heterogeneous nuclear ribonucleoprotein-A2/B1 (hnRNP-A2/B1)

Function: - role with pre-mRNA processing - forms complexes (ribonucleosomes) with at least 20 other different hnRNP & heterogeneous nuclear RNA in the nucleous - identified in the spliceosome C complex Structure: contains 2 RRM domain (RNA recognition motif)s Compartment: - nucleus, nucleoplasm, cytoplasm - component of ribonucleosomes - predominantly nucleoplasmic; however, isoform A2 is also found in the cytoplasm of cells in some tissues - not found in the nucleolus Alternative splicing: named isoforms=2; B1, A2

Specific

hnRNP-A2 hnRNP-B1

General

heterogeneous nuclear ribonucleoprotein (hnRNP) phosphoprotein RNA-binding protein

Properties

SIZE: entity length = 353 aa MW = 37 kD COMPARTMENT: cytoplasm cell nucleus MOTIF: acetylation site SITE: N-TERMINUS EFFECTOR-BOUND: acetyl nuclear translocation signal {9-15} RNP motif NAME: RNP motif SITE: 21-104 FOR-BINDING-OF: ribonucleic acid MOTIF: ribonucleoprotein-1 motif NAME: ribonucleoprotein-1 motif FOR-BINDING-OF: ribonucleic acid MOTIF: ribonucleoprotein-1 motif ribonucleoprotein-2 motif ribonucleoprotein-2 motif FOR-BINDING-OF: ribonucleic acid MOTIF: ribonucleoprotein-1 motif ribonucleoprotein-2 motif Ser phosphorylation site {S85} RNP motif NAME: RNP motif SITE: 112-191 FOR-BINDING-OF: ribonucleic acid MOTIF: ribonucleoprotein-1 motif NAME: ribonucleoprotein-1 motif FOR-BINDING-OF: ribonucleic acid MOTIF: ribonucleoprotein-1 motif ribonucleoprotein-2 motif ribonucleoprotein-2 motif FOR-BINDING-OF: ribonucleic acid MOTIF: ribonucleoprotein-1 motif ribonucleoprotein-2 motif Thr phosphorylation site {T176} glycine-rich region {202-353} MOTIF: Ser phosphorylation site {S212} Ser phosphorylation site {S225} Ser phosphorylation site {S259} nuclear translocation signal {308-347} Ser phosphorylation site {S324} Ser phosphorylation site {S341} Ser phosphorylation site {S344} Tyr phosphorylation site {Y347}

Database Correlations

OMIM 600124 UniProt P22626 Pfam PF00076 Entrez Gene 3181 Kegg hsa:3181

References

UniProt :accession P22626