TOX4_MOUSE - dbPTM
TOX4_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TOX4_MOUSE
UniProt AC Q8BU11
Protein Name TOX high mobility group box family member 4
Gene Name Tox4
Organism Mus musculus (Mouse).
Sequence Length 619
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 MEFPGGNDNYLTITGPSHPFLSGAETFHTPSLGDEEFEIPPISLDSDPSLAVSDVVGHFDDLADPSSSQDGSFSAQYGVQTLDMPVGMTHGLMEQGGGLLSGGLTMDLDHSIGTQYSANPPVTIDVPMTDMTSGLMGHSQLTTIDQSELSSQLGLSLGGGTILPPAQSPEDRLSTTPSPTNSLHEDGVDDFRRQLPAQKTVVVETGKKQKAPKKRKKKDPNEPQKPVSAYALFFRDTQAAIKGQNPNATFGEVSKIVASMWDSLGEEQKQVYKRKTEAAKKEYLKALAAYKDNQECQATVETVELDPVPQSQTPSPPPVTAADPASPAPASTESPALPPCIIVNSTLSSYVANQASSGPGGQPNITKLIITKQMLPSSITMSQGGMVTVIPATVVTSRGLQVGQTSTATIQPSQQAQIVTRSVLQAAAAAAASMQLPPPRLQPPPLQQMPQPPTQQQVTILQQPPPLQAMQQPPPQKVRINLQQQPPPLQSKIVPPPTLKIQTTVVPPTVESSPEQPMNSSPEAHTVEATSPETICEMIADVVPEVESPSQMDVELVSGSPVALSPQPRCVRSGCENPPVVSKDWDNEYCSNECVVKHCRDVFLAWVASRNPNSVVFVK
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
174PhosphorylationQSPEDRLSTTPSPTN
CCHHHHCCCCCCCCC
31.0021082442
175PhosphorylationSPEDRLSTTPSPTNS
CHHHHCCCCCCCCCC
47.5226824392
176PhosphorylationPEDRLSTTPSPTNSL
HHHHCCCCCCCCCCC
20.5626824392
178PhosphorylationDRLSTTPSPTNSLHE
HHCCCCCCCCCCCCC
42.1127087446
180PhosphorylationLSTTPSPTNSLHEDG
CCCCCCCCCCCCCCC
41.6022942356
182PhosphorylationTTPSPTNSLHEDGVD
CCCCCCCCCCCCCHH
33.3127087446
207AcetylationTVVVETGKKQKAPKK
EEEEECCCCCCCCCC
60.497611849
218AcetylationAPKKRKKKDPNEPQK
CCCCCCCCCCCCCCC
79.888277309
249PhosphorylationKGQNPNATFGEVSKI
CCCCCCCCHHHHHHH
38.52-
254PhosphorylationNATFGEVSKIVASMW
CCCHHHHHHHHHHHH
16.62-
313PhosphorylationDPVPQSQTPSPPPVT
CCCCCCCCCCCCCCC
30.86-
315PhosphorylationVPQSQTPSPPPVTAA
CCCCCCCCCCCCCCC
54.12-
479Asymmetric dimethylarginineQPPPQKVRINLQQQP
CCCCCCEEEECCCCC
21.07-
479MethylationQPPPQKVRINLQQQP
CCCCCCEEEECCCCC
21.0724129315
531PhosphorylationAHTVEATSPETICEM
CEEEECCCHHHHHHH
27.99-
548PhosphorylationDVVPEVESPSQMDVE
HHCCCCCCCCCCCEE
34.72-
550PhosphorylationVPEVESPSQMDVELV
CCCCCCCCCCCEEEE
47.63-
558PhosphorylationQMDVELVSGSPVALS
CCCEEEECCCCCEEC
46.29-
560PhosphorylationDVELVSGSPVALSPQ
CEEEECCCCCEECCC
14.54-
565PhosphorylationSGSPVALSPQPRCVR
CCCCCEECCCCCCCC
16.26-

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_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TOX4_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 TOX4_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
KAD2_HUMANAK2physical
26496610
PP1A_HUMANPPP1CAphysical
26496610
PP1B_HUMANPPP1CBphysical
26496610
PP1G_HUMANPPP1CCphysical
26496610
PP1RA_HUMANPPP1R10physical
26496610
TAP2_HUMANTAP2physical
26496610
MED14_HUMANMED14physical
26496610
PALLD_HUMANPALLDphysical
26496610
PAF1_HUMANPAF1physical
26496610
CDC73_HUMANCDC73physical
26496610
WDR82_HUMANWDR82physical
26496610

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TOX4_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-182, AND MASSSPECTROMETRY.

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