ID   ROA0_HUMAN              Reviewed;         305 AA.
AC   Q13151; Q6IB18;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   27-MAR-2024, entry version 217.
DE   RecName: Full=Heterogeneous nuclear ribonucleoprotein A0;
DE            Short=hnRNP A0;
GN   Name=HNRNPA0; Synonyms=HNRPA0;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 143-154 AND 287-305.
RC   TISSUE=Placenta;
RX   PubMed=7585247;
RA   Myer V.E., Steitz J.A.;
RT   "Isolation and characterization of a novel, low abundance hnRNP protein:
RT   A0.";
RL   RNA 1:171-182(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT   "Cloning of human full open reading frames in Gateway(TM) system entry
RT   vector (pDONR201).";
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [3]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain, Eye, Lung, Muscle, Placenta, and Skin;
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   [5]
RP   PROTEIN SEQUENCE OF 9-24; 99-126; 140-154; 173-189 AND 285-305, METHYLATION
RP   AT ARG-291, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Colon carcinoma, and Ovarian carcinoma;
RA   Bienvenut W.V., Zebisch A., Lilla S., von Kriegsheim A., Lempens A.,
RA   Kolch W.;
RL   Submitted (DEC-2008) to UniProtKB.
RN   [6]
RP   FUNCTION, AND RNA-BINDING.
RX   PubMed=12456657; DOI=10.1093/emboj/cdf639;
RA   Rousseau S., Morrice N., Peggie M., Campbell D.G., Gaestel M., Cohen P.;
RT   "Inhibition of SAPK2a/p38 prevents hnRNP A0 phosphorylation by MAPKAP-K2
RT   and its interaction with cytokine mRNAs.";
RL   EMBO J. 21:6505-6514(2002).
RN   [7]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP   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   [8]
RP   RNA-BINDING, AND PHOSPHORYLATION AT SER-84 BY MAPKAPK2.
RX   PubMed=20932473; DOI=10.1016/j.molcel.2010.09.018;
RA   Reinhardt H.C., Hasskamp P., Schmedding I., Morandell S., van Vugt M.A.,
RA   Wang X., Linding R., Ong S.E., Weaver D., Carr S.A., Yaffe M.B.;
RT   "DNA damage activates a spatially distinct late cytoplasmic cell-cycle
RT   checkpoint network controlled by MK2-mediated RNA stabilization.";
RL   Mol. Cell 40:34-49(2010).
RN   [9]
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   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-188, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA   Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT   "System-wide temporal characterization of the proteome and phosphoproteome
RT   of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [11]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA   Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA   Giglione C.;
RT   "Comparative large-scale characterisation of plant vs. mammal proteins
RT   reveals similar and idiosyncratic N-alpha acetylation features.";
RL   Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN   [12]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=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   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-68, AND IDENTIFICATION BY
RP   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   [14]
RP   METHYLATION [LARGE SCALE ANALYSIS] AT ARG-139; ARG-284 AND ARG-291, AND
RP   IDENTIFICATION BY MASS 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., 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   [15]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-172 AND LYS-176, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25218447; DOI=10.1038/nsmb.2890;
RA   Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA   Vertegaal A.C.;
RT   "Uncovering global SUMOylation signaling networks in a site-specific
RT   manner.";
RL   Nat. Struct. Mol. Biol. 21:927-936(2014).
RN   [16]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-80; LYS-96; LYS-98; LYS-99;
RP   LYS-106; LYS-154; LYS-159 AND LYS-176, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE 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-modification
RT   with phosphorylation.";
RL   Nat. Struct. Mol. Biol. 24:325-336(2017).
CC   -!- FUNCTION: mRNA-binding component of ribonucleosomes. Specifically binds
CC       AU-rich element (ARE)-containing mRNAs. Involved in post-
CC       transcriptional regulation of cytokines mRNAs.
CC       {ECO:0000269|PubMed:12456657}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Component of
CC       ribonucleosomes. {ECO:0000250}.
CC   -!- PTM: Phosphorylated at Ser-84 by MAPKAPK2 in response to LPS treatment,
CC       promoting stabilization of GADD45A mRNA. {ECO:0000269|PubMed:20932473}.
CC   -!- PTM: Arg-291 is dimethylated, probably to asymmetric dimethylarginine.
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DR   EMBL; U23803; AAA65094.1; -; mRNA.
DR   EMBL; CR456986; CAG33267.1; -; mRNA.
DR   EMBL; CH471062; EAW62182.1; -; Genomic_DNA.
DR   EMBL; BC001008; AAH01008.1; -; mRNA.
DR   EMBL; BC007271; AAH07271.1; -; mRNA.
DR   EMBL; BC009284; AAH09284.1; -; mRNA.
DR   EMBL; BC011972; AAH11972.1; -; mRNA.
DR   EMBL; BC012980; AAH12980.1; -; mRNA.
DR   EMBL; BC018949; AAH18949.1; -; mRNA.
DR   EMBL; BC019271; AAH19271.1; -; mRNA.
DR   EMBL; BC028976; AAH28976.1; -; mRNA.
DR   EMBL; BC030249; AAH30249.1; -; mRNA.
DR   CCDS; CCDS4193.1; -.
DR   RefSeq; NP_006796.1; NM_006805.3.
DR   AlphaFoldDB; Q13151; -.
DR   SMR; Q13151; -.
DR   BioGRID; 116149; 325.
DR   IntAct; Q13151; 86.
DR   MINT; Q13151; -.
DR   STRING; 9606.ENSP00000316042; -.
DR   GlyCosmos; Q13151; 2 sites, 2 glycans.
DR   GlyGen; Q13151; 2 sites, 2 O-linked glycans (2 sites).
DR   iPTMnet; Q13151; -.
DR   PhosphoSitePlus; Q13151; -.
DR   SwissPalm; Q13151; -.
DR   BioMuta; HNRNPA0; -.
DR   DMDM; 8134660; -.
DR   REPRODUCTION-2DPAGE; Q13151; -.
DR   EPD; Q13151; -.
DR   jPOST; Q13151; -.
DR   MassIVE; Q13151; -.
DR   MaxQB; Q13151; -.
DR   PaxDb; 9606-ENSP00000316042; -.
DR   PeptideAtlas; Q13151; -.
DR   ProteomicsDB; 59192; -.
DR   Pumba; Q13151; -.
DR   Antibodypedia; 14786; 211 antibodies from 30 providers.
DR   DNASU; 10949; -.
DR   Ensembl; ENST00000314940.7; ENSP00000316042.4; ENSG00000177733.7.
DR   GeneID; 10949; -.
DR   KEGG; hsa:10949; -.
DR   MANE-Select; ENST00000314940.7; ENSP00000316042.4; NM_006805.4; NP_006796.1.
DR   UCSC; uc003lbt.4; human.
DR   AGR; HGNC:5030; -.
DR   CTD; 10949; -.
DR   DisGeNET; 10949; -.
DR   GeneCards; HNRNPA0; -.
DR   HGNC; HGNC:5030; HNRNPA0.
DR   HPA; ENSG00000177733; Low tissue specificity.
DR   MIM; 609409; gene.
DR   neXtProt; NX_Q13151; -.
DR   OpenTargets; ENSG00000177733; -.
DR   PharmGKB; PA162391106; -.
DR   VEuPathDB; HostDB:ENSG00000177733; -.
DR   eggNOG; KOG0118; Eukaryota.
DR   GeneTree; ENSGT00940000154808; -.
DR   HOGENOM; CLU_012062_1_4_1; -.
DR   InParanoid; Q13151; -.
DR   OMA; MKGPPFG; -.
DR   OrthoDB; 3127428at2759; -.
DR   PhylomeDB; Q13151; -.
DR   TreeFam; TF351342; -.
DR   PathwayCommons; Q13151; -.
DR   SignaLink; Q13151; -.
DR   SIGNOR; Q13151; -.
DR   BioGRID-ORCS; 10949; 59 hits in 1154 CRISPR screens.
DR   ChiTaRS; HNRNPA0; human.
DR   GeneWiki; HNRNPA0; -.
DR   GenomeRNAi; 10949; -.
DR   Pharos; Q13151; Tbio.
DR   PRO; PR:Q13151; -.
DR   Proteomes; UP000005640; Chromosome 5.
DR   RNAct; Q13151; Protein.
DR   Bgee; ENSG00000177733; Expressed in adult organism and 214 other cell types or tissues.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProtKB-KW.
DR   GO; GO:0045202; C:synapse; IEA:Ensembl.
DR   GO; GO:0035925; F:mRNA 3'-UTR AU-rich region binding; IDA:GO_Central.
DR   GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR   GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR   GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR   GO; GO:0070935; P:3'-UTR-mediated mRNA stabilization; ISS:UniProtKB.
DR   GO; GO:0006954; P:inflammatory response; ISS:UniProtKB.
DR   GO; GO:0006397; P:mRNA processing; TAS:ProtInc.
DR   GO; GO:0032496; P:response to lipopolysaccharide; ISS:UniProtKB.
DR   CDD; cd12326; RRM1_hnRNPA0; 1.
DR   CDD; cd12579; RRM2_hnRNPA0; 1.
DR   Gene3D; 3.30.70.330; -; 2.
DR   InterPro; IPR034801; hnRNPA0_RRM1.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR   InterPro; IPR035979; RBD_domain_sf.
DR   InterPro; IPR000504; RRM_dom.
DR   PANTHER; PTHR48026:SF23; HNRPA0L PROTEIN; 1.
DR   PANTHER; PTHR48026; HOMOLOGOUS TO DROSOPHILA SQD (SQUID) PROTEIN; 1.
DR   Pfam; PF00076; RRM_1; 2.
DR   SMART; SM00360; RRM; 2.
DR   SUPFAM; SSF54928; RNA-binding domain, RBD; 2.
DR   PROSITE; PS50102; RRM; 2.
DR   SWISS-2DPAGE; Q13151; -.
DR   Genevisible; Q13151; HS.
PE   1: Evidence at protein level;
KW   Acetylation; Direct protein sequencing; Isopeptide bond; Methylation;
KW   Nucleus; Phosphoprotein; Reference proteome; Repeat; Ribonucleoprotein;
KW   RNA-binding; Ubl conjugation.
FT   CHAIN           1..305
FT                   /note="Heterogeneous nuclear ribonucleoprotein A0"
FT                   /id="PRO_0000081826"
FT   DOMAIN          7..86
FT                   /note="RRM 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   DOMAIN          98..175
FT                   /note="RRM 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   REGION          174..214
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          262..305
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0007744|PubMed:19413330,
FT                   ECO:0007744|PubMed:22223895"
FT   MOD_RES         68
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:24275569"
FT   MOD_RES         84
FT                   /note="Phosphoserine; by MAPKAPK2"
FT                   /evidence="ECO:0000269|PubMed:20932473"
FT   MOD_RES         133
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9CX86"
FT   MOD_RES         139
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0007744|PubMed:24129315"
FT   MOD_RES         188
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21406692"
FT   MOD_RES         284
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0007744|PubMed:24129315"
FT   MOD_RES         291
FT                   /note="Asymmetric dimethylarginine; alternate"
FT                   /evidence="ECO:0007744|PubMed:24129315"
FT   MOD_RES         291
FT                   /note="Dimethylated arginine; alternate"
FT                   /evidence="ECO:0000269|Ref.5"
FT   MOD_RES         291
FT                   /note="Omega-N-methylarginine; alternate"
FT                   /evidence="ECO:0007744|PubMed:24129315"
FT   CROSSLNK        80
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        96
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        98
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        99
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        106
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        154
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        159
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        172
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:25218447"
FT   CROSSLNK        176
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:25218447,
FT                   ECO:0007744|PubMed:28112733"
SQ   SEQUENCE   305 AA;  30841 MW;  9A976A39345AA149 CRC64;
     MENSQLCKLF IGGLNVQTSE SGLRGHFEAF GTLTDCVVVV NPQTKRSRCF GFVTYSNVEE
     ADAAMAASPH AVDGNTVELK RAVSREDSAR PGAHAKVKKL FVGGLKGDVA EGDLIEHFSQ
     FGTVEKAEII ADKQSGKKRG FGFVYFQNHD AADKAAVVKF HPIQGHRVEV KKAVPKEDIY
     SGGGGGGSRS SRGGRGGRGR GGGRDQNGLS KGGGGGYNSY GGYGGGGGGG YNAYGGGGGG
     SSYGGSDYGN GFGGFGSYSQ HQSSYGPMKS GGGGGGGGSS WGGRSNSGPY RGGYGGGGGY
     GGSSF
//