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Sep. 10, 2014:
A total of 174 experimentally verified S-nitrosylation sites on 94 S-nitrosylated proteins from individualized human colorectal cancer tissues using a label-free quantitation strategy.

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Protein Name: Ubiquitin carboxyl-terminal hydrolase 9X

UniprotKB/SwissProt ID: Q93008 (Q93008)

Gene Name: USP9X

Organism: Homo sapiens (Human)

Function: Deubiquitinase involved both in the processing of ubiquitin precursors and of ubiquitinated proteins (PubMed:18254724, PubMed:19135894, PubMed:22371489, PubMed:25944111, PubMed:29626158, PubMed:30914461, PubMed:37454738). May therefore play an important regulatory role at the level of protein turnover by preventing degradation of proteins through the removal of conjugated ubiquitin (PubMed:18254724, PubMed:19135894, PubMed:22371489, PubMed:25944111, PubMed:29626158, PubMed:30914461, PubMed:37454738). Specifically hydrolyzes 'Lys-11'-, followed by 'Lys-63'-, 'Lys-48'- and 'Lys-6'-linked polyubiquitins chains (PubMed:30914461). Essential component of TGF-beta/BMP signaling cascade (PubMed:19135894). Specifically deubiquitinates monoubiquitinated SMAD4, opposing the activity of E3 ubiquitin-protein ligase TRIM33 (PubMed:19135894). Deubiquitinates alkylation repair enzyme ALKBH3 (PubMed:25944111). OTUD4 recruits USP7 and USP9X to stabilize ALKBH3, thereby promoting the repair of alkylated DNA lesions (PubMed:25944111). Deubiquitinates RNA demethylase enzyme ALKBH5, promoting its stability (PubMed:37454738). Deubiquitinates mTORC2 complex component RICTOR at 'Lys-294' by removing 'Lys-63'-linked polyubiquitin chains, stabilizing RICTOR and enhancing its binding to MTOR, thus promoting mTORC2 complex assembly (PubMed:33378666). Regulates chromosome alignment and segregation in mitosis by regulating the localization of BIRC5/survivin to mitotic centromeres (PubMed:16322459). Involved in axonal growth and neuronal cell migration (PubMed:24607389). Regulates cellular clock function by enhancing the protein stability and transcriptional activity of the core circadian protein BMAL1 via its deubiquitinating activity (PubMed:29626158). Acts as a regulator of peroxisome import by mediating deubiquitination of PEX5: specifically deubiquitinates PEX5 monoubiquitinated at 'Cys-11' following its retrotranslocation into the cytosol, resetting PEX5 for a subsequent import cycle (PubMed:22371489). Deubiquitinates PEG10 (By similarity). Inhibits the activation of the Hippo signaling pathway via deubiquitination of AMOTL2 at 'Lys-347' and 'Lys-408' which prohibits its interaction with and activation of LATS2. Loss of LATS2 activation and subsequent loss of YAP1 phosphorylation results in an increase in YAP1-driven transcription of target genes (PubMed:26598551, PubMed:34404733)

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization: Cytoplasm, cytosol. Cell projection, growth cone. Cytoplasm, cytoskeleton, cilium axoneme

Graphical Visualization of S-nitrosylation Sites:
InterPro ID Domain Name
IPR016024 ARM-type_fold
IPR056850 ARM_UBP34_24_USP9X_Y
IPR021905 DUF3517
IPR038765 Papain-like_cys_pep_sf
IPR050164 Peptidase_C19
IPR001394 Peptidase_C19_UCH
IPR055176 UBP24/USP9X/USP9Y_UBL
IPR018200 USP_CS
IPR028889 USP_dom

The S-nitrosylation sites of Q93008

No. Position S-nitrosylated Peptide Secondary Structure of S-nitrosylated Peptide Solvent Accessibility of nitrosylated Site PubMed ID
1 1237 DEASRYMPDI C VIRAIQKIIW   
2 1340 QVAQEQFFLM C TRCCMGHRPL   
3 1733 ICQGCPHRYE C EESFTTLNVD   
4 2075 GSASDWYDAL C ILLRHSKNVR   
5 2107 SNRFSEYLLE C PSAEVRGAFA   
6 2293 TSYVKKIIED C SNSEETVKLL   
7 471 SPEQLDHLFD C FKASWTNASK   
8 577 IPALKQIREI C SLFGEAPQNL   
9 819 VVIHEDFIQS C FDRLKASYDT   
10 831 DRLKASYDTL C VLDGDKDSVN   
11 842 VLDGDKDSVN C ARQEAVRMVR   
12 864 LTVLREYINE C DSDYHEERTI