P09651

FUNCTION: Involved in the packaging of pre-mRNA into hnRNP particles, transport of poly(A) mRNA from the nucleus to the cytoplasm and may modulate splice site selection. May play a role in HCV RNA replication. SUBUNIT: Identified in the spliceosome C complex. Identified in a mRNP granule complex, at least composed of ACTB, ACTN4, DHX9, ERG, HNRNPA1, HNRNPA2B1, HNRNPAB, HNRNPD, HNRNPL, HNRNPR, HNRNPU, HSPA1, HSPA8, IGF2BP1, ILF2, ILF3, NCBP1, NCL, PABPC1, PABPC4, PABPN1, RPLP0, RPS3, RPS3A, RPS4X, RPS8, RPS9, SYNCRIP, TROVE2, YBX1 and untranslated mRNAs. Interacts with SEPT6. Interacts with HCV NS5B and with the 5'-UTR and 3'-UTR of HCV RNA. SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Shuttles continuously between the nucleus and the cytoplasm along with mRNA. Component of ribonucleosomes. In the course of viral infection, colocalizes with HCV NS5B at speckles in the cytoplasm in a HCV-replication dependent manner. ALTERNATIVE PRODUCTS: Event=Alternative splicing; Named isoforms=3; Name=A1-B; IsoId=P09651-1; Sequence=Displayed; Name=A1-A; IsoId=P09651-2; Sequence=VSP_005824; Note=Is twenty times more abundant than isoform A1-B; Name=2; IsoId=P09651-3; Sequence=VSP_034076; Note=No experimental confirmation available; PTM: Arg-194, Arg-206 and Arg-225 are dimethylated, probably to asymmetric dimethylarginine. PTM: Sumoylated. SIMILARITY: Contains 2 RRM (RNA recognition motif) domains. GENE SYNONYMS:HNRNPA1 HNRPA1. COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License., SEQUENCE 372 AA; 38747 MW; A06683571C6C109F CRC64;

ROA1_HUMAN

urn:biopax:ModificationFeature:ROA1_HUMAN_1, urn:biopax:ModificationFeature:ROA1_HUMAN_10, urn:biopax:ModificationFeature:ROA1_HUMAN_11, urn:biopax:ModificationFeature:ROA1_HUMAN_12, urn:biopax:ModificationFeature:ROA1_HUMAN_13, urn:biopax:ModificationFeature:ROA1_HUMAN_14, urn:biopax:ModificationFeature:ROA1_HUMAN_15, urn:biopax:ModificationFeature:ROA1_HUMAN_16, urn:biopax:ModificationFeature:ROA1_HUMAN_17, urn:biopax:ModificationFeature:ROA1_HUMAN_18, urn:biopax:ModificationFeature:ROA1_HUMAN_19, urn:biopax:ModificationFeature:ROA1_HUMAN_2, urn:biopax:ModificationFeature:ROA1_HUMAN_20, urn:biopax:ModificationFeature:ROA1_HUMAN_21, urn:biopax:ModificationFeature:ROA1_HUMAN_22, urn:biopax:ModificationFeature:ROA1_HUMAN_23, urn:biopax:ModificationFeature:ROA1_HUMAN_24, urn:biopax:ModificationFeature:ROA1_HUMAN_25, urn:biopax:ModificationFeature:ROA1_HUMAN_26, urn:biopax:ModificationFeature:ROA1_HUMAN_27, urn:biopax:ModificationFeature:ROA1_HUMAN_28, urn:biopax:ModificationFeature:ROA1_HUMAN_29, urn:biopax:ModificationFeature:ROA1_HUMAN_3, urn:biopax:ModificationFeature:ROA1_HUMAN_4, urn:biopax:ModificationFeature:ROA1_HUMAN_5, urn:biopax:ModificationFeature:ROA1_HUMAN_6, urn:biopax:ModificationFeature:ROA1_HUMAN_7, urn:biopax:ModificationFeature:ROA1_HUMAN_8, urn:biopax:ModificationFeature:ROA1_HUMAN_9

MSKSESPKEPEQLRKLFIGGLSFETTDESLRSHFEQWGTLTDCVVMRDPNTKRSRGFGFVTYATVEEVDAAMNARPHKVDGRVVEPKRAVSREDSQRPGAHLTVKKIFVGGIKEDTEEHHLRDYFEQYGKIEVIEIMTDRGSGKKRGFAFVTFDDHDSVDKIVIQKYHTVNGHNCEVRKALSKQEMASASSSQRGRSGSGNFGGGRGGGFGGNDNFGRGGNFSGRGGFGGSRGGGGYGGSGDGYNGFGNDGGYGGGGPGYSGGSRGYGSGGQGYGNQGSGYGGSGSYDSYNNGGGGGFGGGSGSNFGGGGSYNDFGNYNNQSSNFGPMKGGNFGGRSSGPYGGGGQYFAKPRNQGGYGGSSSSSSYGSGRRF