ID   ROA0_MOUSE              Reviewed;         305 AA.
AC   Q9CX86;
DT   25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   27-MAR-2024, entry version 171.
DE   RecName: Full=Heterogeneous nuclear ribonucleoprotein A0;
DE            Short=hnRNP A0;
GN   Name=Hnrnpa0; Synonyms=Hnrpa0;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Head;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   FUNCTION, RNA-BINDING, AND PHOSPHORYLATION AT SER-84 BY MAPKAPK2.
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   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Pancreas, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [5]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-133, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA   Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA   Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT   "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT   pathways.";
RL   Mol. Cell 50:919-930(2013).
RN   [6]
RP   METHYLATION [LARGE SCALE ANALYSIS] AT ARG-139; ARG-286 AND ARG-293, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, and Embryo;
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).
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:12456657}.
CC   -!- PTM: Arg-293 is dimethylated, probably to asymmetric dimethylarginine.
CC       {ECO:0000250}.
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DR   EMBL; AK019388; BAB31694.1; -; mRNA.
DR   EMBL; AC165251; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   CCDS; CCDS49280.1; -.
DR   RefSeq; NP_084148.1; NM_029872.1.
DR   AlphaFoldDB; Q9CX86; -.
DR   SMR; Q9CX86; -.
DR   BioGRID; 218538; 27.
DR   IntAct; Q9CX86; 3.
DR   MINT; Q9CX86; -.
DR   STRING; 10090.ENSMUSP00000007980; -.
DR   GlyGen; Q9CX86; 2 sites, 1 O-linked glycan (2 sites).
DR   iPTMnet; Q9CX86; -.
DR   PhosphoSitePlus; Q9CX86; -.
DR   SwissPalm; Q9CX86; -.
DR   EPD; Q9CX86; -.
DR   jPOST; Q9CX86; -.
DR   MaxQB; Q9CX86; -.
DR   PaxDb; 10090-ENSMUSP00000007980; -.
DR   PeptideAtlas; Q9CX86; -.
DR   ProteomicsDB; 300431; -.
DR   Pumba; Q9CX86; -.
DR   Antibodypedia; 14786; 211 antibodies from 30 providers.
DR   Ensembl; ENSMUST00000007980.7; ENSMUSP00000007980.7; ENSMUSG00000007836.7.
DR   GeneID; 77134; -.
DR   KEGG; mmu:77134; -.
DR   UCSC; uc007qtf.2; mouse.
DR   AGR; MGI:1924384; -.
DR   CTD; 10949; -.
DR   MGI; MGI:1924384; Hnrnpa0.
DR   VEuPathDB; HostDB:ENSMUSG00000007836; -.
DR   eggNOG; KOG0118; Eukaryota.
DR   GeneTree; ENSGT00940000154808; -.
DR   HOGENOM; CLU_012062_1_4_1; -.
DR   InParanoid; Q9CX86; -.
DR   OMA; MKGPPFG; -.
DR   OrthoDB; 3127428at2759; -.
DR   PhylomeDB; Q9CX86; -.
DR   TreeFam; TF351342; -.
DR   BioGRID-ORCS; 77134; 6 hits in 81 CRISPR screens.
DR   ChiTaRS; Hnrnpa0; mouse.
DR   PRO; PR:Q9CX86; -.
DR   Proteomes; UP000000589; Chromosome 13.
DR   RNAct; Q9CX86; Protein.
DR   Bgee; ENSMUSG00000007836; Expressed in manus and 232 other cell types or tissues.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
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; IDA:SynGO.
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; ISO:MGI.
DR   GO; GO:0070935; P:3'-UTR-mediated mRNA stabilization; IDA:UniProtKB.
DR   GO; GO:0006954; P:inflammatory response; IDA:UniProtKB.
DR   GO; GO:0032496; P:response to lipopolysaccharide; IDA:UniProtKB.
DR   CDD; cd12326; RRM1_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   Genevisible; Q9CX86; MM.
PE   1: Evidence at protein level;
KW   Acetylation; Isopeptide bond; Methylation; Nucleus; Phosphoprotein;
KW   Reference proteome; Repeat; Ribonucleoprotein; RNA-binding;
KW   Ubl conjugation.
FT   CHAIN           1..305
FT                   /note="Heterogeneous nuclear ribonucleoprotein A0"
FT                   /id="PRO_0000415269"
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          178..211
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          265..305
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:Q13151"
FT   MOD_RES         68
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q13151"
FT   MOD_RES         84
FT                   /note="Phosphoserine; by MAPKAPK2"
FT                   /evidence="ECO:0000269|PubMed:12456657"
FT   MOD_RES         133
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         139
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0007744|PubMed:24129315"
FT   MOD_RES         286
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0007744|PubMed:24129315"
FT   MOD_RES         293
FT                   /note="Asymmetric dimethylarginine; alternate"
FT                   /evidence="ECO:0007744|PubMed:24129315"
FT   MOD_RES         293
FT                   /note="Dimethylated arginine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q13151"
FT   MOD_RES         293
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:0000250|UniProtKB:Q13151"
FT   CROSSLNK        96
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q13151"
FT   CROSSLNK        98
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q13151"
FT   CROSSLNK        99
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q13151"
FT   CROSSLNK        106
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q13151"
FT   CROSSLNK        154
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q13151"
FT   CROSSLNK        159
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q13151"
FT   CROSSLNK        172
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q13151"
FT   CROSSLNK        176
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q13151"
SQ   SEQUENCE   305 AA;  30530 MW;  B3F3BB8C5480BB56 CRC64;
     MENSQLCKLF IGGLNVQTSE SGLRGHFEAF GTLTDCVVVV NPQTKRSRCF GFVTYSNVEE
     ADAAMAASPH AVDGNTVELK RAVSREDSAR PGAHAKVKKL FVGGLKGDVA EGDLIEHFSQ
     FGAVEKAEII ADKQSGKKRG FGFVYFQSHD AADKAAVVKF HPIQGHRVEV KKAVPKEDIH
     AGGGGARAAR GGRGGGRGRG GGGGGGGRDQ NGLAKGGGGG GGGYNSYGGY GGYGAYGGGG
     GGGGSYGGSD YGNGFGGFGS YSQHQSSYGP MKSGGGGGGG GSWGGRSNSG PYRGGYGGGY
     GGGSF
//