Description: Homo sapiens SUMO1/sentrin specific peptidase 5 (SENP5), mRNA. RefSeq Summary (NM_152699): The reversible posttranslational modification of proteins by the addition of small ubiquitin-like SUMO proteins (see SUMO1; MIM 601912) is required for numerous biologic processes. SUMO-specific proteases, such as SENP5, are responsible for the initial processing of SUMO precursors to generate a C-terminal diglycine motif required for the conjugation reaction. They also have isopeptidase activity for the removal of SUMO from high molecular mass SUMO conjugates (Di Bacco et al., 2006 [PubMed 16738315]).[supplied by OMIM, Jun 2009]. Transcript (Including UTRs) Position: hg19 chr3:196,594,727-196,661,584 Size: 66,858 Total Exon Count: 10 Strand: + Coding Region Position: hg19 chr3:196,612,053-196,657,794 Size: 45,742 Coding Exon Count: 9
ID:SENP5_HUMAN DESCRIPTION: RecName: Full=Sentrin-specific protease 5; EC=3.4.22.68; AltName: Full=Sentrin/SUMO-specific protease SENP5; FUNCTION: Protease that catalyzes two essential functions in the SUMO pathway: processing of full-length SUMO3 to its mature form and deconjugation of SUMO2 and SUMO3 from targeted proteins. Has weak proteolytic activity against full-length SUMO1 or SUMO1 conjugates. Required for cell division. CATALYTIC ACTIVITY: Hydrolysis of the alpha-linked peptide bond in the sequence Gly-Gly-|-Ala-Thr-Tyr at the C-terminal end of the small ubiquitin-like modifier (SUMO) propeptide, Smt3, leading to the mature form of the protein. A second reaction involves the cleavage of an epsilon-linked peptide bond between the C-terminal glycine of the mature SUMO and the lysine epsilon-amino group of the target protein. INTERACTION: P03372:ESR1; NbExp=2; IntAct=EBI-3895753, EBI-78473; SUBCELLULAR LOCATION: Nucleus, nucleolus. SIMILARITY: Belongs to the peptidase C48 family. SEQUENCE CAUTION: Sequence=AAK69630.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
The RNAfold program from the Vienna RNA Package is used to perform the secondary structure predictions and folding calculations. The estimated folding energy is in kcal/mol. The more negative the energy, the more secondary structure the RNA is likely to have.
ModBase Predicted Comparative 3D Structure on Q96HI0
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Orthologous Genes in Other Species
Orthologies between human, mouse, and rat are computed by taking the best BLASTP hit, and filtering out non-syntenic hits. For more distant species reciprocal-best BLASTP hits are used. Note that the absence of an ortholog in the table below may reflect incomplete annotations in the other species rather than a true absence of the orthologous gene.