USP9X_MOUSE - dbPTM
USP9X_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID USP9X_MOUSE
UniProt AC P70398
Protein Name Probable ubiquitin carboxyl-terminal hydrolase FAF-X
Gene Name Usp9x
Organism Mus musculus (Mouse).
Sequence Length 2559
Subcellular Localization Cytoplasm . Cell projection, growth cone .
Protein Description 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]
Protein Sequence MTATTRGSPVGGNDNQGQAPDGQSQPPLQQNQTSSPDSSNENSPATPPDEQGQGDAPPQIEDEEPAFPHTDLAKLDDMINRPRWVVPVLPKGELEVLLEAAIDLSKKGLDVKSEACQRFFRDGLTISFTKILTDEAVSGWKFEIHRCIINNTHRLVELCVAKLAQDWFPLLELLAMALNPHCKFHIYNGTRPCESVSSSVQLPEDELFARSPDPRSPKGWLVDLLNKFGTLNGFQILHDRFINGSALNVQIIAALIKPFGQCYEFLTLHTVKKYFLPIIEMVPQFLENLTDEELKKEAKNEAKNDALSMIIKSLKNLASRVPGQEETVKNLEIFRLKMILRLLQISSFNGKMNALNEVNKVISSVSYYTHRHGSSEDEEWLTAERMAEWIQQNNILSIVLRDSLHQPQYVEKLEKILRFVIKEKALTLQDLDNIWAAQAGKHEAIVKNVHDLLAKLAWDFSPEQLDHLFDCFKASWTNASKKQREKLLELIRRLAEDDKDGVMAHKVLNLLWNLAHSDDVPVDIMDLALSAHIKILDYSCSQDRDTQKIQWIDRFIEELRTNDKWVIPALKQIREICSLFGEAPQNLSQSQRSPHVFYRHDLINQLQHNHALVTLVAENLATYMESMRMYGRDNEDYDPQTVRLGSRYSHVQEVQERLNFLRFLLKDGQLWLCAPQAKQIWKCLAENAVYLCDREACFKWYSKLMGDEPDLDPDINKDFFESNVLQLDPSLLTENGMKCFERFFKAVNCREGKLVAKRRAYMMDDLELIGLDYLWRVVIQSNDDIACRAIDLLKEIYTNLGPRLQVNQVVIHEDFIQSCFDRLKASYDTLCVLDGDKDSINCARQEAVRMVRVLTVLREYINECDSDYHEERTILPMSRAFRGKHLSFIVRFPNQGRQVDDLEVWSHTNDTIGSVRRCILNRIKANVAHTKIELFVGGELIDPGDDRKLIGQLNLKDKSLITAKLTQISSNMPSSPDSSSDSSTGSPGNHGNHYSDGPNPEVESCLPGVIMSLHPRYISFLWQVADLGSSLNMPPLRDGARVLMKLMPPDSTTIEKLRAICLDHAKLGESSLSPSLDSLFFGPSASQVLYLTEVVYALLMPAGAPLTDDSSDFQFHFLKSGGLPLVLSMLTRNNFLPNADMETRRGAYLNALKIAKLLLTAIGYGHVRAVAEACQPGVEGVNPMTSVNQVTHDQAVVLQSALQSIPNPSSECMLRNVSVRLAQQISDEASRYMPDICVIRAIQKIIWTSGCGGLQLVFSPNEEVTKIYEKTNAGNEPDLEDEQVCCEALEVMTLCFALIPTALDALSKEKAWQTFIIDLLLHCHSKTVRQVAQEQFFLMCTRCCMGHRPLLFFITLLFTVLGSTARERAKHSGDYFTLLRHLLNYAYNSNINVPNAEVLLNNEIDWLKRIRDDVKRTGETGVEETILEGHLGVTKELLAFQTPEKKFHIGCEKGGANLIKELIDDFIFPASNVYLQYMRNGELPAEQAIPVCGSPATINAGFELLVALAVGCVRNLKQIVDSLTEMYYIGTAITTCEALTEWEYLPPVGPRPPKGFVGLKNAGATCYMNSVIQQLYMIPSIRNGILAIEGTGSDVDDDMSGDEKQDNESNVDPRDDVFGYPQQFEDKPPLSKTEDRKEYNIGVLRHLQVIFGHLAASRLQYYVPRGFWKQFRLWGEPVNLREQHDALEFFNSLVDSLDEALKALGHPAMLSKVLGGSFADQKICQGCPHRYECEESFTTLNVDIRNHQNLLDSLEQYVKGDLLEGANAYHCEKCNKKVDTVKRLLIKKLPPVLAIQLKRFDYDWERECAIKFNDYFEFPRELDMEPYTVAGVAKLEGDNVNPESQLIQQNEQSESEKAGSTKYRLVGVLVHSGQASGGHYYSYIIQRNGGDGEKNRWYKFDDGDVTECKMDDDEEMKNQCFGGEYMGEVFDHMMKRMSYRRQKRWWNAYILFYERMDTIGHDDEVIRYISEIAITTRPHQIVMPSAIERSVRKQNVQFMHNRMQYSLEYFQFMKKLLTCNGVYLNPPPGQDHLSPEAEEITMISIQLAARFLFTTGFHTKKIVRGSASDWYDALCILLRHSKNVRFWFAHNVLFNVSNRFSEYLLECPSAEVRGAFAKLIVFIAHFSLQDGPCPSPFASPGPSSQAYDNLSLSDHLLRAVLNLLRREVSEHGRHLQQYFNLFVMYANLGVAEKTQLLKLSVPATFMLVSLDEGPGPPIKYQYAELGKLYSVVSQLIRCCNVSSRMQSSINGNPSLPNPFGDPNLSQPIMPIQQNVVDILFVRTSYVKKIIEDCSNSDETVKLLRFCCWENPQFSSTVLSELLWQVAYSYTYELRPYLDLLLQILLIEDSWQTHRIHNALKGIPDDRDGLFDTIQRSKNHYQKRAYQCIKCMVALFSSCPVAYQILQGNGDLKRKWTWAVEWLGDELERRPYTGNPQYTYNNWSPPVQSNETSNGYFLERSHSARMTLAKACELCPEEEPDDQDAPDEHESPPPEDAPLYPHSPGSQYQQNNHVHGQPYTGPAAHHMNNPQRTGQRAQENYEGGEEVSPPQTKGSVKCTY
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
112UbiquitinationSKKGLDVKSEACQRF
HHCCCCCCHHHHHHH		42.0922790023
303UbiquitinationKEAKNEAKNDALSMI
HHHHHHHHHHHHHHH		49.5422790023
313PhosphorylationALSMIIKSLKNLASR
HHHHHHHHHHHHHHC		33.8821454597
315UbiquitinationSMIIKSLKNLASRVP
HHHHHHHHHHHHCCC		57.9422790023
367PhosphorylationKVISSVSYYTHRHGS
HHHHHHHHCCCCCCC		15.3818563927
374PhosphorylationYYTHRHGSSEDEEWL
HCCCCCCCCCCHHHH		25.1627742792
375PhosphorylationYTHRHGSSEDEEWLT
CCCCCCCCCCHHHHH		54.3727742792
412UbiquitinationHQPQYVEKLEKILRF
CCHHHHHHHHHHHHH		52.4822790023
588PhosphorylationGEAPQNLSQSQRSPH
CCCCCCCCCCCCCCC		35.0225521595
590PhosphorylationAPQNLSQSQRSPHVF
CCCCCCCCCCCCCCC		24.9627818261
593PhosphorylationNLSQSQRSPHVFYRH
CCCCCCCCCCCCCCH		16.2421743459
745UbiquitinationKCFERFFKAVNCREG
HHHHHHHHHHCCCCC		49.0322790023
787S-nitrosocysteineQSNDDIACRAIDLLK
CCCCHHHHHHHHHHH		2.85-
787S-nitrosylationQSNDDIACRAIDLLK
CCCCHHHHHHHHHHH		2.8521278135
837UbiquitinationLCVLDGDKDSINCAR
EEEECCCHHHHHHHH		59.9322790023
860PhosphorylationVLTVLREYINECDSD
HHHHHHHHHHHCCCC		11.5622802335
866PhosphorylationEYINECDSDYHEERT
HHHHHCCCCHHHHHC		52.2926525534
868PhosphorylationINECDSDYHEERTIL
HHHCCCCHHHHHCCC		18.3230635358
887PhosphorylationAFRGKHLSFIVRFPN
HHCCCEEEEEEECCC		16.7919060867
914PhosphorylationHTNDTIGSVRRCILN
CCCCCHHHHHHHHHH		14.4825338131
1045UbiquitinationDGARVLMKLMPPDST
CCCHHHHHHCCCCCC		37.1622790023
1066UbiquitinationAICLDHAKLGESSLS
HHHHCHHHCCCCCCC		54.31-
1226PhosphorylationVRLAQQISDEASRYM
HHHHHHHCHHHHHHC		25.6730635358
1230PhosphorylationQQISDEASRYMPDIC
HHHCHHHHHHCCCHH		23.1530635358
1314PhosphorylationSKEKAWQTFIIDLLL
CCHHHHHHHHHHHHH		13.1925777480
1325PhosphorylationDLLLHCHSKTVRQVA
HHHHHCCCHHHHHHH		35.1025777480
1340S-palmitoylationQEQFFLMCTRCCMGH
HHHHHHHHHHHHCCC		2.0628680068
1370UbiquitinationSTARERAKHSGDYFT
HHHHHHHHHCCCHHH		44.5222790023
1435UbiquitinationEGHLGVTKELLAFQT
CCCCCCCHHHHCCCC		43.9122790023
1453UbiquitinationKFHIGCEKGGANLIK
CEECCCCCCCHHHHH		67.7222790023
1591PhosphorylationGILAIEGTGSDVDDD
CEEEEECCCCCCCCC		22.2624925903
1593PhosphorylationLAIEGTGSDVDDDMS
EEEECCCCCCCCCCC		34.0124925903
1599OxidationGSDVDDDMSGDEKQD
CCCCCCCCCCCCCCC		6.5817242355
1600PhosphorylationSDVDDDMSGDEKQDN
CCCCCCCCCCCCCCC		50.5225521595
1609PhosphorylationDEKQDNESNVDPRDD
CCCCCCCCCCCCCCC		48.7025521595
1627UbiquitinationYPQQFEDKPPLSKTE
CCCCCCCCCCCCCCC		41.1422790023
1631PhosphorylationFEDKPPLSKTEDRKE
CCCCCCCCCCCCCHH		43.2225338131
1632UbiquitinationEDKPPLSKTEDRKEY
CCCCCCCCCCCCHHH		64.7122790023
1637UbiquitinationLSKTEDRKEYNIGVL
CCCCCCCHHHHHHHH		76.5022790023
1669UbiquitinationYVPRGFWKQFRLWGE
HCCCCHHHHHHCCCC		36.9822790023
1712UbiquitinationGHPAMLSKVLGGSFA
CCHHHHHHHHCCCHH		37.2022790023
1722MalonylationGGSFADQKICQGCPH
CCCHHCCCCCCCCCC		46.1026320211
1798UbiquitinationPVLAIQLKRFDYDWE
CEEEEEEECCCCCCH		34.3422790023
1811UbiquitinationWERECAIKFNDYFEF
CHHHHEEEECCCCCC		21.4222790023
1815PhosphorylationCAIKFNDYFEFPREL
HEEEECCCCCCCCCC		13.2017947660
1899UbiquitinationGEKNRWYKFDDGDVT
CCCCCEEECCCCCCC		35.0422790023
2103PhosphorylationVSNRFSEYLLECPSA
CHHHHHHHHHHCCCH		18.5223567750
2109PhosphorylationEYLLECPSAEVRGAF
HHHHHCCCHHHHHHH		49.0423567750
2185PhosphorylationYFNLFVMYANLGVAE
HHHHHHHHHCCCHHH		6.24-
2194PhosphorylationNLGVAEKTQLLKLSV
CCCHHHHHHHHHCCC		18.89-
2219UbiquitinationEGPGPPIKYQYAELG
CCCCCCCEEEHHHHH		31.88-
2242PhosphorylationLIRCCNVSSRMQSSI
HHHHCCCHHHHHHHH		9.7622802335
2243PhosphorylationIRCCNVSSRMQSSIN
HHHCCCHHHHHHHHC		27.7322802335
2247PhosphorylationNVSSRMQSSINGNPS
CCHHHHHHHHCCCCC		24.6822802335
2248PhosphorylationVSSRMQSSINGNPSL
CHHHHHHHHCCCCCC		11.8122802335
2254PhosphorylationSSINGNPSLPNPFGD
HHHCCCCCCCCCCCC		61.5322802335
2265PhosphorylationPFGDPNLSQPIMPIQ
CCCCCCCCCCCCCCC		40.3222802335
2288UbiquitinationVRTSYVKKIIEDCSN
EEHHHHHHHHHHCCC		38.5822790023
2360UbiquitinationHRIHNALKGIPDDRD
HHHHHHHCCCCCCCC		53.0022790023
2431PhosphorylationDELERRPYTGNPQYT
HHHHCCCCCCCCCCC		26.0129472430
2432PhosphorylationELERRPYTGNPQYTY
HHHCCCCCCCCCCCC		32.9227087446
2437PhosphorylationPYTGNPQYTYNNWSP
CCCCCCCCCCCCCCC		16.6726745281
2438PhosphorylationYTGNPQYTYNNWSPP
CCCCCCCCCCCCCCC		17.9626745281
2439PhosphorylationTGNPQYTYNNWSPPV
CCCCCCCCCCCCCCC		11.1025521595
2443PhosphorylationQYTYNNWSPPVQSNE
CCCCCCCCCCCCCCC		22.8125521595
2448PhosphorylationNWSPPVQSNETSNGY
CCCCCCCCCCCCCCC		36.5527087446
2451PhosphorylationPPVQSNETSNGYFLE
CCCCCCCCCCCCCCC		31.5726160508
2452PhosphorylationPVQSNETSNGYFLER
CCCCCCCCCCCCCCC		23.2926160508
2455PhosphorylationSNETSNGYFLERSHS
CCCCCCCCCCCCCHH		14.8326160508
2460PhosphorylationNGYFLERSHSARMTL
CCCCCCCCHHHHHHH		16.6526745281
2462PhosphorylationYFLERSHSARMTLAK
CCCCCCHHHHHHHHH		20.8626745281
2466PhosphorylationRSHSARMTLAKACEL
CCHHHHHHHHHHHHH		20.2926745281
2490PhosphorylationDAPDEHESPPPEDAP
CCCCCCCCCCCCCCC		44.6122668510
2507PhosphorylationPHSPGSQYQQNNHVH
CCCCCCCCCCCCCCC		17.4822668510
2540PhosphorylationGQRAQENYEGGEEVS
CCHHHHHCCCCCCCC		18.3925619855
2547PhosphorylationYEGGEEVSPPQTKGS
CCCCCCCCCCCCCCC		33.8625521595
2551PhosphorylationEEVSPPQTKGSVKCT
CCCCCCCCCCCCCCC		43.0525619855
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of USP9X_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of USP9X_MOUSE !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of USP9X_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CTNB1_MOUSECtnnb1physical
15607950
LAT_MOUSELatphysical
26936881
IQCB1_HUMANIQCB1physical
28498859
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of USP9X_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1600, AND MASSSPECTROMETRY.
"Quantitative time-resolved phosphoproteomic analysis of mast cellsignaling.";
Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,Kawakami T., Salomon A.R.;
J. Immunol. 179:5864-5876(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1815 AND TYR-2540, ANDMASS SPECTROMETRY.

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