:cytoplasmic stress granule; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0016607; C:nuclear speck; ISS:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0016071; P:mRNA metabolic process; ISO:MGI.
DR GO; GO:0034063; P:stress granule assembly; IBA:GO_Central.
DR InterPro; IPR009818; Ataxin-2_C.
DR InterPro; IPR045117; ATXN2-like.
DR InterPro; IPR009604; LsmAD_domain.
DR InterPro; IPR025852; SM_dom_ATX.
DR PANTHER; PTHR12854; PTHR12854; 1.
DR Pfam; PF06741; LsmAD; 1.
DR Pfam; PF07145; PAM2; 1.
DR Pfam; PF14438; SM-ATX; 1.
DR SMART; SM01272; LsmAD; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cytoplasm; Isopeptide bond; Membrane;
KW Methylation; Nucleus; Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1..1049
FT /note="Ataxin-2-like protein"
FT /id="PRO_0000064755"
FT REGION 1..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 96..119
FT /note="Interaction with MPL"
FT /evidence="ECO:0000250"
FT REGION 314..522
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 554..573
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 578..704
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 736..772
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 824..852
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 868..944
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 999..1049
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 477..503
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 656..704
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 868..922
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 925..939
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1026..1043
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q8WWM7"
FT MOD_RES 27
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 45
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 109
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19131326, ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 116
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q8WWM7"
FT MOD_RES 205
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 236
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 262
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q8WWM7"
FT MOD_RES 304
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WWM7"
FT MOD_RES 307
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q8WWM7"
FT MOD_RES 333
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WWM7"
FT MOD_RES 337
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WWM7"
FT MOD_RES 347
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q8WWM7"
FT MOD_RES 359
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q8WWM7"
FT MOD_RES 389
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WWM7"
FT MOD_RES 407
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 453
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WWM7"
FT MOD_RES 496
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 499
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 560
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 561
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WWM7"
FT MOD_RES 562
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WWM7"
FT MOD_RES 597
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 635
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8WWM7"
FT MOD_RES 637
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 677
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WWM7"
FT MOD_RES 683
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WWM7"
FT MOD_RES 687
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WWM7"
FT CROSSLNK 346
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8WWM7"
FT VAR_SEQ 439..444
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_011595"
FT VAR_SEQ 1034..1049
FT /note="VQSHPSQQLPFHPPGN -> GEQPGQAPGFPGGADDRIREFSLAGGIWHGRA
FT EGLQVGQDARVLGGD (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_011596"
SQ SEQUENCE 1049 AA; 110649 MW; 27ECCFE500688D45 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 ASVPPTSAAL PFLPVGRMYP PRSPKSAAPA PVSASCPEPP IGSAVASSAS
IPVTSSVVDP GAGSISPASP KLSLTPTDVK ELPTKEPSRN LEAQELARIA GKVPGLQNEQ
KRFQLEELRK FGAQFKLQPS SSPETGLDPF PSRILKEEAK GKEKEVDGLL TSDPMGSPVS
SKTESILDKE DKVPMAGVGG TEGPEQLPAP CPSQTGSPPV GLIKGDEKEE GPVTEQVKKS
TLNPNAKEFN PTKPLLSVNK STSTPTSPGP RTHSTPSIPV LTAGQSGLYS PQYISYIPQI
HMGPAVQAPQ MYPYPVSNSV PGQQGKYRGA KGSLPPQRSD QHQPASAPPM MQAAAAAAGP
PLVAATPYSS YIPYNPQQFP GQPAMMQPMA HYPSQPVFAP MLQSNPRMLT SGSHPQAIVS
SSTPQYPAAE QPTPQALYAT VHQSYPHHAT QLHGHQPQPA TTPTGSQPQS QHAAPSPVQH
QAGQAPHLGS GQPQQNLYHP GALTGTPPSL PPGPSAQSPQ SSFPQPAAVY AIHPHQQLPH
GFTNMAHVTQ AHVQTGVTAA PPPHPGAPHP PQVMLLHPPQ GHGGPPQGAV PPSGVPALSA
STPSPYPYIG HPQVQSHPSQ QLPFHPPGN
