ROA2_PONAB
ID ROA2_PONAB Reviewed; 353 AA.
AC Q5RBU8;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 104.
DE RecName: Full=Heterogeneous nuclear ribonucleoproteins A2/B1;
DE Short=hnRNP A2/B1;
GN Name=HNRNPA2B1; Synonyms=HNRPA2B1;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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). {ECO:0000250|UniProtKB:A7VJC2,
CC ECO:0000250|UniProtKB:P22626}.
CC -!- SUBUNIT: Identified in the spliceosome C complex. Identified in a
CC IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs.
CC Interacts with IGF2BP1. Interacts with C9orf72. Interacts with DGCR8.
CC Interacts with TARDBP. Interacts with CKAP5 (By similarity). Interacts
CC with PPIA/CYPA (By similarity). {ECO:0000250|UniProtKB:P22626}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
CC {ECO:0000250|UniProtKB:P22626}. 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 follwong sumoylation.
CC {ECO:0000250|UniProtKB:P22626}.
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}.
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DR EMBL; CR858535; CAH90762.1; -; mRNA.
DR RefSeq; NP_001127331.1; NM_001133859.2.
DR AlphaFoldDB; Q5RBU8; -.
DR SMR; Q5RBU8; -.
DR STRING; 9601.ENSPPYP00000019858; -.
DR GeneID; 100174392; -.
DR KEGG; pon:100174392; -.
DR CTD; 3181; -.
DR eggNOG; KOG0118; Eukaryota.
DR InParanoid; Q5RBU8; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:1990904; C:ribonucleoprotein complex; ISS:UniProtKB.
DR GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
DR GO; GO:0035198; F:miRNA binding; ISS:UniProtKB.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; ISS:UniProtKB.
DR GO; GO:1990247; F:N6-methyladenosine-containing RNA binding; ISS:UniProtKB.
DR GO; GO:0043047; F:single-stranded telomeric DNA binding; ISS:UniProtKB.
DR GO; GO:1990428; P:miRNA transport; ISS:UniProtKB.
DR GO; GO:0006406; P:mRNA export from nucleus; ISS:UniProtKB.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; ISS:UniProtKB.
DR GO; GO:0031053; P:primary miRNA processing; ISS:UniProtKB.
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 2: Evidence at transcript level;
KW Acetylation; 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_0000273980"
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:0000250|UniProtKB:P22626"
FT MOD_RES 38
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:O88569"
FT MOD_RES 85
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P22626"
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:0000250|UniProtKB:O88569"
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:0000250|UniProtKB:P22626"
FT MOD_RES 212
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P22626"
FT MOD_RES 213
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:O88569"
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:0000250|UniProtKB:P22626"
FT MOD_RES 225
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P22626"
FT MOD_RES 228
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P22626"
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:0000250|UniProtKB:P22626"
FT MOD_RES 259
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P22626"
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:0000250|UniProtKB:P22626"
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:0000250|UniProtKB:P22626"
FT MOD_RES 331
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P22626"
FT MOD_RES 341
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P22626"
FT MOD_RES 344
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P22626"
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:0000250|UniProtKB:P22626"
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"
SQ SEQUENCE 353 AA; 37404 MW; AD2571AF73888C6E CRC64;
MEKTLETVPL ERKKREKEQF RKLFIGGLSF ETTEESLRNY YEQWGKLTDC VVMRDPASKR
SRGFGFVTFS SMAEVDAAMA ARPHSIDGRV VEPKRAVARE ESGKPGAHVT VKKLFVGGIK
EDTEEHHLRD YFEEYGKIDT IEIITDRQSG KKRGFGFVTF DDHDPVDKIV LQKHHTINGH
NAEVRKALSR QEMQEVQSSR SGRGGNFGFG DSRGGGGNFG PGPGSNFRGG SDGYGSGRGF
GDGYNGYGGG PGGGNFGGSP GYGGGRGGYG GGGPGYGNQG GGYGGGYDNY GGGNYGSGNY
NDFGNYNQQP SNYGPMKSGN FGGSRNMGGP YGGGNYGPGG SGGSGGYGGR SRY
