Binds pre-mRNA and nucleates the assembly of 40S hnRNP particles (PubMed:8264621). Specifically recognizes and binds N6-methyladenosine (m6A)-containing RNAs, a modification present at internal sites of mRNAs that affects mRNA splicing, processing and stability. M6A alters the local structure in mRNAs and long non-coding RNAs (lncRNAs) via a mechanism named 'm(6)A-switch' to facilitate binding of HNRNPC, leading to regulation of mRNA splicing (PubMed:25719671). Single HNRNPC tetramers bind 230-240 nucleotides. Trimers of HNRNPC tetramers bind 700 nucleotides. May play a role in the early steps of spliceosome assembly and pre-mRNA splicing. Interacts with poly-U tracts in the 3'-UTR or 5'-UTR of mRNA and modulates the stability and the level of translation of bound mRNA molecules (PubMed:12509468, PubMed:16010978, PubMed:7567451, PubMed:8264621).
Belongs to the RRM HNRPC family. RALY subfamily. Contains 1 RRM (RNA recognition motif) domain.
Phosphorylated on Ser-260 and Ser-299 in resting cells. Phosphorylated on Ser-253 and on 1 serine residue in the poly-Ser stretch at position 238 in response to hydrogen peroxide. Sumoylated. Sumoylation reduces affinity for mRNA.
Varjak M et al. Magnetic fractionation and proteomic dissection of cellular organelles occupied by the late replication complexes of Semliki Forest virus. J Virol87:10295-312 (2013).
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