SSB

La is involved in diverse aspects of RNA metabolism, including binding and protecting 3-prime UUU(OH) elements of newly RNA polymerase III (see MIM 606007)-transcribed RNA, processing 5-prime and 3-prime ends of pre-tRNA precursors, acting as an RNA chaperone, and binding viral RNAs associated with hepatitis C virus. La protein was originally defined by its reactivity with autoantibodies from patients with Sjogren syndrome (MIM 270150) and systemic lupus erythematosus (SLE; MIM 152700) (Teplova et al., 2006 [PubMed 16387655]).[supplied by OMIM

Sjogren syndrome antigen B (autoantigen La)

Binds to the 3' poly(U) terminus of nascent RNA polymerase III transcripts, protecting them from exonuclease digestion and facilitating their folding and maturation (PubMed:3192525, PubMed:2470590).
In case of Coxsackievirus B3 infection, binds to the viral internal ribosome entry site (IRES) and stimulates the IRES-mediated translation (PubMed:12384597).

Biological Process histone mRNA metabolic processManual Assertion Based On ExperimentTAS:ProtInc
Biological Process IRES-dependent viral translational initiationManual Assertion Based On ExperimentIDA:UniProtKB
Biological Process nuclear histone mRNA catabolic processManual Assertion Based On ExperimentIMP:CAFA
Biological Process protein localization to cytoplasmic stress granuleManual Assertion Based On ExperimentIDA:AgBase
Biological Process tRNA 3'-end processingManual Assertion Based On ExperimentIGI:CAFA
Biological Process tRNA 5'-leader removalManual Assertion Based On ExperimentIGI:CAFA
Biological Process tRNA export from nucleusManual Assertion Based On ExperimentIMP:CAFA
Biological Process tRNA modificationManual Assertion Based On ExperimentTAS:ProtInc
Biological Process tRNA processingManual Assertion Based On ExperimentIMP:CAFA

Nucleus

Phosphorylated. The phosphorylation sites are at the C-terminal part of the protein.
The N-terminus is blocked.