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Heterogeneous nuclear ribonucleoproteins A2/B1 (hnRNP A2/B1)

 ROA2_HUMAN              Reviewed;         353 AA.
P22626; A0A024RA27; A0A024RA61; A8K064; P22627; Q9UC98; Q9UDJ2;
01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
01-NOV-1991, sequence version 2.
27-SEP-2017, entry version 197.
RecName: Full=Heterogeneous nuclear ribonucleoproteins A2/B1;
Short=hnRNP A2/B1;
Name=HNRNPA2B1; Synonyms=HNRPA2B1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS B1 AND A2).
PubMed=2557628; DOI=10.1073/pnas.86.24.9788;
Burd C.G., Swanson M.S., Goerlach M., Dreyfuss G.;
"Primary structures of the heterogeneous nuclear ribonucleoprotein A2,
B1, and C2 proteins: a diversity of RNA binding proteins is generated
by small peptide inserts.";
Proc. Natl. Acad. Sci. U.S.A. 86:9788-9792(1989).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Liver;
PubMed=8029005; DOI=10.1093/nar/22.11.1996;
Biamonti G., Ruggiu M., Saccone S., Della Valle G., Riva S.;
"Two homologous genes, originated by duplication, encode the human
hnRNP proteins A2 and A1.";
Nucleic Acids Res. 22:1996-2002(1994).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=7789969; DOI=10.1016/0888-7543(95)80035-K;
Kozu T., Henrich B., Schaefer K.P.;
"Structure and expression of the gene (HNRPA2B1) encoding the human
hnRNP protein A2/B1.";
Genomics 25:365-371(1995).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B1).
TISSUE=Glial tumor;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[6]
PROTEIN SEQUENCE OF 1-12; 22-59; 63-89; 100-147; 153-185; 201-266 AND
326-350, ACETYLATION AT MET-1, METHYLATION AT LYS-104; ARG-203 AND
ARG-213, AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Ovarian carcinoma;
Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W.,
Dozynkiewicz M., Norman J.C.;
Submitted (JUN-2009) to UniProtKB.
[7]
PROTEIN SEQUENCE OF 22-38; 154-168; 174-185; 214-228 AND 326-350, AND
IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
Lubec G., Vishwanath V., Chen W.-Q., Sun Y.;
Submitted (DEC-2008) to UniProtKB.
[8]
PROTEIN SEQUENCE OF 39-46; 154-168; 204-228 AND 267-286.
TISSUE=Cervix carcinoma;
PubMed=1522214; DOI=10.1172/JCI115921;
Steiner G., Hartmuth K., Skriner K., Maurer-Fogy I., Sinski A.,
Thalmann E., Hassfeld W., Barta A., Smolen J.S.;
"Purification and partial sequencing of the nuclear autoantigen RA33
shows that it is indistinguishable from the A2 protein of the
heterogeneous nuclear ribonucleoprotein complex.";
J. Clin. Invest. 90:1061-1066(1992).
[9]
PROTEIN SEQUENCE OF 80-100.
TISSUE=Cervix carcinoma;
PubMed=7980541; DOI=10.1006/bbrc.1994.2526;
Prasad S., Walent J., Dritschilo A.;
"ADP-ribosylation of heterogeneous ribonucleoproteins in HeLa cells.";
Biochem. Biophys. Res. Commun. 204:772-779(1994).
[10]
PROTEIN SEQUENCE OF 100-107; 121-128 AND 174-180.
PubMed=3733753;
Kumar A., Willams K.R., Szer W.;
"Purification and domain structure of core hnRNP proteins A1 and A2
and their relationship to single-stranded DNA-binding proteins.";
J. Biol. Chem. 261:11266-11273(1986).
[11]
PROTEIN SEQUENCE OF 154-160; 204-212 AND 214-228.
PubMed=1699755; DOI=10.1002/elps.1150110703;
Bauw G., Rasmussen H.H., van den Bulcke M., van Damme J., Puype M.,
Gesser B., Celis J.E., Vandekerckhove J.;
"Two-dimensional gel electrophoresis, protein electroblotting and
microsequencing: a direct link between proteins and genes.";
Electrophoresis 11:528-536(1990).
[12]
FUNCTION, AND RNA-BINDING.
PubMed=10567417; DOI=10.1074/jbc.274.48.34389;
Munro T.P., Magee R.J., Kidd G.J., Carson J.H., Barbarese E.,
Smith L.M., Smith R.;
"Mutational analysis of a heterogeneous nuclear ribonucleoprotein A2
response element for RNA trafficking.";
J. Biol. Chem. 274:34389-34395(1999).
[13]
SUBCELLULAR LOCATION (ISOFORM A2), AND METHYLATION.
PubMed=10772824; DOI=10.1006/excr.2000.4827;
Nichols R.C., Wang X.W., Tang J., Hamilton B.J., High F.A.,
Herschman H.R., Rigby W.F.;
"The RGG domain in hnRNP A2 affects subcellular localization.";
Exp. Cell Res. 256:522-532(2000).
[14]
IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE
SPLICEOSOMAL C COMPLEX.
PubMed=11991638; DOI=10.1017/S1355838202021088;
Jurica M.S., Licklider L.J., Gygi S.P., Grigorieff N., Moore M.J.;
"Purification and characterization of native spliceosomes suitable for
three-dimensional structural analysis.";
RNA 8:426-439(2002).
[15]
FUNCTION (MICROBIAL INFECTION).
PubMed=15294897; DOI=10.1074/jbc.M404691200;
Beriault V., Clement J.F., Levesque K., Lebel C., Yong X., Chabot B.,
Cohen E.A., Cochrane A.W., Rigby W.F., Mouland A.J.;
"A late role for the association of hnRNP A2 with the HIV-1 hnRNP A2
response elements in genomic RNA, Gag, and Vpr localization.";
J. Biol. Chem. 279:44141-44153(2004).
[16]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-203, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=15782174; DOI=10.1038/nmeth715;
Ong S.E., Mittler G., Mann M.;
"Identifying and quantifying in vivo methylation sites by heavy methyl
SILAC.";
Nat. Methods 1:119-126(2004).
[17]
INTERACTION WITH CKAP5.
PubMed=15703215; DOI=10.1091/mbc.E04-08-0709;
Kosturko L.D., Maggipinto M.J., D'Sa C., Carson J.H., Barbarese E.;
"The microtubule-associated protein tumor overexpressed gene binds to
the RNA trafficking protein heterogeneous nuclear ribonucleoprotein
A2.";
Mol. Biol. Cell 16:1938-1947(2005).
[18]
FUNCTION (MICROBIAL INFECTION).
PubMed=17004321; DOI=10.1111/j.1600-0854.2006.00461.x;
Levesque K., Halvorsen M., Abrahamyan L., Chatel-Chaix L., Poupon V.,
Gordon H., DesGroseillers L., Gatignol A., Mouland A.J.;
"Trafficking of HIV-1 RNA is mediated by heterogeneous nuclear
ribonucleoprotein A2 expression and impacts on viral assembly.";
Traffic 7:1177-1193(2006).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-259 AND SER-341, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17924679; DOI=10.1021/pr070152u;
Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
"Improved titanium dioxide enrichment of phosphopeptides from HeLa
cells and high confident phosphopeptide identification by cross-
validation of MS/MS and MS/MS/MS spectra.";
J. Proteome Res. 6:4150-4162(2007).
[20]
IDENTIFICATION IN A MRNP GRANULE COMPLEX, INTERACTION WITH IGF2BP1,
SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=17289661; DOI=10.1074/mcp.M600346-MCP200;
Joeson L., Vikesaa J., Krogh A., Nielsen L.K., Hansen T., Borup R.,
Johnsen A.H., Christiansen J., Nielsen F.C.;
"Molecular composition of IMP1 ribonucleoprotein granules.";
Mol. Cell. Proteomics 6:798-811(2007).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-259 AND SER-341, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18220336; DOI=10.1021/pr0705441;
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
efficient phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-259, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-259; SER-341 AND
SER-344, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[24]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[25]
REVIEW.
PubMed=19099192; DOI=10.1007/s00018-008-8532-1;
He Y., Smith R.;
"Nuclear functions of heterogeneous nuclear ribonucleoproteins A/B.";
Cell. Mol. Life Sci. 66:1239-1256(2009).
[26]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-259, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[27]
INTERACTION WITH TARDBP.
PubMed=19429692; DOI=10.1093/nar/gkp342;
D'Ambrogio A., Buratti E., Stuani C., Guarnaccia C., Romano M.,
Ayala Y.M., Baralle F.E.;
"Functional mapping of the interaction between TDP-43 and hnRNP A2 in
vivo.";
Nucleic Acids Res. 37:4116-4126(2009).
[28]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-85; SER-212; SER-259 AND
SER-344, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[29]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-168 AND LYS-173, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[30]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-85; SER-149; SER-212;
SER-225; SER-231; SER-259; SER-341 AND SER-344, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[31]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[32]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-212; SER-225; SER-231;
SER-236; SER-259; SER-324; TYR-331 AND SER-344, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[33]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22905912; DOI=10.1021/pr300539b;
Rosenow A., Noben J.P., Jocken J., Kallendrusch S.,
Fischer-Posovszky P., Mariman E.C., Renes J.;
"Resveratrol-induced changes of the human adipocyte secretion
profile.";
J. Proteome Res. 11:4733-4743(2012).
[34]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[35]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-4; SER-29; THR-140;
THR-159; THR-176; SER-189; SER-201; SER-212; SER-225; SER-259;
SER-324; TYR-331; SER-341 AND SER-344, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[36]
FUNCTION, SUBCELLULAR LOCATION, AND SUMOYLATION.
PubMed=24356509; DOI=10.1038/ncomms3980;
Villarroya-Beltri C., Gutierrez-Vazquez C., Sanchez-Cabo F.,
Perez-Hernandez D., Vazquez J., Martin-Cofreces N.,
Martinez-Herrera D.J., Pascual-Montano A., Mittelbrunn M.,
Sanchez-Madrid F.;
"Sumoylated hnRNPA2B1 controls the sorting of miRNAs into exosomes
through binding to specific motifs.";
Nat. Commun. 4:2980-2980(2013).
[37]
SUBCELLULAR LOCATION (ISOFORM A2).
PubMed=24098712; DOI=10.1371/journal.pone.0075669;
Friend L.R., Landsberg M.J., Nouwens A.S., Wei Y., Rothnagel J.A.,
Smith R.;
"Arginine methylation of hnRNP A2 does not directly govern its
subcellular localization.";
PLoS ONE 8:E75669-E75669(2013).
[38]
INTERACTION WITH C9ORF72.
PubMed=24549040; DOI=10.1093/hmg/ddu068;
Farg M.A., Sundaramoorthy V., Sultana J.M., Yang S., Atkinson R.A.,
Levina V., Halloran M.A., Gleeson P.A., Blair I.P., Soo K.Y.,
King A.E., Atkin J.D.;
"C9ORF72, implicated in amytrophic lateral sclerosis and
frontotemporal dementia, regulates endosomal trafficking.";
Hum. Mol. Genet. 23:3579-3595(2014).
[39]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29; SER-85; SER-212;
SER-225; SER-231; SER-341; SER-344 AND TYR-347, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[40]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-203; ARG-213; ARG-228;
ARG-238; ARG-266; ARG-325 AND ARG-350, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Colon carcinoma;
PubMed=24129315; DOI=10.1074/mcp.O113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
Vemulapalli V., Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
[41]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-120 AND LYS-186, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25218447; DOI=10.1038/nsmb.2890;
Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
Vertegaal A.C.;
"Uncovering global SUMOylation signaling networks in a site-specific
manner.";
Nat. Struct. Mol. Biol. 21:927-936(2014).
[42]
DOMAIN, AND MUTAGENESIS OF PHE-207; PHE-209; PHE-219; PHE-227;
TYR-234; PHE-240; TYR-244; TYR-247; PHE-256; TYR-262; TYR-269;
TYR-276; TYR-283; TYR-287; TYR-290; TYR-295; TYR-300; PHE-303;
TYR-306; TYR-313; PHE-321; TYR-331; TYR-336; TYR-347 AND TYR-353.
PubMed=26544936; DOI=10.1016/j.cell.2015.10.040;
Xiang S., Kato M., Wu L.C., Lin Y., Ding M., Zhang Y., Yu Y.,
McKnight S.L.;
"The LC domain of hnRNPA2 adopts similar conformations in hydrogel
polymers, liquid-like droplets, and nuclei.";
Cell 163:829-839(2015).
[43]
FUNCTION, MIRNA-BINDING, AND INTERACTION WITH DGCR8.
PubMed=26321680; DOI=10.1016/j.cell.2015.08.011;
Alarcon C.R., Goodarzi H., Lee H., Liu X., Tavazoie S., Tavazoie S.F.;
"HNRNPA2B1 is a mediator of m(6)A-dependent nuclear RNA processing
events.";
Cell 162:1299-1308(2015).
[44]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-120, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25755297; DOI=10.1074/mcp.O114.044792;
Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
Vertegaal A.C.;
"System-wide analysis of SUMOylation dynamics in response to
replication stress reveals novel small ubiquitin-like modified target
proteins and acceptor lysines relevant for genome stability.";
Mol. Cell. Proteomics 14:1419-1434(2015).
[45]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[46]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-22; LYS-104; LYS-112;
LYS-120; LYS-137; LYS-152; LYS-168 AND LYS-173, SUMOYLATION [LARGE
SCALE ANALYSIS] AT LYS-5 (ISOFORM A2), AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[47]
STRUCTURE BY NMR OF 1-103.
RIKEN structural genomics initiative (RSGI);
"Solution structure of RRM domain in heterogeneous nuclear
ribonucleoproteins A2/B1.";
Submitted (NOV-2005) to the PDB data bank.
[48]
VARIANT IBMPFD2 VAL-302.
PubMed=23455423; DOI=10.1038/nature11922;
Kim H.J., Kim N.C., Wang Y.D., Scarborough E.A., Moore J., Diaz Z.,
MacLea K.S., Freibaum B., Li S., Molliex A., Kanagaraj A.P.,
Carter R., Boylan K.B., Wojtas A.M., Rademakers R., Pinkus J.L.,
Greenberg S.A., Trojanowski J.Q., Traynor B.J., Smith B.N., Topp S.,
Gkazi A.S., Miller J., Shaw C.E., Kottlors M., Kirschner J.,
Pestronk A., Li Y.R., Ford A.F., Gitler A.D., Benatar M., King O.D.,
Kimonis V.E., Ross E.D., Weihl C.C., Shorter J., Taylor J.P.;
"Mutations in prion-like domains in hnRNPA2B1 and hnRNPA1 cause
multisystem proteinopathy and ALS.";
Nature 495:467-473(2013).
-!- FUNCTION: Heterogeneous nuclear ribonucleoprotein (hnRNP) that
associates with nascent pre-mRNAs, packaging them into hnRNP
particles. The hnRNP particle arrangement on nascent hnRNA is non-
random and sequence-dependent and serves to condense and stabilize
the transcripts and minimize tangling and knotting. Packaging
plays a role in various processes such as transcription, pre-mRNA
processing, RNA nuclear export, subcellular location, mRNA
translation and stability of mature mRNAs (PubMed:19099192). Forms
hnRNP particles with at least 20 other different hnRNP and
heterogeneous nuclear RNA in the nucleus. Involved in transport of
specific mRNAs to the cytoplasm in oligodendrocytes and neurons:
acts by specifically recognizing and binding the A2RE (21
nucleotide hnRNP A2 response element) or the A2RE11 (derivative 11
nucleotide oligonucleotide) sequence motifs present on some mRNAs,
and promotes their transport to the cytoplasm (PubMed:10567417).
Specifically binds single-stranded telomeric DNA sequences,
protecting telomeric DNA repeat against endonuclease digestion (By
similarity). Also binds other RNA molecules, such as primary miRNA
(pri-miRNAs): acts as a nuclear 'reader' of the N6-methyladenosine
(m6A) mark by specifically recognizing and binding a subset of
nuclear m6A-containing pri-miRNAs. Binding to m6A-containing pri-
miRNAs promotes pri-miRNA processing by enhancing binding of DGCR8
to pri-miRNA transcripts (PubMed:26321680). Involved in miRNA
sorting into exosomes following sumoylation, possibly by binding
(m6A)-containing pre-miRNAs (PubMed:24356509). Acts as a regulator
of efficiency of mRNA splicing, possibly by binding to m6A-
containing pre-mRNAs (PubMed:26321680).
{ECO:0000250|UniProtKB:A7VJC2, ECO:0000269|PubMed:10567417,
ECO:0000269|PubMed:24356509, ECO:0000269|PubMed:26321680,
ECO:0000303|PubMed:19099192}.
-!- FUNCTION: (Microbial infection) Involved in the transport of HIV-1
genomic RNA out of the nucleus, to the microtubule organizing
center (MTOC), and then from the MTOC to the cytoplasm: acts by
specifically recognizing and binding the A2RE (21 nucleotide hnRNP
A2 response element) sequence motifs present on HIV-1 genomic RNA,
and promotes its transport. {ECO:0000269|PubMed:15294897,
ECO:0000269|PubMed:17004321}.
-!- SUBUNIT: Identified in the spliceosome C complex
(PubMed:11991638). Identified in a IGF2BP1-dependent mRNP granule
complex containing untranslated mRNAs (PubMed:17289661). Interacts
with IGF2BP1 (PubMed:17289661). Interacts with C9orf72
(PubMed:24549040). Interacts with DGCR8 (PubMed:26321680).
Interacts with TARDBP (PubMed:19429692). Interacts with CKAP5
(PubMed:15703215). {ECO:0000269|PubMed:11991638,
ECO:0000269|PubMed:15703215, ECO:0000269|PubMed:17289661,
ECO:0000269|PubMed:19429692, ECO:0000269|PubMed:24549040,
ECO:0000269|PubMed:26321680}.
-!- INTERACTION:
Q9HA38:ZMAT3; NbExp=3; IntAct=EBI-299649, EBI-2548480;
-!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
{ECO:0000269|PubMed:17289661}. Cytoplasmic granule
{ECO:0000269|PubMed:17289661, ECO:0000269|PubMed:24356509}.
Secreted, exosome {ECO:0000269|PubMed:24356509}. Note=Localized in
cytoplasmic mRNP granules containing untranslated mRNAs
(PubMed:17289661). Component of ribonucleosomes (PubMed:17289661).
Not found in the nucleolus (PubMed:17289661). Found in exosomes
follwong sumoylation (PubMed:24356509).
{ECO:0000269|PubMed:17289661, ECO:0000269|PubMed:24356509}.
-!- SUBCELLULAR LOCATION: Isoform A2: Nucleus
{ECO:0000269|PubMed:10772824, ECO:0000269|PubMed:17289661,
ECO:0000269|PubMed:24098712}. Cytoplasm
{ECO:0000269|PubMed:10772824, ECO:0000269|PubMed:17289661}.
Note=Predominantly nucleoplasmic, however is also found in the
cytoplasm of cells in some tissues (PubMed:17289661).
{ECO:0000269|PubMed:17289661}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=B1; Synonyms=hnRNP B1;
IsoId=P22626-1; Sequence=Displayed;
Name=A2; Synonyms=hnRNP A2;
IsoId=P22626-2; Sequence=VSP_005830;
Note=Contains a glycyl lysine isopeptide (Lys-Gly) (interchain
with G-Cter in SUMO2) at position 5.
{ECO:0000244|PubMed:28112733};
-!- DOMAIN: The low complexity (LC) region is intrinsically
disordered. When incubated at high concentration, it is able to
polymerize into labile, amyloid-like fibers and form cross-beta
polymerization structures, probably driving the formation of
hydrogels. In contrast to irreversible, pathogenic amyloids, the
fibers polymerized from LC regions disassemble upon dilution. A
number of evidences suggest that formation of cross-beta
structures by LC regions mediate the formation of RNA granules,
liquid-like droplets, and hydrogels.
{ECO:0000269|PubMed:26544936}.
-!- PTM: Sumoylated in exosomes, promoting miRNAs-binding.
{ECO:0000269|PubMed:24356509}.
-!- PTM: Asymmetric dimethylation at Arg-266 constitutes the major
methylation site (By similarity). According to a report,
methylation affects subcellular location and promotes nuclear
localization (PubMed:10772824). According to another report,
methylation at Arg-266 does not influence nucleocytoplasmic
shuttling (By similarity). {ECO:0000250|UniProtKB:A7VJC2,
ECO:0000269|PubMed:10772824}.
-!- DISEASE: Inclusion body myopathy with early-onset Paget disease
with or without frontotemporal dementia 2 (IBMPFD2) [MIM:615422]:
An autosomal dominant disease characterized by disabling muscle
weakness clinically resembling to limb girdle muscular dystrophy,
osteolytic bone lesions consistent with Paget disease, and
premature frontotemporal dementia. Clinical features show
incomplete penetrance. {ECO:0000269|PubMed:23455423}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-----------------------------------------------------------------------
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EMBL; M29064; AAA60271.1; -; mRNA.
EMBL; M29065; AAA36574.1; -; mRNA.
EMBL; U09123; AAB60650.1; -; Genomic_DNA.
EMBL; U09120; AAB60650.1; JOINED; Genomic_DNA.
EMBL; U09121; AAB60650.1; JOINED; Genomic_DNA.
EMBL; U09122; AAB60650.1; JOINED; Genomic_DNA.
EMBL; D28877; BAA06031.1; -; Genomic_DNA.
EMBL; D28877; BAA06032.1; -; Genomic_DNA.
EMBL; AK289429; BAF82118.1; -; mRNA.
EMBL; CH471073; EAW93835.1; -; Genomic_DNA.
EMBL; CH471073; EAW93836.1; -; Genomic_DNA.
EMBL; CH471073; EAW93837.1; -; Genomic_DNA.
EMBL; CH471073; EAW93839.1; -; Genomic_DNA.
CCDS; CCDS43557.1; -. [P22626-1]
CCDS; CCDS5397.1; -. [P22626-2]
PIR; A56845; B34504.
RefSeq; NP_002128.1; NM_002137.3. [P22626-2]
RefSeq; NP_112533.1; NM_031243.2. [P22626-1]
RefSeq; XP_005249786.1; XM_005249729.1. [P22626-1]
RefSeq; XP_016867598.1; XM_017012109.1. [P22626-2]
RefSeq; XP_016867599.1; XM_017012110.1. [P22626-2]
UniGene; Hs.487774; -.
PDB; 1X4B; NMR; -; A=1-103.
PDB; 5EN1; X-ray; 2.58 A; A=12-195.
PDB; 5HO4; X-ray; 1.85 A; A=15-193.
PDBsum; 1X4B; -.
PDBsum; 5EN1; -.
PDBsum; 5HO4; -.
ProteinModelPortal; P22626; -.
SMR; P22626; -.
BioGrid; 109422; 196.
CORUM; P22626; -.
DIP; DIP-32877N; -.
IntAct; P22626; 102.
MINT; MINT-4998934; -.
STRING; 9606.ENSP00000346694; -.
iPTMnet; P22626; -.
PhosphoSitePlus; P22626; -.
SwissPalm; P22626; -.
BioMuta; HNRNPA2B1; -.
DMDM; 133257; -.
REPRODUCTION-2DPAGE; IPI00396378; -.
REPRODUCTION-2DPAGE; IPI00414696; -.
REPRODUCTION-2DPAGE; P22626; -.
SWISS-2DPAGE; P22626; -.
UCD-2DPAGE; P22626; -.
EPD; P22626; -.
MaxQB; P22626; -.
PaxDb; P22626; -.
PeptideAtlas; P22626; -.
PRIDE; P22626; -.
TopDownProteomics; P22626-1; -. [P22626-1]
TopDownProteomics; P22626-2; -. [P22626-2]
Ensembl; ENST00000354667; ENSP00000346694; ENSG00000122566. [P22626-1]
Ensembl; ENST00000356674; ENSP00000349101; ENSG00000122566. [P22626-2]
Ensembl; ENST00000360787; ENSP00000354021; ENSG00000122566. [P22626-1]
GeneID; 3181; -.
KEGG; hsa:3181; -.
UCSC; uc003sxr.5; human. [P22626-1]
CTD; 3181; -.
DisGeNET; 3181; -.
EuPathDB; HostDB:ENSG00000122566.20; -.
GeneCards; HNRNPA2B1; -.
HGNC; HGNC:5033; HNRNPA2B1.
HPA; CAB012403; -.
HPA; HPA001666; -.
HPA; HPA005812; -.
HPA; HPA065537; -.
MalaCards; HNRNPA2B1; -.
MIM; 600124; gene.
MIM; 615422; phenotype.
neXtProt; NX_P22626; -.
OpenTargets; ENSG00000122566; -.
Orphanet; 52430; Inclusion body myopathy with Paget disease of bone and frontotemporal dementia.
PharmGKB; PA162391140; -.
eggNOG; KOG0118; Eukaryota.
eggNOG; COG0724; LUCA.
GeneTree; ENSGT00760000118873; -.
HOGENOM; HOG000234442; -.
HOVERGEN; HBG002295; -.
InParanoid; P22626; -.
KO; K13158; -.
OMA; QDEHTID; -.
OrthoDB; EOG091G1CPI; -.
PhylomeDB; P22626; -.
TreeFam; TF351342; -.
Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
Reactome; R-HSA-72203; Processing of Capped Intron-Containing Pre-mRNA.
Reactome; R-HSA-8950505; Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulation.
SIGNOR; P22626; -.
ChiTaRS; HNRNPA2B1; human.
EvolutionaryTrace; P22626; -.
GeneWiki; HNRPA2B1; -.
GenomeRNAi; 3181; -.
PMAP-CutDB; P22626; -.
PRO; PR:P22626; -.
Proteomes; UP000005640; Chromosome 7.
Bgee; ENSG00000122566; -.
CleanEx; HS_HNRNPA2B1; -.
ExpressionAtlas; P22626; baseline and differential.
Genevisible; P22626; HS.
GO; GO:0015030; C:Cajal body; ISS:BHF-UCL.
GO; GO:0071013; C:catalytic step 2 spliceosome; IDA:UniProtKB.
GO; GO:0000781; C:chromosome, telomeric region; ISS:BHF-UCL.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0030529; C:intracellular ribonucleoprotein complex; IDA:UniProtKB.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0016363; C:nuclear matrix; ISS:BHF-UCL.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005681; C:spliceosomal complex; IDA:HGNC.
GO; GO:0098505; F:G-rich strand telomeric DNA binding; ISS:BHF-UCL.
GO; GO:0035198; F:miRNA binding; IDA:UniProtKB.
GO; GO:0003730; F:mRNA 3'-UTR binding; IDA:UniProtKB.
GO; GO:1990247; F:N6-methyladenosine-containing RNA binding; IDA:UniProtKB.
GO; GO:0097157; F:pre-mRNA intronic binding; IEA:Ensembl.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0043047; F:single-stranded telomeric DNA binding; IDA:HGNC.
GO; GO:0044806; P:G-quadruplex DNA unwinding; ISS:BHF-UCL.
GO; GO:0035722; P:interleukin-12-mediated signaling pathway; TAS:Reactome.
GO; GO:1990428; P:miRNA transport; IDA:UniProtKB.
GO; GO:0006406; P:mRNA export from nucleus; IDA:UniProtKB.
GO; GO:0006397; P:mRNA processing; IDA:HGNC.
GO; GO:0000398; P:mRNA splicing, via spliceosome; IMP:UniProtKB.
GO; GO:0048025; P:negative regulation of mRNA splicing, via spliceosome; IEA:Ensembl.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IEA:Ensembl.
GO; GO:1905663; P:positive regulation of telomerase RNA reverse transcriptase activity; ISS:BHF-UCL.
GO; GO:1904358; P:positive regulation of telomere maintenance via telomere lengthening; ISS:BHF-UCL.
GO; GO:0031053; P:primary miRNA processing; IDA:UniProtKB.
GO; GO:0016070; P:RNA metabolic process; TAS:Reactome.
GO; GO:0050658; P:RNA transport; IDA:HGNC.
CDD; cd12762; RRM1_hnRNPA2B1; 1.
InterPro; IPR034489; hnRNP_A2/B1.
InterPro; IPR034486; hnRNPA2B1_RRM1.
InterPro; IPR000504; RRM_dom.
PANTHER; PTHR24012:SF539; PTHR24012:SF539; 1.
Pfam; PF00076; RRM_1; 2.
SMART; SM00360; RRM; 2.
SUPFAM; SSF54928; SSF54928; 2.
PROSITE; PS50102; RRM; 2.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Complete proteome;
Cytoplasm; Direct protein sequencing; Disease mutation;
Isopeptide bond; Methylation; mRNA processing; mRNA splicing;
mRNA transport; Nucleus; Phosphoprotein; Reference proteome; Repeat;
Ribonucleoprotein; RNA-binding; Secreted; Spliceosome; Transport;
Ubl conjugation.
CHAIN 1 353 Heterogeneous nuclear ribonucleoproteins
A2/B1.
/FTId=PRO_0000081836.
DOMAIN 21 104 RRM 1. {ECO:0000255|PROSITE-
ProRule:PRU00176}.
DOMAIN 112 191 RRM 2. {ECO:0000255|PROSITE-
ProRule:PRU00176}.
REGION 193 353 Low complexity (LC) region.
{ECO:0000269|PubMed:26544936}.
REGION 308 347 Nuclear targeting sequence.
{ECO:0000250}.
MOTIF 9 15 Nuclear localization signal.
{ECO:0000255}.
COMPBIAS 202 353 Gly-rich.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000244|PubMed:22814378,
ECO:0000269|Ref.6}.
MOD_RES 4 4 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 29 29 Phosphoserine.
{ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 38 38 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:O88569}.
MOD_RES 85 85 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:24275569}.
MOD_RES 104 104 N6,N6-dimethyllysine; alternate.
{ECO:0000269|Ref.6}.
MOD_RES 140 140 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 149 149 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 159 159 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 168 168 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:19608861}.
MOD_RES 173 173 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:19608861}.
MOD_RES 176 176 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 189 189 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 201 201 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 203 203 Asymmetric dimethylarginine; alternate.
{ECO:0000250|UniProtKB:O88569}.
MOD_RES 203 203 Dimethylated arginine; alternate.
{ECO:0000269|Ref.6}.
MOD_RES 203 203 Omega-N-methylarginine; alternate.
{ECO:0000244|PubMed:15782174,
ECO:0000244|PubMed:24129315,
ECO:0000269|Ref.6}.
MOD_RES 212 212 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 213 213 Asymmetric dimethylarginine; alternate.
{ECO:0000250|UniProtKB:O88569}.
MOD_RES 213 213 Dimethylated arginine; alternate.
{ECO:0000269|Ref.6}.
MOD_RES 213 213 Omega-N-methylarginine; alternate.
{ECO:0000244|PubMed:24129315,
ECO:0000269|Ref.6}.
MOD_RES 225 225 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 228 228 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 231 231 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:24275569}.
MOD_RES 236 236 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 238 238 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 259 259 Phosphoserine.
{ECO:0000244|PubMed:17924679,
ECO:0000244|PubMed:18220336,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 266 266 Asymmetric dimethylarginine; alternate.
{ECO:0000250|UniProtKB:A7VJC2}.
MOD_RES 266 266 Omega-N-methylarginine; alternate.
{ECO:0000244|PubMed:24129315}.
MOD_RES 324 324 Phosphoserine.
{ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 325 325 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 331 331 Phosphotyrosine.
{ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 341 341 Phosphoserine.
{ECO:0000244|PubMed:17924679,
ECO:0000244|PubMed:18220336,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 344 344 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 347 347 Phosphotyrosine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 350 350 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
CROSSLNK 22 22 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 104 104 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:28112733}.
CROSSLNK 112 112 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 120 120 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:28112733}.
CROSSLNK 137 137 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 152 152 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 168 168 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:28112733}.
CROSSLNK 173 173 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:28112733}.
CROSSLNK 186 186 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447}.
VAR_SEQ 3 14 Missing (in isoform A2).
{ECO:0000303|PubMed:2557628}.
/FTId=VSP_005830.
VARIANT 302 302 D -> V (in IBMPFD2; dbSNP:rs397515326).
{ECO:0000269|PubMed:23455423}.
/FTId=VAR_070591.
MUTAGEN 207 207 F->S: Does not affect hydrogel-binding.
{ECO:0000269|PubMed:26544936}.
MUTAGEN 209 209 F->S: Does not affect hydrogel-binding.
{ECO:0000269|PubMed:26544936}.
MUTAGEN 219 219 F->S: Does not affect hydrogel-binding.
{ECO:0000269|PubMed:26544936}.
MUTAGEN 227 227 F->S: Does not affect hydrogel-binding.
{ECO:0000269|PubMed:26544936}.
MUTAGEN 234 234 Y->S: Does not affect hydrogel-binding.
{ECO:0000269|PubMed:26544936}.
MUTAGEN 240 240 F->S: Does not affect hydrogel-binding.
{ECO:0000269|PubMed:26544936}.
MUTAGEN 244 244 Y->S: Does not affect hydrogel-binding.
{ECO:0000269|PubMed:26544936}.
MUTAGEN 247 247 Y->S: Slightly affects hydrogel-binding.
{ECO:0000269|PubMed:26544936}.
MUTAGEN 256 256 F->S: Does not affect hydrogel-binding.
{ECO:0000269|PubMed:26544936}.
MUTAGEN 262 262 Y->S: Slightly affects hydrogel-binding.
{ECO:0000269|PubMed:26544936}.
MUTAGEN 269 269 Y->S: Does not affect hydrogel-binding.
{ECO:0000269|PubMed:26544936}.
MUTAGEN 276 276 Y->S: Impairs hydrogel-binding.
{ECO:0000269|PubMed:26544936}.
MUTAGEN 283 283 Y->S: Slightly affects hydrogel-binding.
{ECO:0000269|PubMed:26544936}.
MUTAGEN 287 287 Y->S: Does not affect hydrogel-binding.
{ECO:0000269|PubMed:26544936}.
MUTAGEN 290 290 Y->S: Impairs hydrogel-binding.
{ECO:0000269|PubMed:26544936}.
MUTAGEN 295 295 Y->S: Impairs hydrogel-binding.
{ECO:0000269|PubMed:26544936}.
MUTAGEN 300 300 Y->S: Slightly affects hydrogel-binding.
{ECO:0000269|PubMed:26544936}.
MUTAGEN 303 303 F->S: Impairs hydrogel-binding.
{ECO:0000269|PubMed:26544936}.
MUTAGEN 306 306 Y->S: Slightly affects hydrogel-binding.
{ECO:0000269|PubMed:26544936}.
MUTAGEN 313 313 Y->S: Slightly affects hydrogel-binding.
{ECO:0000269|PubMed:26544936}.
MUTAGEN 321 321 F->S: Impairs hydrogel-binding.
{ECO:0000269|PubMed:26544936}.
MUTAGEN 331 331 Y->S: Impairs hydrogel-binding.
{ECO:0000269|PubMed:26544936}.
MUTAGEN 336 336 Y->S: Slightly affects hydrogel-binding.
{ECO:0000269|PubMed:26544936}.
MUTAGEN 347 347 Y->S: Does not affect hydrogel-binding.
{ECO:0000269|PubMed:26544936}.
MUTAGEN 353 353 Y->S: Does not affect hydrogel-binding.
{ECO:0000269|PubMed:26544936}.
CONFLICT 205 205 G -> S (in Ref. 4; BAF82118).
{ECO:0000305}.
HELIX 18 21 {ECO:0000244|PDB:5HO4}.
STRAND 22 27 {ECO:0000244|PDB:5HO4}.
HELIX 34 41 {ECO:0000244|PDB:5HO4}.
HELIX 42 44 {ECO:0000244|PDB:5HO4}.
STRAND 47 54 {ECO:0000244|PDB:5HO4}.
TURN 56 58 {ECO:0000244|PDB:5HO4}.
STRAND 61 71 {ECO:0000244|PDB:5HO4}.
HELIX 72 80 {ECO:0000244|PDB:5HO4}.
STRAND 83 86 {ECO:0000244|PDB:1X4B}.
STRAND 92 95 {ECO:0000244|PDB:5HO4}.
HELIX 99 101 {ECO:0000244|PDB:5HO4}.
TURN 105 108 {ECO:0000244|PDB:5HO4}.
STRAND 112 117 {ECO:0000244|PDB:5HO4}.
TURN 120 122 {ECO:0000244|PDB:5EN1}.
HELIX 125 132 {ECO:0000244|PDB:5HO4}.
HELIX 133 135 {ECO:0000244|PDB:5HO4}.
STRAND 138 145 {ECO:0000244|PDB:5HO4}.
TURN 147 149 {ECO:0000244|PDB:5HO4}.
STRAND 152 163 {ECO:0000244|PDB:5HO4}.
HELIX 164 169 {ECO:0000244|PDB:5HO4}.
STRAND 174 177 {ECO:0000244|PDB:5HO4}.
STRAND 180 186 {ECO:0000244|PDB:5HO4}.
TURN 190 192 {ECO:0000244|PDB:5HO4}.
SEQUENCE 353 AA; 37430 MW; 4C2560A3D8E99D62 CRC64;
MEKTLETVPL ERKKREKEQF RKLFIGGLSF ETTEESLRNY YEQWGKLTDC VVMRDPASKR
SRGFGFVTFS SMAEVDAAMA ARPHSIDGRV VEPKRAVARE ESGKPGAHVT VKKLFVGGIK
EDTEEHHLRD YFEEYGKIDT IEIITDRQSG KKRGFGFVTF DDHDPVDKIV LQKYHTINGH
NAEVRKALSR QEMQEVQSSR SGRGGNFGFG DSRGGGGNFG PGPGSNFRGG SDGYGSGRGF
GDGYNGYGGG PGGGNFGGSP GYGGGRGGYG GGGPGYGNQG GGYGGGYDNY GGGNYGSGNY
NDFGNYNQQP SNYGPMKSGN FGGSRNMGGP YGGGNYGPGG SGGSGGYGGR SRY


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