ROA1_PANTR
ID ROA1_PANTR Reviewed; 320 AA.
AC A5A6H4; Q564E0;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Heterogeneous nuclear ribonucleoprotein A1;
DE Short=hnRNP A1;
DE AltName: Full=Helix-destabilizing protein;
DE AltName: Full=Single-strand-binding protein;
DE AltName: Full=hnRNP core protein A1;
DE Contains:
DE RecName: Full=Heterogeneous nuclear ribonucleoprotein A1, N-terminally processed;
GN Name=HNRNPA1; Synonyms=HNRPA1;
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Cerebellum;
RX PubMed=17574350; DOI=10.1016/j.gene.2007.04.013;
RA Sakate R., Suto Y., Imanishi T., Tanoue T., Hida M., Hayasaka I.,
RA Kusuda J., Gojobori T., Hashimoto K., Hirai M.;
RT "Mapping of chimpanzee full-length cDNAs onto the human genome unveils
RT large potential divergence of the transcriptome.";
RL Gene 399:1-10(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164055; DOI=10.1038/nature02564;
RA Watanabe H., Fujiyama A., Hattori M., Taylor T.D., Toyoda A., Kuroki Y.,
RA Noguchi H., BenKahla A., Lehrach H., Sudbrak R., Kube M., Taenzer S.,
RA Galgoczy P., Platzer M., Scharfe M., Nordsiek G., Bloecker H., Hellmann I.,
RA Khaitovich P., Paeaebo S., Reinhardt R., Zheng H.-J., Zhang X.-L.,
RA Zhu G.-F., Wang B.-F., Fu G., Ren S.-X., Zhao G.-P., Chen Z., Lee Y.-S.,
RA Cheong J.-E., Choi S.-H., Wu K.-M., Liu T.-T., Hsiao K.-J., Tsai S.-F.,
RA Kim C.-G., Oota S., Kitano T., Kohara Y., Saitou N., Park H.-S.,
RA Wang S.-Y., Yaspo M.-L., Sakaki Y.;
RT "DNA sequence and comparative analysis of chimpanzee chromosome 22.";
RL Nature 429:382-388(2004).
CC -!- FUNCTION: Involved in the packaging of pre-mRNA into hnRNP particles,
CC transport of poly(A) mRNA from the nucleus to the cytoplasm and
CC modulation of splice site selection. Plays a role in the splicing of
CC pyruvate kinase PKM by binding repressively to sequences flanking PKM
CC exon 9, inhibiting exon 9 inclusion and resulting in exon 10 inclusion
CC and production of the PKM M2 isoform. Binds to the IRES and thereby
CC inhibits the translation of the apoptosis protease activating factor
CC APAF1. May bind to specific miRNA hairpins.
CC {ECO:0000250|UniProtKB:P09651}.
CC -!- SUBUNIT: Identified in the spliceosome C complex. Identified in a
CC IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs.
CC Interacts with SEPT6. Interacts with C9orf72. Interacts with KHDRBS1.
CC Interacts with UBQLN2 (By similarity). Interacts with PPIA/CYPA (By
CC similarity). {ECO:0000250|UniProtKB:P09651}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P09651}. Cytoplasm
CC {ECO:0000250|UniProtKB:P09651}. Note=Localized in cytoplasmic mRNP
CC granules containing untranslated mRNAs. Shuttles continuously between
CC the nucleus and the cytoplasm along with mRNA. Component of
CC ribonucleosomes. {ECO:0000250|UniProtKB:P09651}.
CC -!- PTM: Sumoylated. {ECO:0000250}.
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DR EMBL; AB222102; BAF62347.1; -; mRNA.
DR EMBL; AL954201; CAH18571.1; -; Genomic_DNA.
DR RefSeq; NP_001091892.1; NM_001098422.2.
DR RefSeq; NP_001184040.1; NM_001197111.1.
DR AlphaFoldDB; A5A6H4; -.
DR BMRB; A5A6H4; -.
DR SMR; A5A6H4; -.
DR STRING; 9598.ENSPTRP00000048316; -.
DR PaxDb; A5A6H4; -.
DR PRIDE; A5A6H4; -.
DR Ensembl; ENSPTRT00000090598; ENSPTRP00000065492; ENSPTRG00000049417.
DR GeneID; 739306; -.
DR GeneID; 747284; -.
DR KEGG; ptr:739306; -.
DR KEGG; ptr:747284; -.
DR CTD; 3178; -.
DR CTD; 739306; -.
DR eggNOG; KOG0118; Eukaryota.
DR GeneTree; ENSGT00950000183123; -.
DR HOGENOM; CLU_012062_1_0_1; -.
DR InParanoid; A5A6H4; -.
DR OrthoDB; 1202220at2759; -.
DR TreeFam; TF351342; -.
DR Proteomes; UP000002277; Chromosome 12.
DR Bgee; ENSPTRG00000049417; Expressed in fibroblast and 20 other tissues.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:1990904; C:ribonucleoprotein complex; ISS:UniProtKB.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; IBA:GO_Central.
DR GO; GO:1903936; P:cellular response to sodium arsenite; ISS:UniProtKB.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR CDD; cd12761; RRM1_hnRNPA1; 1.
DR CDD; cd12580; RRM2_hnRNPA1; 1.
DR Gene3D; 3.30.70.330; -; 2.
DR InterPro; IPR021662; HnRNPA1_C.
DR InterPro; IPR034845; hnRNPA1_RRM1.
DR InterPro; IPR034803; hnRNPA1_RRM2.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF11627; HnRNPA1; 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; Cytoplasm; Isopeptide bond; Methylation; mRNA processing;
KW mRNA splicing; mRNA transport; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; Ribonucleoprotein; RNA-binding; Spliceosome; Transport;
KW Ubl conjugation.
FT CHAIN 1..320
FT /note="Heterogeneous nuclear ribonucleoprotein A1"
FT /id="PRO_0000424512"
FT INIT_MET 1
FT /note="Removed; alternate"
FT /evidence="ECO:0000250|UniProtKB:P09651"
FT CHAIN 2..320
FT /note="Heterogeneous nuclear ribonucleoprotein A1, N-
FT terminally processed"
FT /id="PRO_0000295287"
FT DOMAIN 14..97
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 105..184
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 4..94
FT /note="Globular A domain"
FT REGION 95..185
FT /note="Globular B domain"
FT REGION 182..216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 218..240
FT /note="RNA-binding RGG-box"
FT REGION 268..305
FT /note="Nuclear targeting sequence"
FT /evidence="ECO:0000250"
FT REGION 274..320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 184..199
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 303..320
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P09651"
FT MOD_RES 2
FT /note="N-acetylserine; in Heterogeneous nuclear
FT ribonucleoprotein A1, N-terminally processed"
FT /evidence="ECO:0000250|UniProtKB:P09651"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P09651"
FT MOD_RES 3
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P09651"
FT MOD_RES 4
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P09651"
FT MOD_RES 6
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P09651"
FT MOD_RES 22
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49312"
FT MOD_RES 192
FT /note="Phosphoserine; by MKNK2"
FT /evidence="ECO:0000250|UniProtKB:P09651"
FT MOD_RES 194
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P09867"
FT MOD_RES 194
FT /note="Dimethylated arginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P09651"
FT MOD_RES 194
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P49312"
FT MOD_RES 199
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P09651"
FT MOD_RES 206
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P09651"
FT MOD_RES 206
FT /note="Dimethylated arginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P09651"
FT MOD_RES 206
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P09651"
FT MOD_RES 218
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P09651"
FT MOD_RES 218
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P09651"
FT MOD_RES 225
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P09651"
FT MOD_RES 225
FT /note="Dimethylated arginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P09651"
FT MOD_RES 225
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P09651"
FT MOD_RES 232
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P04256"
FT MOD_RES 232
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P09651"
FT MOD_RES 284
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P09651"
FT MOD_RES 285
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P09651"
FT MOD_RES 298
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P09651"
FT MOD_RES 300
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P09651"
FT MOD_RES 309
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P09651"
FT MOD_RES 310
FT /note="Phosphoserine; by MKNK2"
FT /evidence="ECO:0000250|UniProtKB:P09651"
FT MOD_RES 311
FT /note="Phosphoserine; by MKNK2"
FT /evidence="ECO:0000250|UniProtKB:P09651"
FT MOD_RES 312
FT /note="Phosphoserine; by MKNK2"
FT /evidence="ECO:0000250|UniProtKB:P09651"
FT MOD_RES 313
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P09651"
FT MOD_RES 316
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P09651"
FT MOD_RES 318
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P09651"
FT CROSSLNK 3
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P09651"
FT CROSSLNK 8
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P09651"
FT CROSSLNK 78
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P09651"
FT CROSSLNK 113
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250"
FT CROSSLNK 179
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P09651"
FT CROSSLNK 183
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P09651"
FT CROSSLNK 298
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P09651"
SQ SEQUENCE 320 AA; 34196 MW; 59485C9FA1FF8AE1 CRC64;
MSKSESPKEP EQLRKLFIGG LSFETTDESL RSHFEQWGTL TDCVVMRDPN TKRSRGFGFV
TYATVEEVDA AMNARPHKVD GRVVEPKRAV SREDSQRPGA HLTVKKIFVG GIKEDTEEHH
LRDYFEQYGK IEVIEIMTDR GSGKKRGFAF VTFDDHDSVD KIVIQKYHTV NGHNCEVRKA
LSKQEMASAS SSQRGRSGSG NFGGGRGGGF GGNDNFGRGG NFSGRGGFGG SRGGGGYGGS
GDGYNGFGND GSNFGGGGSY NDFGNYNNQS SNFGPMKGGN FGGRSSGPYG GGGQYFAKPR
NQGGYGGSSS SSSYGSGRRF
