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<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{Infobox_gene}}
{{PBB_Controls
'''Probable ubiquitin carboxyl-terminal hydrolase FAF-X''' is an [[enzyme]] that in humans is encoded by the ''USP9X'' [[gene]].<ref name="pmid8922996">{{cite journal | vauthors = Jones MH, Furlong RA, Burkin H, Chalmers IJ, Brown GM, Khwaja O, Affara NA | title = The Drosophila developmental gene fat facets has a human homologue in Xp11.4 which escapes X-inactivation and has related sequences on Yq11.2 | journal = Hum. Mol. Genet. | volume = 5 | issue = 11 | pages = 1695–701 | year = 1996 | pmid = 8922996 | pmc =  | doi = 10.1093/hmg/5.11.1695 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: USP9X ubiquitin specific peptidase 9, X-linked| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8239| accessdate = }}</ref>
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}


<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Function ==
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Ubiquitin specific peptidase 9, X-linked
| HGNCid = 12632
| Symbol = USP9X
| AltSymbols =; FAF; DFFRX
| OMIM = 300072
| ECnumber = 
| Homologene = 3418
| MGIid = 894681
| GeneAtlas_image1 = PBB_GE_USP9X_201099_at_tn.png
| GeneAtlas_image2 = PBB_GE_USP9X_201100_s_at_tn.png
| Function = {{GNF_GO|id=GO:0004197 |text = cysteine-type endopeptidase activity}} {{GNF_GO|id=GO:0004221 |text = ubiquitin thiolesterase activity}}
| Component =
| Process = {{GNF_GO|id=GO:0006511 |text = ubiquitin-dependent protein catabolic process}} {{GNF_GO|id=GO:0006512 |text = ubiquitin cycle}} {{GNF_GO|id=GO:0007292 |text = female gamete generation}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 8239
    | Hs_Ensembl = ENSG00000124486
    | Hs_RefseqProtein = NP_001034679
    | Hs_RefseqmRNA = NM_001039590
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = X
    | Hs_GenLoc_start = 40829832
    | Hs_GenLoc_end = 40980776
    | Hs_Uniprot = Q93008
    | Mm_EntrezGene = 22284
    | Mm_Ensembl = ENSMUSG00000031010
    | Mm_RefseqmRNA = NM_009481
    | Mm_RefseqProtein = NP_033507
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = X
    | Mm_GenLoc_start = 12228496
    | Mm_GenLoc_end = 12338841
    | Mm_Uniprot = Q4FE56
  }}
}}
'''Ubiquitin specific peptidase 9, X-linked''', also known as '''USP9X''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: USP9X ubiquitin specific peptidase 9, X-linked| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8239| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
This gene is a member of the [[peptidase]] C19 family and encodes a protein that is similar to [[ubiquitin]]-specific proteases. Though this gene is located on the X chromosome, it escapes [[X-inactivation]].
{{PBB_Summary
| section_title =
| summary_text = This gene is a member of the peptidase C19 family and encodes a protein that is similar to ubiquitin-specific proteases. Though this gene is located on the X chromosome, it escapes X-inactivation. Mutations in this gene have been associated with Turner syndrome. Alternate transcriptional splice variants, encoding different isoforms, have been characterized.<ref name="entrez">{{cite web | title = Entrez Gene: USP9X ubiquitin specific peptidase 9, X-linked| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8239| accessdate = }}</ref>
}}


==References==
Depletion of USP9X from two-cell mouse embryos halts blastocyst development and results in slower blastomere cleavage rate, impaired cell adhesion and a loss of cell polarity. It has also been implicated that USP9X is likely to influence developmental processes through signaling pathways of Notch, Wnt, EGF, and mTOR. USP9X has been recognized in studies of mouse and human stem cells involving embryonic, neural and hematopoietic stem cells.<ref>{{Cite journal|last = Murtaza|first = Mariyam|last2 = Jolly|first2 = Lachlan A.|last3 = Gecz|first3 = Jozef|last4 = Wood|first4 = Stephen A.|date = 2015-01-01|title = La FAM fatale: USP9X in development and disease|journal = Cellular and Molecular Life Sciences|volume = 72|issue = 11|pages = 2075–2089|doi = 10.1007/s00018-015-1851-0|issn = 1420-682X|pmc = 4427618|pmid = 25672900}}</ref> High expression is retained in undifferentiated progenitor and stem cells and decreases as differentiation continues. USP9X is a protein-coding gene that has been implicated either directly through mutations or indirectly in a number of neurodevelopmental and neurodegenerative disorders. Three mutations have been connected with X-linked intellectual disability and disrupt neuronal growth and cell migration. Neurodegenerative disorders, such as Alzheimer's, Parkinson's and Huntington's disease, have also been linked to USP9X. Specifically, USP9X has been implicated in the regulation of the phosphorylation and expression of the microtule-associated protein [[tau]], which forms pathological aggregates in Alzheimer's and other tauopathies.<ref>{{Cite journal|last = Köglsberger|first = Sandra |last2 = Cordero-Maldonado|first2 = Maria L.|last3 = Antony|first3 = Paul|last4 = Forster|first4 = Julia I.|last5 = Garcia|first5 = Pierre|last6 = Buttini|first6 = Manuel|last7 = Crawford|first7 = Alex|last8 = Glaab|first8 = Enrico|date = 2016-12-01|title = Gender-Specific Expression of Ubiquitin-Specific Peptidase 9 Modulates Tau Expression and Phosphorylation: Possible Implications for Tauopathies|journal = Molecular Neurobiology|volume = in press|issue = 10 |pages = 7979–7993|doi = 10.1007/s12035-016-0299-z|pmid =    27878758
{{reflist|2}}
|pmc = 5684262 }}</ref> Scientists have generated a knockout model where they isolated hippocampal neurons from an USP9X-knockout male mouse, which showed a 43% reduction in axonal length and aborization compared to wildtype.<ref>{{Cite web|url = http://www.omim.org/entry/300072|title = OMIM Entry              - * 300072 - UBIQUITIN-SPECIFIC PROTEASE 9, X-LINKED; USP9X|website = www.omim.org|access-date = 2016-04-12}}</ref>
==Further reading==
 
== Interactions ==
 
USP9X has been shown to [[Protein-protein interaction|interact]] with:
* [[Beta-catenin]],<ref name = pmid10620020>{{cite journal | vauthors = Taya S, Yamamoto T, Kanai-Azuma M, Wood SA, Kaibuchi K | title = The deubiquitinating enzyme Fam interacts with and stabilizes beta-catenin | journal = Genes Cells | volume = 4 | issue = 12 | pages = 757–67  | date = Dec 1999 | pmid = 10620020 | doi = 10.1046/j.1365-2443.1999.00297.x }}</ref>
* [[MARK4]],<ref name = pmid18254724>{{cite journal | vauthors = Al-Hakim AK, Zagorska A, Chapman L, Deak M, Peggie M, Alessi DR | title = Control of AMPK-related kinases by USP9X and atypical Lys(29)/Lys(33)-linked polyubiquitin chains | journal = Biochem. J. | volume = 411 | issue = 2 | pages = 249–60  | date = Apr 2008 | pmid = 18254724 | doi = 10.1042/BJ20080067 }}</ref>
* [[MLLT4]],<ref name = pmid10620020/><ref name = pmid9722616>{{cite journal | vauthors = Taya S, Yamamoto T, Kano K, Kawano Y, Iwamatsu A, Tsuchiya T, Tanaka K, Kanai-Azuma M, Wood SA, Mattick JS, Kaibuchi K | title = The Ras target AF-6 is a substrate of the fam deubiquitinating enzyme | journal = J. Cell Biol. | volume = 142 | issue = 4 | pages = 1053–62  | date = Aug 1998 | pmid = 9722616 | pmc = 2132865 | doi = 10.1083/jcb.142.4.1053 }}</ref> and
* [[NUAK1]].<ref name = pmid18254724/>
* [[ERG (gene)|ERG]].<ref name="pmid24591637">{{cite journal |vauthors = Wang S, Kollipara RK, Srivastava N, Li R, Ravindranathan P, Hernandez E, Freeman E, Humphries CG, Kapur P, Lotan Y, Fazli L, Gleave ME, Plymate SR, Raj GV, Hsieh JT, Kittler R |title = Ablation of the oncogenic transcription factor ERG by deubiquitinase inhibition in prostate cancer |journal = Proc. Natl. Acad. Sci. U.S.A. |volume = 111 |issue = 11 |pages = 4251–6 |year = 2014 |pmid = 24591637 |pmc = 3964108 |doi = 10.1073/pnas.1322198111 }}</ref>
* [[AZI1|CEP131]]<ref>{{Cite journal|last=Li|first=Xin|last2=Song|first2=Nan|last3=Liu|first3=Ling|last4=Liu|first4=Xinhua|last5=Ding|first5=Xiang|last6=Song|first6=Xin|last7=Yang|first7=Shangda|last8=Shan|first8=Lin|last9=Zhou|first9=Xing|date=2017-03-31|title=USP9X regulates centrosome duplication and promotes breast carcinogenesis|journal=Nature Communications|language=en|volume=8|pages=14866|doi=10.1038/ncomms14866|pmid=28361952|pmc=5380967|issn=2041-1723}}</ref>
 
== References ==
{{reflist}}
 
== Further reading ==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
* {{cite journal | vauthors = D'Andrea A, Pellman D | title = Deubiquitinating enzymes: a new class of biological regulators | journal = Crit. Rev. Biochem. Mol. Biol. | volume = 33 | issue = 5 | pages = 337–52 | year = 1998 | pmid = 9827704 | doi = 10.1080/10409239891204251 }}
| citations =
* {{cite journal | vauthors = Andersson B, Wentland MA, Ricafrente JY, Liu W, Gibbs RA | title = A "double adaptor" method for improved shotgun library construction | journal = Anal. Biochem. | volume = 236 | issue = 1 | pages = 107–13 | year = 1996 | pmid = 8619474 | doi = 10.1006/abio.1996.0138 }}
*{{cite journal | author=D'Andrea A, Pellman D |title=Deubiquitinating enzymes: a new class of biological regulators. |journal=Crit. Rev. Biochem. Mol. Biol. |volume=33 |issue= 5 |pages= 337-52 |year= 1999 |pmid= 9827704 |doi= }}
* {{cite journal | vauthors = Yu W, Andersson B, Worley KC, Muzny DM, Ding Y, Liu W, Ricafrente JY, Wentland MA, Lennon G, Gibbs RA | title = Large-scale concatenation cDNA sequencing | journal = Genome Res. | volume = 7 | issue = 4 | pages = 353–8 | year = 1997 | pmid = 9110174 | pmc = 139146 | doi = 10.1101/gr.7.4.353 }}
*{{cite journal | author=Andersson B, Wentland MA, Ricafrente JY, ''et al.'' |title=A "double adaptor" method for improved shotgun library construction. |journal=Anal. Biochem. |volume=236 |issue= 1 |pages= 107-13 |year= 1996 |pmid= 8619474 |doi= 10.1006/abio.1996.0138 }}
* {{cite journal | vauthors = Dias Neto E, Correa RG, Verjovski-Almeida S, Briones MR, Nagai MA, da Silva W, Zago MA, Bordin S, Costa FF, Goldman GH, Carvalho AF, Matsukuma A, Baia GS, Simpson DH, Brunstein A, de Oliveira PS, Bucher P, Jongeneel CV, O'Hare MJ, Soares F, Brentani RR, Reis LF, de Souza SJ, Simpson AJ | title = Shotgun sequencing of the human transcriptome with ORF expressed sequence tags | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 97 | issue = 7 | pages = 3491–6 | year = 2000 | pmid = 10737800 | pmc = 16267 | doi = 10.1073/pnas.97.7.3491 }}
*{{cite journal | author=Jones MH, Furlong RA, Burkin H, ''et al.'' |title=The Drosophila developmental gene fat facets has a human homologue in Xp11.4 which escapes X-inactivation and has related sequences on Yq11.2. |journal=Hum. Mol. Genet. |volume=5 |issue= 11 |pages= 1695-701 |year= 1997 |pmid= 8922996 |doi=  }}
* {{cite journal | vauthors = Noma T, Kanai Y, Kanai-Azuma M, Ishii M, Fujisawa M, Kurohmaru M, Kawakami H, Wood SA, Hayashi Y | title = Stage- and sex-dependent expressions of Usp9x, an X-linked mouse ortholog of Drosophila Fat facets, during gonadal development and oogenesis in mice | journal = Gene Expr. Patterns | volume = 2 | issue = 1–2 | pages = 87–91 | year = 2002 | pmid = 12617843 | doi = 10.1016/S0925-4773(02)00290-3 }}
*{{cite journal  | author=Yu W, Andersson B, Worley KC, ''et al.'' |title=Large-scale concatenation cDNA sequencing. |journal=Genome Res. |volume=7 |issue= 4 |pages= 353-8 |year= 1997 |pmid= 9110174 |doi= }}
* {{cite journal | vauthors = Murray RZ, Jolly LA, Wood SA | title = The FAM deubiquitylating enzyme localizes to multiple points of protein trafficking in epithelia, where it associates with E-cadherin and beta-catenin | journal = Mol. Biol. Cell | volume = 15 | issue = 4 | pages = 1591–9 | year = 2004 | pmid = 14742711 | pmc = 379258 | doi = 10.1091/mbc.E03-08-0630 }}
*{{cite journal  | author=Taya S, Yamamoto T, Kano K, ''et al.'' |title=The Ras target AF-6 is a substrate of the fam deubiquitinating enzyme. |journal=J. Cell Biol. |volume=142 |issue= 4 |pages= 1053-62 |year= 1998 |pmid= 9722616 |doi=  }}
* {{cite journal | vauthors = Bouwmeester T, Bauch A, Ruffner H, Angrand PO, Bergamini G, Croughton K, Cruciat C, Eberhard D, Gagneur J, Ghidelli S, Hopf C, Huhse B, Mangano R, Michon AM, Schirle M, Schlegl J, Schwab M, Stein MA, Bauer A, Casari G, Drewes G, Gavin AC, Jackson DB, Joberty G, Neubauer G, Rick J, Kuster B, Superti-Furga G | title = A physical and functional map of the human TNF-alpha/NF-kappa B signal transduction pathway | journal = Nat. Cell Biol. | volume = 6 | issue = 2 | pages = 97–105 | year = 2004 | pmid = 14743216 | doi = 10.1038/ncb1086 }}
*{{cite journal  | author=Taya S, Yamamoto T, Kanai-Azuma M, ''et al.'' |title=The deubiquitinating enzyme Fam interacts with and stabilizes beta-catenin. |journal=Genes Cells |volume=4 |issue= 12 |pages= 757-67 |year= 2000 |pmid= 10620020 |doi=  }}
* {{cite journal | vauthors = Fu GK, Wang JT, Yang J, Au-Young J, Stuve LL | title = Circular rapid amplification of cDNA ends for high-throughput extension cloning of partial genes | journal = Genomics | volume = 84 | issue = 1 | pages = 205–10 | year = 2004 | pmid = 15203218 | doi = 10.1016/j.ygeno.2004.01.011 }}
*{{cite journal | author=Dias Neto E, Correa RG, Verjovski-Almeida S, ''et al.'' |title=Shotgun sequencing of the human transcriptome with ORF expressed sequence tags. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=97 |issue= 7 |pages= 3491-6 |year= 2000 |pmid= 10737800 |doi=  }}
* {{cite journal | vauthors = Rush J, Moritz A, Lee KA, Guo A, Goss VL, Spek EJ, Zhang H, Zha XM, Polakiewicz RD, Comb MJ | title = Immunoaffinity profiling of tyrosine phosphorylation in cancer cells | journal = Nat. Biotechnol. | volume = 23 | issue = 1 | pages = 94–101 | year = 2005 | pmid = 15592455 | doi = 10.1038/nbt1046 }}
*{{cite journal  | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
* {{cite journal | vauthors = Al-Hakim AK, Göransson O, Deak M, Toth R, Campbell DG, Morrice NA, Prescott AR, Alessi DR | title = 14-3-3 cooperates with LKB1 to regulate the activity and localization of QSK and SIK | journal = J. Cell Sci. | volume = 118 | issue = Pt 23 | pages = 5661–73 | year = 2005 | pmid = 16306228 | doi = 10.1242/jcs.02670 }}
*{{cite journal | author=Noma T, Kanai Y, Kanai-Azuma M, ''et al.'' |title=Stage- and sex-dependent expressions of Usp9x, an X-linked mouse ortholog of Drosophila Fat facets, during gonadal development and oogenesis in mice. |journal=Gene Expr. Patterns |volume=2 |issue= 1-2 |pages= 87-91 |year= 2003 |pmid= 12617843 |doi= }}
* {{cite journal | vauthors = Kimura K, Wakamatsu A, Suzuki Y, Ota T, Nishikawa T, Yamashita R, Yamamoto J, Sekine M, Tsuritani K, Wakaguri H, Ishii S, Sugiyama T, Saito K, Isono Y, Irie R, Kushida N, Yoneyama T, Otsuka R, Kanda K, Yokoi T, Kondo H, Wagatsuma M, Murakawa K, Ishida S, Ishibashi T, Takahashi-Fujii A, Tanase T, Nagai K, Kikuchi H, Nakai K, Isogai T, Sugano S | title = Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes | journal = Genome Res. | volume = 16 | issue = 1 | pages = 55–65 | year = 2006 | pmid = 16344560 | pmc = 1356129 | doi = 10.1101/gr.4039406 }}
*{{cite journal | author=Murray RZ, Jolly LA, Wood SA |title=The FAM deubiquitylating enzyme localizes to multiple points of protein trafficking in epithelia, where it associates with E-cadherin and beta-catenin. |journal=Mol. Biol. Cell |volume=15 |issue= 4 |pages= 1591-9 |year= 2004 |pmid= 14742711 |doi= 10.1091/mbc.E03-08-0630 }}
* {{cite journal | vauthors = Beausoleil SA, Villén J, Gerber SA, Rush J, Gygi SP | title = A probability-based approach for high-throughput protein phosphorylation analysis and site localization | journal = Nat. Biotechnol. | volume = 24 | issue = 10 | pages = 1285–92 | year = 2006 | pmid = 16964243 | doi = 10.1038/nbt1240 }}
*{{cite journal | author=Bouwmeester T, Bauch A, Ruffner H, ''et al.'' |title=A physical and functional map of the human TNF-alpha/NF-kappa B signal transduction pathway. |journal=Nat. Cell Biol. |volume=6 |issue= 2 |pages= 97-105 |year= 2004 |pmid= 14743216 |doi= 10.1038/ncb1086 }}
* {{cite journal | vauthors = Mouchantaf R, Azakir BA, McPherson PS, Millard SM, Wood SA, Angers A | title = The ubiquitin ligase itch is auto-ubiquitylated in vivo and in vitro but is protected from degradation by interacting with the deubiquitylating enzyme FAM/USP9X | journal = J. Biol. Chem. | volume = 281 | issue = 50 | pages = 38738–47 | year = 2006 | pmid = 17038327 | doi = 10.1074/jbc.M605959200 }}
*{{cite journal | author=Fu GK, Wang JT, Yang J, ''et al.'' |title=Circular rapid amplification of cDNA ends for high-throughput extension cloning of partial genes. |journal=Genomics |volume=84 |issue= 1 |pages= 205-10 |year= 2005 |pmid= 15203218 |doi= 10.1016/j.ygeno.2004.01.011 }}
* {{cite journal | vauthors = Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M | title = Global, in vivo, and site-specific phosphorylation dynamics in signaling networks | journal = Cell | volume = 127 | issue = 3 | pages = 635–48 | year = 2006 | pmid = 17081983 | doi = 10.1016/j.cell.2006.09.026 }}
*{{cite journal | author=Rush J, Moritz A, Lee KA, ''et al.'' |title=Immunoaffinity profiling of tyrosine phosphorylation in cancer cells. |journal=Nat. Biotechnol. |volume=23 |issue= 1 |pages= 94-101 |year= 2005 |pmid= 15592455 |doi= 10.1038/nbt1046 }}
*{{cite journal | author=Ross MT, Grafham DV, Coffey AJ, ''et al.'' |title=The DNA sequence of the human X chromosome. |journal=Nature |volume=434 |issue= 7031 |pages= 325-37 |year= 2005 |pmid= 15772651 |doi= 10.1038/nature03440 }}
*{{cite journal  | author=Al-Hakim AK, Göransson O, Deak M, ''et al.'' |title=14-3-3 cooperates with LKB1 to regulate the activity and localization of QSK and SIK. |journal=J. Cell. Sci. |volume=118 |issue= Pt 23 |pages= 5661-73 |year= 2006 |pmid= 16306228 |doi= 10.1242/jcs.02670 }}
*{{cite journal | author=Kimura K, Wakamatsu A, Suzuki Y, ''et al.'' |title=Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes. |journal=Genome Res. |volume=16 |issue= 1 |pages= 55-65 |year= 2006 |pmid= 16344560 |doi= 10.1101/gr.4039406 }}
*{{cite journal | author=Beausoleil SA, Villén J, Gerber SA, ''et al.'' |title=A probability-based approach for high-throughput protein phosphorylation analysis and site localization. |journal=Nat. Biotechnol. |volume=24 |issue= 10 |pages= 1285-92 |year= 2006 |pmid= 16964243 |doi= 10.1038/nbt1240 }}
*{{cite journal | author=Mouchantaf R, Azakir BA, McPherson PS, ''et al.'' |title=The ubiquitin ligase itch is auto-ubiquitylated in vivo and in vitro but is protected from degradation by interacting with the deubiquitylating enzyme FAM/USP9X. |journal=J. Biol. Chem. |volume=281 |issue= 50 |pages= 38738-47 |year= 2007 |pmid= 17038327 |doi= 10.1074/jbc.M605959200 }}
*{{cite journal | author=Olsen JV, Blagoev B, Gnad F, ''et al.'' |title=Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. |journal=Cell |volume=127 |issue= 3 |pages= 635-48 |year= 2006 |pmid= 17081983 |doi= 10.1016/j.cell.2006.09.026 }}
}}
{{refend}}
{{refend}}
{{protein-stub}}
{{WikiDoc Sources}}

Latest revision as of 10:48, 12 January 2019

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Probable ubiquitin carboxyl-terminal hydrolase FAF-X is an enzyme that in humans is encoded by the USP9X gene.[1][2]

Function

This gene is a member of the peptidase C19 family and encodes a protein that is similar to ubiquitin-specific proteases. Though this gene is located on the X chromosome, it escapes X-inactivation.

Depletion of USP9X from two-cell mouse embryos halts blastocyst development and results in slower blastomere cleavage rate, impaired cell adhesion and a loss of cell polarity. It has also been implicated that USP9X is likely to influence developmental processes through signaling pathways of Notch, Wnt, EGF, and mTOR. USP9X has been recognized in studies of mouse and human stem cells involving embryonic, neural and hematopoietic stem cells.[3] High expression is retained in undifferentiated progenitor and stem cells and decreases as differentiation continues. USP9X is a protein-coding gene that has been implicated either directly through mutations or indirectly in a number of neurodevelopmental and neurodegenerative disorders. Three mutations have been connected with X-linked intellectual disability and disrupt neuronal growth and cell migration. Neurodegenerative disorders, such as Alzheimer's, Parkinson's and Huntington's disease, have also been linked to USP9X. Specifically, USP9X has been implicated in the regulation of the phosphorylation and expression of the microtule-associated protein tau, which forms pathological aggregates in Alzheimer's and other tauopathies.[4] Scientists have generated a knockout model where they isolated hippocampal neurons from an USP9X-knockout male mouse, which showed a 43% reduction in axonal length and aborization compared to wildtype.[5]

Interactions

USP9X has been shown to interact with:

References

  1. ↑ Jones MH, Furlong RA, Burkin H, Chalmers IJ, Brown GM, Khwaja O, Affara NA (1996). "The Drosophila developmental gene fat facets has a human homologue in Xp11.4 which escapes X-inactivation and has related sequences on Yq11.2". Hum. Mol. Genet. 5 (11): 1695–701. doi:10.1093/hmg/5.11.1695. PMID 8922996.
  2. ↑ "Entrez Gene: USP9X ubiquitin specific peptidase 9, X-linked".
  3. ↑ Murtaza, Mariyam; Jolly, Lachlan A.; Gecz, Jozef; Wood, Stephen A. (2015-01-01). "La FAM fatale: USP9X in development and disease". Cellular and Molecular Life Sciences. 72 (11): 2075–2089. doi:10.1007/s00018-015-1851-0. ISSN 1420-682X. PMC 4427618. PMID 25672900.
  4. ↑ Köglsberger, Sandra; Cordero-Maldonado, Maria L.; Antony, Paul; Forster, Julia I.; Garcia, Pierre; Buttini, Manuel; Crawford, Alex; Glaab, Enrico (2016-12-01). "Gender-Specific Expression of Ubiquitin-Specific Peptidase 9 Modulates Tau Expression and Phosphorylation: Possible Implications for Tauopathies". Molecular Neurobiology. in press (10): 7979–7993. doi:10.1007/s12035-016-0299-z. PMC 5684262. PMID 27878758.
  5. ↑ "OMIM Entry - * 300072 - UBIQUITIN-SPECIFIC PROTEASE 9, X-LINKED; USP9X". www.omim.org. Retrieved 2016-04-12.
  6. ↑ 6.0 6.1 Taya S, Yamamoto T, Kanai-Azuma M, Wood SA, Kaibuchi K (Dec 1999). "The deubiquitinating enzyme Fam interacts with and stabilizes beta-catenin". Genes Cells. 4 (12): 757–67. doi:10.1046/j.1365-2443.1999.00297.x. PMID 10620020.
  7. ↑ 7.0 7.1 Al-Hakim AK, Zagorska A, Chapman L, Deak M, Peggie M, Alessi DR (Apr 2008). "Control of AMPK-related kinases by USP9X and atypical Lys(29)/Lys(33)-linked polyubiquitin chains". Biochem. J. 411 (2): 249–60. doi:10.1042/BJ20080067. PMID 18254724.
  8. ↑ Taya S, Yamamoto T, Kano K, Kawano Y, Iwamatsu A, Tsuchiya T, Tanaka K, Kanai-Azuma M, Wood SA, Mattick JS, Kaibuchi K (Aug 1998). "The Ras target AF-6 is a substrate of the fam deubiquitinating enzyme". J. Cell Biol. 142 (4): 1053–62. doi:10.1083/jcb.142.4.1053. PMC 2132865. PMID 9722616.
  9. ↑ Wang S, Kollipara RK, Srivastava N, Li R, Ravindranathan P, Hernandez E, Freeman E, Humphries CG, Kapur P, Lotan Y, Fazli L, Gleave ME, Plymate SR, Raj GV, Hsieh JT, Kittler R (2014). "Ablation of the oncogenic transcription factor ERG by deubiquitinase inhibition in prostate cancer". Proc. Natl. Acad. Sci. U.S.A. 111 (11): 4251–6. doi:10.1073/pnas.1322198111. PMC 3964108. PMID 24591637.
  10. ↑ Li, Xin; Song, Nan; Liu, Ling; Liu, Xinhua; Ding, Xiang; Song, Xin; Yang, Shangda; Shan, Lin; Zhou, Xing (2017-03-31). "USP9X regulates centrosome duplication and promotes breast carcinogenesis". Nature Communications. 8: 14866. doi:10.1038/ncomms14866. ISSN 2041-1723. PMC 5380967. PMID 28361952.

Further reading

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