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SENP1

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SENP1
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesSENP1, SuPr-2, SUMO1/sentrin specific peptidase 1, SUMO specific peptidase 1
External IDsOMIM: 612157; MGI: 2445054; HomoloGene: 8731; GeneCards: SENP1; OMA:SENP1 - orthologs
Orthologs
SpeciesHumanMouse
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 MbChr 15: 97.94 – 97.99 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

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

General

So far there are seven SUMO proteases in humans that have been designated SENP1-7 (sentrin/SUMO-specific protease).1 The seven 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 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 weight of 73 kDa, EC number in humans 3.4.22.B70, which adopts a conformation that identifies it as a member of the superfamily of cysteine proteases contain a catalytic triad with characterized three amino acids: a cysteine at position 602, a histidine at position 533 and aspartic acid at position 550. The important 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 a beta sheet end. [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 that is 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 SUMO protein (small ubiquitin-related modifier), which causes hydrolysis peptide bond of SUMO is in a conserved sequence Gly-Gly-|-Ala-Thr-Tyr at the C-terminal [11] to be added to the conjugation of other proteins (sumoylation).[12] In vertebrates there are three members of the family of SUMO: SUMO-1, -2 and -3. SENP1 can catalyze any of these three. This conjugation of SUMO toward other proteins is a lot like ubiquitination, however these modifications leads to different results depending on the type of protein been modified.[13]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000079387 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000033075 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Gong L, Millas S, Maul GG, Yeh ET (Feb 2000). "Differential regulation of sentrinized proteins by a novel sentrin-specific protease". The Journal of Biological Chemistry. 275 (5): 3355–9. doi:10.1074/jbc.275.5.3355. PMID 10652325.{{cite journal}}: CS1 maint: unflagged free DOI (link)
  6. ^ Bailey D, O'Hare P (Jan 2004). "Characterization of the localization and proteolytic activity of the SUMO-specific protease, SENP1". The Journal of Biological Chemistry. 279 (1): 692–703. doi:10.1074/jbc.M306195200. PMID 14563852.{{cite journal}}: CS1 maint: unflagged free DOI (link)
  7. ^ "Entrez Gene: SENP1 SUMO1/sentrin specific peptidase 1".
  8. ^ Xu Z, Chau SF, Lam KH, Chan HY, Ng TB, Au SW (Sep 2006). "Crystal structure of the SENP1 mutant C603S-SUMO complex reveals the hydrolytic mechanism of SUMO-specific protease". The Biochemical Journal. 398 (3): 345–52. doi:10.1042/BJ20060526. PMC 1559472. PMID 16712526.
  9. ^ Shen LN, Dong C, Liu H, Naismith JH, Hay RT (2006). "The structure of SENP1-SUMO-2 complex suggests a structural basis for discrimination between SUMO paralogues during processing". The Biochemical Journal. 397 (2): 279–288. doi:10.1042/BJ20052030. PMC 1513277. PMID 16553580.
  10. ^ Kim YH, Sung KS, Lee SJ, Kim YO, Choi CY, Kim Y (2005). "Desumoylation of homeodomain-interacting protein kinase 2 (HIPK2) through the cytoplasmic-nuclear shuttling of the SUMO-specific protease SENP1". FEBS Letters. 579 (27): 6272–6278. doi:10.1016/j.febslet.2005.10.010. PMID 16253240.
  11. ^ http://www.uniprot.org/uniprot/Q9P0U3#ptm_processing
  12. ^ Xu Z, Au SW (2005). "Mapping residues of SUMO precursors essential in differential maturation by SUMO-specific protease, SENP1". The Biochemical Journal. 386 (Pt 2): 325–330. doi:10.1042/BJ20041210. PMC 1134797. PMID 15487983.
  13. ^ Xu Z, Chau SF, Lam KH, Chan HY, Ng TB, Au SW (2006). "Crystal structure of the SENP1 mutant C603S-SUMO complex reveals the hydrolytic mechanism of SUMO-specific protease". The Biochemical Journal. 398 (3): 345–52. doi:10.1042/BJ20060526. PMC 1559472. PMID 16712526.

Further reading

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