ROA1_HUMAN
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 03-AUG-2022, entry version 264.
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 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; 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}. Note=The disease is caused by variants
CC affecting the gene represented in this 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 -!- CAUTION: Variant Val-314 has been originally associated with IBMPFD3
CC and variant Asn-314 with ALS20 (PubMed:25616961). However in another
CC report, variant Val-314 is associated with amyotrophic lateral
CC sclerosis (ALS) but this variant is not supported by clinical data in
CC this publication (PubMed:25616961). {ECO:0000305}.
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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 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 AlphaFoldDB; P09651; -.
DR BMRB; P09651; -.
DR SMR; P09651; -.
DR BioGRID; 109420; 818.
DR CORUM; P09651; -.
DR DIP; DIP-29338N; -.
DR IntAct; P09651; 263.
DR MINT; P09651; -.
DR STRING; 9606.ENSP00000341826; -.
DR BindingDB; P09651; -.
DR ChEMBL; CHEMBL1955709; -.
DR GlyGen; P09651; 5 sites, 1 O-linked glycan (5 sites).
DR iPTMnet; P09651; -.
DR MetOSite; P09651; -.
DR PhosphoSitePlus; P09651; -.
DR SwissPalm; P09651; -.
DR BioMuta; HNRNPA1; -.
DR DMDM; 288558857; -.
DR SWISS-2DPAGE; P09651; -.
DR EPD; P09651; -.
DR jPOST; P09651; -.
DR MassIVE; P09651; -.
DR MaxQB; P09651; -.
DR PaxDb; P09651; -.
DR PeptideAtlas; P09651; -.
DR PRIDE; P09651; -.
DR ProteomicsDB; 52258; -. [P09651-1]
DR ProteomicsDB; 52259; -. [P09651-2]
DR ProteomicsDB; 52260; -. [P09651-3]
DR TopDownProteomics; P09651-1; -. [P09651-1]
DR TopDownProteomics; P09651-2; -. [P09651-2]
DR TopDownProteomics; P09651-3; -. [P09651-3]
DR Antibodypedia; 7969; 514 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 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; APRNSWD; -.
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 SignaLink; P09651; -.
DR SIGNOR; P09651; -.
DR BioGRID-ORCS; 3178; 117 hits in 1020 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 202 other tissues.
DR ExpressionAtlas; P09651; baseline and differential.
DR Genevisible; P09651; HS.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:HGNC-UCL.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HGNC-UCL.
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: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: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: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: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; cd12580; RRM2_hnRNPA1; 1.
DR DisProt; DP00324; -.
DR Gene3D; 3.30.70.330; -; 2.
DR IDEAL; IID00119; -.
DR InterPro; IPR021662; HnRNPA1_C.
DR InterPro; IPR034845; hnRNPA1_RRM1.
DR InterPro; IPR034803; hnRNPA1_RRM2.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF11627; HnRNPA1; 1.
DR Pfam; PF00076; RRM_1; 2.
DR SMART; SM00360; RRM; 2.
DR SUPFAM; SSF54928; SSF54928; 2.
DR PROSITE; PS50102; RRM; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing;
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; unknown pathological
FT 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
