TOX4_HUMAN - dbPTM
TOX4_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TOX4_HUMAN
UniProt AC O94842
Protein Name TOX high mobility group box family member 4
Gene Name TOX4
Organism Homo sapiens (Human).
Sequence Length 621
Subcellular Localization Nucleus . Associated with chromatin.
Protein Description Component of the PTW/PP1 phosphatase complex, which plays a role in the control of chromatin structure and cell cycle progression during the transition from mitosis into interphase..
Protein Sequence MEFPGGNDNYLTITGPSHPFLSGAETFHTPSLGDEEFEIPPISLDSDPSLAVSDVVGHFDDLADPSSSQDGSFSAQYGVQTLDMPVGMTHGLMEQGGGLLSGGLTMDLDHSIGTQYSANPPVTIDVPMTDMTSGLMGHSQLTTIDQSELSSQLGLSLGGGTILPPAQSPEDRLSTTPSPTSSLHEDGVEDFRRQLPSQKTVVVEAGKKQKAPKKRKKKDPNEPQKPVSAYALFFRDTQAAIKGQNPNATFGEVSKIVASMWDSLGEEQKQVYKRKTEAAKKEYLKALAAYKDNQECQATVETVELDPAPPSQTPSPPPMATVDPASPAPASIEPPALSPSIVVNSTLSSYVANQASSGAGGQPNITKLIITKQMLPSSITMSQGGMVTVIPATVVTSRGLQLGQTSTATIQPSQQAQIVTRSVLQAAAAAAAAASMQLPPPRLQPPPLQQMPQPPTQQQVTILQQPPPLQAMQQPPPQKVRINLQQQPPPLQIKSVPLPTLKMQTTLVPPTVESSPERPMNNSPEAHTVEAPSPETICEMITDVVPEVESPSQMDVELVSGSPVALSPQPRCVRSGCENPPIVSKDWDNEYCSNECVVKHCRDVFLAWVASRNSNTVVFVK
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
31PhosphorylationAETFHTPSLGDEEFE
CCEECCCCCCCCCCC		46.2522468782
67PhosphorylationDDLADPSSSQDGSFS
HHCCCCCCCCCCCCC		37.0920058876
111PhosphorylationLTMDLDHSIGTQYSA
EEEECCCCCCCCCCC		23.5226074081
114PhosphorylationDLDHSIGTQYSANPP
ECCCCCCCCCCCCCC		23.7526074081
116PhosphorylationDHSIGTQYSANPPVT
CCCCCCCCCCCCCEE		15.0226074081
155PhosphorylationELSSQLGLSLGGGTI
HHHHHHCCCCCCCCC		5.3432142685
174PhosphorylationQSPEDRLSTTPSPTS
CCHHHHHCCCCCCCC		31.0029255136
175PhosphorylationSPEDRLSTTPSPTSS
CHHHHHCCCCCCCCC		47.5229255136
176PhosphorylationPEDRLSTTPSPTSSL
HHHHHCCCCCCCCCC		20.5629255136
176UbiquitinationPEDRLSTTPSPTSSL
HHHHHCCCCCCCCCC		20.5633845483
178PhosphorylationDRLSTTPSPTSSLHE
HHHCCCCCCCCCCCC		38.4229255136
180PhosphorylationLSTTPSPTSSLHEDG
HCCCCCCCCCCCCCC		34.9729255136
181PhosphorylationSTTPSPTSSLHEDGV
CCCCCCCCCCCCCCH		34.0029255136
182PhosphorylationTTPSPTSSLHEDGVE
CCCCCCCCCCCCCHH		35.9029255136
184AcetylationPSPTSSLHEDGVEDF
CCCCCCCCCCCHHHH		32.80-
185UbiquitinationSPTSSLHEDGVEDFR
CCCCCCCCCCHHHHH		62.85-
199UbiquitinationRRQLPSQKTVVVEAG
HHHCCCCCEEEECCC		47.8533845483
199AcetylationRRQLPSQKTVVVEAG
HHHCCCCCEEEECCC		47.8525953088
200PhosphorylationRQLPSQKTVVVEAGK
HHCCCCCEEEECCCC		15.7624505115
207AcetylationTVVVEAGKKQKAPKK
EEEECCCCCCCCCCC		60.1123954790
2072-HydroxyisobutyrylationTVVVEAGKKQKAPKK
EEEECCCCCCCCCCC		60.11-
208AcetylationVVVEAGKKQKAPKKR
EEECCCCCCCCCCCC		56.9926051181
219UbiquitinationPKKRKKKDPNEPQKP
CCCCCCCCCCCCCCC		61.20-
228PhosphorylationNEPQKPVSAYALFFR
CCCCCCCEEEEEEEH		24.8828555341
232UbiquitinationKPVSAYALFFRDTQA
CCCEEEEEEEHHHHH		2.4432015554
242UbiquitinationRDTQAAIKGQNPNAT
HHHHHHHCCCCCCCC		50.1229967540
255UbiquitinationATFGEVSKIVASMWD
CCHHHHHHHHHHHHH		46.5032015554
283PhosphorylationTEAAKKEYLKALAAY
HHHHHHHHHHHHHHH		23.5320736484
290PhosphorylationYLKALAAYKDNQECQ
HHHHHHHHCCCHHCE		17.1722817900
311PhosphorylationELDPAPPSQTPSPPP
ECCCCCCCCCCCCCC		45.7020068231
313PhosphorylationDPAPPSQTPSPPPMA
CCCCCCCCCCCCCCC		30.0320068231
315PhosphorylationAPPSQTPSPPPMATV
CCCCCCCCCCCCCCC		54.1220068231
321PhosphorylationPSPPPMATVDPASPA
CCCCCCCCCCCCCCC		21.1320068231
377PhosphorylationITKQMLPSSITMSQG
EEECCCCCCEEECCC		30.3421955146
378PhosphorylationTKQMLPSSITMSQGG
EECCCCCCEEECCCC		21.8221955146
380PhosphorylationQMLPSSITMSQGGMV
CCCCCCEEECCCCEE		16.8421955146
380O-linked_GlycosylationQMLPSSITMSQGGMV
CCCCCCEEECCCCEE		16.8430059200
382O-linked_GlycosylationLPSSITMSQGGMVTV
CCCCEEECCCCEEEE		19.6130059200
382PhosphorylationLPSSITMSQGGMVTV
CCCCEEECCCCEEEE		19.6120068231
388PhosphorylationMSQGGMVTVIPATVV
ECCCCEEEEEECEEE		12.1121955146
393PhosphorylationMVTVIPATVVTSRGL
EEEEEECEEEECCCE		15.3420068231
396PhosphorylationVIPATVVTSRGLQLG
EEECEEEECCCEECC		14.3621955146
397O-linked_GlycosylationIPATVVTSRGLQLGQ
EECEEEECCCEECCC		16.8530059200
397PhosphorylationIPATVVTSRGLQLGQ
EECEEEECCCEECCC		16.8520068231
405O-linked_GlycosylationRGLQLGQTSTATIQP
CCEECCCCCCCCCCH		26.6730059200
406O-linked_GlycosylationGLQLGQTSTATIQPS
CEECCCCCCCCCCHH		14.2530059200
407O-linked_GlycosylationLQLGQTSTATIQPSQ
EECCCCCCCCCCHHH		31.0730059200
409O-linked_GlycosylationLGQTSTATIQPSQQA
CCCCCCCCCCHHHHH		21.8930059200
413O-linked_GlycosylationSTATIQPSQQAQIVT
CCCCCCHHHHHHHHH		20.6730059200
420O-linked_GlycosylationSQQAQIVTRSVLQAA
HHHHHHHHHHHHHHH		20.8930059200
481MethylationQPPPQKVRINLQQQP
CCCCCEEEEECCCCC		21.0724129315
481Asymmetric dimethylarginineQPPPQKVRINLQQQP
CCCCCEEEEECCCCC		21.07-
494AcetylationQPPPLQIKSVPLPTL
CCCCCEEEEECCCCC		32.2325953088
511PhosphorylationQTTLVPPTVESSPER
EEEECCCCCCCCCCC		30.7329255136
514PhosphorylationLVPPTVESSPERPMN
ECCCCCCCCCCCCCC		47.0226074081
515PhosphorylationVPPTVESSPERPMNN
CCCCCCCCCCCCCCC		19.7826074081
523PhosphorylationPERPMNNSPEAHTVE
CCCCCCCCCCCCCCC		21.0722468782
533PhosphorylationAHTVEAPSPETICEM
CCCCCCCCHHHHHHH		42.2826074081
536PhosphorylationVEAPSPETICEMITD
CCCCCHHHHHHHHHH		34.0226074081
550PhosphorylationDVVPEVESPSQMDVE
HHCCCCCCCCCCCEE		34.7226074081
552PhosphorylationVPEVESPSQMDVELV
CCCCCCCCCCCEEEE		47.6326074081
560PhosphorylationQMDVELVSGSPVALS
CCCEEEECCCCCEEC		46.2926074081
562PhosphorylationDVELVSGSPVALSPQ
CEEEECCCCCEECCC		14.5426074081
567PhosphorylationSGSPVALSPQPRCVR
CCCCCEECCCCCCCC		16.2614702039
575PhosphorylationPQPRCVRSGCENPPI
CCCCCCCCCCCCCCC		27.6526074081
584PhosphorylationCENPPIVSKDWDNEY
CCCCCCCCCCCCCCC		26.1426074081
585AcetylationENPPIVSKDWDNEYC
CCCCCCCCCCCCCCC		52.5226051181
599AcetylationCSNECVVKHCRDVFL
CCCHHHHHHHHHHHH		19.3126051181
611PhosphorylationVFLAWVASRNSNTVV
HHHHHHHCCCCCEEE		23.5224719451
614PhosphorylationAWVASRNSNTVVFVK
HHHHCCCCCEEEEEC		32.5428555341
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 TOX4_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TOX4_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 TOX4_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
WDR82_HUMANWDR82physical
20516061
PP1A_HUMANPPP1CAphysical
20516061
PP1B_HUMANPPP1CBphysical
20516061
PP1G_HUMANPPP1CCphysical
20516061
TOX4_HUMANTOX4physical
20516061
PP1RA_HUMANPPP1R10physical
20516061
HSP74_HUMANHSPA4physical
20516061
VIME_HUMANVIMphysical
20516061
BANP_HUMANBANPphysical
25416956
MLRA_HUMANMYL7physical
25416956
FND3B_HUMANFNDC3Bphysical
25416956
GEMI6_HUMANGEMIN6physical
25416956
ZMY19_HUMANZMYND19physical
25416956
PP1RA_HUMANPPP1R10physical
28514442
KLK7_HUMANKLK7physical
28514442
SPA12_HUMANSERPINA12physical
28514442
CYTM_HUMANCST6physical
28514442
KPRP_HUMANKPRPphysical
28514442
LX12B_HUMANALOX12Bphysical
28514442
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TOX4_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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 THR-176; SER-178 ANDTHR-180, AND MASS SPECTROMETRY.
"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-178; THR-180; SER-181AND SER-182, AND MASS SPECTROMETRY.

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