ATX2L_HUMAN
ID ATX2L_HUMAN Reviewed; 1075 AA.
AC Q8WWM7; A8K1R6; B9EGM2; E9PAR9; O95135; Q63ZY4; Q6NVJ8; Q6PJW6; Q8IU61;
AC Q8IU95; Q8WWM3; Q8WWM4; Q8WWM5; Q8WWM6; Q99703;
DT 13-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 2.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Ataxin-2-like protein;
DE AltName: Full=Ataxin-2 domain protein;
DE AltName: Full=Ataxin-2-related protein;
GN Name=ATXN2L; Synonyms=A2D, A2LG, A2LP, A2RP;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 4 AND 5), SUBCELLULAR
RP LOCATION, PHOSPHORYLATION, TISSUE SPECIFICITY, AND INTERACTION WITH MPL AND
RP EPOR.
RX PubMed=11784712; DOI=10.1074/jbc.m105970200;
RA Meunier C.F., Bordereaux D., Porteu F., Gisselbrecht S., Chretien S.,
RA Courtois G.;
RT "Cloning and characterization of a family of proteins associated with
RT Mpl.";
RL J. Biol. Chem. 277:9139-9147(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=14769358; DOI=10.1016/s0014-4886(03)00287-5;
RA Figueroa K.P., Pulst S.M.;
RT "Identification and expression of the gene for human ataxin-2-related
RT protein on chromosome 16.";
RL Exp. Neurol. 184:669-678(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 6).
RC TISSUE=Brain;
RA Xia J.-H., Liu C.-Y., Wang D.-A., Ruan Q.-G., Deng H.-X.;
RT "A splicing form of human ataxin-2 like gene obtained from adult brain.";
RL Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 8).
RC TISSUE=Hippocampus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 4 AND 9).
RC TISSUE=Lymph, Skin, and Testis;
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 [7]
RP PROTEIN SEQUENCE OF 1-25; 141-150; 156-165; 197-218; 259-283; 302-310;
RP 383-399; 421-443; 499-507; 517-525; 540-546 AND 554-570, ACETYLATION AT
RP MET-1, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Colon carcinoma;
RA Bienvenut W.V., Heiserich L., Boulahbel H., Gottlieb E.;
RL Submitted (JUL-2007) to UniProtKB.
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 54-1075 (ISOFORM 7).
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-111; TYR-264; TYR-309 AND
RP TYR-349, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=15144186; DOI=10.1021/ac035352d;
RA Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,
RA Peters E.C.;
RT "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from
RT human T cells using immobilized metal affinity chromatography and tandem
RT mass spectrometry.";
RL Anal. Chem. 76:2763-2772(2004).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-496 AND SER-594, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-111 AND SER-594, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-111, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-103; SER-111; SER-559;
RP SER-594; SER-634 AND SER-684, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-111 AND SER-594, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-111; TYR-118; SER-238;
RP SER-558; SER-559 AND SER-594, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-111; SER-335; SER-339;
RP SER-409; SER-449; SER-493; SER-496; SER-559 AND SER-594, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-111; SER-409; SER-496 AND
RP SER-594, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [20]
RP FUNCTION, INTERACTION WITH ATXN2; DDX6 AND G3BP1, AND SUBCELLULAR LOCATION.
RX PubMed=23209657; DOI=10.1371/journal.pone.0050134;
RA Kaehler C., Isensee J., Nonhoff U., Terrey M., Hucho T., Lehrach H.,
RA Krobitsch S.;
RT "Ataxin-2-like is a regulator of stress granules and processing bodies.";
RL PLoS ONE 7:E50134-E50134(2012).
RN [21]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-111; SER-306; SER-335;
RP SER-339; SER-391; SER-409; SER-558; SER-559; SER-563; SER-594; SER-674;
RP SER-680 AND SER-684, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-594 AND THR-632, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [24]
RP INTERACTION WITH PRMT1, SUBCELLULAR LOCATION, METHYLATION AT ARG-361, AND
RP MUTAGENESIS OF ARG-361 AND ARG-370.
RX PubMed=25748791; DOI=10.1016/j.yexcr.2015.02.022;
RA Kaehler C., Guenther A., Uhlich A., Krobitsch S.;
RT "PRMT1-mediated arginine methylation controls ATXN2L localization.";
RL Exp. Cell Res. 334:114-125(2015).
RN [25]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [26]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-348, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
CC -!- FUNCTION: Involved in the regulation of stress granule and P-body
CC formation. {ECO:0000269|PubMed:23209657}.
CC -!- SUBUNIT: Interacts with MPL/TPOR and EPOR and dissociates after ligand
CC stimulation (PubMed:11784712). Interacts with DDX6, G3BP1, and ATXN2
CC (PubMed:23209657). Interacts with PRMT1 (PubMed:25748791). Interacts
CC with CIC and ATXN1 (By similarity). {ECO:0000250|UniProtKB:Q7TQH0,
CC ECO:0000269|PubMed:11784712, ECO:0000269|PubMed:23209657,
CC ECO:0000269|PubMed:25748791}.
CC -!- INTERACTION:
CC Q8WWM7; P19235: EPOR; NbExp=2; IntAct=EBI-948363, EBI-617321;
CC Q8WWM7; Q13283: G3BP1; NbExp=6; IntAct=EBI-948363, EBI-1047359;
CC Q8WWM7-9; Q8N9W6-4: BOLL; NbExp=3; IntAct=EBI-12053753, EBI-11983447;
CC Q8WWM7-9; P60329: KRTAP12-4; NbExp=3; IntAct=EBI-12053753, EBI-10176396;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:11784712};
CC Peripheral membrane protein {ECO:0000269|PubMed:11784712}. Cytoplasm
CC {ECO:0000269|PubMed:23209657}. Nucleus speckle
CC {ECO:0000269|PubMed:23209657}. Cytoplasmic granule
CC {ECO:0000269|PubMed:23209657}. Note=Predominantly cytoplasmic but is
CC also detected in nuclear speckles (PubMed:23209657). Component of
CC cytoplasmic stress granules (PubMed:23209657). Inhibition of
CC methylation alters nuclear localization (PubMed:25748791). Methylation
CC does not seem to be required for localization to stress granules under
CC stress conditions (PubMed:25748791). {ECO:0000269|PubMed:23209657,
CC ECO:0000269|PubMed:25748791}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=9;
CC Name=1; Synonyms=A2D-A;
CC IsoId=Q8WWM7-1; Sequence=Displayed;
CC Name=2; Synonyms=A2D-B;
CC IsoId=Q8WWM7-2; Sequence=VSP_011593;
CC Name=3; Synonyms=A2D-C;
CC IsoId=Q8WWM7-3; Sequence=VSP_011594;
CC Name=4; Synonyms=A2D-D;
CC IsoId=Q8WWM7-4; Sequence=VSP_011591;
CC Name=5; Synonyms=A2D-E;
CC IsoId=Q8WWM7-5; Sequence=VSP_011592;
CC Name=6;
CC IsoId=Q8WWM7-6; Sequence=VSP_011589, VSP_011590;
CC Name=7;
CC IsoId=Q8WWM7-7; Sequence=VSP_011587, VSP_011588;
CC Name=8;
CC IsoId=Q8WWM7-8; Sequence=VSP_044243;
CC Name=9;
CC IsoId=Q8WWM7-9; Sequence=VSP_047122;
CC -!- TISSUE SPECIFICITY: Expressed at high levels in thymus, lymph node,
CC spleen, fetal kidney and adult testis. Constitutively associated with
CC MPL and EPOR in hematopoietic cells. {ECO:0000269|PubMed:11784712}.
CC -!- PTM: Thrombopoietin triggers the phosphorylation on tyrosine residues
CC in a way that is dependent on MPL C-terminal domain.
CC {ECO:0000269|PubMed:11784712}.
CC -!- PTM: Asymmetrically dimethylated. Probably methylated by PRMT1.
CC {ECO:0000269|PubMed:25748791}.
CC -!- MISCELLANEOUS: [Isoform 6]: Due to intron retention. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the ataxin-2 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC69607.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAO12056.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAO12057.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAO12058.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAO12058.1; Type=Miscellaneous discrepancy; Note=Exon duplication.; Evidence={ECO:0000305};
CC Sequence=AAO12059.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAO12059.1; Type=Miscellaneous discrepancy; Note=Exon duplication.; Evidence={ECO:0000305};
CC Sequence=AAO12060.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAO12060.1; Type=Miscellaneous discrepancy; Note=Exon duplication.; Evidence={ECO:0000305};
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DR EMBL; AJ317970; CAC38068.1; -; mRNA.
DR EMBL; AJ317971; CAC38069.3; -; mRNA.
DR EMBL; AJ317972; CAC38070.3; -; mRNA.
DR EMBL; AJ317973; CAC38071.3; -; mRNA.
DR EMBL; AJ317974; CAC38072.3; -; mRNA.
DR EMBL; AY188334; AAO12056.1; ALT_FRAME; mRNA.
DR EMBL; AY188335; AAO12057.1; ALT_FRAME; mRNA.
DR EMBL; AY188336; AAO12058.1; ALT_SEQ; mRNA.
DR EMBL; AY188337; AAO12059.1; ALT_SEQ; mRNA.
DR EMBL; AY188338; AAO12060.1; ALT_SEQ; mRNA.
DR EMBL; AF034373; AAC69607.1; ALT_FRAME; mRNA.
DR EMBL; AK289981; BAF82670.1; -; mRNA.
DR EMBL; AC116346; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC133550; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC145285; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC010239; AAH10239.1; -; mRNA.
DR EMBL; BC068012; AAH68012.1; ALT_SEQ; mRNA.
DR EMBL; BC082760; AAH82760.1; -; mRNA.
DR EMBL; BC136584; AAI36585.1; -; mRNA.
DR EMBL; U70671; AAB19201.1; -; mRNA.
DR CCDS; CCDS10639.1; -. [Q8WWM7-4]
DR CCDS; CCDS10640.1; -. [Q8WWM7-3]
DR CCDS; CCDS10641.1; -. [Q8WWM7-1]
DR CCDS; CCDS32423.1; -. [Q8WWM7-2]
DR CCDS; CCDS45451.1; -. [Q8WWM7-8]
DR CCDS; CCDS58443.1; -. [Q8WWM7-9]
DR RefSeq; NP_009176.2; NM_007245.3. [Q8WWM7-1]
DR RefSeq; NP_059867.3; NM_017492.3. [Q8WWM7-9]
DR RefSeq; NP_663760.1; NM_145714.2. [Q8WWM7-2]
DR RefSeq; NP_680780.1; NM_148414.2. [Q8WWM7-3]
DR RefSeq; NP_680781.1; NM_148415.2. [Q8WWM7-4]
DR RefSeq; NP_680782.1; NM_148416.2. [Q8WWM7-8]
DR RefSeq; XP_005255123.1; XM_005255066.1. [Q8WWM7-3]
DR AlphaFoldDB; Q8WWM7; -.
DR SMR; Q8WWM7; -.
DR BioGRID; 116429; 204.
DR IntAct; Q8WWM7; 67.
DR MINT; Q8WWM7; -.
DR STRING; 9606.ENSP00000378917; -.
DR GlyConnect; 2892; 1 O-Linked glycan (2 sites).
DR GlyGen; Q8WWM7; 9 sites, 1 O-linked glycan (9 sites).
DR iPTMnet; Q8WWM7; -.
DR MetOSite; Q8WWM7; -.
DR PhosphoSitePlus; Q8WWM7; -.
DR SwissPalm; Q8WWM7; -.
DR BioMuta; ATXN2L; -.
DR DMDM; 52000729; -.
DR EPD; Q8WWM7; -.
DR jPOST; Q8WWM7; -.
DR MassIVE; Q8WWM7; -.
DR MaxQB; Q8WWM7; -.
DR PaxDb; Q8WWM7; -.
DR PeptideAtlas; Q8WWM7; -.
DR PRIDE; Q8WWM7; -.
DR ProteomicsDB; 1849; -.
DR ProteomicsDB; 65904; -.
DR ProteomicsDB; 74906; -. [Q8WWM7-1]
DR ProteomicsDB; 74907; -. [Q8WWM7-2]
DR ProteomicsDB; 74908; -. [Q8WWM7-3]
DR ProteomicsDB; 74909; -. [Q8WWM7-4]
DR ProteomicsDB; 74910; -. [Q8WWM7-5]
DR ProteomicsDB; 74911; -. [Q8WWM7-6]
DR ProteomicsDB; 74912; -. [Q8WWM7-7]
DR Antibodypedia; 26552; 126 antibodies from 24 providers.
DR Ensembl; ENST00000325215.10; ENSP00000315650.6; ENSG00000168488.19. [Q8WWM7-2]
DR Ensembl; ENST00000336783.9; ENSP00000338718.4; ENSG00000168488.19. [Q8WWM7-1]
DR Ensembl; ENST00000340394.12; ENSP00000341459.8; ENSG00000168488.19. [Q8WWM7-4]
DR Ensembl; ENST00000382686.8; ENSP00000372133.4; ENSG00000168488.19. [Q8WWM7-8]
DR Ensembl; ENST00000395547.6; ENSP00000378917.2; ENSG00000168488.19. [Q8WWM7-3]
DR Ensembl; ENST00000570200.5; ENSP00000454516.1; ENSG00000168488.19. [Q8WWM7-9]
DR GeneID; 11273; -.
DR KEGG; hsa:11273; -.
DR MANE-Select; ENST00000336783.9; ENSP00000338718.4; NM_007245.4; NP_009176.2.
DR UCSC; uc002dqy.5; human. [Q8WWM7-1]
DR CTD; 11273; -.
DR DisGeNET; 11273; -.
DR GeneCards; ATXN2L; -.
DR HGNC; HGNC:31326; ATXN2L.
DR HPA; ENSG00000168488; Low tissue specificity.
DR MIM; 607931; gene.
DR neXtProt; NX_Q8WWM7; -.
DR OpenTargets; ENSG00000168488; -.
DR PharmGKB; PA128394585; -.
DR VEuPathDB; HostDB:ENSG00000168488; -.
DR eggNOG; KOG2375; Eukaryota.
DR GeneTree; ENSGT00940000157795; -.
DR HOGENOM; CLU_003766_0_0_1; -.
DR InParanoid; Q8WWM7; -.
DR OMA; MRVYQDQ; -.
DR OrthoDB; 282700at2759; -.
DR PhylomeDB; Q8WWM7; -.
DR TreeFam; TF326591; -.
DR PathwayCommons; Q8WWM7; -.
DR SignaLink; Q8WWM7; -.
DR SIGNOR; Q8WWM7; -.
DR BioGRID-ORCS; 11273; 51 hits in 1086 CRISPR screens.
DR ChiTaRS; ATXN2L; human.
DR GeneWiki; ATXN2L; -.
DR GenomeRNAi; 11273; -.
DR Pharos; Q8WWM7; Tbio.
DR PRO; PR:Q8WWM7; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q8WWM7; protein.
DR Bgee; ENSG00000168488; Expressed in left testis and 182 other tissues.
DR ExpressionAtlas; Q8WWM7; baseline and differential.
DR Genevisible; Q8WWM7; HS.
DR GO; GO:0010494; C:cytoplasmic stress granule; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0016607; C:nuclear speck; IDA:UniProtKB.
DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0016071; P:mRNA metabolic process; IMP:UniProtKB.
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; Direct protein sequencing;
KW Isopeptide bond; Membrane; Methylation; Nucleus; Phosphoprotein;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1..1075
FT /note="Ataxin-2-like protein"
FT /id="PRO_0000064754"
FT REGION 1..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 98..121
FT /note="Interaction with MPL"
FT /evidence="ECO:0000269|PubMed:11784712"
FT REGION 316..521
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 551..697
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 733..770
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 820..849
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 865..940
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1022..1045
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..23
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 316..332
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 431..453
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 468..490
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 568..586
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 617..633
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 655..697
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 865..918
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 921..935
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000269|Ref.7, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22814378"
FT MOD_RES 103
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 111
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15144186,
FT ECO:0007744|PubMed:16964243, ECO:0007744|PubMed:18220336,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19369195,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 118
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 207
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q7TQH0"
FT MOD_RES 238
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 264
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:15144186"
FT MOD_RES 306
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 309
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:15144186"
FT MOD_RES 335
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 339
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 349
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:15144186"
FT MOD_RES 361
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000269|PubMed:25748791"
FT MOD_RES 391
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 409
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 449
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 493
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 496
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692"
FT MOD_RES 557
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7TQH0"
FT MOD_RES 558
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 559
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 563
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 594
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 632
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 634
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 674
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 680
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 684
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT CROSSLNK 348
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 354..400
FT /note="QRVREGPRGGVRCSSSRGGRPGLSSLPPRGPHHLDNSSPGPGSEARG -> H
FT RGQGQGPAGVGGSCSAPARPHPVLPSHPLIYSPAGDGRSFIFYYL (in isoform
FT 7)"
FT /evidence="ECO:0000303|PubMed:8896555"
FT /id="VSP_011587"
FT VAR_SEQ 401..1075
FT /note="Missing (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:8896555"
FT /id="VSP_011588"
FT VAR_SEQ 896..967
FT /note="HQAGQAPHLGSGQPQQNLYHPGALTGTPPSLPPGPSAQSPQSSFPQPAAVYA
FT IHHQQLPHGFTNMAHVTQAH -> VPAMGGAEWSWCRNGWPEEGIELGVISEWRGLGAS
FT ELLACVALNLPLPSSIRRGRPHTWAVDSHSRICTTQGP (in isoform 6)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_011589"
FT VAR_SEQ 968..1075
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_011590"
FT VAR_SEQ 1029..1075
FT /note="GEQPGQAPGFPGGADDRIREFSLAGGIWHGRAEGLQVGQDARVLGGE -> V
FT QSHPSQQLPFHPPGN (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:11784712,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_011591"
FT VAR_SEQ 1029..1075
FT /note="GEQPGQAPGFPGGADDRIREFSLAGGIWHGRAEGLQVGQDARVLGGE -> A
FT PFPPPGELKIVLAAT (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:11784712"
FT /id="VSP_011592"
FT VAR_SEQ 1029..1075
FT /note="GEQPGQAPGFPGGADDRIREFSLAGGIWHGRAEGLQVGQDARVLGGE -> A
FT PLPPPGELKIVLAAT (in isoform 8)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_044243"
FT VAR_SEQ 1047..1075
FT /note="REFSLAGGIWHGRAEGLQVGQDARVLGGE -> PPLPPPGELKIVLAAT
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11784712"
FT /id="VSP_011593"
FT VAR_SEQ 1047..1075
FT /note="REFSLAGGIWHGRAEGLQVGQDARVLGGE -> LCRVGRSHSRRRQGLAPGS
FT VLCFPPSSLSCDPAAPLPTASPALSDPDCLLT (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:11784712"
FT /id="VSP_011594"
FT VAR_SEQ 1047..1075
FT /note="REFSLAGGIWHGRAEGLQVGQDARVLGGE -> LQSHPSQQLPFHPPGN
FT (in isoform 9)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_047122"
FT MUTAGEN 361
FT /note="R->Q: No effect on localization to stress granules
FT under stress conditions."
FT /evidence="ECO:0000269|PubMed:25748791"
FT MUTAGEN 370
FT /note="R->Q: No effect on localization to stress granules
FT under stress conditions."
FT /evidence="ECO:0000269|PubMed:25748791"
FT CONFLICT 337
FT /note="R -> RG (in Ref. 8; AAB19201)"
FT /evidence="ECO:0000305"
FT CONFLICT 689
FT /note="T -> S (in Ref. 1; CAC38068/CAC38069/CAC38070/
FT CAC38071/CAC38072)"
FT /evidence="ECO:0000305"
FT CONFLICT 726
FT /note="P -> T (in Ref. 1; CAC38068/CAC38069/CAC38070/
FT CAC38071/CAC38072)"
FT /evidence="ECO:0000305"
FT CONFLICT 895
FT /note="Q -> QQ (in Ref. 6; AAH10239)"
FT /evidence="ECO:0000305"
FT CONFLICT Q8WWM7-2:1049
FT /note="L -> F (in Ref. 1; CAC38069)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1075 AA; 113374 MW; 805E8B02E853C20E CRC64;
MLKPQPLQQP SQPQQPPPTQ QAVARRPPGG TSPPNGGLPG PLATSAAPPG PPAAASPCLG
PVAAAGSGLR RGAEGILAPQ PPPPQQHQER PGAAAIGSAR GQSTGKGPPQ SPVFEGVYNN
SRMLHFLTAV VGSTCDVKVK NGTTYEGIFK TLSSKFELAV DAVHRKASEP AGGPRREDIV
DTMVFKPSDV MLVHFRNVDF NYATKDKFTD SAIAMNSKVN GEHKEKVLQR WEGGDSNSDD
YDLESDMSNG WDPNEMFKFN EENYGVKTTY DSSLSSYTVP LEKDNSEEFR QRELRAAQLA
REIESSPQYR LRIAMENDDG RTEEEKHSAV QRQGSGRESP SLASREGKYI PLPQRVREGP
RGGVRCSSSR GGRPGLSSLP PRGPHHLDNS SPGPGSEARG INGGPSRMSP KAQRPLRGAK
TLSSPSNRPS GETSVPPPPA VGRMYPPRSP KSAAPAPISA SCPEPPIGSA VPTSSASIPV
TSSVSDPGVG SISPASPKIS LAPTDVKELS TKEPGRTLEP QELARIAGKV PGLQNEQKRF
QLEELRKFGA QFKLQPSSSP ENSLDPFPPR ILKEEPKGKE KEVDGLLTSE PMGSPVSSKT
ESVSDKEDKP PLAPSGGTEG PEQPPPPCPS QTGSPPVGLI KGEDKDEGPV AEQVKKSTLN
PNAKEFNPTK PLLSVNKSTS TPTSPGPRTH STPSIPVLTA GQSGLYSPQY ISYIPQIHMG
PAVQAPQMYP YPVSNSVPGQ QGKYRGAKGS LPPQRSDQHQ PASAPPMMQA AAAAGPPLVA
ATPYSSYIPY NPQQFPGQPA MMQPMAHYPS QPVFAPMLQS NPRMLTSGSH PQAIVSSSTP
QYPSAEQPTP QALYATVHQS YPHHATQLHA HQPQPATTPT GSQPQSQHAA PSPVQHQAGQ
APHLGSGQPQ QNLYHPGALT GTPPSLPPGP SAQSPQSSFP QPAAVYAIHH QQLPHGFTNM
AHVTQAHVQT GITAAPPPHP GAPHPPQVML LHPPQSHGGP PQGAVPQSGV PALSASTPSP
YPYIGHPQGE QPGQAPGFPG GADDRIREFS LAGGIWHGRA EGLQVGQDAR VLGGE
