Protein Name:
Ubiquitin carboxyl-terminal hydrolase 5
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UniprotKB/SwissProt ID: P45974 (P45974)
Gene Name:
USP5
Organism: Homo sapiens (Human)
Function: Deubiquitinating enzyme that participates in a wide range of cellular processes by specifically cleaving isopeptide bonds between ubiquitin and substrate proteins or ubiquitin itself. Affects thereby important cellular signaling pathways such as NF-kappa-B, Wnt/beta-catenin, and cytokine production by regulating ubiquitin-dependent protein degradation. Participates in the activation of the Wnt signaling pathway by promoting FOXM1 deubiquitination and stabilization that induces the recruitment of beta-catenin to Wnt target gene promoter (PubMed:26912724). Regulates the assembly and disassembly of heat-induced stress granules by mediating the hydrolysis of unanchored ubiquitin chains (PubMed:29567855). Promotes lipopolysaccharide-induced apoptosis and inflammatory response by stabilizing the TXNIP protein (PubMed:37534934). Affects T-cell biology by stabilizing the inhibitory receptor on T-cells PDC1 (PubMed:37208329). Acts as a negative regulator of autophagy by regulating ULK1 at both protein and mRNA levels (PubMed:37607937). Acts also as a negative regulator of type I interferon production by simultaneously removing both 'Lys-48'-linked unanchored and 'Lys-63'-linked anchored polyubiquitin chains on the transcription factor IRF3 (PubMed:39761299). Modulates the stability of DNA mismatch repair protein MLH1 and counteracts the effect of the ubiquitin ligase UBR4 (PubMed:39032648). Upon activation by insulin, it gets phosphorylated through mTORC1-mediated phosphorylation to enhance YTHDF1 stability by removing 'Lys-11'-linked polyubiquitination (PubMed:39900921). May also deubiquitinate other substrates such as the calcium channel CACNA1H (By similarity)
Other Modifications: View all modification sites in dbPTM
Protein Subcellular Localization: Cytoplasm. Cytoplasm, Stress granule. Nucleus
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Graphical Visualization of S-nitrosylation Sites:
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The S-nitrosylation sites of P45974
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| No. |
Position |
S-nitrosylated Peptide |
Secondary Structure of S-nitrosylated Peptide |
Solvent Accessibility of nitrosylated Site |
PubMed ID |
| 1 |
195 |
QLDNPARIPP C GWKCSKCDMR |
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| 2 |
219 |
WLNLTDGSIL C GRRYFDGSGG |
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| 3 |
335 |
YTGIRNLGNS C YLNSVVQVLF |
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| 4 |
532 |
LVRAQVPFSS C LEAYGAPEQV |
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| 5 |
838 |
RWVIYNDQKV C ASEKPPKDLG |
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