hnRNP C1+C2 Recombinant Rabbit Monoclonal Antibody [SN0652] (ET1611-2)

UNIPROT #

P07910

PROTEIN NAME

hnRNP C1+C2

SYNONYMS

C1 antibody;C2 antibody;Heterogeneous nuclear ribonucleoprotein C (C1/C2) antibody;Heterogeneous nuclear ribonucleoprotein C antibody;Heterogeneous nuclear ribonucleoproteins C1/C2 antibody;HNRNP antibody;hnRNP C1 / hnRNP C2 antibody;hnRNP C1/C2 antibody;Hnrnpc antibody;HNRPC antibody;HNRPC_HUMAN antibody;MGC104306 antibody;MGC105117 antibody;MGC117353 antibody;MGC131677 antibody;Nuclear ribonucleoprotein particle C1 protein antibody;Nuclear ribonucleoprotein particle C2 protein antibody;SNRPC antibody

SEQUENCE SIMILARITIES

Belongs to the RRM HNRPC family. RALY subfamily.

POST-TRANSLATIONAL MODIFICATION

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.

SUBCELLULAR LOCATION

Nucleus.

FUNCTION

Heterogeneous nuclear ribonucleoproteins (hnRNPs) constitute a set of polypeptides that contribute to pre-mRNA processing and transport, and also bind heterogeneous nuclear RNA (hnRNA), which are the transcripts produced by RNA polymerase II. hnRNP complexes are the major constituents of the spliceosome and, in particular, the hnRNP A1 protein is one of the major pre-mRNA/mRNA binding proteins and also one of the most abundant proteins in the nucleus. hnRNP A1 and A2/B1 regulate the processing of pre-mRNA by directly antagonizing the association of various splicing factors and by influencing the splice site selection on pre-mRNA. The majority of hnRNP proteins components are localized to the nucleus; however, some shuttle between the nucleus and the cytoplasm. Most hnRNP proteins, in-cluding hnRNP C1 and C2, contain one or more RNA binding domains and are implicated in the processing of pre-mRNA. hnRNPs F and H are largely related factors that preferentially associate with poly(rG) regions on RNA. Isoforms of these proteins are often generated by alternative processing of the pre-mRNA and by posttranslational modifications such as phosphorylation on serines and threonines and methylation of arginines.