ROA2_SAGOE
ID ROA2_SAGOE Reviewed; 341 AA.
AC Q9TTV2;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 101.
DE RecName: Full=Heterogeneous nuclear ribonucleoproteins A2/B1;
DE Short=hnRNP A2/B1;
DE AltName: Full=Vitamin D response element-binding protein 2;
DE Short=VDRE-BP 2;
GN Name=HNRNPA2B1; Synonyms=HNRPA2B1;
OS Saguinus oedipus (Cotton-top tamarin).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Callitrichinae; Saguinus.
OX NCBI_TaxID=9490;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=10948206; DOI=10.1074/jbc.m007117200;
RA Chen H., Hu B., Allegretto E.A., Adams J.S.;
RT "The vitamin D response element-binding protein. A novel dominant-negative
RT regulator of vitamin D-directed transactivation.";
RL J. Biol. Chem. 275:35557-35564(2000).
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-254 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-254 does
CC not influence nucleocytoplasmic shuttling (By similarity).
CC {ECO:0000250|UniProtKB:A7VJC2, ECO:0000250|UniProtKB:P22626}.
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DR EMBL; AF192348; AAF06330.1; -; mRNA.
DR AlphaFoldDB; Q9TTV2; -.
DR SMR; Q9TTV2; -.
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 1: Evidence at protein level;
KW Acetylation; Direct protein sequencing; Isopeptide bond; Methylation;
KW mRNA processing; mRNA splicing; mRNA transport; Nucleus; Phosphoprotein;
KW Repeat; Ribonucleoprotein; RNA-binding; Secreted; Spliceosome; Transport;
KW Ubl conjugation.
FT CHAIN 1..341
FT /note="Heterogeneous nuclear ribonucleoproteins A2/B1"
FT /id="PRO_0000273981"
FT DOMAIN 9..92
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 100..179
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 181..341
FT /note="Disordered"
FT /evidence="ECO:0000250|UniProtKB:P22626"
FT REGION 296..335
FT /note="Nuclear targeting sequence"
FT /evidence="ECO:0000250"
FT COMPBIAS 179..193
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 17
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P22626"
FT MOD_RES 26
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:O88569"
FT MOD_RES 73
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P22626"
FT MOD_RES 92
FT /note="N6,N6-dimethyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P22626"
FT MOD_RES 128
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P22626"
FT MOD_RES 137
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P22626"
FT MOD_RES 147
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P22626"
FT MOD_RES 156
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P22626"
FT MOD_RES 161
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P22626"
FT MOD_RES 164
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P22626"
FT MOD_RES 177
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P22626"
FT MOD_RES 189
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P22626"
FT MOD_RES 191
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:O88569"
FT MOD_RES 191
FT /note="Dimethylated arginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P22626"
FT MOD_RES 191
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P22626"
FT MOD_RES 200
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P22626"
FT MOD_RES 201
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:O88569"
FT MOD_RES 201
FT /note="Dimethylated arginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P22626"
FT MOD_RES 201
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P22626"
FT MOD_RES 213
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P22626"
FT MOD_RES 216
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P22626"
FT MOD_RES 219
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P22626"
FT MOD_RES 224
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P22626"
FT MOD_RES 226
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P22626"
FT MOD_RES 247
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P22626"
FT MOD_RES 254
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:A7VJC2"
FT MOD_RES 254
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P22626"
FT MOD_RES 312
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P22626"
FT MOD_RES 313
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P22626"
FT MOD_RES 319
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P22626"
FT MOD_RES 329
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P22626"
FT MOD_RES 332
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P22626"
FT MOD_RES 335
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P22626"
FT MOD_RES 338
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P22626"
FT CROSSLNK 10
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P22626"
FT CROSSLNK 92
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P22626"
FT CROSSLNK 100
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P22626"
FT CROSSLNK 108
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P22626"
FT CROSSLNK 125
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P22626"
FT CROSSLNK 140
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P22626"
FT CROSSLNK 156
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P22626"
FT CROSSLNK 161
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P22626"
FT CROSSLNK 174
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P22626"
SQ SEQUENCE 341 AA; 35947 MW; 8B4CBFD5AC314740 CRC64;
MEREKEQFRK LFIGGLSFQT TEESLRNYYE QWGKLTDCVV MRDPASKRSR GFGFVTFSSM
AEVDAAMAAR PHSIDGRVVE PKRAVAREES GKPGAHVTVK KLFVGGIKED TEEHHLRDYF
AEYGKIDTIE IITDRQSGKK RGFGFVTFDD HDPVDKIVLQ KYHTINGHNA EVRKALSRQE
MQEVQSSRSG RGGNFGFGDS RGGGGNFGPG PGSNFRGGSD GYGSGRGFGD GYNGYGGGPG
GGNFGGSPGY GGGRGGYGGG GPGYGNQGGG YGGGYDNYGG GNYGSGNYND FGNYNQQPSN
YGPMKSGNFG GSRNMGGPYG GGNYGPGGSG GSGGYGGRSR Y
