(data stored in SCRATCH zone)

SWISSPROT: 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   30-AUG-2017, entry version 227.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; 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
RT   for 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
RT   multiple 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.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   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.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA   Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA   Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
RA   Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
RA   Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
RA   Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
RA   Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
RA   Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
RA   Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
RA   Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
RA   Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
RA   Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
RA   Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
RA   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.,
RA   Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
RA   Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
RA   Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
RA   Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
RA   Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
RA   Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
RA   Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
RA   Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
RA   Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
RA   Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
RA   Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
RA   Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
RA   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.,
RA   Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
RA   Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
RA   Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
RA   Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
RA   Kucherlapati R., Weinstock G., 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.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   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
RT   project: 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;
RA   Riva S., Morandi C., Tsoulfas P., Pandolfo M., Biamonti G.,
RA   Merrill B., Williams K.R., Multhaup G., Beyreuther K., Werr H.,
RA   Heinrich B., Schaefer K.P.;
RT   "Mammalian single-stranded DNA binding protein UP I is derived from
RT   the 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
RP   MASS 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;
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
RT   generates 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;
RA   Weighardt F., Biamonti G., Riva S.;
RT   "Nucleo-cytoplasmic distribution of human hnRNP proteins: a search for
RT   the targeting domains in hnRNP A1.";
RL   J. Cell Sci. 108:545-555(1995).
RN   [15]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE
RP   SPLICEOSOMAL 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,
RP   AND 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
RT   biosynthesis and phosphorylate and regulate hnRNP A1.";
RL   Immunity 23:177-189(2005).
RN   [19]
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.,
RA   Mann M.;
RT   "Global, in vivo, and site-specific phosphorylation dynamics in
RT   signaling networks.";
RL   Cell 127:635-648(2006).
RN   [20]
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
RT   Bcl-x.";
RL   J. Cell Biol. 176:929-939(2007).
RN   [21]
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
RT   cells and high confident phosphopeptide identification by cross-
RT   validation of MS/MS and MS/MS/MS spectra.";
RL   J. Proteome Res. 6:4150-4162(2007).
RN   [22]
RP   INTERACTION WITH SEPT6, INTERACTION WITH HCV NS5B (MICROBIAL
RP   INFECTION), FUNCTION (MICROBIAL INFECTION), AND SUBCELLULAR LOCATION
RP   (MICROBIAL 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   [23]
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   [24]
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
RT   sequential IMAC and titanium oxide enrichment.";
RL   J. Proteome Res. 7:5167-5176(2008).
RN   [25]
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   [26]
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.,
RA   Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT   a refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [27]
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   [28]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-3 AND LYS-350, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA   Walther T.C., 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   [29]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE
RP   SCALE ANALYSIS] AT SER-2; SER-4 AND SER-6, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA   Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full
RT   phosphorylation site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [30]
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.,
RA   Buerckstuemmer T., 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   [31]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4; SER-6; SER-199;
RP   SER-365 AND SER-368, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
RP   SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA   Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA   Blagoev B.;
RT   "System-wide temporal characterization of the proteome and
RT   phosphoproteome of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [32]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND SER-2, CLEAVAGE OF
RP   INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY
RP   MASS 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.,
RA   Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA   Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-
RT   terminal acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [33]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2; SER-4; SER-6;
RP   SER-337; SER-361; SER-364; SER-365 AND SER-368, AND IDENTIFICATION BY
RP   MASS 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   [34]
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.,
RA   King A.E., Atkin J.D.;
RT   "C9ORF72, implicated in amytrophic lateral sclerosis and
RT   frontotemporal dementia, regulates endosomal trafficking.";
RL   Hum. Mol. Genet. 23:3579-3595(2014).
RN   [35]
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.,
RA   Wang L., Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human
RT   liver phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [36]
RP   METHYLATION [LARGE SCALE ANALYSIS] AT ARG-206; ARG-218; ARG-225;
RP   ARG-232; ARG-336; ARG-352 AND ARG-370, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [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.,
RA   Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
RA   Vemulapalli V., 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   [37]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-8, AND IDENTIFICATION BY
RP   MASS 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
RT   replication stress reveals novel small ubiquitin-like modified target
RT   proteins and acceptor lysines relevant for genome stability.";
RL   Mol. Cell. Proteomics 14:1419-1434(2015).
RN   [38]
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.,
RA   Ayoub D., 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   [39]
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
RP   SCALE 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-
RT   modification with phosphorylation.";
RL   Nat. Struct. Mol. Biol. 24:325-336(2017).
RN   [40]
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   [41]
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   [42]
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
RT   two RNA-recognition motifs.";
RL   Structure 5:559-570(1997).
RN   [43]
RP   VARIANT IBMPFD3 VAL-314, VARIANTS ALS20 ASN-314 AND SER-319,
RP   INVOLVEMENT IN 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.,
RA   Carter R., Boylan K.B., Wojtas A.M., Rademakers R., Pinkus J.L.,
RA   Greenberg S.A., Trojanowski J.Q., Traynor B.J., Smith B.N., Topp S.,
RA   Gkazi A.S., Miller J., Shaw C.E., Kottlors M., Kirschner J.,
RA   Pestronk A., Li Y.R., Ford A.F., Gitler A.D., Benatar M., King O.D.,
RA   Kimonis V.E., Ross E.D., Weihl C.C., Shorter J., Taylor J.P.;
RT   "Mutations in prion-like domains in hnRNPA2B1 and hnRNPA1 cause
RT   multisystem proteinopathy and ALS.";
RL   Nature 495:467-473(2013).
RN   [44]
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
RT   between ubiquilin-2 and hnRNPA1.";
RL   Hum. Mol. Genet. 24:2565-2577(2015).
RN   [45]
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
CC       particles, transport of poly(A) mRNA from the nucleus to the
CC       cytoplasm and may modulate splice site selection.
CC       {ECO:0000269|PubMed:17371836}.
CC   -!- FUNCTION: (Microbial infection) May play a role in HCV RNA
CC       replication. {ECO:0000269|PubMed:17229681}.
CC   -!- SUBUNIT: Identified in the spliceosome C complex
CC       (PubMed:11991638). Identified in a IGF2BP1-dependent mRNP granule
CC       complex containing untranslated mRNAs (PubMed:17289661). Interacts
CC       with SEPT6 (PubMed:17229681). Interacts with C9orf72
CC       (PubMed:24549040). Interacts with KHDRBS1 (PubMed:17371836).
CC       Interacts with UBQLN2 (PubMed:25616961).
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   -!- SUBUNIT: (Microbial infection) Interacts with HCV NS5B and with
CC       the 5'-UTR and 3'-UTR of HCV RNA. {ECO:0000269|PubMed:17229681}.
CC   -!- INTERACTION:
CC       P27958:- (xeno); NbExp=4; IntAct=EBI-352662, EBI-6904388;
CC       P31942:HNRNPH3; NbExp=3; IntAct=EBI-352662, EBI-711437;
CC       Q07666:KHDRBS1; NbExp=9; IntAct=EBI-352662, EBI-1364;
CC       Q14141:SEPT6; NbExp=3; IntAct=EBI-352662, EBI-745901;
CC       Q9UHD9:UBQLN2; NbExp=4; IntAct=EBI-352677, EBI-947187;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17289661,
CC       ECO:0000269|PubMed:27694260}. Cytoplasm
CC       {ECO:0000269|PubMed:17289661}. Note=Localized in cytoplasmic mRNP
CC       granules containing untranslated mRNAs. Shuttles continuously
CC       between the nucleus and the cytoplasm along with mRNA. Component
CC       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   -!- 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         Note=Is twenty times more abundant than isoform A1-B.;
CC       Name=2;
CC         IsoId=P09651-3; Sequence=VSP_034076;
CC         Note=No experimental confirmation available.;
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
CC       with or without frontotemporal dementia 3 (IBMPFD3) [MIM:615424]:
CC       An autosomal dominant disease characterized by disabling muscle
CC       weakness clinically resembling to limb girdle muscular dystrophy,
CC       osteolytic bone lesions consistent with Paget disease, and
CC       premature frontotemporal dementia. Clinical features show
CC       incomplete penetrance. {ECO:0000269|PubMed:23455423}. Note=The
CC       disease is caused by mutations affecting the gene represented in
CC       this entry.
CC   -!- DISEASE: Amyotrophic lateral sclerosis 20 (ALS20) [MIM:615426]: A
CC       neurodegenerative disorder affecting upper motor neurons in the
CC       brain and lower motor neurons in the brain stem and spinal cord,
CC       resulting in fatal paralysis. Sensory abnormalities are absent.
CC       The pathologic hallmarks of the disease include pallor of the
CC       corticospinal tract due to loss of motor neurons, presence of
CC       ubiquitin-positive inclusions within surviving motor neurons, and
CC       deposition of pathologic aggregates. The etiology of amyotrophic
CC       lateral sclerosis is likely to be multifactorial, involving both
CC       genetic and environmental factors. The disease is inherited in 5-
CC       10% of the cases. {ECO:0000269|PubMed:23455423,
CC       ECO:0000269|PubMed:27694260}. Note=The disease is caused by
CC       mutations affecting the gene represented in this entry.
CC   -!- CAUTION: Variant Val-314 has been originally associated with
CC       IBMPFD3 and variant Asn-314 with ALS20 (PubMed:25616961). However
CC       in another report, variant Val-314 is associated with amyotrophic
CC       lateral sclerosis (ALS) but this variant is not supported by
CC       clinical data in this publication (PubMed:25616961).
CC       {ECO:0000305}.
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. [P09651-1]
DR   UniGene; Hs.546261; -.
DR   UniGene; Hs.655424; -.
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   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   DisProt; DP00324; -.
DR   ProteinModelPortal; P09651; -.
DR   SMR; P09651; -.
DR   BioGrid; 109420; 530.
DR   DIP; DIP-29338N; -.
DR   IntAct; P09651; 163.
DR   MINT; MINT-1035550; -.
DR   STRING; 9606.ENSP00000341826; -.
DR   BindingDB; P09651; -.
DR   ChEMBL; CHEMBL1955709; -.
DR   iPTMnet; P09651; -.
DR   PhosphoSitePlus; P09651; -.
DR   SwissPalm; P09651; -.
DR   BioMuta; HNRNPA1; -.
DR   DMDM; 288558857; -.
DR   SWISS-2DPAGE; P09651; -.
DR   EPD; P09651; -.
DR   MaxQB; P09651; -.
DR   PaxDb; P09651; -.
DR   PeptideAtlas; P09651; -.
DR   PRIDE; P09651; -.
DR   TopDownProteomics; P09651-1; -. [P09651-1]
DR   TopDownProteomics; P09651-2; -. [P09651-2]
DR   TopDownProteomics; P09651-3; -. [P09651-3]
DR   Ensembl; ENST00000340913; ENSP00000341826; ENSG00000135486. [P09651-1]
DR   Ensembl; ENST00000546500; ENSP00000448617; ENSG00000135486. [P09651-2]
DR   Ensembl; ENST00000547276; ENSP00000447260; ENSG00000135486. [P09651-3]
DR   Ensembl; ENST00000547566; ENSP00000449913; ENSG00000135486. [P09651-2]
DR   GeneID; 3178; -.
DR   KEGG; hsa:3178; -.
DR   UCSC; uc001sfl.4; human. [P09651-1]
DR   CTD; 3178; -.
DR   DisGeNET; 3178; -.
DR   GeneCards; HNRNPA1; -.
DR   H-InvDB; HIX0032087; -.
DR   H-InvDB; HIX0040127; -.
DR   H-InvDB; HIX0202582; -.
DR   HGNC; HGNC:5031; HNRNPA1.
DR   HPA; CAB010894; -.
DR   HPA; HPA001609; -.
DR   HPA; HPA001666; -.
DR   HPA; HPA005812; -.
DR   HPA; HPA007185; -.
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   eggNOG; KOG0118; Eukaryota.
DR   eggNOG; COG0724; LUCA.
DR   GeneTree; ENSGT00760000118873; -.
DR   HOGENOM; HOG000234442; -.
DR   HOVERGEN; HBG002295; -.
DR   InParanoid; P09651; -.
DR   KO; K12741; -.
DR   OMA; IMTDRNT; -.
DR   OrthoDB; EOG091G1CPI; -.
DR   PhylomeDB; P09651; -.
DR   TreeFam; TF314808; -.
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   SIGNOR; P09651; -.
DR   ChiTaRS; HNRNPA1; human.
DR   EvolutionaryTrace; P09651; -.
DR   GeneWiki; Heterogeneous_nuclear_ribonucleoprotein_A1; -.
DR   GenomeRNAi; 3178; -.
DR   PRO; PR:P09651; -.
DR   Proteomes; UP000005640; Chromosome 12.
DR   Bgee; ENSG00000135486; -.
DR   CleanEx; HS_HNRNPA1; -.
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.
DR   GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
DR   GO; GO:0030529; C:intracellular ribonucleoprotein complex; IDA:UniProtKB.
DR   GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HGNC.
DR   GO; GO:0005634; C:nucleus; 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:0036002; F:pre-mRNA binding; IDA:CAFA.
DR   GO; GO:0019904; F:protein domain specific binding; IPI:UniProtKB.
DR   GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
DR   GO; GO:0003697; F:single-stranded DNA binding; IDA:HGNC.
DR   GO; GO:0003727; F:single-stranded RNA binding; IC:HGNC.
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:0008543; P:fibroblast growth factor receptor signaling pathway; TAS:Reactome.
DR   GO; GO:0006397; P:mRNA processing; TAS:ProtInc.
DR   GO; GO:0000398; P:mRNA splicing, via spliceosome; TAS:Reactome.
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.
DR   GO; GO:0051170; P:nuclear import; IDA:HGNC.
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:0006405; P:RNA export from nucleus; TAS:ProtInc.
DR   GO; GO:0016070; P:RNA metabolic process; TAS:Reactome.
DR   GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
DR   CDD; cd12761; RRM1_hnRNPA1; 1.
DR   CDD; cd12580; RRM2_hnRNPA1; 1.
DR   InterPro; IPR021662; HnRNPA1.
DR   InterPro; IPR034845; hnRNPA1_RRM1.
DR   InterPro; IPR034803; hnRNPA1_RRM2.
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;
DR   PRODOM; P09651.
DR   SWISS-2DPAGE; P09651.
KW   3D-structure; Acetylation; Alternative splicing;
KW   Amyotrophic lateral sclerosis; Complete proteome; Cytoplasm;
KW   Direct protein sequencing; Disease mutation; Host-virus interaction;
KW   Isopeptide bond; Methylation; mRNA processing; mRNA splicing;
KW   mRNA transport; Neurodegeneration; Nucleus; Phosphoprotein;
KW   Polymorphism; Reference proteome; Repeat; Ribonucleoprotein;
KW   RNA-binding; Spliceosome; Transport; Ubl conjugation.
FT   CHAIN         1    372       Heterogeneous nuclear ribonucleoprotein
FT                                A1.
FT                                /FTId=PRO_0000424509.
FT   INIT_MET      1      1       Removed; alternate.
FT                                {ECO:0000244|PubMed:20068231,
FT                                ECO:0000244|PubMed:22814378,
FT                                ECO:0000269|Ref.9}.
FT   CHAIN         2    372       Heterogeneous nuclear ribonucleoprotein
FT                                A1, N-terminally processed.
FT                                /FTId=PRO_0000081828.
FT   DOMAIN       14     97       RRM 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00176}.
FT   DOMAIN      105    184       RRM 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00176}.
FT   REGION        4     94       Globular A domain.
FT   REGION       95    185       Globular B domain.
FT   REGION      218    240       RNA-binding RGG-box.
FT   REGION      320    357       Nuclear targeting sequence (M9).
FT   COMPBIAS    195    372       Gly-rich.
FT   MOD_RES       1      1       N-acetylmethionine.
FT                                {ECO:0000244|PubMed:22814378}.
FT   MOD_RES       2      2       N-acetylserine; in Heterogeneous nuclear
FT                                ribonucleoprotein A1, N-terminally
FT                                processed. {ECO:0000244|PubMed:20068231,
FT                                ECO:0000244|PubMed:22814378,
FT                                ECO:0000269|Ref.9}.
FT   MOD_RES       2      2       Phosphoserine.
FT                                {ECO:0000244|PubMed:20068231,
FT                                ECO:0000244|PubMed:23186163}.
FT   MOD_RES       3      3       N6-acetyllysine; alternate.
FT                                {ECO:0000244|PubMed:19608861}.
FT   MOD_RES       4      4       Phosphoserine.
FT                                {ECO:0000244|PubMed:20068231,
FT                                ECO:0000244|PubMed:21406692,
FT                                ECO:0000244|PubMed:23186163}.
FT   MOD_RES       6      6       Phosphoserine.
FT                                {ECO:0000244|PubMed:18669648,
FT                                ECO:0000244|PubMed:20068231,
FT                                ECO:0000244|PubMed:21406692,
FT                                ECO:0000244|PubMed:23186163}.
FT   MOD_RES      22     22       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P49312}.
FT   MOD_RES     192    192       Phosphoserine; by MKNK2.
FT                                {ECO:0000269|PubMed:16111636}.
FT   MOD_RES     194    194       Asymmetric dimethylarginine; alternate.
FT                                {ECO:0000250|UniProtKB:P09867}.
FT   MOD_RES     194    194       Dimethylated arginine; alternate.
FT                                {ECO:0000244|PubMed:15782174}.
FT   MOD_RES     194    194       Omega-N-methylarginine; alternate.
FT                                {ECO:0000250|UniProtKB:P49312}.
FT   MOD_RES     199    199       Phosphoserine.
FT                                {ECO:0000244|PubMed:21406692}.
FT   MOD_RES     206    206       Asymmetric dimethylarginine; alternate.
FT                                {ECO:0000244|PubMed:24129315,
FT                                ECO:0000269|Ref.9}.
FT   MOD_RES     206    206       Dimethylated arginine; alternate.
FT                                {ECO:0000244|PubMed:15782174}.
FT   MOD_RES     206    206       Omega-N-methylarginine; alternate.
FT                                {ECO:0000244|PubMed:24129315,
FT                                ECO:0000269|Ref.9}.
FT   MOD_RES     218    218       Asymmetric dimethylarginine; alternate.
FT                                {ECO:0000244|PubMed:24129315}.
FT   MOD_RES     218    218       Omega-N-methylarginine; alternate.
FT                                {ECO:0000244|PubMed:24129315}.
FT   MOD_RES     225    225       Asymmetric dimethylarginine; alternate.
FT                                {ECO:0000244|PubMed:24129315,
FT                                ECO:0000269|Ref.9}.
FT   MOD_RES     225    225       Dimethylated arginine; alternate.
FT                                {ECO:0000244|PubMed:15782174}.
FT   MOD_RES     225    225       Omega-N-methylarginine; alternate.
FT                                {ECO:0000244|PubMed:24129315,
FT                                ECO:0000269|Ref.9}.
FT   MOD_RES     232    232       Asymmetric dimethylarginine; alternate.
FT                                {ECO:0000250|UniProtKB:P04256}.
FT   MOD_RES     232    232       Omega-N-methylarginine; alternate.
FT                                {ECO:0000244|PubMed:24129315}.
FT   MOD_RES     336    336       Omega-N-methylarginine.
FT                                {ECO:0000244|PubMed:24129315}.
FT   MOD_RES     337    337       Phosphoserine.
FT                                {ECO:0000244|PubMed:23186163}.
FT   MOD_RES     350    350       N6-acetyllysine; alternate.
FT                                {ECO:0000244|PubMed:19608861}.
FT   MOD_RES     352    352       Omega-N-methylarginine.
FT                                {ECO:0000244|PubMed:24129315}.
FT   MOD_RES     361    361       Phosphoserine.
FT                                {ECO:0000244|PubMed:23186163}.
FT   MOD_RES     362    362       Phosphoserine; by MKNK2.
FT                                {ECO:0000269|PubMed:16111636}.
FT   MOD_RES     363    363       Phosphoserine; by MKNK2.
FT                                {ECO:0000269|PubMed:16111636}.
FT   MOD_RES     364    364       Phosphoserine; by MKNK2.
FT                                {ECO:0000244|PubMed:23186163,
FT                                ECO:0000269|PubMed:16111636}.
FT   MOD_RES     365    365       Phosphoserine.
FT                                {ECO:0000244|PubMed:21406692,
FT                                ECO:0000244|PubMed:23186163}.
FT   MOD_RES     368    368       Phosphoserine.
FT                                {ECO:0000244|PubMed:18669648,
FT                                ECO:0000244|PubMed:21406692,
FT                                ECO:0000244|PubMed:23186163}.
FT   MOD_RES     370    370       Omega-N-methylarginine.
FT                                {ECO:0000244|PubMed:24129315}.
FT   CROSSLNK      3      3       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2);
FT                                alternate. {ECO:0000244|PubMed:28112733}.
FT   CROSSLNK      8      8       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:25755297,
FT                                ECO:0000244|PubMed:28112733}.
FT   CROSSLNK     78     78       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:28112733}.
FT   CROSSLNK    113    113       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO).
FT                                {ECO:0000269|PubMed:15161980}.
FT   CROSSLNK    179    179       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:28112733}.
FT   CROSSLNK    183    183       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:28112733}.
FT   CROSSLNK    350    350       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2);
FT                                alternate. {ECO:0000244|PubMed:28112733}.
FT   VAR_SEQ     203    307       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_034076.
FT   VAR_SEQ     252    303       Missing (in isoform A1-A).
FT                                {ECO:0000303|PubMed:14702039,
FT                                ECO:0000303|PubMed:15489334,
FT                                ECO:0000303|PubMed:2836799,
FT                                ECO:0000303|Ref.3}.
FT                                /FTId=VSP_005824.
FT   VARIANT     277    277       Q -> K (in ALS20; unknown pathological
FT                                significance).
FT                                {ECO:0000269|PubMed:27694260}.
FT                                /FTId=VAR_077531.
FT   VARIANT     283    283       G -> R (probable polymorphism;
FT                                dbSNP:rs375259222).
FT                                {ECO:0000269|PubMed:27694260}.
FT                                /FTId=VAR_077532.
FT   VARIANT     314    314       D -> N (in ALS20; dbSNP:rs397518453).
FT                                {ECO:0000269|PubMed:23455423}.
FT                                /FTId=VAR_070588.
FT   VARIANT     314    314       D -> V (in IBMPFD3; reduces binding to
FT                                UBQLN2; dbSNP:rs397518452).
FT                                {ECO:0000269|PubMed:23455423,
FT                                ECO:0000269|PubMed:25616961}.
FT                                /FTId=VAR_070589.
FT   VARIANT     319    319       N -> S (in ALS20; dbSNP:rs397518454).
FT                                {ECO:0000269|PubMed:23455423}.
FT                                /FTId=VAR_070590.
FT   VARIANT     340    340       P -> S (in ALS20; increases subcellular
FT                                localization of HNRNPA1 in cytoplasmic
FT                                inclusions with stress granules).
FT                                {ECO:0000269|PubMed:27694260}.
FT                                /FTId=VAR_077533.
FT   MUTAGEN     326    326       G->A: No nuclear import nor export.
FT                                {ECO:0000269|PubMed:7730395}.
FT   MUTAGEN     327    327       P->A: No nuclear import nor export.
FT                                {ECO:0000269|PubMed:7730395}.
FT   MUTAGEN     334    335       GG->LL: Normal nuclear import and export.
FT                                {ECO:0000269|PubMed:7730395}.
FT   CONFLICT    128    128       Y -> F (in Ref. 2; CAA29922).
FT                                {ECO:0000305}.
FT   CONFLICT    140    140       R -> P (in Ref. 8; CAA27874).
FT                                {ECO:0000305}.
FT   CONFLICT    146    146       R -> K (in Ref. 2; CAA29922).
FT                                {ECO:0000305}.
FT   HELIX        11     14       {ECO:0000244|PDB:1L3K}.
FT   STRAND       15     20       {ECO:0000244|PDB:1L3K}.
FT   HELIX        27     34       {ECO:0000244|PDB:1L3K}.
FT   HELIX        35     37       {ECO:0000244|PDB:1L3K}.
FT   STRAND       40     47       {ECO:0000244|PDB:1L3K}.
FT   TURN         49     51       {ECO:0000244|PDB:1L3K}.
FT   STRAND       54     64       {ECO:0000244|PDB:1L3K}.
FT   HELIX        65     73       {ECO:0000244|PDB:1L3K}.
FT   STRAND       76     79       {ECO:0000244|PDB:1U1R}.
FT   STRAND       85     88       {ECO:0000244|PDB:1L3K}.
FT   HELIX        94     96       {ECO:0000244|PDB:1U1Q}.
FT   TURN         98    101       {ECO:0000244|PDB:1U1Q}.
FT   STRAND      105    110       {ECO:0000244|PDB:1L3K}.
FT   TURN        113    115       {ECO:0000244|PDB:1L3K}.
FT   HELIX       118    125       {ECO:0000244|PDB:1L3K}.
FT   TURN        126    128       {ECO:0000244|PDB:1L3K}.
FT   STRAND      131    138       {ECO:0000244|PDB:1L3K}.
FT   TURN        140    142       {ECO:0000244|PDB:1L3K}.
FT   STRAND      145    155       {ECO:0000244|PDB:1L3K}.
FT   HELIX       156    164       {ECO:0000244|PDB:1L3K}.
FT   STRAND      168    170       {ECO:0000244|PDB:1U1Q}.
FT   STRAND      176    179       {ECO:0000244|PDB:1L3K}.
FT   HELIX       183    188       {ECO:0000244|PDB:1U1Q}.
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
//

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