TPD54_MOUSE - dbPTM
TPD54_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TPD54_MOUSE
UniProt AC Q9CYZ2
Protein Name Tumor protein D54
Gene Name Tpd52l2
Organism Mus musculus (Mouse).
Sequence Length 220
Subcellular Localization
Protein Description
Protein Sequence MDSASQDINLNSPNKGVLSDFMTDVPVDPGVVHRTPVVEGLTEGEEEELRAELAKVEEEIVTLRQVLAAKERHCGELKRRLGLSTLGELKQNLSRSWHDVQVSTAYVKTSEKLGEWNEKVTQSDLYKKTQETLSQAGQKTSAALSTMGSAISRKLGDMSSYSIRHSISMPVMRNSATFKSFEDRVGTIKSKVVGGRENGSDNLPPSPGSGDQTLPDHAPF
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
1Acetylation-------MDSASQDI
-------CCCCCCCC
9.19-
3Phosphorylation-----MDSASQDINL
-----CCCCCCCCCC
28.6425619855
5Phosphorylation---MDSASQDINLNS
---CCCCCCCCCCCC
32.1326824392
12PhosphorylationSQDINLNSPNKGVLS
CCCCCCCCCCCCCCH
32.7726824392
19PhosphorylationSPNKGVLSDFMTDVP
CCCCCCCHHHHCCCC
26.7925619855
23PhosphorylationGVLSDFMTDVPVDPG
CCCHHHHCCCCCCCC
33.5625619855
35PhosphorylationDPGVVHRTPVVEGLT
CCCCCCCCCCCCCCC
12.9328066266
55UbiquitinationELRAELAKVEEEIVT
HHHHHHHHHHHHHHH
63.90-
85PhosphorylationKRRLGLSTLGELKQN
HHHHCCCHHHHHHHH
43.7727180971
90UbiquitinationLSTLGELKQNLSRSW
CCHHHHHHHHHCCCC
32.60-
94PhosphorylationGELKQNLSRSWHDVQ
HHHHHHHCCCCCCEE
31.6426745281
96PhosphorylationLKQNLSRSWHDVQVS
HHHHHCCCCCCEEEE
25.9523684622
103PhosphorylationSWHDVQVSTAYVKTS
CCCCEEEEEEEEEHH
7.1026745281
104PhosphorylationWHDVQVSTAYVKTSE
CCCEEEEEEEEEHHH
24.1325367039
106PhosphorylationDVQVSTAYVKTSEKL
CEEEEEEEEEHHHHH
11.5425777480
108UbiquitinationQVSTAYVKTSEKLGE
EEEEEEEEHHHHHHH
33.39-
112UbiquitinationAYVKTSEKLGEWNEK
EEEEHHHHHHHHCHH
62.65-
121O-linked_GlycosylationGEWNEKVTQSDLYKK
HHHCHHCCHHHHHHH
33.1655414323
126PhosphorylationKVTQSDLYKKTQETL
HCCHHHHHHHHHHHH
18.5429514104
134PhosphorylationKKTQETLSQAGQKTS
HHHHHHHHHHHHHHH
25.9618779572
145PhosphorylationQKTSAALSTMGSAIS
HHHHHHHHHHHHHHH
16.1829514104
146PhosphorylationKTSAALSTMGSAISR
HHHHHHHHHHHHHHH
26.8022807455
149PhosphorylationAALSTMGSAISRKLG
HHHHHHHHHHHHHHC
16.1729176673
152PhosphorylationSTMGSAISRKLGDMS
HHHHHHHHHHHCCCC
24.0723140645
159PhosphorylationSRKLGDMSSYSIRHS
HHHHCCCCHHCHHHC
30.7529176673
160PhosphorylationRKLGDMSSYSIRHSI
HHHCCCCHHCHHHCC
19.0929176673
162PhosphorylationLGDMSSYSIRHSISM
HCCCCHHCHHHCCCC
18.3329176673
166PhosphorylationSSYSIRHSISMPVMR
CHHCHHHCCCCCEEC
13.4022324799
168PhosphorylationYSIRHSISMPVMRNS
HCHHHCCCCCEECCC
21.7625521595
175PhosphorylationSMPVMRNSATFKSFE
CCCEECCCCCCCCHH
20.5125619855
177PhosphorylationPVMRNSATFKSFEDR
CEECCCCCCCCHHHH
31.2727742792
180PhosphorylationRNSATFKSFEDRVGT
CCCCCCCCHHHHHCC
29.6726824392
187PhosphorylationSFEDRVGTIKSKVVG
CHHHHHCCCEEEECC
23.5226824392
200PhosphorylationVGGRENGSDNLPPSP
CCCCCCCCCCCCCCC
34.6026824392
206PhosphorylationGSDNLPPSPGSGDQT
CCCCCCCCCCCCCCC
39.7025521595
209PhosphorylationNLPPSPGSGDQTLPD
CCCCCCCCCCCCCCC
42.4527087446
213PhosphorylationSPGSGDQTLPDHAPF
CCCCCCCCCCCCCCC
45.0225521595

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 TPD54_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TPD54_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 TPD54_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of TPD54_MOUSE !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TPD54_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large scale localization of protein phosphorylation by use ofelectron capture dissociation mass spectrometry.";
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
Mol. Cell. Proteomics 8:904-912(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-180 AND SER-206, ANDMASS SPECTROMETRY.
"Specific phosphopeptide enrichment with immobilized titanium ionaffinity chromatography adsorbent for phosphoproteome analysis.";
Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
J. Proteome Res. 7:3957-3967(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-180, AND MASSSPECTROMETRY.
"Phosphoproteomic analysis of the developing mouse brain.";
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
Mol. Cell. Proteomics 3:1093-1101(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-206, AND MASSSPECTROMETRY.

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