SMART: Pfam domain UCH

The domain within your query sequence starts at position 8 and ends at position 114; the E-value for the UCH_N domain shown below is 8.3e-34.

GLVQIRSTNRSKHTRASQWKEAVIEIVERKQKVNLVVSFKLEERRRVFQLGDNVTGVVVS
GELGLYHLDLTLRDDTSLLIDKLSSADVEHLKSFLDSSTPCESQQPM

UCH_N

PFAM accession number:	PF16674
Interpro abstract (IPR032069):	This entry represents a pleckstrin homology (PH)-like domain found at the N terminus of some ubiquitin carboxyl-terminal hydrolases, including USP26, USP29 and USP37. USP37 antagonizes the anaphase-promoting complex (APC/C) during G1/S transition by mediating deubiquitination of cyclin-A (CCNA1 and CCNA2), resulting in promoting S phase entry [ (PUBMED:21596315) ]. USP26 is a regulator of androgen receptor (AR) signaling [ (PUBMED:20501646) ]. Both USP26 and USP37 are critical for double-strand breaks repair by homologous recombination [ (PUBMED:26101254) ]. USP29 plays a role in apoptosis and oxidative stress [ (PUBMED:21285945) ]. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner [ (PUBMED:22728242) ]. They share little sequence conservation, but all have a common fold, which is electrostatically polarized.

PFAM accession number:

PF16674

Interpro abstract (IPR032069):

This entry represents a pleckstrin homology (PH)-like domain found at the N terminus of some ubiquitin carboxyl-terminal hydrolases, including USP26, USP29 and USP37. USP37 antagonizes the anaphase-promoting complex (APC/C) during G1/S transition by mediating deubiquitination of cyclin-A (CCNA1 and CCNA2), resulting in promoting S phase entry [ (PUBMED:21596315) ]. USP26 is a regulator of androgen receptor (AR) signaling [ (PUBMED:20501646) ]. Both USP26 and USP37 are critical for double-strand breaks repair by homologous recombination [ (PUBMED:26101254) ]. USP29 plays a role in apoptosis and oxidative stress [ (PUBMED:21285945) ].

PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner [ (PUBMED:22728242) ]. They share little sequence conservation, but all have a common fold, which is electrostatically polarized.

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