USP9X_HUMAN - dbPTM
USP9X_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID USP9X_HUMAN
UniProt AC Q93008
Protein Name Probable ubiquitin carboxyl-terminal hydrolase FAF-X
Gene Name USP9X {ECO:0000312|HGNC:HGNC:12632}
Organism Homo sapiens (Human).
Sequence Length 2570
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. [PubMed: 25944111 Regulates chromosome alignment and segregation in mitosis by regulating the localization of BIRC5/survivin to mitotic centromeres. Involved in axonal growth and neuronal cell migration]
Protein Sequence MTATTRGSPVGGNDNQGQAPDGQSQPPLQQNQTSSPDSSNENSPATPPDEQGQGDAPPQLEDEEPAFPHTDLAKLDDMINRPRWVVPVLPKGELEVLLEAAIDLSKKGLDVKSEACQRFFRDGLTISFTKILTDEAVSGWKFEIHRCIINNTHRLVELCVAKLSQDWFPLLELLAMALNPHCKFHIYNGTRPCESVSSSVQLPEDELFARSPDPRSPKGWLVDLLNKFGTLNGFQILHDRFINGSALNVQIIAALIKPFGQCYEFLTLHTVKKYFLPIIEMVPQFLENLTDEELKKEAKNEAKNDALSMIIKSLKNLASRVPGQEETVKNLEIFRLKMILRLLQISSFNGKMNALNEVNKVISSVSYYTHRHGNPEEEEWLTAERMAEWIQQNNILSIVLRDSLHQPQYVEKLEKILRFVIKEKALTLQDLDNIWAAQAGKHEAIVKNVHDLLAKLAWDFSPEQLDHLFDCFKASWTNASKKQREKLLELIRRLAEDDKDGVMAHKVLNLLWNLAHSDDVPVDIMDLALSAHIKILDYSCSQDRDTQKIQWIDRFIEELRTNDKWVIPALKQIREICSLFGEAPQNLSQTQRSPHVFYRHDLINQLQHNHALVTLVAENLATYMESMRLYARDHEDYDPQTVRLGSRYSHVQEVQERLNFLRFLLKDGQLWLCAPQAKQIWKCLAENAVYLCDREACFKWYSKLMGDEPDLDPDINKDFFESNVLQLDPSLLTENGMKCFERFFKAVNCREGKLVAKRRAYMMDDLELIGLDYLWRVVIQSNDDIASRAIDLLKEIYTNLGPRLQVNQVVIHEDFIQSCFDRLKASYDTLCVLDGDKDSVNCARQEAVRMVRVLTVLREYINECDSDYHEERTILPMSRAFRGKHLSFVVRFPNQGRQVDDLEVWSHTNDTIGSVRRCILNRIKANVAHTKIELFVGGELIDPADDRKLIGQLNLKDKSLITAKLTQISSNMPSSPDSSSDSSTGSPGNHGNHYSDGPNPEVESCLPGVIMSLHPRYISFLWQVADLGSSLNMPPLRDGARVLMKLMPPDSTTIEKLRAICLDHAKLGESSLSPSLDSLFFGPSASQVLYLTEVVYALLMPAGAPLADDSSDFQFHFLKSGGLPLVLSMLTRNNFLPNADMETRRGAYLNALKIAKLLLTAIGYGHVRAVAEACQPGVEGVNPMTQINQVTHDQAVVLQSALQSIPNPSSECMLRNVSVRLAQQISDEASRYMPDICVIRAIQKIIWASGCGSLQLVFSPNEEITKIYEKTNAGNEPDLEDEQVCCEALEVMTLCFALIPTALDALSKEKAWQTFIIDLLLHCHSKTVRQVAQEQFFLMCTRCCMGHRPLLFFITLLFTVLGSTARERAKHSGDYFTLLRHLLNYAYNSNINVPNAEVLLNNEIDWLKRIRDDVKRTGETGIEETILEGHLGVTKELLAFQTSEKKFHIGCEKGGANLIKELIDDFIFPASNVYLQYMRNGELPAEQAIPVCGSPPTINAGFELLVALAVGCVRNLKQIVDSLTEMYYIGTAITTCEALTEWEYLPPVGPRPPKGFVGLKNAGATCYMNSVIQQLYMIPSIRNGILAIEGTGSDVDDDMSGDEKQDNESNVDPRDDVFGYPQQFEDKPALSKTEDRKEYNIGVLRHLQVIFGHLAASRLQYYVPRGFWKQFRLWGEPVNLREQHDALEFFNSLVDSLDEALKALGHPAMLSKVLGGSFADQKICQGCPHRYECEESFTTLNVDIRNHQNLLDSLEQYVKGDLLEGANAYHCEKCNKKVDTVKRLLIKKLPPVLAIQLKRFDYDWERECAIKFNDYFEFPRELDMEPYTVAGVAKLEGDNVNPESQLIQQSEQSESETAGSTKYRLVGVLVHSGQASGGHYYSYIIQRNGGDGERNRWYKFDDGDVTECKMDDDEEMKNQCFGGEYMGEVFDHMMKRMSYRRQKRWWNAYILFYERMDTIDQDDELIRYISELAITTRPHQIIMPSAIERSVRKQNVQFMHNRMQYSMEYFQFMKKLLTCNGVYLNPPPGQDHLLPEAEEITMISIQLAARFLFTTGFHTKKVVRGSASDWYDALCILLRHSKNVRFWFAHNVLFNVSNRFSEYLLECPSAEVRGAFAKLIVFIAHFSLQDGPCPSPFASPGPSSQAYDNLSLSDHLLRAVLNLLRREVSEHGRHLQQYFNLFVMYANLGVAEKTQLLKLSVPATFMLVSLDEGPGPPIKYQYAELGKLYSVVSQLIRCCNVSSRMQSSINGNPPLPNPFGDPNLSQPIMPIQQNVADILFVRTSYVKKIIEDCSNSEETVKLLRFCCWENPQFSSTVLSELLWQVAYSYTYELRPYLDLLLQILLIEDSWQTHRIHNALKGIPDDRDGLFDTIQRSKNHYQKRAYQCIKCMVALFSNCPVAYQILQGNGDLKRKWTWAVEWLGDELERRPYTGNPQYTYNNWSPPVQSNETSNGYFLERSHSARMTLAKACELCPEEVKKATSVQQIEMEESKEPDDQDAPDEHESPPPEDAPLYPHSPGSQYQQNNHVHGQPYTGPAAHHMNNPQRTGQRAQENYEGSEEVSPPQTKDQ
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
46PhosphorylationSNENSPATPPDEQGQ
CCCCCCCCCCCCCCC		38.4424275569
127PhosphorylationFRDGLTISFTKILTD
HCCCCEEEEEEECCC		22.9424719451
199PhosphorylationPCESVSSSVQLPEDE
CCCCCCCCCCCCHHH		13.33-
218UbiquitinationSPDPRSPKGWLVDLL
CCCCCCCCCHHHHHH		65.0621890473
218 (in isoform 1)Ubiquitination-65.0621890473
303AcetylationKEAKNEAKNDALSMI
HHHHHHHHHHHHHHH		49.5411794961
303MalonylationKEAKNEAKNDALSMI
HHHHHHHHHHHHHHH		49.5426320211
308PhosphorylationEAKNDALSMIIKSLK
HHHHHHHHHHHHHHH		15.0621712546
313PhosphorylationALSMIIKSLKNLASR
HHHHHHHHHHHHHHC		33.8820068231
313 (in isoform 1)Phosphorylation-33.88-
315AcetylationSMIIKSLKNLASRVP
HHHHHHHHHHHHCCC		57.947683809
315UbiquitinationSMIIKSLKNLASRVP
HHHHHHHHHHHHCCC		57.9421890473
319PhosphorylationKSLKNLASRVPGQEE
HHHHHHHHCCCCCHH		36.6630619164
327PhosphorylationRVPGQEETVKNLEIF
CCCCCHHHHHHHHHH		35.7130619164
329UbiquitinationPGQEETVKNLEIFRL
CCCHHHHHHHHHHHH		64.3321890473
329 (in isoform 1)Ubiquitination-64.3321890473
364PhosphorylationEVNKVISSVSYYTHR
HHHHHHHHHHHHCCC		12.1728555341
366PhosphorylationNKVISSVSYYTHRHG
HHHHHHHHHHCCCCC		17.8621945579
367PhosphorylationKVISSVSYYTHRHGN
HHHHHHHHHCCCCCC		15.3821945579
368PhosphorylationVISSVSYYTHRHGNP
HHHHHHHHCCCCCCH		6.6421945579
369PhosphorylationISSVSYYTHRHGNPE
HHHHHHHCCCCCCHH		12.2821945579
403PhosphorylationLSIVLRDSLHQPQYV
HHHHHHCCCCCHHHH		22.71-
409PhosphorylationDSLHQPQYVEKLEKI
CCCCCHHHHHHHHHH		19.77-
424UbiquitinationLRFVIKEKALTLQDL
HHHHHHHCCCCHHHH		43.6321890473
486UbiquitinationASKKQREKLLELIRR
CCHHHHHHHHHHHHH		61.6421890473
503SulfoxidationEDDKDGVMAHKVLNL
HCCCCCHHHHHHHHH		3.8530846556
560MethylationDRFIEELRTNDKWVI
HHHHHHHHCCCCCHH		34.46-
571UbiquitinationKWVIPALKQIREICS
CCHHHHHHHHHHHHH		45.8721890473
571 (in isoform 1)Ubiquitination-45.8721890473
588PhosphorylationGEAPQNLSQTQRSPH
CCCCCCCCCCCCCCC		38.4426055452
590PhosphorylationAPQNLSQTQRSPHVF
CCCCCCCCCCCCCCC		23.6721712546
590 (in isoform 1)Phosphorylation-23.67-
593PhosphorylationNLSQTQRSPHVFYRH
CCCCCCCCCCCCCHH		15.0020873877
646PhosphorylationPQTVRLGSRYSHVQE
CCHHCCCCCCHHHHH		32.4123090842
701PhosphorylationREACFKWYSKLMGDE
HHHHHHHHHHHHCCC		9.1220068231
701 (in isoform 1)Phosphorylation-9.12-
702PhosphorylationEACFKWYSKLMGDEP
HHHHHHHHHHHCCCC		20.4220068231
702 (in isoform 1)Phosphorylation-20.42-
794UbiquitinationSRAIDLLKEIYTNLG
HHHHHHHHHHHHHCC		49.7321890473
797PhosphorylationIDLLKEIYTNLGPRL
HHHHHHHHHHCCCCC		7.23-
844MethylationKDSVNCARQEAVRMV
CCHHHHHHHHHHHHH		36.7512019981
866PhosphorylationEYINECDSDYHEERT
HHHHHCCCCHHHHHC		52.2928348404
868PhosphorylationINECDSDYHEERTIL
HHHCCCCHHHHHCCC		18.3223312004
887PhosphorylationAFRGKHLSFVVRFPN
HHCCCCEEEEEECCC		18.7330108239
930PhosphorylationIKANVAHTKIELFVG
HHHCCCCCEEEEEEC		24.79-
974PhosphorylationQISSNMPSSPDSSSD
HHHHCCCCCCCCCCC		43.6728348404
975PhosphorylationISSNMPSSPDSSSDS
HHHCCCCCCCCCCCC		27.1928348404
978PhosphorylationNMPSSPDSSSDSSTG
CCCCCCCCCCCCCCC		34.8228348404
979PhosphorylationMPSSPDSSSDSSTGS
CCCCCCCCCCCCCCC		45.6128348404
980PhosphorylationPSSPDSSSDSSTGSP
CCCCCCCCCCCCCCC		45.5228348404
982PhosphorylationSPDSSSDSSTGSPGN
CCCCCCCCCCCCCCC		31.5728348404
983PhosphorylationPDSSSDSSTGSPGNH
CCCCCCCCCCCCCCC		41.6028348404
984PhosphorylationDSSSDSSTGSPGNHG
CCCCCCCCCCCCCCC		45.7028348404
986PhosphorylationSSDSSTGSPGNHGNH
CCCCCCCCCCCCCCC		29.7128348404
994PhosphorylationPGNHGNHYSDGPNPE
CCCCCCCCCCCCCHH		16.6828348404
995PhosphorylationGNHGNHYSDGPNPEV
CCCCCCCCCCCCHHH		28.6528348404
1045UbiquitinationDGARVLMKLMPPDST
CCCHHHHHHCCCCCC		37.1621890473
1045 (in isoform 1)Ubiquitination-37.1621890473
1051PhosphorylationMKLMPPDSTTIEKLR
HHHCCCCCCHHHHHH		32.9720071362
1066UbiquitinationAICLDHAKLGESSLS
HHHHCHHHCCCCCCC		54.31-
1141SulfoxidationNFLPNADMETRRGAY
CCCCCCCCHHHCHHH		5.4221406390
1148PhosphorylationMETRRGAYLNALKIA
CHHHCHHHHHHHHHH		11.87-
1153UbiquitinationGAYLNALKIAKLLLT
HHHHHHHHHHHHHHH		37.9021890473
1232PhosphorylationISDEASRYMPDICVI
HCHHHHHHCCCHHHH		15.54-
1370UbiquitinationSTARERAKHSGDYFT
HHHHHHHHHCCCHHH		44.5221890473
1370 (in isoform 1)Ubiquitination-44.5221890473
1375PhosphorylationRAKHSGDYFTLLRHL
HHHHCCCHHHHHHHH		11.29-
1435UbiquitinationEGHLGVTKELLAFQT
CCCCCCCHHHHCCCC		43.91-
1445UbiquitinationLAFQTSEKKFHIGCE
HCCCCCCCCEECCCC		61.58-
1445 (in isoform 1)Ubiquitination-61.58-
1446UbiquitinationAFQTSEKKFHIGCEK
CCCCCCCCEECCCCC		37.82-
1446 (in isoform 1)Ubiquitination-37.82-
1453UbiquitinationKFHIGCEKGGANLIK
CEECCCCCCCHHHHH		67.72-
1453 (in isoform 1)Ubiquitination-67.72-
1522PhosphorylationNLKQIVDSLTEMYYI
CHHHHHHHHHHHHHH		26.7124043423
1524PhosphorylationKQIVDSLTEMYYIGT
HHHHHHHHHHHHHHH		23.7424043423
1527PhosphorylationVDSLTEMYYIGTAIT
HHHHHHHHHHHHHHH		5.9124043423
1528PhosphorylationDSLTEMYYIGTAITT
HHHHHHHHHHHHHHH		7.4924043423
1531PhosphorylationTEMYYIGTAITTCEA
HHHHHHHHHHHHHHH		12.8224043423
1534PhosphorylationYYIGTAITTCEALTE
HHHHHHHHHHHHHHC		23.9524043423
1535PhosphorylationYIGTAITTCEALTEW
HHHHHHHHHHHHHCC		11.3924043423
1540PhosphorylationITTCEALTEWEYLPP
HHHHHHHHCCCCCCC		46.2124043423
1544PhosphorylationEALTEWEYLPPVGPR
HHHHCCCCCCCCCCC		26.1124043423
1565PhosphorylationGLKNAGATCYMNSVI
CCCCCCCCHHHHHHH		11.8424719451
1576PhosphorylationNSVIQQLYMIPSIRN
HHHHHHHHCCHHHCC		6.6724719451
1580PhosphorylationQQLYMIPSIRNGILA
HHHHCCHHHCCCEEE		24.2124719451
1591PhosphorylationGILAIEGTGSDVDDD
CEEEEECCCCCCCCC		22.2630278072
1593PhosphorylationLAIEGTGSDVDDDMS
EEEECCCCCCCCCCC		34.0130278072
1593 (in isoform 1)Phosphorylation-34.01-
1600PhosphorylationSDVDDDMSGDEKQDN
CCCCCCCCCCCCCCC		50.5229255136
1600 (in isoform 1)Phosphorylation-50.52-
1602PhosphorylationVDDDMSGDEKQDNES
CCCCCCCCCCCCCCC		53.2518669648
1609PhosphorylationDEKQDNESNVDPRDD
CCCCCCCCCCCCCCC		48.7029255136
1609 (in isoform 1)Phosphorylation-48.70-
1620PhosphorylationPRDDVFGYPQQFEDK
CCCCCCCCCCCCCCC		6.0821406692
1620UbiquitinationPRDDVFGYPQQFEDK
CCCCCCCCCCCCCCC		6.0821139048
1627UbiquitinationYPQQFEDKPALSKTE
CCCCCCCCCCCCCCC		25.6221890473
1627 (in isoform 1)Ubiquitination-25.6221890473
1631PhosphorylationFEDKPALSKTEDRKE
CCCCCCCCCCCCHHH		39.3729759185
1632UbiquitinationEDKPALSKTEDRKEY
CCCCCCCCCCCHHHH		57.7021890473
1632 (in isoform 1)Ubiquitination-57.7021890473
1637UbiquitinationLSKTEDRKEYNIGVL
CCCCCCHHHHCHHHH		76.5021890473
1661PhosphorylationLAASRLQYYVPRGFW
HHHHHCHHHCCCCHH		15.8323917254
1669UbiquitinationYVPRGFWKQFRLWGE
HCCCCHHHHHHCCCC		36.9821890473
1712UbiquitinationGHPAMLSKVLGGSFA
CCHHHHHHHHCCCHH		37.2021890473
1712 (in isoform 1)Ubiquitination-37.2021890473
1722AcetylationGGSFADQKICQGCPH
CCCHHCCCCCCCCCC		46.10-
1722UbiquitinationGGSFADQKICQGCPH
CCCHHCCCCCCCCCC		46.1021890473
1722 (in isoform 1)Ubiquitination-46.1021890473
1736PhosphorylationHRYECEESFTTLNVD
CCCCCCCCEEEECCC		12.9528787133
1738PhosphorylationYECEESFTTLNVDIR
CCCCCCEEEECCCCC		39.3928787133
1767N-linked_GlycosylationGDLLEGANAYHCEKC
CCCCCCCCCCCCCCC		52.46-
1767N-linked_GlycosylationGDLLEGANAYHCEKC
CCCCCCCCCCCCCCC		52.4619349973
1767 (in isoform 1)N-linked_Glycosylation-52.46-
1780PhosphorylationKCNKKVDTVKRLLIK
CCCCCCHHHHHHHHH		30.8023403867
1798UbiquitinationPVLAIQLKRFDYDWE
CEEEEEEECCCCCCH		34.3421890473
1798 (in isoform 1)Ubiquitination-34.3421890473
1811UbiquitinationWERECAIKFNDYFEF
CHHHHEEEECCCCCC		21.4221890473
1811 (in isoform 1)Ubiquitination-21.4221890473
1815PhosphorylationCAIKFNDYFEFPREL
HEEEECCCCCCCCCC		13.2021082442
1844PhosphorylationGDNVNPESQLIQQSE
CCCCCHHHHHHHHCC		31.3829970186
1862UbiquitinationSETAGSTKYRLVGVL
CCCCCCCCEEEEEEE		30.0321890473
1862 (in isoform 1)Ubiquitination-30.0321890473
1872PhosphorylationLVGVLVHSGQASGGH
EEEEEEECCCCCCCE		25.7228152594
1876PhosphorylationLVHSGQASGGHYYSY
EEECCCCCCCEEEEE		37.1028152594
1880PhosphorylationGQASGGHYYSYIIQR
CCCCCCEEEEEEEEE		9.4428152594
1881PhosphorylationQASGGHYYSYIIQRN
CCCCCEEEEEEEEEC		6.8528152594
1882PhosphorylationASGGHYYSYIIQRNG
CCCCEEEEEEEEECC		11.5928152594
1883PhosphorylationSGGHYYSYIIQRNGG
CCCEEEEEEEEECCC		5.9728152594
1899UbiquitinationGERNRWYKFDDGDVT
CCCCCEEECCCCCCC		35.04-
1935UbiquitinationEVFDHMMKRMSYRRQ
HHHHHHHHHHHHHHH		37.06-
1935 (in isoform 1)Ubiquitination-37.0621890473
1949PhosphorylationQKRWWNAYILFYERM
HHHHHHHHHHHHHHH		8.5724043423
1953PhosphorylationWNAYILFYERMDTID
HHHHHHHHHHHCCCC		10.1224043423
1968PhosphorylationQDDELIRYISELAIT
CCHHHHHHHHHHHCC		11.2127642862
2219UbiquitinationEGPGPPIKYQYAELG
CCCCCCCEEEHHHHH		31.88-
2301UbiquitinationSNSEETVKLLRFCCW
CCCHHHHHHHHHHHC		49.5821890473
2301 (in isoform 1)Ubiquitination-49.5821890473
2360UbiquitinationHRIHNALKGIPDDRD
HHHHHHHCCCCCCCC		53.0021890473
2360 (in isoform 1)Ubiquitination-53.0021890473
2366MethylationLKGIPDDRDGLFDTI
HCCCCCCCCCHHHHH		47.48-
2396PhosphorylationKCMVALFSNCPVAYQ
HHHHHHHCCCCHHHH		38.0720068231
2402PhosphorylationFSNCPVAYQILQGNG
HCCCCHHHHHHCCCC		9.0520068231
2402 (in isoform 1)Phosphorylation-9.05-
2431PhosphorylationDELERRPYTGNPQYT
HHHHCCCCCCCCCCC		26.0128450419
2432PhosphorylationELERRPYTGNPQYTY
HHHCCCCCCCCCCCC		32.9228450419
2436PhosphorylationRPYTGNPQYTYNNWS
CCCCCCCCCCCCCCC		47.3918669648
2437PhosphorylationPYTGNPQYTYNNWSP
CCCCCCCCCCCCCCC		16.6730206219
2438PhosphorylationYTGNPQYTYNNWSPP
CCCCCCCCCCCCCCC		17.9628348404
2439PhosphorylationTGNPQYTYNNWSPPV
CCCCCCCCCCCCCCC		11.1019276368
2443PhosphorylationQYTYNNWSPPVQSNE
CCCCCCCCCCCCCCC		22.8125159151
2443 (in isoform 1)Phosphorylation-22.81-
2448PhosphorylationNWSPPVQSNETSNGY
CCCCCCCCCCCCCCC		36.5530175587
2448 (in isoform 1)Phosphorylation-36.55-
2451PhosphorylationPPVQSNETSNGYFLE
CCCCCCCCCCCCCCC		31.5723663014
2452PhosphorylationPVQSNETSNGYFLER
CCCCCCCCCCCCCCC		23.2923663014
2455PhosphorylationSNETSNGYFLERSHS
CCCCCCCCCCCCCHH		14.8328450419
2460PhosphorylationNGYFLERSHSARMTL
CCCCCCCCHHHHHHH		16.6526074081
2462PhosphorylationYFLERSHSARMTLAK
CCCCCCHHHHHHHHH		20.8626074081
2466PhosphorylationRSHSARMTLAKACEL
CCHHHHHHHHHHHHH		20.2924719451
2490 (in isoform 1)Phosphorylation-46.4525137130
2492PhosphorylationQQIEMEESKEPDDQD
CEECHHHCCCCCCCC		29.0721815630
2502 (in isoform 1)Phosphorylation-72.1625137130
2533PhosphorylationNNHVHGQPYTGPAAH
CCCCCCCCCCCCCHH		32.9915592455
2540PhosphorylationPYTGPAAHHMNNPQR
CCCCCCHHHCCCHHH		23.8818669648
2540 (in isoform 1)Phosphorylation-23.88-
2547PhosphorylationHHMNNPQRTGQRAQE
HHCCCHHHHCHHHHH		41.9219664994
2547 (in isoform 1)Phosphorylation-41.92-
2551PhosphorylationNPQRTGQRAQENYEG
CHHHHCHHHHHHCCC		39.3120068231
2551 (in isoform 1)Phosphorylation-39.31-
2556PhosphorylationGQRAQENYEGSEEVS
CHHHHHHCCCCCCCC		22.4021945579
2559PhosphorylationAQENYEGSEEVSPPQ
HHHHCCCCCCCCCCC		20.7421945579
2563PhosphorylationYEGSEEVSPPQTKDQ
CCCCCCCCCCCCCCC		33.8619664994
2567PhosphorylationEEVSPPQTKDQ----
CCCCCCCCCCC----		42.2221945579
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
2547SPhosphorylationKinaseCDK1P06493
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of USP9X_HUMAN !!
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_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CTNB1_HUMANCTNNB1physical
10620020
AFAD_HUMANMLLT4physical
9722616
NUAK1_HUMANNUAK1physical
18254724
MARK4_HUMANMARK4physical
18254724
CTNB1_HUMANCTNNB1physical
14742711
CADH1_HUMANCDH1physical
14742711
M3K5_HUMANMAP3K5physical
20005844
MCL1_HUMANMCL1physical
21907705
PSD4_HUMANPSD4physical
20339350
MCL1_HUMANMCL1physical
20023629
HUWE1_HUMANHUWE1physical
20023629
MCL1_HUMANMCL1physical
21566062
SYUA_HUMANSNCAphysical
22065755
DCX_HUMANDCXphysical
15607950
PEX5_HUMANPEX5physical
22371489
MTOR_HUMANMTORphysical
22544753
RPTOR_HUMANRPTORphysical
22544753
RICTR_HUMANRICTORphysical
22544753
MAGD1_HUMANMAGED1physical
22544753
PJA1_HUMANPJA1physical
22544753
MARH7_HUMANMARCH7physical
22544753
RUVB1_HUMANRUVBL1physical
22544753
ZYX_HUMANZYXphysical
22939629
VATF_HUMANATP6V1Fphysical
22939629
YAP1_HUMANYAP1physical
22939629
ANCHR_HUMANZFYVE19physical
22939629
MCL1_HUMANMCL1physical
23097624
SMUF1_HUMANSMURF1physical
23184937
UBC_HUMANUBCphysical
23287719
TCPD_HUMANCCT4physical
22863883
TCPA_HUMANTCP1physical
22863883
ERG_HUMANERGphysical
24591637
PRP8_HUMANPRPF8physical
26344197
OTUD4_HUMANOTUD4physical
25944111
AMOL2_HUMANAMOTL2physical
26598551
YAP1_HUMANYAP1physical
26598551
GEMI2_HUMANGEMIN2physical
23112048
DDX20_HUMANDDX20physical
23112048
GEMI4_HUMANGEMIN4physical
23112048
GEMI5_HUMANGEMIN5physical
23112048
GEMI8_HUMANGEMIN8physical
23112048
RSMB_HUMANSNRPBphysical
23112048
TDRD3_HUMANTDRD3physical
28101374
CTNB1_HUMANCTNNB1physical
27783990
AMOT_HUMANAMOTphysical
27462448
VHL_HUMANVHLphysical
27517496
SMAD4_HUMANSMAD4physical
28115363
ERG_HUMANERGphysical
27626314
LATS2_HUMANLATS2physical
28720576
SAV1_HUMANSAV1physical
28720576
KIBRA_HUMANWWC1physical
28720576
LATS1_HUMANLATS1physical
28720576
IQCB1_HUMANIQCB1physical
28498859
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
300919Mental retardation, X-linked 99 (MRX99)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of USP9X_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1600, AND MASSSPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2563, AND MASSSPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1600; SER-2443 ANDSER-2563, AND MASS SPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-590; SER-1600 ANDSER-2563, AND MASS SPECTROMETRY.
"Quantitative phosphoproteome profiling of Wnt3a-mediated signalingnetwork: indicating the involvement of ribonucleoside-diphosphatereductase M2 subunit phosphorylation at residue serine 20 in canonicalWnt signal transduction.";
Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S.,Li S.-J., Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.;
Mol. Cell. Proteomics 6:1952-1967(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2443, AND MASSSPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2563, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1600, AND MASSSPECTROMETRY.
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells.";
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.;
Nat. Biotechnol. 23:94-101(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-2556, AND MASSSPECTROMETRY.

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