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Heterogeneous nuclear ribonucleoprotein A0 (hnRNP A0)

 ROA0_HUMAN              Reviewed;         305 AA.
Q13151; Q6IB18;
30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
05-DEC-2018, entry version 185.
RecName: Full=Heterogeneous nuclear ribonucleoprotein A0;
Short=hnRNP A0;
Name=HNRNPA0; Synonyms=HNRPA0;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 143-154 AND
287-305.
TISSUE=Placenta;
PubMed=7585247;
Myer V.E., Steitz J.A.;
"Isolation and characterization of a novel, low abundance hnRNP
protein: A0.";
RNA 1:171-182(1995).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain, Eye, Lung, Muscle, Placenta, and Skin;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
PROTEIN SEQUENCE OF 9-24; 99-126; 140-154; 173-189 AND 285-305,
METHYLATION AT ARG-291, AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Colon carcinoma, and Ovarian carcinoma;
Bienvenut W.V., Zebisch A., Lilla S., von Kriegsheim A., Lempens A.,
Kolch W.;
Submitted (DEC-2008) to UniProtKB.
[6]
FUNCTION, AND RNA-BINDING.
PubMed=12456657; DOI=10.1093/emboj/cdf639;
Rousseau S., Morrice N., Peggie M., Campbell D.G., Gaestel M.,
Cohen P.;
"Inhibition of SAPK2a/p38 prevents hnRNP A0 phosphorylation by MAPKAP-
K2 and its interaction with cytokine mRNAs.";
EMBO J. 21:6505-6514(2002).
[7]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[8]
RNA-BINDING, AND PHOSPHORYLATION AT SER-84 BY MAPKAPK2.
PubMed=20932473; DOI=10.1016/j.molcel.2010.09.018;
Reinhardt H.C., Hasskamp P., Schmedding I., Morandell S.,
van Vugt M.A., Wang X., Linding R., Ong S.E., Weaver D., Carr S.A.,
Yaffe M.B.;
"DNA damage activates a spatially distinct late cytoplasmic cell-cycle
checkpoint network controlled by MK2-mediated RNA stabilization.";
Mol. Cell 40:34-49(2010).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-188, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[11]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-68, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[14]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-139; ARG-284 AND ARG-291,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Colon carcinoma;
PubMed=24129315; DOI=10.1074/mcp.O113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
Vemulapalli V., Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
[15]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-172 AND LYS-176, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25218447; DOI=10.1038/nsmb.2890;
Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
Vertegaal A.C.;
"Uncovering global SUMOylation signaling networks in a site-specific
manner.";
Nat. Struct. Mol. Biol. 21:927-936(2014).
[16]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-80; LYS-96; LYS-98; LYS-99;
LYS-106; LYS-154; LYS-159 AND LYS-176, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
-!- FUNCTION: mRNA-binding component of ribonucleosomes. Specifically
binds AU-rich element (ARE)-containing mRNAs. Involved in post-
transcriptional regulation of cytokines mRNAs.
{ECO:0000269|PubMed:12456657}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Component of
ribonucleosomes. {ECO:0000250}.
-!- PTM: Phosphorylated at Ser-84 by MAPKAPK2 in response to LPS
treatment, promoting stabilization of GADD45A mRNA.
{ECO:0000269|PubMed:20932473}.
-!- PTM: Arg-291 is dimethylated, probably to asymmetric
dimethylarginine.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; U23803; AAA65094.1; -; mRNA.
EMBL; CR456986; CAG33267.1; -; mRNA.
EMBL; CH471062; EAW62182.1; -; Genomic_DNA.
EMBL; BC001008; AAH01008.1; -; mRNA.
EMBL; BC007271; AAH07271.1; -; mRNA.
EMBL; BC009284; AAH09284.1; -; mRNA.
EMBL; BC011972; AAH11972.1; -; mRNA.
EMBL; BC012980; AAH12980.1; -; mRNA.
EMBL; BC018949; AAH18949.1; -; mRNA.
EMBL; BC019271; AAH19271.1; -; mRNA.
EMBL; BC028976; AAH28976.1; -; mRNA.
EMBL; BC030249; AAH30249.1; -; mRNA.
CCDS; CCDS4193.1; -.
RefSeq; NP_006796.1; NM_006805.3.
UniGene; Hs.645902; -.
UniGene; Hs.96996; -.
ProteinModelPortal; Q13151; -.
SMR; Q13151; -.
BioGrid; 116149; 176.
IntAct; Q13151; 42.
MINT; Q13151; -.
STRING; 9606.ENSP00000316042; -.
iPTMnet; Q13151; -.
PhosphoSitePlus; Q13151; -.
SwissPalm; Q13151; -.
BioMuta; HNRNPA0; -.
DMDM; 8134660; -.
REPRODUCTION-2DPAGE; Q13151; -.
SWISS-2DPAGE; Q13151; -.
EPD; Q13151; -.
MaxQB; Q13151; -.
PaxDb; Q13151; -.
PeptideAtlas; Q13151; -.
PRIDE; Q13151; -.
ProteomicsDB; 59192; -.
DNASU; 10949; -.
Ensembl; ENST00000314940; ENSP00000316042; ENSG00000177733.
GeneID; 10949; -.
KEGG; hsa:10949; -.
UCSC; uc003lbt.4; human.
CTD; 10949; -.
DisGeNET; 10949; -.
EuPathDB; HostDB:ENSG00000177733.6; -.
GeneCards; HNRNPA0; -.
HGNC; HGNC:5030; HNRNPA0.
HPA; HPA036569; -.
HPA; HPA059404; -.
MIM; 609409; gene.
neXtProt; NX_Q13151; -.
OpenTargets; ENSG00000177733; -.
PharmGKB; PA162391106; -.
eggNOG; ENOG410IQWQ; Eukaryota.
eggNOG; ENOG4111C8J; LUCA.
GeneTree; ENSGT00940000154808; -.
HOGENOM; HOG000234442; -.
HOVERGEN; HBG002295; -.
InParanoid; Q13151; -.
KO; K12894; -.
OMA; PKEDIHA; -.
OrthoDB; EOG091G1CPI; -.
PhylomeDB; Q13151; -.
TreeFam; TF351342; -.
Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
Reactome; R-HSA-72203; Processing of Capped Intron-Containing Pre-mRNA.
GeneWiki; HNRNPA0; -.
GenomeRNAi; 10949; -.
PRO; PR:Q13151; -.
Proteomes; UP000005640; Chromosome 5.
Bgee; ENSG00000177733; Expressed in 247 organ(s), highest expression level in forebrain.
CleanEx; HS_HNRNPA0; -.
Genevisible; Q13151; HS.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; TAS:ProtInc.
GO; GO:1990904; C:ribonucleoprotein complex; IBA:GO_Central.
GO; GO:0017091; F:AU-rich element binding; IDA:UniProtKB.
GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
GO; GO:0070935; P:3'-UTR-mediated mRNA stabilization; ISS:UniProtKB.
GO; GO:0006954; P:inflammatory response; ISS:UniProtKB.
GO; GO:0006397; P:mRNA processing; TAS:ProtInc.
GO; GO:0000398; P:mRNA splicing, via spliceosome; TAS:Reactome.
GO; GO:0032496; P:response to lipopolysaccharide; ISS:UniProtKB.
GO; GO:0016070; P:RNA metabolic process; TAS:Reactome.
CDD; cd12326; RRM1_hnRNPA0; 1.
Gene3D; 3.30.70.330; -; 2.
InterPro; IPR034801; hnRNPA0_RRM1.
InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
InterPro; IPR035979; RBD_domain_sf.
InterPro; IPR000504; RRM_dom.
Pfam; PF00076; RRM_1; 2.
SMART; SM00360; RRM; 2.
SUPFAM; SSF54928; SSF54928; 2.
PROSITE; PS50102; RRM; 2.
1: Evidence at protein level;
Acetylation; Complete proteome; Direct protein sequencing;
Isopeptide bond; Methylation; Nucleus; Phosphoprotein;
Reference proteome; Repeat; Ribonucleoprotein; RNA-binding;
Ubl conjugation.
CHAIN 1 305 Heterogeneous nuclear ribonucleoprotein
A0.
/FTId=PRO_0000081826.
DOMAIN 7 86 RRM 1. {ECO:0000255|PROSITE-
ProRule:PRU00176}.
DOMAIN 98 175 RRM 2. {ECO:0000255|PROSITE-
ProRule:PRU00176}.
COMPBIAS 191 305 Gly-rich.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895}.
MOD_RES 68 68 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 84 84 Phosphoserine; by MAPKAPK2.
{ECO:0000269|PubMed:20932473}.
MOD_RES 133 133 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q9CX86}.
MOD_RES 139 139 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 188 188 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 284 284 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 291 291 Asymmetric dimethylarginine; alternate.
{ECO:0000244|PubMed:24129315}.
MOD_RES 291 291 Dimethylated arginine; alternate.
{ECO:0000269|Ref.5}.
MOD_RES 291 291 Omega-N-methylarginine; alternate.
{ECO:0000244|PubMed:24129315}.
CROSSLNK 80 80 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 96 96 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 98 98 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 99 99 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 106 106 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 154 154 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 159 159 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 172 172 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447}.
CROSSLNK 176 176 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:28112733}.
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


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