SMART: Pfam domain AROS

The domain within your query sequence starts at position 23 and ends at position 141; the E-value for the AROS domain shown below is 6.4e-42.

PGQVQASGTPAKRTRRARAKASQALKLRNSAKGKAPKSALAEYQKRQCRDHLKANLKFMT
SMRSTVPESVTQQILQQNQGRKACDRLVAKTKNKKKKKKKAEGTVFTEEDFQKFQREYF

AROS

PFAM accession number:	PF15684
Interpro abstract (IPR023262):	Human SIRT1, an NAD+-dependent deacetylase, plays a role in cell death/ survival, senescence, and endocrine signalling [ (PUBMED:17964266) ]. Its substrates are well characterised, but evidence for the identity of its direct regulators has been wanting. Recently, the nuclear protein AROS (also termed 40S ribosomal protein S19-binding protein 1 [ (PUBMED:16289379) ]) has been implicated in the direct regulation of SIRT1 function - this protein has been dubbed 'active regulator of SIRT1. The protein has been shown to enhance SIRT1-mediated deacetylation of p53, in vitro and in vivo, and to inhibit p53-mediated transcriptional activity. It is the first direct SIRT1 regulator to have been identified that modulates p53-mediated growth regulation.

PFAM accession number:

PF15684

Interpro abstract (IPR023262):

Human SIRT1, an NAD+-dependent deacetylase, plays a role in cell death/ survival, senescence, and endocrine signalling [ (PUBMED:17964266) ]. Its substrates are well characterised, but evidence for the identity of its direct regulators has been wanting. Recently, the nuclear protein AROS (also termed 40S ribosomal protein S19-binding protein 1 [ (PUBMED:16289379) ]) has been implicated in the direct regulation of SIRT1 function - this protein has been dubbed 'active regulator of SIRT1. The protein has been shown to enhance SIRT1-mediated deacetylation of p53, in vitro and in vivo, and to inhibit p53-mediated transcriptional activity. It is the first direct SIRT1 regulator to have been identified that modulates p53-mediated growth regulation.

This is a PFAM domain. For full annotation and more information, please see the PFAM entry AROS