ROA2_HUMAN
ID ROA2_HUMAN Reviewed; 353 AA.
AC P22626; A0A024RA27; A0A024RA61; A8K064; P22627; Q9UC98; Q9UDJ2;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 2.
DT 03-AUG-2022, entry version 230.
DE RecName: Full=Heterogeneous nuclear ribonucleoproteins A2/B1;
DE Short=hnRNP A2/B1;
GN Name=HNRNPA2B1; Synonyms=HNRPA2B1;
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 B1 AND A2).
RX PubMed=2557628; DOI=10.1073/pnas.86.24.9788;
RA Burd C.G., Swanson M.S., Goerlach M., Dreyfuss G.;
RT "Primary structures of the heterogeneous nuclear ribonucleoprotein A2, B1,
RT and C2 proteins: a diversity of RNA binding proteins is generated by small
RT peptide inserts.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:9788-9792(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Liver;
RX PubMed=8029005; DOI=10.1093/nar/22.11.1996;
RA Biamonti G., Ruggiu M., Saccone S., Della Valle G., Riva S.;
RT "Two homologous genes, originated by duplication, encode the human hnRNP
RT proteins A2 and A1.";
RL Nucleic Acids Res. 22:1996-2002(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7789969; DOI=10.1016/0888-7543(95)80035-k;
RA Kozu T., Henrich B., Schaefer K.P.;
RT "Structure and expression of the gene (HNRPA2B1) encoding the human hnRNP
RT protein A2/B1.";
RL Genomics 25:365-371(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B1).
RC TISSUE=Glial tumor;
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].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP PROTEIN SEQUENCE OF 1-12; 22-59; 63-89; 100-147; 153-185; 201-266 AND
RP 326-350, ACETYLATION AT MET-1, METHYLATION AT LYS-104; ARG-203 AND ARG-213,
RP AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Ovarian carcinoma;
RA Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W.,
RA Dozynkiewicz M., Norman J.C.;
RL Submitted (JUN-2009) to UniProtKB.
RN [7]
RP PROTEIN SEQUENCE OF 22-38; 154-168; 174-185; 214-228 AND 326-350, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
RA Lubec G., Vishwanath V., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [8]
RP PROTEIN SEQUENCE OF 39-46; 154-168; 204-228 AND 267-286.
RC TISSUE=Cervix carcinoma;
RX PubMed=1522214; DOI=10.1172/jci115921;
RA Steiner G., Hartmuth K., Skriner K., Maurer-Fogy I., Sinski A.,
RA Thalmann E., Hassfeld W., Barta A., Smolen J.S.;
RT "Purification and partial sequencing of the nuclear autoantigen RA33 shows
RT that it is indistinguishable from the A2 protein of the heterogeneous
RT nuclear ribonucleoprotein complex.";
RL J. Clin. Invest. 90:1061-1066(1992).
RN [9]
RP PROTEIN SEQUENCE OF 80-100.
RC TISSUE=Cervix carcinoma;
RX PubMed=7980541; DOI=10.1006/bbrc.1994.2526;
RA Prasad S., Walent J., Dritschilo A.;
RT "ADP-ribosylation of heterogeneous ribonucleoproteins in HeLa cells.";
RL Biochem. Biophys. Res. Commun. 204:772-779(1994).
RN [10]
RP PROTEIN SEQUENCE OF 100-107; 121-128 AND 174-180.
RX PubMed=3733753; DOI=10.1016/s0021-9258(18)67378-8;
RA Kumar A., Willams K.R., Szer W.;
RT "Purification and domain structure of core hnRNP proteins A1 and A2 and
RT their relationship to single-stranded DNA-binding proteins.";
RL J. Biol. Chem. 261:11266-11273(1986).
RN [11]
RP PROTEIN SEQUENCE OF 154-160; 204-212 AND 214-228.
RX PubMed=1699755; DOI=10.1002/elps.1150110703;
RA Bauw G., Rasmussen H.H., van den Bulcke M., van Damme J., Puype M.,
RA Gesser B., Celis J.E., Vandekerckhove J.;
RT "Two-dimensional gel electrophoresis, protein electroblotting and
RT microsequencing: a direct link between proteins and genes.";
RL Electrophoresis 11:528-536(1990).
RN [12]
RP FUNCTION, AND RNA-BINDING.
RX PubMed=10567417; DOI=10.1074/jbc.274.48.34389;
RA Munro T.P., Magee R.J., Kidd G.J., Carson J.H., Barbarese E., Smith L.M.,
RA Smith R.;
RT "Mutational analysis of a heterogeneous nuclear ribonucleoprotein A2
RT response element for RNA trafficking.";
RL J. Biol. Chem. 274:34389-34395(1999).
RN [13]
RP SUBCELLULAR LOCATION (ISOFORM A2), AND METHYLATION.
RX PubMed=10772824; DOI=10.1006/excr.2000.4827;
RA Nichols R.C., Wang X.W., Tang J., Hamilton B.J., High F.A., Herschman H.R.,
RA Rigby W.F.;
RT "The RGG domain in hnRNP A2 affects subcellular localization.";
RL Exp. Cell Res. 256:522-532(2000).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE SPLICEOSOMAL
RP C COMPLEX.
RX PubMed=11991638; DOI=10.1017/s1355838202021088;
RA Jurica M.S., Licklider L.J., Gygi S.P., Grigorieff N., Moore M.J.;
RT "Purification and characterization of native spliceosomes suitable for
RT three-dimensional structural analysis.";
RL RNA 8:426-439(2002).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Lymphoblast;
RX PubMed=14654843; DOI=10.1038/nature02166;
RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.;
RT "Proteomic characterization of the human centrosome by protein correlation
RT profiling.";
RL Nature 426:570-574(2003).
RN [16]
RP FUNCTION (MICROBIAL INFECTION).
RX PubMed=15294897; DOI=10.1074/jbc.m404691200;
RA Beriault V., Clement J.F., Levesque K., Lebel C., Yong X., Chabot B.,
RA Cohen E.A., Cochrane A.W., Rigby W.F., Mouland A.J.;
RT "A late role for the association of hnRNP A2 with the HIV-1 hnRNP A2
RT response elements in genomic RNA, Gag, and Vpr localization.";
RL J. Biol. Chem. 279:44141-44153(2004).
RN [17]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-203, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=15782174; DOI=10.1038/nmeth715;
RA Ong S.E., Mittler G., Mann M.;
RT "Identifying and quantifying in vivo methylation sites by heavy methyl
RT SILAC.";
RL Nat. Methods 1:119-126(2004).
RN [18]
RP INTERACTION WITH CKAP5.
RX PubMed=15703215; DOI=10.1091/mbc.e04-08-0709;
RA Kosturko L.D., Maggipinto M.J., D'Sa C., Carson J.H., Barbarese E.;
RT "The microtubule-associated protein tumor overexpressed gene binds to the
RT RNA trafficking protein heterogeneous nuclear ribonucleoprotein A2.";
RL Mol. Biol. Cell 16:1938-1947(2005).
RN [19]
RP FUNCTION (MICROBIAL INFECTION).
RX PubMed=17004321; DOI=10.1111/j.1600-0854.2006.00461.x;
RA Levesque K., Halvorsen M., Abrahamyan L., Chatel-Chaix L., Poupon V.,
RA Gordon H., DesGroseillers L., Gatignol A., Mouland A.J.;
RT "Trafficking of HIV-1 RNA is mediated by heterogeneous nuclear
RT ribonucleoprotein A2 expression and impacts on viral assembly.";
RL Traffic 7:1177-1193(2006).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-259 AND SER-341, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17924679; DOI=10.1021/pr070152u;
RA Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
RT "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells
RT and high confident phosphopeptide identification by cross-validation of
RT MS/MS and MS/MS/MS spectra.";
RL J. Proteome Res. 6:4150-4162(2007).
RN [21]
RP IDENTIFICATION IN A MRNP GRANULE COMPLEX, INTERACTION WITH IGF2BP1,
RP SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=17289661; DOI=10.1074/mcp.m600346-mcp200;
RA Joeson L., Vikesaa J., Krogh A., Nielsen L.K., Hansen T., Borup R.,
RA Johnsen A.H., Christiansen J., Nielsen F.C.;
RT "Molecular composition of IMP1 ribonucleoprotein granules.";
RL Mol. Cell. Proteomics 6:798-811(2007).
RN [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-259 AND SER-341, AND
RP IDENTIFICATION BY 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 [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-259, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [24]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-259; SER-341 AND SER-344, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [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 [25]
RP IDENTIFICATION BY MASS 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 [26]
RP REVIEW.
RX PubMed=19099192; DOI=10.1007/s00018-008-8532-1;
RA He Y., Smith R.;
RT "Nuclear functions of heterogeneous nuclear ribonucleoproteins A/B.";
RL Cell. Mol. Life Sci. 66:1239-1256(2009).
RN [27]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-259, AND IDENTIFICATION BY
RP 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 [28]
RP INTERACTION WITH TARDBP.
RX PubMed=19429692; DOI=10.1093/nar/gkp342;
RA D'Ambrogio A., Buratti E., Stuani C., Guarnaccia C., Romano M., Ayala Y.M.,
RA Baralle F.E.;
RT "Functional mapping of the interaction between TDP-43 and hnRNP A2 in
RT vivo.";
RL Nucleic Acids Res. 37:4116-4126(2009).
RN [29]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-85; SER-212; SER-259 AND
RP SER-344, AND IDENTIFICATION BY MASS SPECTROMETRY [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 [30]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-168 AND LYS-173, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [31]
RP FUNCTION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=20010808; DOI=10.1038/nature08697;
RA David C.J., Chen M., Assanah M., Canoll P., Manley J.L.;
RT "HnRNP proteins controlled by c-Myc deregulate pyruvate kinase mRNA
RT splicing in cancer.";
RL Nature 463:364-368(2010).
RN [32]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-85; SER-149; SER-212;
RP SER-225; SER-231; SER-259; SER-341 AND SER-344, AND IDENTIFICATION BY MASS
RP 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 [33]
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 [34]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-212; SER-225; SER-231;
RP SER-236; SER-259; SER-324; TYR-331 AND SER-344, AND IDENTIFICATION BY MASS
RP 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 [35]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22905912; DOI=10.1021/pr300539b;
RA Rosenow A., Noben J.P., Jocken J., Kallendrusch S., Fischer-Posovszky P.,
RA Mariman E.C., Renes J.;
RT "Resveratrol-induced changes of the human adipocyte secretion profile.";
RL J. Proteome Res. 11:4733-4743(2012).
RN [36]
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 [37]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-4; SER-29; THR-140; THR-159;
RP THR-176; SER-189; SER-201; SER-212; SER-225; SER-259; SER-324; TYR-331;
RP SER-341 AND SER-344, 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 [38]
RP FUNCTION, SUBCELLULAR LOCATION, AND SUMOYLATION.
RX PubMed=24356509; DOI=10.1038/ncomms3980;
RA Villarroya-Beltri C., Gutierrez-Vazquez C., Sanchez-Cabo F.,
RA Perez-Hernandez D., Vazquez J., Martin-Cofreces N., Martinez-Herrera D.J.,
RA Pascual-Montano A., Mittelbrunn M., Sanchez-Madrid F.;
RT "Sumoylated hnRNPA2B1 controls the sorting of miRNAs into exosomes through
RT binding to specific motifs.";
RL Nat. Commun. 4:2980-2980(2013).
RN [39]
RP SUBCELLULAR LOCATION (ISOFORM A2).
RX PubMed=24098712; DOI=10.1371/journal.pone.0075669;
RA Friend L.R., Landsberg M.J., Nouwens A.S., Wei Y., Rothnagel J.A.,
RA Smith R.;
RT "Arginine methylation of hnRNP A2 does not directly govern its subcellular
RT localization.";
RL PLoS ONE 8:E75669-E75669(2013).
RN [40]
RP INTERACTION WITH C9ORF72.
RX PubMed=24549040; DOI=10.1093/hmg/ddu068;
RA Farg M.A., Sundaramoorthy V., Sultana J.M., Yang S., Atkinson R.A.,
RA Levina V., Halloran M.A., Gleeson P.A., Blair I.P., Soo K.Y., King A.E.,
RA Atkin J.D.;
RT "C9ORF72, implicated in amytrophic lateral sclerosis and frontotemporal
RT dementia, regulates endosomal trafficking.";
RL Hum. Mol. Genet. 23:3579-3595(2014).
RN [41]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29; SER-85; SER-212; SER-225;
RP SER-231; SER-341; SER-344 AND TYR-347, AND IDENTIFICATION BY MASS
RP 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 [42]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-203; ARG-213; ARG-228; ARG-238;
RP ARG-266; ARG-325 AND ARG-350, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
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).
RN [43]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-120 AND LYS-186, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [44]
RP INTERACTION WITH PPIA.
RX PubMed=25678563; DOI=10.1093/brain/awv005;
RA Lauranzano E., Pozzi S., Pasetto L., Stucchi R., Massignan T., Paolella K.,
RA Mombrini M., Nardo G., Lunetta C., Corbo M., Mora G., Bendotti C.,
RA Bonetto V.;
RT "Peptidylprolyl isomerase A governs TARDBP function and assembly in
RT heterogeneous nuclear ribonucleoprotein complexes.";
RL Brain 138:974-991(2015).
RN [45]
RP DOMAIN, AND MUTAGENESIS OF PHE-207; PHE-209; PHE-219; PHE-227; TYR-234;
RP PHE-240; TYR-244; TYR-247; PHE-256; TYR-262; TYR-269; TYR-276; TYR-283;
RP TYR-287; TYR-290; TYR-295; TYR-300; PHE-303; TYR-306; TYR-313; PHE-321;
RP TYR-331; TYR-336; TYR-347 AND TYR-353.
RX PubMed=26544936; DOI=10.1016/j.cell.2015.10.040;
RA Xiang S., Kato M., Wu L.C., Lin Y., Ding M., Zhang Y., Yu Y.,
RA McKnight S.L.;
RT "The LC domain of hnRNPA2 adopts similar conformations in hydrogel
RT polymers, liquid-like droplets, and nuclei.";
RL Cell 163:829-839(2015).
RN [46]
RP FUNCTION, MIRNA-BINDING, AND INTERACTION WITH DGCR8.
RX PubMed=26321680; DOI=10.1016/j.cell.2015.08.011;
RA Alarcon C.R., Goodarzi H., Lee H., Liu X., Tavazoie S., Tavazoie S.F.;
RT "HNRNPA2B1 is a mediator of m(6)A-dependent nuclear RNA processing
RT events.";
RL Cell 162:1299-1308(2015).
RN [47]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-120, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA Vertegaal A.C.;
RT "System-wide analysis of SUMOylation dynamics in response to replication
RT stress reveals novel small ubiquitin-like modified target proteins and
RT acceptor lysines relevant for genome stability.";
RL Mol. Cell. Proteomics 14:1419-1434(2015).
RN [48]
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 [49]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-22; LYS-104; LYS-112; LYS-120;
RP LYS-137; LYS-152; LYS-168 AND LYS-173, SUMOYLATION [LARGE SCALE ANALYSIS]
RP AT LYS-5 (ISOFORM A2), AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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).
RN [50]
RP FUNCTION, SUBUNIT, INTERACTION WITH TBK1; STING1 AND SRC, SUBCELLULAR
RP LOCATION, MUTAGENESIS OF ARG-228, AND METHYLATION AT ARG-228.
RX PubMed=31320558; DOI=10.1126/science.aav0758;
RA Wang L., Wen M., Cao X.;
RT "Nuclear hnRNPA2B1 initiates and amplifies the innate immune response to
RT DNA viruses.";
RL Science 0:0-0(2019).
RN [51]
RP STRUCTURE BY NMR OF 1-103.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of RRM domain in heterogeneous nuclear
RT ribonucleoproteins A2/B1.";
RL Submitted (NOV-2005) to the PDB data bank.
RN [52]
RP VARIANT IBMPFD2 VAL-302.
RX PubMed=23455423; DOI=10.1038/nature11922;
RA Kim H.J., Kim N.C., Wang Y.D., Scarborough E.A., Moore J., Diaz Z.,
RA MacLea K.S., Freibaum B., Li S., Molliex A., Kanagaraj A.P., Carter R.,
RA Boylan K.B., Wojtas A.M., Rademakers R., Pinkus J.L., Greenberg S.A.,
RA Trojanowski J.Q., Traynor B.J., Smith B.N., Topp S., Gkazi A.S., Miller J.,
RA Shaw C.E., Kottlors M., Kirschner J., Pestronk A., Li Y.R., Ford A.F.,
RA Gitler A.D., Benatar M., King O.D., Kimonis V.E., Ross E.D., Weihl C.C.,
RA Shorter J., Taylor J.P.;
RT "Mutations in prion-like domains in hnRNPA2B1 and hnRNPA1 cause multisystem
RT proteinopathy and ALS.";
RL Nature 495:467-473(2013).
CC -!- FUNCTION: Heterogeneous nuclear ribonucleoprotein (hnRNP) that
CC associates with nascent pre-mRNAs, packaging them into hnRNP particles.
CC The hnRNP particle arrangement on nascent hnRNA is non-random and
CC sequence-dependent and serves to condense and stabilize the transcripts
CC and minimize tangling and knotting. Packaging plays a role in various
CC processes such as transcription, pre-mRNA processing, RNA nuclear
CC export, subcellular location, mRNA translation and stability of mature
CC mRNAs (PubMed:19099192). Forms hnRNP particles with at least 20 other
CC different hnRNP and heterogeneous nuclear RNA in the nucleus. Involved
CC in transport of specific mRNAs to the cytoplasm in oligodendrocytes and
CC neurons: acts by specifically recognizing and binding the A2RE (21
CC nucleotide hnRNP A2 response element) or the A2RE11 (derivative 11
CC nucleotide oligonucleotide) sequence motifs present on some mRNAs, and
CC promotes their transport to the cytoplasm (PubMed:10567417).
CC Specifically binds single-stranded telomeric DNA sequences, protecting
CC telomeric DNA repeat against endonuclease digestion (By similarity).
CC Also binds other RNA molecules, such as primary miRNA (pri-miRNAs):
CC acts as a nuclear 'reader' of the N6-methyladenosine (m6A) mark by
CC specifically recognizing and binding a subset of nuclear m6A-containing
CC pri-miRNAs. Binding to m6A-containing pri-miRNAs promotes pri-miRNA
CC processing by enhancing binding of DGCR8 to pri-miRNA transcripts
CC (PubMed:26321680). Involved in miRNA sorting into exosomes following
CC sumoylation, possibly by binding (m6A)-containing pre-miRNAs
CC (PubMed:24356509). Acts as a regulator of efficiency of mRNA splicing,
CC possibly by binding to m6A-containing pre-mRNAs (PubMed:26321680).
CC Plays a role in the splicing of pyruvate kinase PKM by binding
CC repressively to sequences flanking PKM exon 9, inhibiting exon 9
CC inclusion and resulting in exon 10 inclusion and production of the PKM
CC M2 isoform (PubMed:20010808). Also plays a role in the activation of
CC the innate immune response (PubMed:31320558). Mechanistically, senses
CC the presence of viral DNA in the nucleus, homodimerizes and is
CC demethylated by JMJD6 (PubMed:31320558). In turn, translocates to the
CC cytoplasm where it activates the TBK1-IRF3 pathway, leading to
CC interferon alpha/beta production (PubMed:31320558).
CC {ECO:0000250|UniProtKB:A7VJC2, ECO:0000269|PubMed:10567417,
CC ECO:0000269|PubMed:20010808, ECO:0000269|PubMed:24356509,
CC ECO:0000269|PubMed:26321680, ECO:0000303|PubMed:19099192}.
CC -!- FUNCTION: (Microbial infection) Involved in the transport of HIV-1
CC genomic RNA out of the nucleus, to the microtubule organizing center
CC (MTOC), and then from the MTOC to the cytoplasm: acts by specifically
CC recognizing and binding the A2RE (21 nucleotide hnRNP A2 response
CC element) sequence motifs present on HIV-1 genomic RNA, and promotes its
CC transport. {ECO:0000269|PubMed:15294897, ECO:0000269|PubMed:17004321}.
CC -!- SUBUNIT: Homodimer; dimerization is required for nucleocytoplasmic
CC translocation (PubMed:31320558). Identified in the spliceosome C
CC complex (PubMed:11991638). Identified in a IGF2BP1-dependent mRNP
CC granule complex containing untranslated mRNAs (PubMed:17289661).
CC Interacts with IGF2BP1 (PubMed:17289661). Interacts with C9orf72
CC (PubMed:24549040). Interacts with DGCR8 (PubMed:26321680). Interacts
CC with TARDBP (PubMed:19429692). Interacts with CKAP5 (PubMed:15703215).
CC Interacts with TBK1 (PubMed:31320558). Interacts with STING1
CC (PubMed:31320558). Interacts with SRC (PubMed:31320558). Interacts with
CC PPIA/CYPA (PubMed:25678563). {ECO:0000269|PubMed:11991638,
CC ECO:0000269|PubMed:15703215, ECO:0000269|PubMed:17289661,
CC ECO:0000269|PubMed:19429692, ECO:0000269|PubMed:24549040,
CC ECO:0000269|PubMed:25678563, ECO:0000269|PubMed:26321680,
CC ECO:0000269|PubMed:31320558}.
CC -!- INTERACTION:
CC P22626; P09651: HNRNPA1; NbExp=2; IntAct=EBI-299649, EBI-352662;
CC P22626; Q14103: HNRNPD; NbExp=2; IntAct=EBI-299649, EBI-299674;
CC P22626; P14866: HNRNPL; NbExp=2; IntAct=EBI-299649, EBI-719024;
CC P22626; P14866-1: HNRNPL; NbExp=4; IntAct=EBI-299649, EBI-16071645;
CC P22626; Q5T7N2: L1TD1; NbExp=2; IntAct=EBI-299649, EBI-7216220;
CC P22626; Q9HA38: ZMAT3; NbExp=3; IntAct=EBI-299649, EBI-2548480;
CC P22626-2; P22626-2: HNRNPA2B1; NbExp=4; IntAct=EBI-432522, EBI-432522;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:31320558}. Nucleus,
CC nucleoplasm {ECO:0000269|PubMed:17289661}. Cytoplasm
CC {ECO:0000269|PubMed:31320558}. Cytoplasmic granule
CC {ECO:0000269|PubMed:17289661, ECO:0000269|PubMed:24356509}. Secreted,
CC extracellular exosome {ECO:0000269|PubMed:24356509}. Note=Localized in
CC cytoplasmic mRNP granules containing untranslated mRNAs
CC (PubMed:17289661). Component of ribonucleosomes (PubMed:17289661). Not
CC found in the nucleolus (PubMed:17289661). Found in exosomes following
CC sumoylation (PubMed:24356509). {ECO:0000269|PubMed:17289661,
CC ECO:0000269|PubMed:24356509}.
CC -!- SUBCELLULAR LOCATION: [Isoform A2]: Nucleus
CC {ECO:0000269|PubMed:10772824, ECO:0000269|PubMed:17289661,
CC ECO:0000269|PubMed:24098712}. Cytoplasm {ECO:0000269|PubMed:10772824,
CC ECO:0000269|PubMed:17289661}. Note=Predominantly nucleoplasmic, however
CC is also found in the cytoplasm of cells in some tissues
CC (PubMed:17289661). {ECO:0000269|PubMed:17289661}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=B1; Synonyms=hnRNP B1;
CC IsoId=P22626-1; Sequence=Displayed;
CC Name=A2; Synonyms=hnRNP A2;
CC IsoId=P22626-2; Sequence=VSP_005830;
CC -!- DOMAIN: The disordered region, when incubated at high concentration, is
CC able to polymerize into labile, amyloid-like fibers and form cross-beta
CC polymerization structures, probably driving the formation of hydrogels.
CC In contrast to irreversible, pathogenic amyloids, the fibers
CC polymerized from LC regions disassemble upon dilution. A number of
CC evidence suggests that formation of cross-beta structures by LC regions
CC mediate the formation of RNA granules, liquid-like droplets, and
CC hydrogels. {ECO:0000269|PubMed:26544936}.
CC -!- PTM: Sumoylated in exosomes, promoting miRNAs-binding.
CC {ECO:0000269|PubMed:24356509}.
CC -!- PTM: Asymmetric dimethylation at Arg-266 constitutes the major
CC methylation site (By similarity). According to a report, methylation
CC affects subcellular location and promotes nuclear localization
CC (PubMed:10772824). According to another report, methylation at Arg-266
CC does not influence nucleocytoplasmic shuttling (By similarity).
CC {ECO:0000250|UniProtKB:A7VJC2, ECO:0000269|PubMed:10772824}.
CC -!- DISEASE: Inclusion body myopathy with early-onset Paget disease with or
CC without frontotemporal dementia 2 (IBMPFD2) [MIM:615422]: An autosomal
CC dominant disease characterized by disabling muscle weakness clinically
CC resembling to limb girdle muscular dystrophy, osteolytic bone lesions
CC consistent with Paget disease, and premature frontotemporal dementia.
CC Clinical features show incomplete penetrance.
CC {ECO:0000269|PubMed:23455423}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC ---------------------------------------------------------------------------
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DR EMBL; M29064; AAA60271.1; -; mRNA.
DR EMBL; M29065; AAA36574.1; -; mRNA.
DR EMBL; U09123; AAB60650.1; -; Genomic_DNA.
DR EMBL; U09120; AAB60650.1; JOINED; Genomic_DNA.
DR EMBL; U09121; AAB60650.1; JOINED; Genomic_DNA.
DR EMBL; U09122; AAB60650.1; JOINED; Genomic_DNA.
DR EMBL; D28877; BAA06031.1; -; Genomic_DNA.
DR EMBL; D28877; BAA06032.1; -; Genomic_DNA.
DR EMBL; AK289429; BAF82118.1; -; mRNA.
DR EMBL; CH471073; EAW93835.1; -; Genomic_DNA.
DR EMBL; CH471073; EAW93836.1; -; Genomic_DNA.
DR EMBL; CH471073; EAW93837.1; -; Genomic_DNA.
DR EMBL; CH471073; EAW93839.1; -; Genomic_DNA.
DR CCDS; CCDS43557.1; -. [P22626-1]
DR CCDS; CCDS5397.1; -. [P22626-2]
DR PIR; A56845; B34504.
DR RefSeq; NP_002128.1; NM_002137.3. [P22626-2]
DR RefSeq; NP_112533.1; NM_031243.2. [P22626-1]
DR RefSeq; XP_005249786.1; XM_005249729.1. [P22626-1]
DR RefSeq; XP_016867598.1; XM_017012109.1. [P22626-2]
DR RefSeq; XP_016867599.1; XM_017012110.1. [P22626-2]
DR PDB; 1X4B; NMR; -; A=1-103.
DR PDB; 5EN1; X-ray; 2.58 A; A=12-195.
DR PDB; 5HO4; X-ray; 1.85 A; A=15-193.
DR PDB; 5WWE; X-ray; 2.40 A; A=12-195.
DR PDB; 5WWF; X-ray; 2.15 A; A/C=12-195.
DR PDB; 5WWG; X-ray; 2.03 A; A=12-195.
DR PDB; 6WPQ; X-ray; 1.10 A; A=298-303.
DR PDB; 6WQK; EM; 3.10 A; A/B/C/D/E=193-353.
DR PDBsum; 1X4B; -.
DR PDBsum; 5EN1; -.
DR PDBsum; 5HO4; -.
DR PDBsum; 5WWE; -.
DR PDBsum; 5WWF; -.
DR PDBsum; 5WWG; -.
DR PDBsum; 6WPQ; -.
DR PDBsum; 6WQK; -.
DR AlphaFoldDB; P22626; -.
DR SMR; P22626; -.
DR BioGRID; 109422; 487.
DR CORUM; P22626; -.
DR DIP; DIP-32877N; -.
DR IntAct; P22626; 187.
DR MINT; P22626; -.
DR STRING; 9606.ENSP00000346694; -.
DR ChEMBL; CHEMBL3124741; -.
DR DrugBank; DB11638; Artenimol.
DR DrugBank; DB09130; Copper.
DR GlyGen; P22626; 2 sites, 2 O-linked glycans (2 sites).
DR iPTMnet; P22626; -.
DR MetOSite; P22626; -.
DR PhosphoSitePlus; P22626; -.
DR SwissPalm; P22626; -.
DR BioMuta; HNRNPA2B1; -.
DR DMDM; 133257; -.
DR REPRODUCTION-2DPAGE; IPI00396378; -.
DR REPRODUCTION-2DPAGE; IPI00414696; -.
DR REPRODUCTION-2DPAGE; P22626; -.
DR SWISS-2DPAGE; P22626; -.
DR UCD-2DPAGE; P22626; -.
DR EPD; P22626; -.
DR jPOST; P22626; -.
DR MassIVE; P22626; -.
DR MaxQB; P22626; -.
DR PaxDb; P22626; -.
DR PeptideAtlas; P22626; -.
DR PRIDE; P22626; -.
DR ProteomicsDB; 54010; -. [P22626-1]
DR ProteomicsDB; 54011; -. [P22626-2]
DR TopDownProteomics; P22626-1; -. [P22626-1]
DR TopDownProteomics; P22626-2; -. [P22626-2]
DR Antibodypedia; 3240; 460 antibodies from 34 providers.
DR DNASU; 3181; -.
DR Ensembl; ENST00000354667.8; ENSP00000346694.4; ENSG00000122566.22. [P22626-1]
DR Ensembl; ENST00000356674.8; ENSP00000349101.8; ENSG00000122566.22. [P22626-1]
DR Ensembl; ENST00000360787.8; ENSP00000354021.4; ENSG00000122566.22. [P22626-1]
DR Ensembl; ENST00000608362.2; ENSP00000497298.1; ENSG00000122566.22. [P22626-2]
DR Ensembl; ENST00000618183.5; ENSP00000478691.2; ENSG00000122566.22. [P22626-2]
DR Ensembl; ENST00000676497.1; ENSP00000503836.1; ENSG00000122566.22. [P22626-2]
DR Ensembl; ENST00000676524.1; ENSP00000504831.1; ENSG00000122566.22. [P22626-2]
DR Ensembl; ENST00000676746.1; ENSP00000504329.1; ENSG00000122566.22. [P22626-1]
DR Ensembl; ENST00000676749.1; ENSP00000504799.1; ENSG00000122566.22. [P22626-2]
DR Ensembl; ENST00000676903.1; ENSP00000504660.1; ENSG00000122566.22. [P22626-2]
DR Ensembl; ENST00000677339.1; ENSP00000503242.1; ENSG00000122566.22. [P22626-2]
DR Ensembl; ENST00000677396.1; ENSP00000503703.1; ENSG00000122566.22. [P22626-2]
DR Ensembl; ENST00000677574.1; ENSP00000503021.1; ENSG00000122566.22. [P22626-2]
DR Ensembl; ENST00000677631.1; ENSP00000503452.1; ENSG00000122566.22. [P22626-2]
DR Ensembl; ENST00000677656.1; ENSP00000503060.1; ENSG00000122566.22. [P22626-2]
DR Ensembl; ENST00000677839.1; ENSP00000504439.1; ENSG00000122566.22. [P22626-2]
DR Ensembl; ENST00000677906.1; ENSP00000503870.1; ENSG00000122566.22. [P22626-2]
DR Ensembl; ENST00000678431.1; ENSP00000503833.1; ENSG00000122566.22. [P22626-2]
DR Ensembl; ENST00000678449.1; ENSP00000503375.1; ENSG00000122566.22. [P22626-2]
DR Ensembl; ENST00000678501.1; ENSP00000503961.1; ENSG00000122566.22. [P22626-2]
DR Ensembl; ENST00000678675.1; ENSP00000503476.1; ENSG00000122566.22. [P22626-1]
DR Ensembl; ENST00000678697.1; ENSP00000503047.1; ENSG00000122566.22. [P22626-2]
DR Ensembl; ENST00000678779.1; ENSP00000503429.1; ENSG00000122566.22. [P22626-2]
DR Ensembl; ENST00000678884.1; ENSP00000503501.1; ENSG00000122566.22. [P22626-2]
DR Ensembl; ENST00000678935.1; ENSP00000504023.1; ENSG00000122566.22. [P22626-2]
DR Ensembl; ENST00000678962.1; ENSP00000504721.1; ENSG00000122566.22. [P22626-2]
DR Ensembl; ENST00000678998.1; ENSP00000503460.1; ENSG00000122566.22. [P22626-2]
DR Ensembl; ENST00000679001.1; ENSP00000503514.1; ENSG00000122566.22. [P22626-1]
DR Ensembl; ENST00000679021.1; ENSP00000503885.1; ENSG00000122566.22. [P22626-1]
DR Ensembl; ENST00000679123.1; ENSP00000503360.1; ENSG00000122566.22. [P22626-1]
DR Ensembl; ENST00000679243.1; ENSP00000504415.1; ENSG00000122566.22. [P22626-2]
DR Ensembl; ENST00000679318.1; ENSP00000504571.1; ENSG00000122566.22. [P22626-2]
DR GeneID; 3181; -.
DR KEGG; hsa:3181; -.
DR MANE-Select; ENST00000618183.5; ENSP00000478691.2; NM_002137.4; NP_002128.1. [P22626-2]
DR UCSC; uc003sxr.5; human. [P22626-1]
DR CTD; 3181; -.
DR DisGeNET; 3181; -.
DR GeneCards; HNRNPA2B1; -.
DR GeneReviews; HNRNPA2B1; -.
DR HGNC; HGNC:5033; HNRNPA2B1.
DR HPA; ENSG00000122566; Low tissue specificity.
DR MalaCards; HNRNPA2B1; -.
DR MIM; 600124; gene.
DR MIM; 615422; phenotype.
DR neXtProt; NX_P22626; -.
DR OpenTargets; ENSG00000122566; -.
DR Orphanet; 52430; Inclusion body myopathy with Paget disease of bone and frontotemporal dementia.
DR PharmGKB; PA162391140; -.
DR VEuPathDB; HostDB:ENSG00000122566; -.
DR eggNOG; KOG0118; Eukaryota.
DR GeneTree; ENSGT00940000154431; -.
DR HOGENOM; CLU_012062_1_0_1; -.
DR InParanoid; P22626; -.
DR OMA; GCGGQGY; -.
DR OrthoDB; 1202220at2759; -.
DR PhylomeDB; P22626; -.
DR TreeFam; TF351342; -.
DR PathwayCommons; P22626; -.
DR Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
DR Reactome; R-HSA-72203; Processing of Capped Intron-Containing Pre-mRNA.
DR Reactome; R-HSA-8950505; Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulation.
DR SignaLink; P22626; -.
DR SIGNOR; P22626; -.
DR BioGRID-ORCS; 3181; 201 hits in 1086 CRISPR screens.
DR ChiTaRS; HNRNPA2B1; human.
DR EvolutionaryTrace; P22626; -.
DR GeneWiki; HNRPA2B1; -.
DR GenomeRNAi; 3181; -.
DR Pharos; P22626; Tbio.
DR PRO; PR:P22626; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; P22626; protein.
DR Bgee; ENSG00000122566; Expressed in epithelium of nasopharynx and 213 other tissues.
DR ExpressionAtlas; P22626; baseline and differential.
DR Genevisible; P22626; HS.
DR GO; GO:0015030; C:Cajal body; ISS:BHF-UCL.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; IDA:UniProtKB.
DR GO; GO:0000781; C:chromosome, telomeric region; ISS:BHF-UCL.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0016363; C:nuclear matrix; ISS:BHF-UCL.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:1990904; C:ribonucleoprotein complex; IDA:UniProtKB.
DR GO; GO:0005681; C:spliceosomal complex; IDA:HGNC-UCL.
DR GO; GO:0098505; F:G-rich strand telomeric DNA binding; ISS:BHF-UCL.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0035198; F:miRNA binding; IDA:UniProtKB.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; IDA:UniProtKB.
DR GO; GO:1990247; F:N6-methyladenosine-containing RNA binding; IDA:UniProtKB.
DR GO; GO:0097157; F:pre-mRNA intronic binding; IEA:Ensembl.
DR GO; GO:0003723; F:RNA binding; IDA:HGNC-UCL.
DR GO; GO:0043047; F:single-stranded telomeric DNA binding; IDA:HGNC-UCL.
DR GO; GO:0044806; P:G-quadruplex DNA unwinding; ISS:BHF-UCL.
DR GO; GO:1990428; P:miRNA transport; IDA:UniProtKB.
DR GO; GO:0006406; P:mRNA export from nucleus; IDA:UniProtKB.
DR GO; GO:0006397; P:mRNA processing; IDA:HGNC-UCL.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IMP:UniProtKB.
DR GO; GO:0051028; P:mRNA transport; IBA:GO_Central.
DR GO; GO:0048025; P:negative regulation of mRNA splicing, via spliceosome; IEA:Ensembl.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:1905663; P:positive regulation of telomerase RNA reverse transcriptase activity; ISS:BHF-UCL.
DR GO; GO:1904358; P:positive regulation of telomere maintenance via telomere lengthening; ISS:BHF-UCL.
DR GO; GO:0031053; P:primary miRNA processing; IDA:UniProtKB.
DR GO; GO:0050658; P:RNA transport; IDA:HGNC-UCL.
DR CDD; cd12762; RRM1_hnRNPA2B1; 1.
DR DisProt; DP01109; -.
DR Gene3D; 3.30.70.330; -; 2.
DR InterPro; IPR034489; hnRNP_A2/B1.
DR InterPro; IPR034486; hnRNPA2B1_RRM1.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR PANTHER; PTHR48026:SF13; PTHR48026:SF13; 1.
DR Pfam; PF00076; RRM_1; 2.
DR SMART; SM00360; RRM; 2.
DR SUPFAM; SSF54928; SSF54928; 2.
DR PROSITE; PS50102; RRM; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm;
KW Direct protein sequencing; Disease variant; Host-virus interaction;
KW Isopeptide bond; Methylation; mRNA processing; mRNA splicing;
KW mRNA transport; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Ribonucleoprotein; RNA-binding; Secreted; Spliceosome; Transport;
KW Ubl conjugation.
FT CHAIN 1..353
FT /note="Heterogeneous nuclear ribonucleoproteins A2/B1"
FT /id="PRO_0000081836"
FT DOMAIN 21..104
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 112..191
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 193..353
FT /note="Disordered"
FT /evidence="ECO:0000269|PubMed:26544936"
FT REGION 308..347
FT /note="Nuclear targeting sequence"
FT /evidence="ECO:0000250"
FT MOTIF 9..15
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 191..205
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000269|Ref.6, ECO:0007744|PubMed:22814378"
FT MOD_RES 4
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 29
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 38
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:O88569"
FT MOD_RES 85
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:24275569"
FT MOD_RES 104
FT /note="N6,N6-dimethyllysine; alternate"
FT /evidence="ECO:0000269|Ref.6"
FT MOD_RES 140
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 149
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 159
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 168
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 173
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 176
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 189
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 201
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 203
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:O88569"
FT MOD_RES 203
FT /note="Dimethylated arginine; alternate"
FT /evidence="ECO:0000269|Ref.6"
FT MOD_RES 203
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000269|Ref.6, ECO:0007744|PubMed:15782174,
FT ECO:0007744|PubMed:24129315"
FT MOD_RES 212
FT /note="Phosphoserine"
FT /evidence="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 213
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:O88569"
FT MOD_RES 213
FT /note="Dimethylated arginine; alternate"
FT /evidence="ECO:0000269|Ref.6"
FT MOD_RES 213
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000269|Ref.6, ECO:0007744|PubMed:24129315"
FT MOD_RES 225
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 228
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000269|PubMed:31320558,
FT ECO:0007744|PubMed:24129315"
FT MOD_RES 231
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569"
FT MOD_RES 236
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 238
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 259
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17924679,
FT ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:18691976, 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 266
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:A7VJC2"
FT MOD_RES 266
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 324
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 325
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 331
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 341
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17924679,
FT ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 344
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 347
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 350
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT CROSSLNK 22
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 104
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 112
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 120
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:28112733"
FT CROSSLNK 137
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 152
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 168
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 173
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 186
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447"
FT VAR_SEQ 3..14
FT /note="Missing (in isoform A2)"
FT /evidence="ECO:0000303|PubMed:2557628"
FT /id="VSP_005830"
FT VARIANT 302
FT /note="D -> V (in IBMPFD2; dbSNP:rs397515326)"
FT /evidence="ECO:0000269|PubMed:23455423"
FT /id="VAR_070591"
FT MUTAGEN 207
FT /note="F->S: Does not affect hydrogel-binding."
FT /evidence="ECO:0000269|PubMed:26544936"
FT MUTAGEN 209
FT /note="F->S: Does not affect hydrogel-binding."
FT /evidence="ECO:0000269|PubMed:26544936"
FT MUTAGEN 219
FT /note="F->S: Does not affect hydrogel-binding."
FT /evidence="ECO:0000269|PubMed:26544936"
FT MUTAGEN 227
FT /note="F->S: Does not affect hydrogel-binding."
FT /evidence="ECO:0000269|PubMed:26544936"
FT MUTAGEN 228
FT /note="R->A: About 10-fold increase in interferon beta
FT production."
FT /evidence="ECO:0000269|PubMed:26544936"
FT MUTAGEN 234
FT /note="Y->S: Does not affect hydrogel-binding."
FT /evidence="ECO:0000269|PubMed:26544936"
FT MUTAGEN 240
FT /note="F->S: Does not affect hydrogel-binding."
FT /evidence="ECO:0000269|PubMed:26544936"
FT MUTAGEN 244
FT /note="Y->S: Does not affect hydrogel-binding."
FT /evidence="ECO:0000269|PubMed:26544936"
FT MUTAGEN 247
FT /note="Y->S: Slightly affects hydrogel-binding."
FT /evidence="ECO:0000269|PubMed:26544936"
FT MUTAGEN 256
FT /note="F->S: Does not affect hydrogel-binding."
FT /evidence="ECO:0000269|PubMed:26544936"
FT MUTAGEN 262
FT /note="Y->S: Slightly affects hydrogel-binding."
FT /evidence="ECO:0000269|PubMed:26544936"
FT MUTAGEN 269
FT /note="Y->S: Does not affect hydrogel-binding."
FT /evidence="ECO:0000269|PubMed:26544936"
FT MUTAGEN 276
FT /note="Y->S: Impairs hydrogel-binding."
FT /evidence="ECO:0000269|PubMed:26544936"
FT MUTAGEN 283
FT /note="Y->S: Slightly affects hydrogel-binding."
FT /evidence="ECO:0000269|PubMed:26544936"
FT MUTAGEN 287
FT /note="Y->S: Does not affect hydrogel-binding."
FT /evidence="ECO:0000269|PubMed:26544936"
FT MUTAGEN 290
FT /note="Y->S: Impairs hydrogel-binding."
FT /evidence="ECO:0000269|PubMed:26544936"
FT MUTAGEN 295
FT /note="Y->S: Impairs hydrogel-binding."
FT /evidence="ECO:0000269|PubMed:26544936"
FT MUTAGEN 300
FT /note="Y->S: Slightly affects hydrogel-binding."
FT /evidence="ECO:0000269|PubMed:26544936"
FT MUTAGEN 303
FT /note="F->S: Impairs hydrogel-binding."
FT /evidence="ECO:0000269|PubMed:26544936"
FT MUTAGEN 306
FT /note="Y->S: Slightly affects hydrogel-binding."
FT /evidence="ECO:0000269|PubMed:26544936"
FT MUTAGEN 313
FT /note="Y->S: Slightly affects hydrogel-binding."
FT /evidence="ECO:0000269|PubMed:26544936"
FT MUTAGEN 321
FT /note="F->S: Impairs hydrogel-binding."
FT /evidence="ECO:0000269|PubMed:26544936"
FT MUTAGEN 331
FT /note="Y->S: Impairs hydrogel-binding."
FT /evidence="ECO:0000269|PubMed:26544936"
FT MUTAGEN 336
FT /note="Y->S: Slightly affects hydrogel-binding."
FT /evidence="ECO:0000269|PubMed:26544936"
FT MUTAGEN 347
FT /note="Y->S: Does not affect hydrogel-binding."
FT /evidence="ECO:0000269|PubMed:26544936"
FT MUTAGEN 353
FT /note="Y->S: Does not affect hydrogel-binding."
FT /evidence="ECO:0000269|PubMed:26544936"
FT CONFLICT 205
FT /note="G -> S (in Ref. 4; BAF82118)"
FT /evidence="ECO:0000305"
FT HELIX 18..21
FT /evidence="ECO:0007829|PDB:5HO4"
FT STRAND 22..27
FT /evidence="ECO:0007829|PDB:5HO4"
FT HELIX 34..41
FT /evidence="ECO:0007829|PDB:5HO4"
FT HELIX 42..44
FT /evidence="ECO:0007829|PDB:5HO4"
FT STRAND 47..54
FT /evidence="ECO:0007829|PDB:5HO4"
FT TURN 56..58
FT /evidence="ECO:0007829|PDB:5HO4"
FT STRAND 61..71
FT /evidence="ECO:0007829|PDB:5HO4"
FT HELIX 72..80
FT /evidence="ECO:0007829|PDB:5HO4"
FT STRAND 83..86
FT /evidence="ECO:0007829|PDB:1X4B"
FT STRAND 92..95
FT /evidence="ECO:0007829|PDB:5HO4"
FT HELIX 99..101
FT /evidence="ECO:0007829|PDB:5HO4"
FT TURN 105..108
FT /evidence="ECO:0007829|PDB:5HO4"
FT STRAND 112..117
FT /evidence="ECO:0007829|PDB:5HO4"
FT TURN 120..122
FT /evidence="ECO:0007829|PDB:5WWG"
FT HELIX 125..132
FT /evidence="ECO:0007829|PDB:5HO4"
FT HELIX 133..135
FT /evidence="ECO:0007829|PDB:5HO4"
FT STRAND 138..145
FT /evidence="ECO:0007829|PDB:5HO4"
FT TURN 147..149
FT /evidence="ECO:0007829|PDB:5HO4"
FT STRAND 152..163
FT /evidence="ECO:0007829|PDB:5HO4"
FT HELIX 164..169
FT /evidence="ECO:0007829|PDB:5HO4"
FT STRAND 174..177
FT /evidence="ECO:0007829|PDB:5HO4"
FT STRAND 180..186
FT /evidence="ECO:0007829|PDB:5HO4"
FT TURN 190..192
FT /evidence="ECO:0007829|PDB:5HO4"
FT TURN 278..281
FT /evidence="ECO:0007829|PDB:6WQK"
FT STRAND 286..289
FT /evidence="ECO:0007829|PDB:6WQK"
FT STRAND 291..293
FT /evidence="ECO:0007829|PDB:6WQK"
FT STRAND 296..298
FT /evidence="ECO:0007829|PDB:6WQK"
FT STRAND 300..302
FT /evidence="ECO:0007829|PDB:6WQK"
FT STRAND 316..318
FT /evidence="ECO:0007829|PDB:6WQK"
FT STRAND 324..326
FT /evidence="ECO:0007829|PDB:6WQK"
FT CROSSLNK P22626-2:5
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
SQ 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
