SENP1

Sentrin-specific protease 1 is an enzyme that in humans is encoded by the SENP1 gene.^[5][6][7]

SENP1
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2CKG, 2CKH, 2G4D, 2IY0, 2IY1, 2IYC, 2IYD, 2XPH, 2XRE
Identifiers
Aliases	SENP1, SuPr-2, SUMO1/sentrin specific peptidase 1, SUMO specific peptidase 1
External IDs	OMIM: 612157; MGI: 2445054; HomoloGene: 8731; GeneCards: SENP1; OMA:SENP1 - orthologs
Gene location (Human) Chr. Chromosome 12 (human)[1] Band 12q13.11 Start 48,042,897 bp[1] End 48,106,079 bp[1]
Gene location (Mouse) Chr. Chromosome 15 (mouse)[2] Band 15 F1|15 54.04 cM Start 97,936,625 bp[2] End 97,991,625 bp[2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in testicle right testis left testis testicle sperm buccal mucosa cell Achilles tendon ventricular zone bone marrow cell ganglionic eminence Top expressed in zygote secondary oocyte spermatocyte spermatid tail of embryo ascending aorta genital tubercle aortic valve Rostral migratory stream epiblast More reference expression data BioGPS n/a
Gene ontology Molecular function peptidase activity cysteine-type peptidase activity endopeptidase activity protein binding hydrolase activity SUMO-specific endopeptidase activity SUMO-specific protease activity Cellular component cytoplasm nuclear membrane focal adhesion nucleoplasm nucleus Biological process negative regulation of proteasomal ubiquitin-dependent protein catabolic process apoptotic signaling pathway protein desumoylation activation of cysteine-type endopeptidase activity involved in apoptotic process protein sumoylation positive regulation of transcription by RNA polymerase II proteolysis regulation of definitive erythrocyte differentiation Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 29843 223870 Ensembl ENSG00000079387 ENSMUSG00000033075 UniProt Q9P0U3 P59110 RefSeq (mRNA) NM_001267594 NM_001267595 NM_014554 NM_144851 NM_001379573 RefSeq (protein) NP_001254523 NP_001254524 NP_659100 NP_001366502 Location (UCSC) Chr 12: 48.04 – 48.11 Mb Chr 15: 97.94 – 97.99 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

General

There are six known SUMO proteases in humans that have been designated SENP1-3 and SENP5-7 (sentrin/SUMO-specific protease). The six proteases possess a conserved C-terminal domain which are variable in size, and with a distinct N-terminal domain between them. The C-terminal domain shows catalytic activity and the N-terminal domain regulates cell localization and substrate specificity.^[8]

Features

SENP1 (Sentrin-specific protease 1) is a human protease of 643 amino acids with a molecular weight of 73 kDa, EC number in humans 3.4.22.B70. It adopts a conformation that identifies it as a member of the superfamily of cysteine proteases, which contain a catalytic triad with three characterized amino acids: a cysteine at position 603, a histidine at position 533 and aspartic acid at position 550. The primary nucleophile is cysteine located at the N-terminal alpha helix of the protein core. The other two amino acids, aspartate and histidine, are located in the end of a beta sheet. ^[9]

SENP1 The catalytic site consists of three amino acids: Cys 602, His 533 and Asp 550.

Location

Both SENP1 are located in the nucleus and cytosol depending on the cell type, although it has been seen to be exported out from the nucleus to the cytosol through a sequence of nuclear export (NES) that is located at the C-terminus. The mammalian SENP1 is localized mainly in the nucleus.^[10]

Function

SENP1 catalyzes maturation of SUMO protein (small ubiquitin-related modifier). SENP1 causes hydrolysis of a peptide bond of SUMO in the conserved sequence Gly-Gly-|-Ala-Thr-Tyr at the C-terminus,^[11] which can then be conjugated to other proteins (sumoylation).^[12] In vertebrates there are three members of the family of SUMO: SUMO-1, -2 and -3. SENP1 can catalyze the maturation of any of these three. This conjugation of SUMO toward other proteins is similar to ubiquitination, however these modifications can lead to different outcomes depending on the type of protein being modified.^[13]