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Showing Protein Probable ubiquitin carboxyl-terminal hydrolase FAF-X (HMDBP14487)

IdentificationBiological propertiesGene propertiesProtein propertiesExternal linksReferencesXMLShow 1 metabolite
Identification
HMDB Protein ID HMDBP14487
Secondary Accession Numbers None
Name Probable ubiquitin carboxyl-terminal hydrolase FAF-X
Synonyms
  1. Deubiquitinating enzyme FAF-X
  2. Fat facets homolog
  3. Fat facets protein-related, X-linked
  4. Ubiquitin carboxyl-terminal hydrolase FAM
  5. Ubiquitin thioesterase FAF-X
  6. Ubiquitin-specific protease 9, X chromosome
  7. Ubiquitin-specific-processing protease FAF-X
Gene Name USP9X
Protein Type Unknown
Biological Properties
General Function Not Available
Specific Function Deubiquitinase involved both in the processing of ubiquitin precursors and of ubiquitinated proteins. May therefore play an important regulatory role at the level of protein turnover by preventing degradation of proteins through the removal of conjugated ubiquitin. Specifically hydrolyzes 'Lys-48'-, 'Lys-29'- and 'Lys-33'-linked polyubiquitins chains. Essential component of TGF-beta/BMP signaling cascade. Specifically deubiquitinates monoubiquitinated SMAD4, opposing the activity of E3 ubiquitin-protein ligase TRIM33. Deubiquitinates alkylation repair enzyme ALKBH3. OTUD4 recruits USP7 and USP9X to stabilize ALKBH3, thereby promoting the repair of alkylated DNA lesions. Regulates chromosome alignment and segregation in mitosis by regulating the localization of BIRC5/survivin to mitotic centromeres (By similarity). Involved in axonal growth and neuronal cell migration (By similarity) (PubMed:24607389). Regulates cellular clock function by enhancing the protein stability and transcriptional activity of the core circadian protein ARNTL/BMAL1 via its deubiquitinating activity (PubMed:29626158).
Pathways Not Available
Reactions Not Available
GO Classification
Biological Process
cell cycle
protein deubiquitination
cell division
hippocampus development
cerebellar cortex structural organization
neuron projection extension
cell migration
positive regulation of DNA demethylation
protein deubiquitination involved in ubiquitin-dependent protein catabolic process
regulation of T cell receptor signaling pathway
protein stabilization
in utero embryonic development
neuron migration
BMP signaling pathway
chromosome segregation
transforming growth factor beta receptor signaling pathway
regulation of circadian rhythm
rhythmic process
cellular response to transforming growth factor beta stimulus
axon extension
post-embryonic development
Cellular Component
cytosol
apical part of cell
growth cone
cytoplasm
nucleus
Molecular Function
thiol-dependent deubiquitinase
deubiquitinase activity
Lys48-specific deubiquitinase activity
cysteine-type endopeptidase activity
co-SMAD binding
ubiquitin protein ligase binding
Cellular Location Not Available
Gene Properties
Chromosome Location Not Available
Locus Not Available
SNPs Not Available
Gene Sequence Not Available
Protein Properties
Number of Residues 2559
Molecular Weight 290708.47
Theoretical pI 5.875
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence Not Available
GenBank ID Protein Not Available
UniProtKB/Swiss-Prot ID P70398
UniProtKB/Swiss-Prot Entry Name USP9X_MOUSE
PDB IDs Not Available
GenBank Gene ID Not Available
GeneCard ID Not Available
GenAtlas ID Not Available
HGNC ID Not Available
References
General References
  1. Crozet F, el Amraoui A, Blanchard S, Lenoir M, Ripoll C, Vago P, Hamel C, Fizames C, Levi-Acobas F, Depetris D, Mattei MG, Weil D, Pujol R, Petit C: Cloning of the genes encoding two murine and human cochlear unconventional type I myosins. Genomics. 1997 Mar 1;40(2):332-41. [PubMed:9119401 ]
  2. Huttlin EL, Jedrychowski MP, Elias JE, Goswami T, Rad R, Beausoleil SA, Villen J, Haas W, Sowa ME, Gygi SP: A tissue-specific atlas of mouse protein phosphorylation and expression. Cell. 2010 Dec 23;143(7):1174-89. doi: 10.1016/j.cell.2010.12.001. [PubMed:21183079 ]
  3. Church DM, Goodstadt L, Hillier LW, Zody MC, Goldstein S, She X, Bult CJ, Agarwala R, Cherry JL, DiCuccio M, Hlavina W, Kapustin Y, Meric P, Maglott D, Birtle Z, Marques AC, Graves T, Zhou S, Teague B, Potamousis K, Churas C, Place M, Herschleb J, Runnheim R, Forrest D, Amos-Landgraf J, Schwartz DC, Cheng Z, Lindblad-Toh K, Eichler EE, Ponting CP: Lineage-specific biology revealed by a finished genome assembly of the mouse. PLoS Biol. 2009 May 5;7(5):e1000112. doi: 10.1371/journal.pbio.1000112. Epub 2009 May 26. [PubMed:19468303 ]
  4. Villen J, Beausoleil SA, Gerber SA, Gygi SP: Large-scale phosphorylation analysis of mouse liver. Proc Natl Acad Sci U S A. 2007 Jan 30;104(5):1488-93. doi: 10.1073/pnas.0609836104. Epub 2007 Jan 22. [PubMed:17242355 ]
  5. Cao L, Yu K, Banh C, Nguyen V, Ritz A, Raphael BJ, Kawakami Y, Kawakami T, Salomon AR: Quantitative time-resolved phosphoproteomic analysis of mast cell signaling. J Immunol. 2007 Nov 1;179(9):5864-76. doi: 10.4049/jimmunol.179.9.5864. [PubMed:17947660 ]
  6. Wood SA, Pascoe WS, Ru K, Yamada T, Hirchenhain J, Kemler R, Mattick JS: Cloning and expression analysis of a novel mouse gene with sequence similarity to the Drosophila fat facets gene. Mech Dev. 1997 Apr;63(1):29-38. doi: 10.1016/s0925-4773(97)00672-2. [PubMed:9178254 ]
  7. Homan CC, Kumar R, Nguyen LS, Haan E, Raymond FL, Abidi F, Raynaud M, Schwartz CE, Wood SA, Gecz J, Jolly LA: Mutations in USP9X are associated with X-linked intellectual disability and disrupt neuronal cell migration and growth. Am J Hum Genet. 2014 Mar 6;94(3):470-8. doi: 10.1016/j.ajhg.2014.02.004. [PubMed:24607389 ]
  8. Zhang Y, Duan C, Yang J, Chen S, Liu Q, Zhou L, Huang Z, Xu Y, Xu G: Deubiquitinating enzyme USP9X regulates cellular clock function by modulating the ubiquitination and degradation of a core circadian protein BMAL1. Biochem J. 2018 Apr 30;475(8):1507-1522. doi: 10.1042/BCJ20180005. [PubMed:29626158 ]