UniProt functional annotation for P07910



	UniProt functional annotation for P07910

UniProt code: P07910.

Organism: Homo sapiens (Human).

Taxonomy: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.

Function: Binds pre-mRNA and nucleates the assembly of 40S hnRNP particles (PubMed:8264621). 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). Single HNRNPC tetramers bind 230-240 nucleotides. Trimers of HNRNPC tetramers bind 700 nucleotides (PubMed:8264621). May play a role in the early steps of spliceosome assembly and pre-mRNA splicing. N6-methyladenosine (m6A) has been shown to alter the local structure in mRNAs and long non-coding RNAs (lncRNAs) via a mechanism named 'm(6)A-switch', facilitating binding of HNRNPC, leading to regulation of mRNA splicing (PubMed:25719671). {ECO:0000269|PubMed:12509468, ECO:0000269|PubMed:16010978, ECO:0000269|PubMed:25719671, ECO:0000269|PubMed:7567451, ECO:0000269|PubMed:8264621}.

Subunit: Tetramer composed of 3 copies of isoform C1 and 1 copy of isoform C2. Assembly of 3 tetramers with bound pre-mRNA gives rise to a 19S complex that interacts with HNRNPA2B1 tetramers. Component of the 40S hnRNP particle. Identified in the spliceosome C complex. Interacts with IGF2BP1. Interacts with DHX9; this interaction is direct, enhanced probably by their concomitant binding to RNA and mediates the attachment to actin filaments (PubMed:11687588). Interacts with PPIA/CYPA (PubMed:25678563). {ECO:0000269|PubMed:11162094, ECO:0000269|PubMed:11687588, ECO:0000269|PubMed:11991638, ECO:0000269|PubMed:15936032, ECO:0000269|PubMed:17289661, ECO:0000269|PubMed:25678563, ECO:0000269|PubMed:8264621}.

Subcellular location: Nucleus. Note=Component of ribonucleosomes.

Ptm: 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. {ECO:0000269|PubMed:12564933}.

Ptm: Sumoylated. Sumoylation reduces affinity for mRNA. {ECO:0000269|PubMed:15082759}.

Similarity: Belongs to the RRM HNRPC family. RALY subfamily. {ECO:0000305}.

Sequence caution: Sequence=BAD92764.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};

Annotations taken from UniProtKB at the EBI.


Organism:		Homo sapiens (Human).
Taxonomy:		Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.



Function:		Binds pre-mRNA and nucleates the assembly of 40S hnRNP particles (PubMed:8264621). 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). Single HNRNPC tetramers bind 230-240 nucleotides. Trimers of HNRNPC tetramers bind 700 nucleotides (PubMed:8264621). May play a role in the early steps of spliceosome assembly and pre-mRNA splicing. N6-methyladenosine (m6A) has been shown to alter the local structure in mRNAs and long non-coding RNAs (lncRNAs) via a mechanism named 'm(6)A-switch', facilitating binding of HNRNPC, leading to regulation of mRNA splicing (PubMed:25719671). {ECO:0000269\|PubMed:12509468, ECO:0000269\|PubMed:16010978, ECO:0000269\|PubMed:25719671, ECO:0000269\|PubMed:7567451, ECO:0000269\|PubMed:8264621}.


Subunit:		Tetramer composed of 3 copies of isoform C1 and 1 copy of isoform C2. Assembly of 3 tetramers with bound pre-mRNA gives rise to a 19S complex that interacts with HNRNPA2B1 tetramers. Component of the 40S hnRNP particle. Identified in the spliceosome C complex. Interacts with IGF2BP1. Interacts with DHX9; this interaction is direct, enhanced probably by their concomitant binding to RNA and mediates the attachment to actin filaments (PubMed:11687588). Interacts with PPIA/CYPA (PubMed:25678563). {ECO:0000269\|PubMed:11162094, ECO:0000269\|PubMed:11687588, ECO:0000269\|PubMed:11991638, ECO:0000269\|PubMed:15936032, ECO:0000269\|PubMed:17289661, ECO:0000269\|PubMed:25678563, ECO:0000269\|PubMed:8264621}.
Subcellular location:		Nucleus. Note=Component of ribonucleosomes.
Ptm:		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. {ECO:0000269\|PubMed:12564933}.
Ptm:		Sumoylated. Sumoylation reduces affinity for mRNA. {ECO:0000269\|PubMed:15082759}.
Similarity:		Belongs to the RRM HNRPC family. RALY subfamily. {ECO:0000305}.
Sequence caution:		Sequence=BAD92764.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};