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 27-MAR-2024, entry version 239. 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). RN [53] RP INVOLVEMENT IN OPMD2. RX PubMed=35484142; DOI=10.1038/s41467-022-30015-1; RA Kim H.J., Mohassel P., Donkervoort S., Guo L., O'Donovan K., Coughlin M., RA Lornage X., Foulds N., Hammans S.R., Foley A.R., Fare C.M., Ford A.F., RA Ogasawara M., Sato A., Iida A., Munot P., Ambegaonkar G., Phadke R., RA O'Donovan D.G., Buchert R., Grimmel M., Toepf A., Zaharieva I.T., Brady L., RA Hu Y., Lloyd T.E., Klein A., Steinlin M., Kuster A., Mercier S., RA Marcorelles P., Pereon Y., Fleurence E., Manzur A., Ennis S., RA Upstill-Goddard R., Bello L., Bertolin C., Pegoraro E., Salviati L., RA French C.E., Shatillo A., Raymond F.L., Haack T.B., Quijano-Roy S., RA Boehm J., Nelson I., Stojkovic T., Evangelista T., Straub V., Romero N.B., RA Laporte J., Muntoni F., Nishino I., Tarnopolsky M.A., Shorter J., RA Boennemann C.G., Taylor J.P.; RT "Heterozygous frameshift variants in HNRNPA2B1 cause early-onset RT oculopharyngeal muscular dystrophy."; RL Nat. Commun. 13:2306-2306(2022). 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 low complexity (LC) regions disassemble upon dilution. CC A number of evidence suggests that formation of cross-beta structures CC by LC regions mediate the formation of RNA granules, liquid-like CC droplets, and 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 -!- DISEASE: Oculopharyngeal muscular dystrophy 2 (OPMD2) [MIM:620460]: An CC autosomal dominant, early-onset myopathy characterized by progressive CC muscle weakness, ptosis, ophthalmoplegia, dysphagia, and variable CC degrees of respiratory insufficiency. {ECO:0000269|PubMed:35484142}. CC Note=The disease is caused by variants affecting the gene represented CC in this entry. The disease is caused by frameshift variants that CC cluster in the low complexity disordered region. They abolish the CC native stop codon, and extend the reading frame resulting in a common CC C-terminal sequence. All variants escape degradation by the RNA quality CC control system, and mutant proteins accumulate in the cytoplasm due to CC impaired nucleocytoplasmic trafficking. {ECO:0000269|PubMed:35484142}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 PDB; 7WM3; X-ray; 1.62 A; A/B/C/D=15-193. DR PDB; 8DU2; EM; 3.30 A; A/B/C/D/E/F/G/H/I/J=193-353. DR PDB; 8DUW; EM; 3.20 A; A/B/C/D/E/F/G/H/I/J=193-353. DR PDB; 8EC7; EM; 3.90 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O=193-353. DR PDB; 8HNI; X-ray; 2.64 A; A/B/C/D/E/F/G/H/I/J/K/L=15-193. 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 PDBsum; 7WM3; -. DR PDBsum; 8DU2; -. DR PDBsum; 8DUW; -. DR PDBsum; 8EC7; -. DR PDBsum; 8HNI; -. DR AlphaFoldDB; P22626; -. DR EMDB; EMD-27713; -. DR EMDB; EMD-27728; -. DR EMDB; EMD-28014; -. DR SMR; P22626; -. DR BioGRID; 109422; 678. DR CORUM; P22626; -. DR DIP; DIP-32877N; -. DR IntAct; P22626; 191. DR MINT; P22626; -. DR STRING; 9606.ENSP00000346694; -. DR ChEMBL; CHEMBL3124741; -. DR DrugBank; DB11638; Artenimol. DR DrugBank; DB09130; Copper. DR GlyCosmos; P22626; 2 sites, 2 glycans. DR GlyGen; P22626; 3 sites, 2 O-linked glycans (3 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 EPD; P22626; -. DR jPOST; P22626; -. DR MassIVE; P22626; -. DR MaxQB; P22626; -. DR PaxDb; 9606-ENSP00000346694; -. DR PeptideAtlas; P22626; -. DR ProteomicsDB; 54010; -. [P22626-1] DR ProteomicsDB; 54011; -. [P22626-2] DR Pumba; P22626; -. DR TopDownProteomics; P22626-1; -. [P22626-1] DR TopDownProteomics; P22626-2; -. [P22626-2] DR Antibodypedia; 3240; 508 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 AGR; HGNC:5033; -. 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 MIM; 620460; 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; RYGSYMG; -. DR OrthoDB; 3127428at2759; -. 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; 210 hits in 1176 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 215 other cell types or tissues. DR ExpressionAtlas; P22626; baseline and differential. 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:0140693; F:molecular condensate scaffold activity; IDA:DisProt. DR GO; GO:0003730; F:mRNA 3'-UTR binding; IDA:UniProtKB. DR GO; GO:1990247; F:N6-methyladenosine-containing RNA reader activity; 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 CDD; cd12581; RRM2_hnRNPA2B1; 1. DR DisProt; DP01109; -. DR Gene3D; 3.30.70.330; -; 2. DR InterPro; IPR021662; HnRNPA1/A2_C. 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; HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEINS A2_B1; 1. DR PANTHER; PTHR48026; HOMOLOGOUS TO DROSOPHILA SQD (SQUID) PROTEIN; 1. DR Pfam; PF11627; HnRNPA1_LC; 1. DR Pfam; PF00076; RRM_1; 2. DR SMART; SM00360; RRM; 2. DR SUPFAM; SSF54928; RNA-binding domain, RBD; 2. DR PROSITE; PS50102; RRM; 2. DR SWISS-2DPAGE; P22626; -. DR UCD-2DPAGE; P22626; -. DR Genevisible; P22626; HS. 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:7WM3" FT STRAND 22..27 FT /evidence="ECO:0007829|PDB:7WM3" FT HELIX 34..41 FT /evidence="ECO:0007829|PDB:7WM3" FT HELIX 42..44 FT /evidence="ECO:0007829|PDB:7WM3" FT STRAND 47..54 FT /evidence="ECO:0007829|PDB:7WM3" FT TURN 56..58 FT /evidence="ECO:0007829|PDB:7WM3" FT STRAND 61..71 FT /evidence="ECO:0007829|PDB:7WM3" FT HELIX 72..80 FT /evidence="ECO:0007829|PDB:7WM3" FT STRAND 84..86 FT /evidence="ECO:0007829|PDB:7WM3" FT STRAND 89..95 FT /evidence="ECO:0007829|PDB:7WM3" FT HELIX 99..101 FT /evidence="ECO:0007829|PDB:7WM3" FT TURN 105..108 FT /evidence="ECO:0007829|PDB:7WM3" FT STRAND 112..117 FT /evidence="ECO:0007829|PDB:7WM3" FT TURN 120..122 FT /evidence="ECO:0007829|PDB:7WM3" FT HELIX 125..132 FT /evidence="ECO:0007829|PDB:7WM3" FT HELIX 133..135 FT /evidence="ECO:0007829|PDB:7WM3" FT STRAND 138..145 FT /evidence="ECO:0007829|PDB:7WM3" FT TURN 147..149 FT /evidence="ECO:0007829|PDB:7WM3" FT STRAND 152..162 FT /evidence="ECO:0007829|PDB:7WM3" FT HELIX 163..169 FT /evidence="ECO:0007829|PDB:7WM3" FT STRAND 174..177 FT /evidence="ECO:0007829|PDB:7WM3" FT STRAND 180..186 FT /evidence="ECO:0007829|PDB:7WM3" FT HELIX 190..192 FT /evidence="ECO:0007829|PDB:7WM3" 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 //