ID ROA1_HUMAN Reviewed; 372 AA. AC P09651; A8K4Z8; Q3MIB7; Q6PJZ7; DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot. DT 09-FEB-2010, sequence version 5. DT 27-MAR-2024, entry version 273. DE RecName: Full=Heterogeneous nuclear ribonucleoprotein A1; DE Short=hnRNP A1; DE AltName: Full=Helix-destabilizing protein; DE AltName: Full=Single-strand RNA-binding protein; DE AltName: Full=hnRNP core protein A1; DE Contains: DE RecName: Full=Heterogeneous nuclear ribonucleoprotein A1, N-terminally processed; GN Name=HNRNPA1; Synonyms=HNRPA1; 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 [GENOMIC DNA] (ISOFORM A1-A). RC TISSUE=Liver; RX PubMed=2760922; DOI=10.1016/0022-2836(89)90459-2; RA Biamonti G., Buvoli M., Bassi M.T., Morandi C., Cobianchi F., Riva S.; RT "Isolation of an active gene encoding human hnRNP protein A1. Evidence for RT alternative splicing."; RL J. Mol. Biol. 207:491-503(1989). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A1-A). RC TISSUE=Fibroblast; RX PubMed=2836799; DOI=10.1093/nar/16.9.3751; RA Buvoli M., Biamonti G., Ghetti A., Riva S., Bassi M.T., Horandi C.; RT "cDNA cloning of human hnRNP protein A1 reveals the existence of multiple RT mRNA isoforms."; RL Nucleic Acids Res. 16:3751-3770(1988). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A1-A). RC TISSUE=Lung; RA Knudsen S.M., Leffers H.; RL Submitted (JUN-1994) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A1-A). RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16541075; DOI=10.1038/nature04569; RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., RA Gibbs R.A.; RT "The finished DNA sequence of human chromosome 12."; RL Nature 440:346-351(2006). RN [6] 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 [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS A1-A AND 2). RC TISSUE=Bone marrow, Cervix, Eye, Kidney, Liver, Lung, and Lymph; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [8] RP PARTIAL NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Liver; RX PubMed=3023065; DOI=10.1002/j.1460-2075.1986.tb04494.x; RA Riva S., Morandi C., Tsoulfas P., Pandolfo M., Biamonti G., Merrill B., RA Williams K.R., Multhaup G., Beyreuther K., Werr H., Heinrich B., RA Schaefer K.P.; RT "Mammalian single-stranded DNA binding protein UP I is derived from the RT hnRNP core protein A1."; RL EMBO J. 5:2267-2273(1986). RN [9] RP PROTEIN SEQUENCE OF 2-47; 56-78; 93-140; 146-178; 197-232 AND 337-370, RP CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, METHYLATION AT RP ARG-206 AND ARG-225, AND IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Cervix carcinoma, and Ovarian carcinoma; RA Bienvenut W.V., Calvo F., Lilla S., von Kriegsheim A., Lempens A., RA Kolch W.; RL Submitted (DEC-2008) to UniProtKB. RN [10] RP PROTEIN SEQUENCE OF 15-47; 147-161 AND 353-370, AND IDENTIFICATION BY MASS RP SPECTROMETRY. RC TISSUE=Fetal brain cortex; RA Lubec G., Chen W.-Q., Sun Y.; RL Submitted (DEC-2008) to UniProtKB. RN [11] RP NUCLEOTIDE SEQUENCE OF 252-303 (ISOFORM A1-B). RX PubMed=1691095; DOI=10.1002/j.1460-2075.1990.tb08230.x; RA Buvoli M., Cobianchi F., Bestagno M.G., Mangiarotti A., Bassi M.T., RA Biamonti G., Riva S.; RT "Alternative splicing in the human gene for the core protein A1 generates RT another hnRNP protein."; RL EMBO J. 9:1229-1235(1990). RN [12] RP NUCLEAR LOCALIZATION SIGNAL, AND MUTAGENESIS OF GLY-326; PRO-327 AND RP 334-GLY-GLY-335. RX PubMed=7730395; DOI=10.1083/jcb.129.3.551; RA Siomi H., Dreyfuss G.; RT "A nuclear localization domain in the hnRNP A1 protein."; RL J. Cell Biol. 129:551-560(1995). RN [13] RP NUCLEAR LOCALIZATION SIGNAL, AND NUCLEAR EXPORT. RX PubMed=8521471; DOI=10.1016/0092-8674(95)90119-1; RA Michael W.M., Choi M., Dreyfuss G.; RT "A nuclear export signal in hnRNP A1: a signal-mediated, temperature- RT dependent nuclear protein export pathway."; RL Cell 83:415-422(1995). RN [14] RP NUCLEAR LOCALIZATION SIGNAL. RX PubMed=7769000; DOI=10.1242/jcs.108.2.545; RA Weighardt F., Biamonti G., Riva S.; RT "Nucleo-cytoplasmic distribution of human hnRNP proteins: a search for the RT targeting domains in hnRNP A1."; RL J. Cell Sci. 108:545-555(1995). RN [15] 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 [16] RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-194; ARG-206 AND ARG-225, AND RP IDENTIFICATION BY MASS 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 [17] RP SUMOYLATION AT LYS-113. RX PubMed=15161980; DOI=10.1073/pnas.0402889101; RA Li T., Evdokimov E., Shen R.F., Chao C.C., Tekle E., Wang T., RA Stadtman E.R., Yang D.C., Chock P.B.; RT "Sumoylation of heterogeneous nuclear ribonucleoproteins, zinc finger RT proteins, and nuclear pore complex proteins: a proteomic analysis."; RL Proc. Natl. Acad. Sci. U.S.A. 101:8551-8556(2004). RN [18] RP PHOSPHORYLATION AT SER-192; SER-362; SER-363 AND SER-364 BY MKNK2. RX PubMed=16111636; DOI=10.1016/j.immuni.2005.06.009; RA Buxade M., Parra J.L., Rousseau S., Shpiro N., Marquez R., Morrice N., RA Bain J., Espel E., Proud C.G.; RT "The Mnks are novel components in the control of TNF alpha biosynthesis and RT phosphorylate and regulate hnRNP A1."; RL Immunity 23:177-189(2005). RN [19] RP INTERACTION WITH SARS-COV NUCLEOPROTEIN (MICROBIAL INFECTION). RX PubMed=15862300; DOI=10.1016/j.febslet.2005.03.080; RA Luo H., Chen Q., Chen J., Chen K., Shen X., Jiang H.; RT "The nucleocapsid protein of SARS coronavirus has a high binding affinity RT to the human cellular heterogeneous nuclear ribonucleoprotein A1."; RL FEBS Lett. 579:2623-2628(2005). RN [20] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [21] RP FUNCTION, AND INTERACTION WITH KHDRBS1. RX PubMed=17371836; DOI=10.1083/jcb.200701005; RA Paronetto M.P., Achsel T., Massiello A., Chalfant C.E., Sette C.; RT "The RNA-binding protein Sam68 modulates the alternative splicing of Bcl- RT x."; RL J. Cell Biol. 176:929-939(2007). RN [22] 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 [23] RP INTERACTION WITH SEPT6, INTERACTION WITH HCV NS5B (MICROBIAL INFECTION), RP FUNCTION (MICROBIAL INFECTION), AND SUBCELLULAR LOCATION (MICROBIAL RP INFECTION). RX PubMed=17229681; DOI=10.1128/jvi.01311-06; RA Kim C.S., Seol S.K., Song O.-K., Park J.H., Jang S.K.; RT "An RNA-binding protein, hnRNP A1, and a scaffold protein, septin 6, RT facilitate hepatitis C virus replication."; RL J. Virol. 81:3852-3865(2007). RN [24] RP IDENTIFICATION IN A MRNP GRANULE COMPLEX, IDENTIFICATION BY MASS RP SPECTROMETRY, AND SUBCELLULAR LOCATION. 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 [25] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=T-cell; RX PubMed=19367720; DOI=10.1021/pr800500r; RA Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.; RT "Phosphorylation analysis of primary human T lymphocytes using sequential RT IMAC and titanium oxide enrichment."; RL J. Proteome Res. 7:5167-5176(2008). RN [26] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6 AND SER-368, 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 [27] 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 [28] RP 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 [29] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-3 AND LYS-350, AND IDENTIFICATION RP 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 [30] 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 [31] RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE RP ANALYSIS] AT SER-2; SER-4 AND SER-6, CLEAVAGE OF INITIATOR METHIONINE RP [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE RP 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 [32] 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 [33] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4; SER-6; SER-199; SER-365 RP AND SER-368, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP 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 [34] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND SER-2, CLEAVAGE OF RP INITIATOR METHIONINE [LARGE SCALE ANALYSIS], 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 [35] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2; SER-4; SER-6; SER-337; RP SER-361; SER-364; SER-365 AND SER-368, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE 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 [36] 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 [37] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [38] RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-206; ARG-218; ARG-225; ARG-232; RP ARG-336; ARG-352 AND ARG-370, 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 [39] 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 [40] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-8, 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 [41] 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 [42] RP FUNCTION, AND MIRNA-BINDING. RX PubMed=28431233; DOI=10.1016/j.molcel.2017.03.014; RA Treiber T., Treiber N., Plessmann U., Harlander S., Daiss J.L., Eichner N., RA Lehmann G., Schall K., Urlaub H., Meister G.; RT "A Compendium of RNA-Binding Proteins that Regulate MicroRNA Biogenesis."; RL Mol. Cell 66:270-284(2017). RN [43] RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, INTERACTION WITH HOXB-AS3 RP PEPTIDE, AND MUTAGENESIS OF ARG-218; ARG-225 AND ARG-232. RX PubMed=28985503; DOI=10.1016/j.molcel.2017.09.015; RA Huang J.Z., Chen M., Chen D., Gao X.C., Zhu S., Huang H., Hu M., Zhu H., RA Yan G.R.; RT "A Peptide Encoded by a Putative lncRNA HOXB-AS3 Suppresses Colon Cancer RT Growth."; RL Mol. Cell 68:171-184(2017). RN [44] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-3; LYS-8; LYS-78; LYS-179; RP LYS-183 AND LYS-350, 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 [45] RP FUNCTION (MICROBIAL INFECTION), AND FUNCTION. RX PubMed=31498791; DOI=10.1371/journal.pone.0221048; RA Li M.L., Lin J.Y., Chen B.S., Weng K.F., Shih S.R., Calderon J.D., RA Tolbert B.S., Brewer G.; RT "EV71 3C protease induces apoptosis by cleavage of hnRNP A1 to promote RT apaf-1 translation."; RL PLoS ONE 14:E0221048-E0221048(2019). RN [46] RP SUBCELLULAR LOCATION (MICROBIAL INFECTION). RX PubMed=33360543; DOI=10.1016/j.bbrc.2020.11.115; RA Kato K., Ikliptikawati D.K., Kobayashi A., Kondo H., Lim K., Hazawa M., RA Wong R.W.; RT "Overexpression of SARS-CoV-2 protein ORF6 dislocates RAE1 and NUP98 from RT the nuclear pore complex."; RL Biochem. Biophys. Res. Commun. 536:59-66(2021). RN [47] RP 3D-STRUCTURE MODELING OF 107-190. RX PubMed=2176620; DOI=10.1016/0014-5793(90)80863-e; RA Ghetti A., Bolognesi M., Cobianchi F., Morandi C.; RT "Modeling by homology of RNA binding domain in A1 hnRNP protein."; RL FEBS Lett. 277:272-276(1990). RN [48] RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 9-181. RX PubMed=9164463; DOI=10.1038/nsb0397-215; RA Shamoo Y., Krueger U., Rice L.M., Williams K.R., Steitz T.A.; RT "Crystal structure of the two RNA binding domains of human hnRNP A1 at RT 1.75-A resolution."; RL Nat. Struct. Biol. 4:215-222(1997). RN [49] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 7-182. RX PubMed=9115444; DOI=10.1016/s0969-2126(97)00211-6; RA Xu R.M., Jokhan L., Cheng X., Mayeda A., Krainer A.R.; RT "Crystal structure of human UP1, the domain of hnRNP A1 that contains two RT RNA-recognition motifs."; RL Structure 5:559-570(1997). RN [50] RP VARIANT IBMPFD3 VAL-314, VARIANTS ALS20 ASN-314 AND SER-319, INVOLVEMENT IN RP IBMPFD3, AND INVOLVEMENT IN ALS20. 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 [51] RP CHARACTERIZATION OF VARIANT IBMPFD3 VAL-314, AND INTERACTION WITH UBQLN2. RX PubMed=25616961; DOI=10.1093/hmg/ddv020; RA Gilpin K.M., Chang L., Monteiro M.J.; RT "ALS-linked mutations in ubiquilin-2 or hnRNPA1 reduce interaction between RT ubiquilin-2 and hnRNPA1."; RL Hum. Mol. Genet. 24:2565-2577(2015). RN [52] RP VARIANTS ALS20 LYS-277 AND SER-340, CHARACTERIZATION OF VARIANT ALS20 RP SER-340, SUBCELLULAR LOCATION, AND VARIANT ARG-283. RX PubMed=27694260; DOI=10.1212/wnl.0000000000003256; RA Liu Q., Shu S., Wang R.R., Liu F., Cui B., Guo X.N., Lu C.X., Li X.G., RA Liu M.S., Peng B., Cui L.Y., Zhang X.; RT "Whole-exome sequencing identifies a missense mutation in hnRNPA1 in a RT family with flail arm ALS."; RL Neurology 87:1763-1769(2016). CC -!- FUNCTION: Involved in the packaging of pre-mRNA into hnRNP particles, CC transport of poly(A) mRNA from the nucleus to the cytoplasm and CC modulation of splice site selection (PubMed:17371836). Plays a role in CC the splicing of pyruvate kinase PKM by binding repressively to CC sequences flanking PKM exon 9, inhibiting exon 9 inclusion and CC resulting in exon 10 inclusion and production of the PKM M2 isoform CC (PubMed:20010808). Binds to the IRES and thereby inhibits the CC translation of the apoptosis protease activating factor APAF1 CC (PubMed:31498791). May bind to specific miRNA hairpins CC (PubMed:28431233). {ECO:0000269|PubMed:17371836, CC ECO:0000269|PubMed:20010808, ECO:0000269|PubMed:28431233, CC ECO:0000269|PubMed:31498791}. CC -!- FUNCTION: (Microbial infection) May play a role in HCV RNA replication. CC {ECO:0000269|PubMed:17229681}. CC -!- FUNCTION: (Microbial infection) Cleavage by Enterovirus 71 protease 3C CC results in increased translation of apoptosis protease activating CC factor APAF1, leading to apoptosis. {ECO:0000269|PubMed:17229681}. CC -!- SUBUNIT: Identified in the spliceosome C complex (PubMed:11991638). CC Identified in a IGF2BP1-dependent mRNP granule complex containing CC untranslated mRNAs (PubMed:17289661). Interacts with SEPT6 CC (PubMed:17229681). Interacts with C9orf72 (PubMed:24549040). Interacts CC with KHDRBS1 (PubMed:17371836). Interacts with UBQLN2 CC (PubMed:25616961). Interacts with PPIA/CYPA (PubMed:25678563). CC Interacts (via the RGG-box) with the HOXB-AS3 peptide; the interaction CC inhibits binding of HNRNPA1 to the intronic sequences flanking exon 9 CC of the PKM gene, preventing inclusion of exon 9 and promoting inclusion CC of exon 10 which suppresses formation of the PKM M2 isoform and CC promotes production of the M1 isoform (PubMed:28985503). CC {ECO:0000269|PubMed:11991638, ECO:0000269|PubMed:17229681, CC ECO:0000269|PubMed:17289661, ECO:0000269|PubMed:17371836, CC ECO:0000269|PubMed:24549040, ECO:0000269|PubMed:25616961, CC ECO:0000269|PubMed:25678563, ECO:0000269|PubMed:28985503}. CC -!- SUBUNIT: (Microbial infection) Interacts with HCV NS5B and with the 5'- CC UTR and 3'-UTR of HCV RNA. {ECO:0000269|PubMed:17229681}. CC -!- SUBUNIT: (Microbial infection) May interact with SARS-CoV CC Nucleoprotein. {ECO:0000305|PubMed:15862300}. CC -!- INTERACTION: CC P09651; P22626: HNRNPA2B1; NbExp=2; IntAct=EBI-352662, EBI-299649; CC P09651; P51991: HNRNPA3; NbExp=2; IntAct=EBI-352662, EBI-1050760; CC P09651; P07910: HNRNPC; NbExp=3; IntAct=EBI-352662, EBI-357966; CC P09651; P31942: HNRNPH3; NbExp=3; IntAct=EBI-352662, EBI-711437; CC P09651; Q07666: KHDRBS1; NbExp=9; IntAct=EBI-352662, EBI-1364; CC P09651; Q8IUH3: RBM45; NbExp=5; IntAct=EBI-352662, EBI-2512147; CC P09651; Q14141: SEPTIN6; NbExp=3; IntAct=EBI-352662, EBI-745901; CC P09651; Q9UHD9: UBQLN2; NbExp=2; IntAct=EBI-352662, EBI-947187; CC P09651; PRO_0000037577 [P27958]; Xeno; NbExp=4; IntAct=EBI-352662, EBI-6904388; CC P09651-2; P09651-2: HNRNPA1; NbExp=5; IntAct=EBI-352677, EBI-352677; CC P09651-2; O00233: PSMD9; NbExp=5; IntAct=EBI-352677, EBI-750973; CC P09651-2; Q92973: TNPO1; NbExp=2; IntAct=EBI-352677, EBI-286693; CC P09651-2; Q9UHD9: UBQLN2; NbExp=4; IntAct=EBI-352677, EBI-947187; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17289661, CC ECO:0000269|PubMed:27694260}. Cytoplasm {ECO:0000269|PubMed:17289661}. CC Note=Localized in cytoplasmic mRNP granules containing untranslated CC mRNAs. Shuttles continuously between the nucleus and the cytoplasm CC along with mRNA. Component of ribonucleosomes (PubMed:17289661). CC {ECO:0000269|PubMed:17289661, ECO:0000269|PubMed:27694260}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17229681}. CC Note=(Microbial infection) In the course of viral infection, CC colocalizes with HCV NS5B at speckles in the cytoplasm in a HCV- CC replication dependent manner. {ECO:0000269|PubMed:17229681}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:33360543}. CC Note=(Microbial infection) SARS coronavirus-2/SARS-CoV-2 ORF6 protein CC increases accumulation to the nucleus. {ECO:0000269|PubMed:33360543}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=A1-B; CC IsoId=P09651-1; Sequence=Displayed; CC Name=A1-A; CC IsoId=P09651-2; Sequence=VSP_005824; CC Name=2; CC IsoId=P09651-3; Sequence=VSP_034076; CC -!- PTM: Arg-194, Arg-206 and Arg-225 are dimethylated, probably to CC asymmetric dimethylarginine. CC -!- PTM: Sumoylated. {ECO:0000269|PubMed:15161980}. CC -!- DISEASE: Inclusion body myopathy with early-onset Paget disease with or CC without frontotemporal dementia 3 (IBMPFD3) [MIM:615424]: 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, ECO:0000269|PubMed:25616961}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- DISEASE: Amyotrophic lateral sclerosis 20 (ALS20) [MIM:615426]: A CC neurodegenerative disorder affecting upper motor neurons in the brain CC and lower motor neurons in the brain stem and spinal cord, resulting in CC fatal paralysis. Sensory abnormalities are absent. The pathologic CC hallmarks of the disease include pallor of the corticospinal tract due CC to loss of motor neurons, presence of ubiquitin-positive inclusions CC within surviving motor neurons, and deposition of pathologic CC aggregates. The etiology of amyotrophic lateral sclerosis is likely to CC be multifactorial, involving both genetic and environmental factors. CC The disease is inherited in 5-10% of the cases. CC {ECO:0000269|PubMed:23455423, ECO:0000269|PubMed:27694260}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- MISCELLANEOUS: [Isoform A1-A]: Is twenty times more abundant than CC isoform A1-B. {ECO:0000305}. 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; X12671; CAA31191.1; -; Genomic_DNA. DR EMBL; X06747; CAA29922.1; -; mRNA. DR EMBL; X79536; CAA56072.1; -; mRNA. DR EMBL; AK291113; BAF83802.1; -; mRNA. DR EMBL; AC078778; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471054; EAW96761.1; -; Genomic_DNA. DR EMBL; BC002355; AAH02355.1; -; mRNA. DR EMBL; BC009600; AAH09600.1; -; mRNA. DR EMBL; BC012158; AAH12158.1; -; mRNA. DR EMBL; BC033714; AAH33714.1; -; mRNA. DR EMBL; BC052296; AAH52296.1; -; mRNA. DR EMBL; BC070315; AAH70315.1; -; mRNA. DR EMBL; BC074502; AAH74502.1; -; mRNA. DR EMBL; BC103707; AAI03708.1; -; mRNA. DR EMBL; X04347; CAA27874.1; -; mRNA. DR CCDS; CCDS41793.1; -. [P09651-2] DR CCDS; CCDS44909.1; -. [P09651-1] DR PIR; S02061; S02061. DR PIR; S12520; S12520. DR RefSeq; NP_002127.1; NM_002136.3. [P09651-2] DR RefSeq; NP_112420.1; NM_031157.3. [P09651-1] DR RefSeq; XP_005268883.1; XM_005268826.1. DR PDB; 1HA1; X-ray; 1.75 A; A=1-184. DR PDB; 1L3K; X-ray; 1.10 A; A=1-196. DR PDB; 1PGZ; X-ray; 2.60 A; A=2-196. DR PDB; 1PO6; X-ray; 2.10 A; A=8-190. DR PDB; 1U1K; X-ray; 2.00 A; A=1-196. DR PDB; 1U1L; X-ray; 2.00 A; A=1-196. DR PDB; 1U1M; X-ray; 2.00 A; A=1-196. DR PDB; 1U1N; X-ray; 2.10 A; A=1-196. DR PDB; 1U1O; X-ray; 2.00 A; A=1-196. DR PDB; 1U1P; X-ray; 1.90 A; A=1-196. DR PDB; 1U1Q; X-ray; 1.80 A; A=1-196. DR PDB; 1U1R; X-ray; 1.80 A; A=1-196. DR PDB; 1UP1; X-ray; 1.90 A; A=3-184. DR PDB; 2H4M; X-ray; 3.05 A; C/D=309-357. DR PDB; 2LYV; NMR; -; A=2-196. DR PDB; 2UP1; X-ray; 2.10 A; A=8-190. DR PDB; 4YOE; X-ray; 1.92 A; A=1-196. DR PDB; 5MPG; NMR; -; A=2-97. DR PDB; 5MPL; NMR; -; A=95-196. DR PDB; 5ZGD; X-ray; 1.40 A; A=209-217. DR PDB; 5ZGL; X-ray; 0.95 A; A/B=234-240. DR PDB; 6BXX; X-ray; 1.10 A; A=243-248. DR PDB; 6DCL; X-ray; 2.50 A; A/B=2-188. DR PDB; 6J60; EM; 0.96 A; A=209-217. DR PDB; 7BX7; EM; 2.80 A; A/B/C/D/E/F=186-372. DR PDB; 7ZJ2; EM; 3.32 A; A/B/C/D/E/F/G/H/I/J/K/L=1-372. DR PDBsum; 1HA1; -. DR PDBsum; 1L3K; -. DR PDBsum; 1PGZ; -. DR PDBsum; 1PO6; -. DR PDBsum; 1U1K; -. DR PDBsum; 1U1L; -. DR PDBsum; 1U1M; -. DR PDBsum; 1U1N; -. DR PDBsum; 1U1O; -. DR PDBsum; 1U1P; -. DR PDBsum; 1U1Q; -. DR PDBsum; 1U1R; -. DR PDBsum; 1UP1; -. DR PDBsum; 2H4M; -. DR PDBsum; 2LYV; -. DR PDBsum; 2UP1; -. DR PDBsum; 4YOE; -. DR PDBsum; 5MPG; -. DR PDBsum; 5MPL; -. DR PDBsum; 5ZGD; -. DR PDBsum; 5ZGL; -. DR PDBsum; 6BXX; -. DR PDBsum; 6DCL; -. DR PDBsum; 6J60; -. DR PDBsum; 7BX7; -. DR PDBsum; 7ZJ2; -. DR AlphaFoldDB; P09651; -. DR BMRB; P09651; -. DR EMDB; EMD-14739; -. DR EMDB; EMD-30235; -. DR SASBDB; P09651; -. DR SMR; P09651; -. DR BioGRID; 109420; 913. DR CORUM; P09651; -. DR DIP; DIP-29338N; -. DR IntAct; P09651; 268. DR MINT; P09651; -. DR STRING; 9606.ENSP00000341826; -. DR BindingDB; P09651; -. DR ChEMBL; CHEMBL1955709; -. DR GlyCosmos; P09651; 5 sites, 1 glycan. DR GlyGen; P09651; 9 sites, 1 O-linked glycan (9 sites). DR iPTMnet; P09651; -. DR MetOSite; P09651; -. DR PhosphoSitePlus; P09651; -. DR SwissPalm; P09651; -. DR BioMuta; HNRNPA1; -. DR DMDM; 288558857; -. DR EPD; P09651; -. DR jPOST; P09651; -. DR MassIVE; P09651; -. DR MaxQB; P09651; -. DR PaxDb; 9606-ENSP00000341826; -. DR PeptideAtlas; P09651; -. DR PRIDE; P09651; -. DR ProteomicsDB; 52258; -. [P09651-1] DR ProteomicsDB; 52259; -. [P09651-2] DR ProteomicsDB; 52260; -. [P09651-3] DR Pumba; P09651; -. DR TopDownProteomics; P09651-1; -. [P09651-1] DR TopDownProteomics; P09651-2; -. [P09651-2] DR TopDownProteomics; P09651-3; -. [P09651-3] DR Antibodypedia; 7969; 564 antibodies from 39 providers. DR DNASU; 3178; -. DR Ensembl; ENST00000340913.11; ENSP00000341826.7; ENSG00000135486.19. [P09651-1] DR Ensembl; ENST00000546500.5; ENSP00000448617.1; ENSG00000135486.19. [P09651-2] DR Ensembl; ENST00000547276.5; ENSP00000447260.1; ENSG00000135486.19. [P09651-3] DR Ensembl; ENST00000547566.5; ENSP00000449913.1; ENSG00000135486.19. [P09651-2] DR Ensembl; ENST00000550482.2; ENSP00000446486.2; ENSG00000135486.19. [P09651-2] DR Ensembl; ENST00000677210.1; ENSP00000503610.1; ENSG00000135486.19. [P09651-1] DR GeneID; 3178; -. DR KEGG; hsa:3178; -. DR MANE-Select; ENST00000340913.11; ENSP00000341826.7; NM_031157.4; NP_112420.1. DR UCSC; uc001sfl.4; human. [P09651-1] DR AGR; HGNC:5031; -. DR CTD; 3178; -. DR DisGeNET; 3178; -. DR GeneCards; HNRNPA1; -. DR GeneReviews; HNRNPA1; -. DR HGNC; HGNC:5031; HNRNPA1. DR HPA; ENSG00000135486; Low tissue specificity. DR MalaCards; HNRNPA1; -. DR MIM; 164017; gene. DR MIM; 615424; phenotype. DR MIM; 615426; phenotype. DR neXtProt; NX_P09651; -. DR OpenTargets; ENSG00000135486; -. DR Orphanet; 803; Amyotrophic lateral sclerosis. DR Orphanet; 52430; Inclusion body myopathy with Paget disease of bone and frontotemporal dementia. DR PharmGKB; PA162391113; -. DR VEuPathDB; HostDB:ENSG00000135486; -. DR eggNOG; KOG0118; Eukaryota. DR GeneTree; ENSGT00950000183123; -. DR HOGENOM; CLU_012062_1_0_1; -. DR InParanoid; P09651; -. DR OMA; ADNYGGM; -. DR OrthoDB; 3127428at2759; -. DR PhylomeDB; P09651; -. DR TreeFam; TF314808; -. DR PathwayCommons; P09651; -. DR Reactome; R-HSA-6803529; FGFR2 alternative splicing. 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-9692914; SARS-CoV-1-host interactions. DR Reactome; R-HSA-9735869; SARS-CoV-1 modulates host translation machinery. DR SignaLink; P09651; -. DR SIGNOR; P09651; -. DR BioGRID-ORCS; 3178; 126 hits in 1098 CRISPR screens. DR ChiTaRS; HNRNPA1; human. DR EvolutionaryTrace; P09651; -. DR GeneWiki; Heterogeneous_nuclear_ribonucleoprotein_A1; -. DR GenomeRNAi; 3178; -. DR Pharos; P09651; Tchem. DR PRO; PR:P09651; -. DR Proteomes; UP000005640; Chromosome 12. DR RNAct; P09651; Protein. DR Bgee; ENSG00000135486; Expressed in ganglionic eminence and 204 other cell types or tissues. DR ExpressionAtlas; P09651; baseline and differential. DR GO; GO:0071013; C:catalytic step 2 spliceosome; IDA:UniProtKB. DR GO; GO:0005737; C:cytoplasm; IDA:HGNC-UCL. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0043232; C:intracellular non-membrane-bounded organelle; IDA:DisProt. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. 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:CAFA. DR GO; GO:0003677; F:DNA binding; EXP:DisProt. DR GO; GO:0098505; F:G-rich strand telomeric DNA binding; IDA: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; IBA:GO_Central. DR GO; GO:0036002; F:pre-mRNA binding; IDA:UniProtKB. DR GO; GO:0019904; F:protein domain specific binding; IPI:UniProtKB. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR GO; GO:0003697; F:single-stranded DNA binding; IDA:HGNC-UCL. DR GO; GO:0003727; F:single-stranded RNA binding; IC:HGNC-UCL. DR GO; GO:0061752; F:telomeric repeat-containing RNA binding; IDA:BHF-UCL. DR GO; GO:1990000; P:amyloid fibril formation; IDA:DisProt. DR GO; GO:0042149; P:cellular response to glucose starvation; IMP:CAFA. DR GO; GO:1903936; P:cellular response to sodium arsenite; IDA:UniProtKB. DR GO; GO:0051170; P:import into nucleus; IDA:HGNC-UCL. DR GO; GO:0051179; P:localization; EXP:DisProt. DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central. DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW. DR GO; GO:0032211; P:negative regulation of telomere maintenance via telomerase; IMP:BHF-UCL. DR GO; GO:0051168; P:nuclear export; IDA:HGNC-UCL. DR GO; GO:0032212; P:positive regulation of telomere maintenance via telomerase; IDA:BHF-UCL. DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; IMP:CAFA. DR GO; GO:0043484; P:regulation of RNA splicing; IDA:UniProtKB. DR GO; GO:0006405; P:RNA export from nucleus; IC:HGNC-UCL. DR CDD; cd12761; RRM1_hnRNPA1; 1. DR CDD; cd12582; RRM2_hnRNPA3; 1. DR DisProt; DP00324; -. DR Gene3D; 3.30.70.330; -; 2. DR IDEAL; IID00119; -. DR InterPro; IPR034516; hnRNPA1/3_RRM2. DR InterPro; IPR021662; HnRNPA1/A2_C. DR InterPro; IPR034845; hnRNPA1_RRM1. DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf. DR InterPro; IPR035979; RBD_domain_sf. DR InterPro; IPR000504; RRM_dom. DR PANTHER; PTHR48026:SF2; HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN A1-RELATED; 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; P09651; -. DR Genevisible; P09651; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; KW Amyotrophic lateral sclerosis; Cytoplasm; Direct protein sequencing; KW Disease variant; Host-virus interaction; Isopeptide bond; Methylation; KW mRNA processing; mRNA splicing; mRNA transport; Neurodegeneration; Nucleus; KW Phosphoprotein; Reference proteome; Repeat; Ribonucleoprotein; RNA-binding; KW Spliceosome; Transport; Ubl conjugation. FT CHAIN 1..372 FT /note="Heterogeneous nuclear ribonucleoprotein A1" FT /id="PRO_0000424509" FT INIT_MET 1 FT /note="Removed; alternate" FT /evidence="ECO:0000269|Ref.9, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:22814378" FT CHAIN 2..372 FT /note="Heterogeneous nuclear ribonucleoprotein A1, N- FT terminally processed" FT /id="PRO_0000081828" FT DOMAIN 14..97 FT /note="RRM 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176" FT DOMAIN 105..184 FT /note="RRM 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176" FT REGION 4..94 FT /note="Globular A domain" FT REGION 95..185 FT /note="Globular B domain" FT REGION 182..216 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 218..240 FT /note="RNA-binding RGG-box" FT REGION 317..372 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 320..357 FT /note="Nuclear targeting sequence (M9)" FT COMPBIAS 184..199 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 355..372 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0007744|PubMed:22814378" FT MOD_RES 2 FT /note="N-acetylserine; in Heterogeneous nuclear FT ribonucleoprotein A1, N-terminally processed" FT /evidence="ECO:0000269|Ref.9, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:22814378" FT MOD_RES 2 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" FT MOD_RES 3 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 4 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" FT MOD_RES 6 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 22 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P49312" FT MOD_RES 192 FT /note="Phosphoserine; by MKNK2" FT /evidence="ECO:0000269|PubMed:16111636" FT MOD_RES 194 FT /note="Asymmetric dimethylarginine; alternate" FT /evidence="ECO:0000250|UniProtKB:P09867" FT MOD_RES 194 FT /note="Dimethylated arginine; alternate" FT /evidence="ECO:0007744|PubMed:15782174" FT MOD_RES 194 FT /note="Omega-N-methylarginine; alternate" FT /evidence="ECO:0000250|UniProtKB:P49312" FT MOD_RES 199 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692" FT MOD_RES 206 FT /note="Asymmetric dimethylarginine; alternate" FT /evidence="ECO:0000269|Ref.9, ECO:0007744|PubMed:24129315" FT MOD_RES 206 FT /note="Dimethylated arginine; alternate" FT /evidence="ECO:0007744|PubMed:15782174" FT MOD_RES 206 FT /note="Omega-N-methylarginine; alternate" FT /evidence="ECO:0000269|Ref.9, ECO:0007744|PubMed:24129315" FT MOD_RES 218 FT /note="Asymmetric dimethylarginine; alternate" FT /evidence="ECO:0007744|PubMed:24129315" FT MOD_RES 218 FT /note="Omega-N-methylarginine; alternate" FT /evidence="ECO:0007744|PubMed:24129315" FT MOD_RES 225 FT /note="Asymmetric dimethylarginine; alternate" FT /evidence="ECO:0000269|Ref.9, ECO:0007744|PubMed:24129315" FT MOD_RES 225 FT /note="Dimethylated arginine; alternate" FT /evidence="ECO:0007744|PubMed:15782174" FT MOD_RES 225 FT /note="Omega-N-methylarginine; alternate" FT /evidence="ECO:0000269|Ref.9, ECO:0007744|PubMed:24129315" FT MOD_RES 232 FT /note="Asymmetric dimethylarginine; alternate" FT /evidence="ECO:0000250|UniProtKB:P04256" FT MOD_RES 232 FT /note="Omega-N-methylarginine; alternate" FT /evidence="ECO:0007744|PubMed:24129315" FT MOD_RES 336 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0007744|PubMed:24129315" FT MOD_RES 337 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 350 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 352 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0007744|PubMed:24129315" FT MOD_RES 361 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 362 FT /note="Phosphoserine; by MKNK2" FT /evidence="ECO:0000269|PubMed:16111636" FT MOD_RES 363 FT /note="Phosphoserine; by MKNK2" FT /evidence="ECO:0000269|PubMed:16111636" FT MOD_RES 364 FT /note="Phosphoserine; by MKNK2" FT /evidence="ECO:0000269|PubMed:16111636, FT ECO:0007744|PubMed:23186163" FT MOD_RES 365 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 368 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" FT MOD_RES 370 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0007744|PubMed:24129315" FT CROSSLNK 3 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 8 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25755297, FT ECO:0007744|PubMed:28112733" FT CROSSLNK 78 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 113 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO)" FT /evidence="ECO:0000269|PubMed:15161980" FT CROSSLNK 179 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 183 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 350 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0007744|PubMed:28112733" FT VAR_SEQ 203..307 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_034076" FT VAR_SEQ 252..303 FT /note="Missing (in isoform A1-A)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:2836799, FT ECO:0000303|Ref.3" FT /id="VSP_005824" FT VARIANT 277 FT /note="Q -> K (in ALS20; uncertain significance)" FT /evidence="ECO:0000269|PubMed:27694260" FT /id="VAR_077531" FT VARIANT 283 FT /note="G -> R (in dbSNP:rs375259222)" FT /evidence="ECO:0000269|PubMed:27694260" FT /id="VAR_077532" FT VARIANT 314 FT /note="D -> N (in ALS20; dbSNP:rs397518453)" FT /evidence="ECO:0000269|PubMed:23455423" FT /id="VAR_070588" FT VARIANT 314 FT /note="D -> V (in IBMPFD3; reduces binding to UBQLN2; FT dbSNP:rs397518452)" FT /evidence="ECO:0000269|PubMed:23455423, FT ECO:0000269|PubMed:25616961" FT /id="VAR_070589" FT VARIANT 319 FT /note="N -> S (in ALS20; dbSNP:rs397518454)" FT /evidence="ECO:0000269|PubMed:23455423" FT /id="VAR_070590" FT VARIANT 340 FT /note="P -> S (in ALS20; increases subcellular localization FT of HNRNPA1 in cytoplasmic inclusions with stress granules)" FT /evidence="ECO:0000269|PubMed:27694260" FT /id="VAR_077533" FT MUTAGEN 218 FT /note="R->A: Abolishes interaction with HOXB-AS3 peptide; FT when associated with A-225 and A-232." FT /evidence="ECO:0000269|PubMed:28985503" FT MUTAGEN 225 FT /note="R->A: Abolishes interaction with HOXB-AS3 peptide; FT when associated with A-218 and A-232." FT /evidence="ECO:0000269|PubMed:28985503" FT MUTAGEN 232 FT /note="R->A: Abolishes interaction with HOXB-AS3 peptide; FT when associated with A-218 and A-225." FT /evidence="ECO:0000269|PubMed:28985503" FT MUTAGEN 326 FT /note="G->A: No nuclear import nor export." FT /evidence="ECO:0000269|PubMed:7730395" FT MUTAGEN 327 FT /note="P->A: No nuclear import nor export." FT /evidence="ECO:0000269|PubMed:7730395" FT MUTAGEN 334..335 FT /note="GG->LL: Normal nuclear import and export." FT /evidence="ECO:0000269|PubMed:7730395" FT CONFLICT 128 FT /note="Y -> F (in Ref. 2; CAA29922)" FT /evidence="ECO:0000305" FT CONFLICT 140 FT /note="R -> P (in Ref. 8; CAA27874)" FT /evidence="ECO:0000305" FT CONFLICT 146 FT /note="R -> K (in Ref. 2; CAA29922)" FT /evidence="ECO:0000305" FT HELIX 11..14 FT /evidence="ECO:0007829|PDB:1L3K" FT STRAND 15..20 FT /evidence="ECO:0007829|PDB:1L3K" FT HELIX 27..34 FT /evidence="ECO:0007829|PDB:1L3K" FT HELIX 35..37 FT /evidence="ECO:0007829|PDB:1L3K" FT STRAND 40..47 FT /evidence="ECO:0007829|PDB:1L3K" FT TURN 49..51 FT /evidence="ECO:0007829|PDB:1L3K" FT STRAND 54..64 FT /evidence="ECO:0007829|PDB:1L3K" FT HELIX 65..73 FT /evidence="ECO:0007829|PDB:1L3K" FT STRAND 76..79 FT /evidence="ECO:0007829|PDB:1U1R" FT STRAND 85..88 FT /evidence="ECO:0007829|PDB:1L3K" FT HELIX 94..96 FT /evidence="ECO:0007829|PDB:1U1Q" FT TURN 98..101 FT /evidence="ECO:0007829|PDB:1U1Q" FT STRAND 105..110 FT /evidence="ECO:0007829|PDB:1L3K" FT TURN 113..115 FT /evidence="ECO:0007829|PDB:1L3K" FT HELIX 118..125 FT /evidence="ECO:0007829|PDB:1L3K" FT TURN 126..128 FT /evidence="ECO:0007829|PDB:1L3K" FT STRAND 131..138 FT /evidence="ECO:0007829|PDB:1L3K" FT TURN 140..142 FT /evidence="ECO:0007829|PDB:1L3K" FT STRAND 145..155 FT /evidence="ECO:0007829|PDB:1L3K" FT HELIX 156..164 FT /evidence="ECO:0007829|PDB:1L3K" FT STRAND 168..170 FT /evidence="ECO:0007829|PDB:1U1Q" FT STRAND 176..179 FT /evidence="ECO:0007829|PDB:1L3K" FT HELIX 183..188 FT /evidence="ECO:0007829|PDB:1U1Q" FT STRAND 305..307 FT /evidence="ECO:0007829|PDB:7BX7" FT STRAND 312..314 FT /evidence="ECO:0007829|PDB:7BX7" FT STRAND 317..326 FT /evidence="ECO:0007829|PDB:7BX7" FT STRAND 330..333 FT /evidence="ECO:0007829|PDB:7BX7" SQ SEQUENCE 372 AA; 38747 MW; A06683571C6C109F CRC64; MSKSESPKEP EQLRKLFIGG LSFETTDESL RSHFEQWGTL TDCVVMRDPN TKRSRGFGFV TYATVEEVDA AMNARPHKVD GRVVEPKRAV SREDSQRPGA HLTVKKIFVG GIKEDTEEHH LRDYFEQYGK IEVIEIMTDR GSGKKRGFAF VTFDDHDSVD KIVIQKYHTV NGHNCEVRKA LSKQEMASAS SSQRGRSGSG NFGGGRGGGF GGNDNFGRGG NFSGRGGFGG SRGGGGYGGS GDGYNGFGND GGYGGGGPGY SGGSRGYGSG GQGYGNQGSG YGGSGSYDSY NNGGGGGFGG GSGSNFGGGG SYNDFGNYNN QSSNFGPMKG GNFGGRSSGP YGGGGQYFAK PRNQGGYGGS SSSSSYGSGR RF //