ATX2_MOUSE
ID ATX2_MOUSE Reviewed; 1285 AA.
AC O70305; P97421;
DT 13-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Ataxin-2;
DE AltName: Full=Spinocerebellar ataxia type 2 protein homolog;
GN Name=Atxn2; Synonyms=Atx2, Sca2;
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] (ISOFORMS 1; 2 AND 3), SUBUNIT, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC TISSUE=Brain;
RX PubMed=9668173; DOI=10.1093/hmg/7.8.1301;
RA Nechiporuk T.T., Huynh D.P., Figueroa K., Sahba S., Nechiporuk A.V.,
RA Pulst S.-M.;
RT "The mouse SCA2 gene: cDNA sequence, alternative splicing and protein
RT expression.";
RL Hum. Mol. Genet. 7:1301-1309(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 145-563.
RX PubMed=8896555; DOI=10.1038/ng1196-269;
RA Pulst S.-M., Nechiporuk A., Nechiporuk T., Gispert S., Chen X.-N.,
RA Lopes-Cendes I., Pearlman S., Starkman S., Orozco-Diaz G., Lunkes A.,
RA DeJong P., Rouleau G.A., Auburger G., Korenberg J.R., Figueroa C.,
RA Sahba S.;
RT "Moderate expansion of a normally biallelic trinucleotide repeat in
RT spinocerebellar ataxia type 2.";
RL Nat. Genet. 14:269-276(1996).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-653; SER-832 AND SER-836, 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 [4]
RP FUNCTION, AND INTERACTION WITH SH3GL2; SH3KBP1 AND CBL.
RX PubMed=18602463; DOI=10.1016/j.cellsig.2008.05.018;
RA Nonis D., Schmidt M.H., van de Loo S., Eich F., Dikic I., Nowock J.,
RA Auburger G.;
RT "Ataxin-2 associates with the endocytosis complex and affects EGF receptor
RT trafficking.";
RL Cell. Signal. 20:1725-1739(2008).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218; SER-219; SER-435;
RP SER-593; SER-653; SER-827; SER-832; SER-836 AND SER-838, 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 [6]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-609, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Embryo;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: Involved in EGFR trafficking, acting as negative regulator of
CC endocytic EGFR internalization at the plasma membrane.
CC {ECO:0000269|PubMed:18602463}.
CC -!- SUBUNIT: Interacts with RBFOX1 (By similarity). Monomer. Can also form
CC homodimers. Interacts with polyribosomes (By similarity). Interacts
CC with EGFR (By similarity). Interacts with SH3GL3 (By similarity).
CC Interacts with SH3GL2, SH3KBP1 and CBL (PubMed:18602463). Interacts
CC with ATXN2L (By similarity). {ECO:0000250|UniProtKB:Q99700,
CC ECO:0000269|PubMed:18602463, ECO:0000269|PubMed:9668173}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9668173}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=Type I;
CC IsoId=O70305-1; Sequence=Displayed;
CC Name=2; Synonyms=Type II;
CC IsoId=O70305-2; Sequence=VSP_011583;
CC Name=3; Synonyms=Type III;
CC IsoId=O70305-3; Sequence=VSP_011583, VSP_011584;
CC -!- TISSUE SPECIFICITY: Expressed in the heart, lung, liver, kidney,
CC skeletal muscle, spleen and intestine. Predominant expression was seen
CC in the brain where a high level expression was found in the pyramidal
CC cortical neurons, large brain stem neurons and cerebellar Purkinje
CC cells. All three isoforms were found in all the tissues except skeletal
CC muscle where only isoform 1 was found. {ECO:0000269|PubMed:9668173}.
CC -!- DEVELOPMENTAL STAGE: Detectable at 8-16 dpc. Lowest expression was seen
CC at 8 dpc. {ECO:0000269|PubMed:9668173}.
CC -!- SIMILARITY: Belongs to the ataxin-2 family. {ECO:0000305}.
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DR EMBL; AF041472; AAC09275.1; -; mRNA.
DR EMBL; U70670; AAB19202.1; -; mRNA.
DR PIR; T14171; T14171.
DR RefSeq; NP_033151.2; NM_009125.2.
DR AlphaFoldDB; O70305; -.
DR SMR; O70305; -.
DR BioGRID; 203084; 59.
DR IntAct; O70305; 5.
DR MINT; O70305; -.
DR STRING; 10090.ENSMUSP00000056715; -.
DR BindingDB; O70305; -.
DR ChEMBL; CHEMBL4630804; -.
DR iPTMnet; O70305; -.
DR PhosphoSitePlus; O70305; -.
DR EPD; O70305; -.
DR jPOST; O70305; -.
DR MaxQB; O70305; -.
DR PaxDb; O70305; -.
DR PeptideAtlas; O70305; -.
DR PRIDE; O70305; -.
DR ProteomicsDB; 277205; -. [O70305-1]
DR ProteomicsDB; 277206; -. [O70305-2]
DR ProteomicsDB; 277207; -. [O70305-3]
DR DNASU; 20239; -.
DR GeneID; 20239; -.
DR KEGG; mmu:20239; -.
DR CTD; 6311; -.
DR MGI; MGI:1277223; Atxn2.
DR eggNOG; KOG2375; Eukaryota.
DR InParanoid; O70305; -.
DR OrthoDB; 282700at2759; -.
DR PhylomeDB; O70305; -.
DR BioGRID-ORCS; 20239; 5 hits in 74 CRISPR screens.
DR ChiTaRS; Atxn2; mouse.
DR PRO; PR:O70305; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; O70305; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0010494; C:cytoplasmic stress granule; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:MGI.
DR GO; GO:0005844; C:polysome; ISO:MGI.
DR GO; GO:1990904; C:ribonucleoprotein complex; ISO:MGI.
DR GO; GO:0005802; C:trans-Golgi network; ISO:MGI.
DR GO; GO:0005154; F:epidermal growth factor receptor binding; ISO:MGI.
DR GO; GO:0008022; F:protein C-terminus binding; ISO:MGI.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0021702; P:cerebellar Purkinje cell differentiation; IMP:MGI.
DR GO; GO:0048872; P:homeostasis of number of cells; IMP:MGI.
DR GO; GO:0040015; P:negative regulation of multicellular organism growth; IMP:MGI.
DR GO; GO:0002091; P:negative regulation of receptor internalization; ISO:MGI.
DR GO; GO:0050905; P:neuromuscular process; IMP:MGI.
DR GO; GO:0048812; P:neuron projection morphogenesis; IMP:MGI.
DR GO; GO:0033962; P:P-body assembly; ISO:MGI.
DR GO; GO:0034063; P:stress granule assembly; ISO:MGI.
DR InterPro; IPR009818; Ataxin-2_C.
DR InterPro; IPR033093; ATXN2.
DR InterPro; IPR045117; ATXN2-like.
DR InterPro; IPR010920; LSM_dom_sf.
DR InterPro; IPR009604; LsmAD_domain.
DR InterPro; IPR025852; SM_dom_ATX.
DR PANTHER; PTHR12854; PTHR12854; 1.
DR PANTHER; PTHR12854:SF11; PTHR12854:SF11; 1.
DR Pfam; PF06741; LsmAD; 1.
DR Pfam; PF07145; PAM2; 1.
DR Pfam; PF14438; SM-ATX; 1.
DR SMART; SM01272; LsmAD; 1.
DR SUPFAM; SSF50182; SSF50182; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Isopeptide bond; Methylation;
KW Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1..1285
FT /note="Ataxin-2"
FT /id="PRO_0000064757"
FT REGION 1..85
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 111..178
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 197..224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 428..925
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1111..1191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 48..65
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 428..457
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 473..512
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 530..545
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 550..571
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 659..676
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 722..750
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 753..772
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 773..787
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 788..810
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 811..862
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 863..880
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 881..903
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1123..1168
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1176..1191
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 218
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 219
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 362
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99700"
FT MOD_RES 435
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 477
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99700"
FT MOD_RES 523
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99700"
FT MOD_RES 593
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 609
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 609
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 611
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99700"
FT MOD_RES 653
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 697
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99700"
FT MOD_RES 710
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q99700"
FT MOD_RES 741
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99700"
FT MOD_RES 753
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99700"
FT MOD_RES 827
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 828
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99700"
FT MOD_RES 832
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 836
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 838
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 859
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99700"
FT MOD_RES 860
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99700"
FT CROSSLNK 864
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q99700"
FT VAR_SEQ 519..588
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:9668173"
FT /id="VSP_011583"
FT VAR_SEQ 589..649
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:9668173"
FT /id="VSP_011584"
FT CONFLICT 145..146
FT /note="VY -> HE (in Ref. 2; AAB19202)"
FT /evidence="ECO:0000305"
FT CONFLICT 528
FT /note="H -> P (in Ref. 2; AAB19202)"
FT /evidence="ECO:0000305"
FT CONFLICT 550
FT /note="H -> P (in Ref. 2; AAB19202)"
FT /evidence="ECO:0000305"
FT CONFLICT 554..563
FT /note="PSRPPSRPSR -> RAEFLQPGDP (in Ref. 2; AAB19202)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1285 AA; 136485 MW; 2C72EF68A79F3793 CRC64;
MRSSTAAVQR PAAGDPEPRR PAGWAARRSL PRTARRGGRG GAVAYPSAGP PPRGPGAPPR
GPRSPPCASD CFGSNGHGAS RPGSRRLLGV CGPPRPFVVV LLALAPAATP ARACPPGVRA
SPPRSGVSSS ARPAPGCPRP ACEPVYGPLT MSLKPQPQPP APATGRKPGG GLLSSPGAAP
ASAAVTSASV VPAPAAPVAS SSAAAGGGRP GLGRGRNSSK GLPQPTISFD GIYANVRMVH
ILTSVVGSKC EVQVKNGGIY EGVFKTYSPK CDLVLDAAHE KSTESSSGPK REEIMESVLF
KCSDFVVVQF KDTDSSYARR DAFTDSALSA KVNGEHKEKD LEPWDAGELT ASEELELEND
VSNGWDPNDM FRYNEENYGV VSTYDSSLSS YTVPLERDNS EEFLKREARA NQLAEEIESS
AQYKARVALE NDDRSEEEKY TAVQRNCSDR EGHGPNTRDN KYIPPGQRNR EVLSWGSGRQ
SSPRMGQPGP GSMPSRAASH TSDFNPNAGS DQRVVNGGVP WPSPCPSHSS RPPSRYQSGP
NSLPPRAATH TRPPSRPPSR PSRPPSHPSA HGSPAPVSTM PKRMSSEGPP RMSPKAQRHP
RNHRVSAGRG SMSSGLEFVS HNPPSEAAAP PVARTSPAGG TWSSVVSGVP RLSPKTHRPR
SPRQSSIGNS PSGPVLASPQ AGIIPAEAVS MPVPAASPTP ASPASNRALT PSIEAKDSRL
QDQRQNSPAG SKENVKASET SPSFSKADNK GMSPVVSEHR KQIDDLKKFK NDFRLQPSST
SESMDQLLSK NREGEKSRDL IKDKTEASAK DSFIDSSSSS SNCTSGSSKT NSPSISPSML
SNAEHKRGPE VTSQGVQTSS PACKQEKDDR EEKKDTTEQV RKSTLNPNAK EFNPRSFSQP
KPSTTPTSPR PQAQPSPSMV GHQQPAPVYT QPVCFAPNMM YPVPVSPGVQ PLYPIPMTPM
PVNQAKTYRA GKVPNMPQQR QDQHHQSTMM HPASAAGPPI VATPPAYSTQ YVAYSPQQFP
NQPLVQHVPH YQSQHPHVYS PVIQGNARMM APPAHAQPGL VSSSAAQFGA HEQTHAMYAC
PKLPYNKETS PSFYFAISTG SLAQQYAHPN AALHPHTPHP QPSATPTGQQ QSQHGGSHPA
PSPVQHHQHQ AAQALHLASP QQQSAIYHAG LAPTPPSMTP ASNTQSPQSS FPAAQQTVFT
IHPSHVQPAY TTPPHMAHVP QAHVQSGMVP SHPTAHAPMM LMTTQPPGPK AALAQSALQP
IPVSTTAHFP YMTHPSVQAH HQQQL
