ROA2_MOUSE
ID ROA2_MOUSE Reviewed; 353 AA.
AC O88569; B9EJ02; Q3UVJ5; Q6PCV9; Q8C2A0; Q8CJ71; Q91ZR9; Q9R204;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 194.
DE RecName: Full=Heterogeneous nuclear ribonucleoproteins A2/B1;
DE Short=hnRNP A2/B1;
GN Name=Hnrnpa2b1; Synonyms=Hnrpa2b1;
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 [MRNA] (ISOFORM 2).
RC STRAIN=C3Heb/FeJ; TISSUE=Brain;
RX PubMed=12243756; DOI=10.1006/excr.2002.5604;
RA Brumwell C., Antolik C., Carson J.H., Barbarese E.;
RT "Intracellular trafficking of hnRNP A2 in oligodendrocytes.";
RL Exp. Cell Res. 279:310-320(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC STRAIN=BALB/cJ;
RX PubMed=12242009; DOI=10.1016/s0378-1119(02)00800-4;
RA Hatfield J.T., Rothnagel J.A., Smith R.;
RT "Characterization of the mouse hnRNP A2/B1/B0 gene and identification of
RT processed pseudogenes.";
RL Gene 295:33-42(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 2).
RX PubMed=12546712; DOI=10.1186/1471-2164-4-2;
RA Roshon M., DeGregori J.V., Ruley H.E.;
RT "Gene trap mutagenesis of hnRNP A2/B1: a cryptic 3' splice site in the
RT neomycin resistance gene allows continued expression of the disrupted
RT cellular gene.";
RL BMC Genomics 4:2-2(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Thymus, and Urinary bladder;
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 [5]
RP PROTEIN SEQUENCE OF 23-38; 47-54; 114-120; 138-147; 154-168; 174-185;
RP 191-200 AND 204-228, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Brain, and Hippocampus;
RA Lubec G., Klug S., Yang J.W., Zigmond M., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC STRAIN=FVB/N; TISSUE=Brain, and Mammary tumor;
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-212, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18630941; DOI=10.1021/pr800223m;
RA Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT "Specific phosphopeptide enrichment with immobilized titanium ion affinity
RT chromatography adsorbent for phosphoproteome analysis.";
RL J. Proteome Res. 7:3957-3967(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29; SER-85; SER-212; SER-225;
RP SER-259; SER-341 AND SER-344, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC 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 [10]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-38; ARG-203; ARG-213; ARG-228;
RP ARG-238; ARG-266; ARG-325 AND ARG-350, AND IDENTIFICATION BY MASS
RP 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).
RN [11]
RP FUNCTION, SUBUNIT, INTERACTION WITH TBK1; STING1 AND SRC, SUBCELLULAR
RP LOCATION, AND METHYLATION AT ARG-228.
RX PubMed=31320558; DOI=10.1126/science.aav0758;
RA Wang L., Wen M., Cao X.;
RT "Nuclear hnRNPA2B1 initiates and amplifies the innate immune response to
RT DNA viruses.";
RL Science 0:0-0(2019).
CC -!- FUNCTION: Heterogeneous nuclear ribonucleoprotein (hnRNP) that
CC associates with nascent pre-mRNAs, packaging them into hnRNP particles.
CC The hnRNP particle arrangement on nascent hnRNA is non-random and
CC sequence-dependent and serves to condense and stabilize the transcripts
CC and minimize tangling and knotting. Packaging plays a role in various
CC processes such as transcription, pre-mRNA processing, RNA nuclear
CC export, subcellular location, mRNA translation and stability of mature
CC mRNAs. Forms hnRNP particles with at least 20 other different hnRNP and
CC heterogeneous nuclear RNA in the nucleus. Involved in transport of
CC specific mRNAs to the cytoplasm in oligodendrocytes and neurons: acts
CC by specifically recognizing and binding the A2RE (21 nucleotide hnRNP
CC A2 response element) or the A2RE11 (derivative 11 nucleotide
CC oligonucleotide) sequence motifs present on some mRNAs, and promotes
CC their transport to the cytoplasm (By similarity). Specifically binds
CC single-stranded telomeric DNA sequences, protecting telomeric DNA
CC repeat against endonuclease digestion (By similarity). Also binds other
CC RNA molecules, such as primary miRNA (pri-miRNAs): acts as a nuclear
CC 'reader' of the N6-methyladenosine (m6A) mark by specifically
CC recognizing and binding a subset of nuclear m6A-containing pri-miRNAs.
CC Binding to m6A-containing pri-miRNAs promotes pri-miRNA processing by
CC enhancing binding of DGCR8 to pri-miRNA transcripts. Involved in miRNA
CC sorting into exosomes following sumoylation, possibly by binding (m6A)-
CC containing pre-miRNAs. Acts as a regulator of efficiency of mRNA
CC splicing, possibly by binding to m6A-containing pre-mRNAs (By
CC similarity). Plays a role in the splicing of pyruvate kinase PKM by
CC binding repressively to sequences flanking PKM exon 9, inhibiting exon
CC 9 inclusion and resulting in exon 10 inclusion and production of the
CC PKM M2 isoform (By similarity). Also plays a role in the activation of
CC the innate immune response. Mechanistically, senses the presence of
CC viral DNA in the nucleus, homodimerizes and is demethylated by JMJD6.
CC In turn, translocates to the cytoplasm where it activates the TBK1-IRF3
CC pathway, leading to interferon alpha/beta production (PubMed:31320558).
CC {ECO:0000250|UniProtKB:A7VJC2, ECO:0000250|UniProtKB:P22626,
CC ECO:0000269|PubMed:31320558}.
CC -!- SUBUNIT: Homodimer; dimerization is required for nucleocytoplasmic
CC translocation (PubMed:31320558). Identified in the spliceosome C
CC complex. Identified in a IGF2BP1-dependent mRNP granule complex
CC containing untranslated mRNAs. Interacts with IGF2BP1. Interacts with
CC C9orf72. Interacts with DGCR8. Interacts with TARDBP. Interacts with
CC CKAP5. Interacts with TBK1 (PubMed:31320558). Interacts with STING1
CC (PubMed:31320558). Interacts with SRC (PubMed:31320558). Interacts with
CC PPIA/CYPA (By similarity). {ECO:0000250|UniProtKB:P22626,
CC ECO:0000269|PubMed:31320558}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:31320558}. Nucleus,
CC nucleoplasm {ECO:0000250|UniProtKB:P22626}. Cytoplasm
CC {ECO:0000269|PubMed:31320558}. Cytoplasmic granule
CC {ECO:0000250|UniProtKB:P22626}. Secreted, extracellular exosome
CC {ECO:0000250|UniProtKB:P22626}. Note=Localized in cytoplasmic mRNP
CC granules containing untranslated mRNAs. Component of ribonucleosomes.
CC Not found in the nucleolus. Found in exosomes following sumoylation.
CC {ECO:0000250|UniProtKB:P22626}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=B1;
CC IsoId=O88569-1; Sequence=Displayed;
CC Name=2; Synonyms=A2;
CC IsoId=O88569-2; Sequence=VSP_022595;
CC Name=3;
CC IsoId=O88569-3; Sequence=VSP_022595, VSP_025012;
CC -!- DOMAIN: The disordered region, when incubated at high concentration, is
CC able to polymerize into labile, amyloid-like fibers and form cross-beta
CC polymerization structures, probably driving the formation of hydrogels.
CC In contrast to irreversible, pathogenic amyloids, the fibers
CC polymerized from LC regions disassemble upon dilution. A number of
CC evidence suggests that formation of cross-beta structures by LC regions
CC mediate the formation of RNA granules, liquid-like droplets, and
CC hydrogels. {ECO:0000250|UniProtKB:P22626}.
CC -!- PTM: Sumoylated in exosomes, promoting miRNAs-binding.
CC {ECO:0000250|UniProtKB:P22626}.
CC -!- PTM: Asymmetric dimethylation at Arg-266 constitutes the major
CC methylation site (By similarity). According to a report, methylation
CC affects subcellular location and promotes nuclear localization (By
CC similarity). According to another report, methylation at Arg-266 does
CC not influence nucleocytoplasmic shuttling (By similarity).
CC {ECO:0000250|UniProtKB:A7VJC2, ECO:0000250|UniProtKB:P22626}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF406651; AAK98601.2; -; mRNA.
DR EMBL; AF452567; AAN16352.1; -; Genomic_DNA.
DR EMBL; AF073990; AAD29846.1; -; Genomic_DNA.
DR EMBL; AF073993; AAC26867.1; -; mRNA.
DR EMBL; AK089012; BAC40700.1; -; mRNA.
DR EMBL; AK137214; BAE23274.1; -; mRNA.
DR EMBL; BC059107; AAH59107.1; -; mRNA.
DR EMBL; BC141253; AAI41254.1; -; mRNA.
DR CCDS; CCDS51773.1; -. [O88569-3]
DR CCDS; CCDS51774.1; -. [O88569-2]
DR CCDS; CCDS90046.1; -. [O88569-1]
DR RefSeq; NP_058086.2; NM_016806.3. [O88569-2]
DR RefSeq; NP_872591.1; NM_182650.4. [O88569-3]
DR RefSeq; XP_006506436.2; XM_006506373.3. [O88569-1]
DR RefSeq; XP_006506437.2; XM_006506374.3.
DR AlphaFoldDB; O88569; -.
DR SMR; O88569; -.
DR BioGRID; 207301; 104.
DR IntAct; O88569; 10.
DR MINT; O88569; -.
DR STRING; 10090.ENSMUSP00000110103; -.
DR iPTMnet; O88569; -.
DR PhosphoSitePlus; O88569; -.
DR SwissPalm; O88569; -.
DR REPRODUCTION-2DPAGE; IPI00405058; -.
DR REPRODUCTION-2DPAGE; O88569; -.
DR SWISS-2DPAGE; O88569; -.
DR CPTAC; non-CPTAC-3743; -.
DR EPD; O88569; -.
DR jPOST; O88569; -.
DR MaxQB; O88569; -.
DR PaxDb; O88569; -.
DR PeptideAtlas; O88569; -.
DR PRIDE; O88569; -.
DR ProteomicsDB; 260912; -. [O88569-1]
DR ProteomicsDB; 260913; -. [O88569-2]
DR ProteomicsDB; 260914; -. [O88569-3]
DR TopDownProteomics; O88569-1; -. [O88569-1]
DR TopDownProteomics; O88569-2; -. [O88569-2]
DR TopDownProteomics; O88569-3; -. [O88569-3]
DR Antibodypedia; 3240; 460 antibodies from 34 providers.
DR DNASU; 53379; -.
DR Ensembl; ENSMUST00000069949; ENSMUSP00000067491; ENSMUSG00000004980. [O88569-3]
DR Ensembl; ENSMUST00000090002; ENSMUSP00000087453; ENSMUSG00000004980. [O88569-2]
DR Ensembl; ENSMUST00000114459; ENSMUSP00000110103; ENSMUSG00000004980. [O88569-1]
DR Ensembl; ENSMUST00000203220; ENSMUSP00000145374; ENSMUSG00000004980. [O88569-2]
DR Ensembl; ENSMUST00000203954; ENSMUSP00000145028; ENSMUSG00000004980. [O88569-1]
DR Ensembl; ENSMUST00000204158; ENSMUSP00000145383; ENSMUSG00000004980. [O88569-3]
DR Ensembl; ENSMUST00000204188; ENSMUSP00000145245; ENSMUSG00000004980. [O88569-3]
DR GeneID; 53379; -.
DR KEGG; mmu:53379; -.
DR UCSC; uc009bxm.2; mouse. [O88569-3]
DR UCSC; uc009bxn.2; mouse. [O88569-2]
DR CTD; 3181; -.
DR MGI; MGI:104819; Hnrnpa2b1.
DR VEuPathDB; HostDB:ENSMUSG00000004980; -.
DR eggNOG; KOG0118; Eukaryota.
DR GeneTree; ENSGT00940000154431; -.
DR HOGENOM; CLU_012062_1_0_1; -.
DR InParanoid; O88569; -.
DR OMA; WGNNRQN; -.
DR OrthoDB; 1202220at2759; -.
DR PhylomeDB; O88569; -.
DR TreeFam; TF351342; -.
DR Reactome; R-MMU-72163; mRNA Splicing - Major Pathway.
DR Reactome; R-MMU-72203; Processing of Capped Intron-Containing Pre-mRNA.
DR BioGRID-ORCS; 53379; 6 hits in 75 CRISPR screens.
DR ChiTaRS; Hnrnpa2b1; mouse.
DR PRO; PR:O88569; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; O88569; protein.
DR Bgee; ENSMUSG00000004980; Expressed in ventricular zone and 252 other tissues.
DR ExpressionAtlas; O88569; baseline and differential.
DR Genevisible; O88569; MM.
DR GO; GO:0015030; C:Cajal body; ISO:MGI.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; ISO:MGI.
DR GO; GO:0000785; C:chromatin; ISO:MGI.
DR GO; GO:0000781; C:chromosome, telomeric region; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; ISS:UniProtKB.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR GO; GO:0043005; C:neuron projection; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0071598; C:neuronal ribonucleoprotein granule; ISO:MGI.
DR GO; GO:0016363; C:nuclear matrix; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0043204; C:perikaryon; ISO:MGI.
DR GO; GO:0099524; C:postsynaptic cytosol; ISO:MGI.
DR GO; GO:1990904; C:ribonucleoprotein complex; ISS:UniProtKB.
DR GO; GO:0005681; C:spliceosomal complex; ISS:HGNC-UCL.
DR GO; GO:0070182; F:DNA polymerase binding; ISO:MGI.
DR GO; GO:0098505; F:G-rich strand telomeric DNA binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0035198; F:miRNA binding; ISS:UniProtKB.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; ISS:UniProtKB.
DR GO; GO:1990715; F:mRNA CDS binding; ISO:MGI.
DR GO; GO:1990247; F:N6-methyladenosine-containing RNA binding; ISS:UniProtKB.
DR GO; GO:0097157; F:pre-mRNA intronic binding; IDA:MGI.
DR GO; GO:0001069; F:regulatory region RNA binding; ISO:MGI.
DR GO; GO:0003723; F:RNA binding; IPI:MGI.
DR GO; GO:0043047; F:single-stranded telomeric DNA binding; ISS:UniProtKB.
DR GO; GO:0044806; P:G-quadruplex DNA unwinding; ISO:MGI.
DR GO; GO:1990428; P:miRNA transport; ISS:UniProtKB.
DR GO; GO:0006406; P:mRNA export from nucleus; ISS:UniProtKB.
DR GO; GO:0006397; P:mRNA processing; ISS:HGNC-UCL.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; ISS:UniProtKB.
DR GO; GO:0051028; P:mRNA transport; IBA:GO_Central.
DR GO; GO:0048025; P:negative regulation of mRNA splicing, via spliceosome; IDA:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IGI:MGI.
DR GO; GO:1905663; P:positive regulation of telomerase RNA reverse transcriptase activity; ISO:MGI.
DR GO; GO:1904358; P:positive regulation of telomere maintenance via telomere lengthening; ISO:MGI.
DR GO; GO:0031053; P:primary miRNA processing; ISS:UniProtKB.
DR GO; GO:0050658; P:RNA transport; ISS:HGNC-UCL.
DR GO; GO:0016233; P:telomere capping; ISO:MGI.
DR CDD; cd12762; RRM1_hnRNPA2B1; 1.
DR Gene3D; 3.30.70.330; -; 2.
DR InterPro; IPR034489; hnRNP_A2/B1.
DR InterPro; IPR034486; hnRNPA2B1_RRM1.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR PANTHER; PTHR48026:SF13; PTHR48026:SF13; 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 Acetylation; Alternative splicing; Cytoplasm; Direct protein sequencing;
KW Isopeptide bond; Methylation; mRNA processing; mRNA splicing;
KW mRNA transport; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Ribonucleoprotein; RNA-binding; Secreted; Spliceosome; Transport;
KW Ubl conjugation.
FT CHAIN 1..353
FT /note="Heterogeneous nuclear ribonucleoproteins A2/B1"
FT /id="PRO_0000081837"
FT DOMAIN 21..104
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 112..191
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 193..353
FT /note="Disordered"
FT /evidence="ECO:0000250|UniProtKB:P22626"
FT REGION 308..347
FT /note="Nuclear targeting sequence"
FT /evidence="ECO:0000250"
FT MOTIF 9..15
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 191..205
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P22626"
FT MOD_RES 4
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P22626"
FT MOD_RES 29
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 38
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 85
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 104
FT /note="N6,N6-dimethyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P22626"
FT MOD_RES 140
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P22626"
FT MOD_RES 149
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P22626"
FT MOD_RES 159
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P22626"
FT MOD_RES 168
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P22626"
FT MOD_RES 173
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P22626"
FT MOD_RES 176
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P22626"
FT MOD_RES 189
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P22626"
FT MOD_RES 201
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P22626"
FT MOD_RES 203
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 203
FT /note="Dimethylated arginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P22626"
FT MOD_RES 203
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 212
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 213
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 213
FT /note="Dimethylated arginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P22626"
FT MOD_RES 213
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 225
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 228
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000269|PubMed:31320558,
FT ECO:0007744|PubMed:24129315"
FT MOD_RES 231
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P22626"
FT MOD_RES 236
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P22626"
FT MOD_RES 238
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 259
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 266
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:A7VJC2"
FT MOD_RES 266
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 324
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P22626"
FT MOD_RES 325
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 331
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P22626"
FT MOD_RES 341
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 344
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 347
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P22626"
FT MOD_RES 350
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT CROSSLNK 22
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P22626"
FT CROSSLNK 104
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P22626"
FT CROSSLNK 112
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P22626"
FT CROSSLNK 120
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P22626"
FT CROSSLNK 137
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P22626"
FT CROSSLNK 152
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P22626"
FT CROSSLNK 168
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P22626"
FT CROSSLNK 173
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P22626"
FT CROSSLNK 186
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P22626"
FT VAR_SEQ 3..14
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:12243756,
FT ECO:0000303|PubMed:12546712, ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_022595"
FT VAR_SEQ 252..291
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_025012"
FT CONFLICT 173
FT /note="K -> E (in Ref. 4; BAE23274)"
FT /evidence="ECO:0000305"
FT CONFLICT 214
FT /note="G -> V (in Ref. 4; BAE23274)"
FT /evidence="ECO:0000305"
FT CONFLICT 299
FT /note="S -> T (in Ref. 3; AAC26867)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 353 AA; 37403 MW; EC387DA3D8E989E4 CRC64;
MEKTLETVPL ERKKREKEQF RKLFIGGLSF ETTEESLRNY YEQWGKLTDC VVMRDPASKR
SRGFGFVTFS SMAEVDAAMA ARPHSIDGRV VEPKRAVARE ESGKPGAHVT VKKLFVGGIK
EDTEEHHLRD YFEEYGKIDT IEIITDRQSG KKRGFGFVTF DDHDPVDKIV LQKYHTINGH
NAEVRKALSR QEMQEVQSSR SGRGGNFGFG DSRGGGGNFG PGPGSNFRGG SDGYGSGRGF
GDGYNGYGGG PGGGNFGGSP GYGGGRGGYG GGGPGYGNQG GGYGGGYDNY GGGNYGSGSY
NDFGNYNQQP SNYGPMKSGN FGGSRNMGGP YGGGNYGPGG SGGSGGYGGR SRY
