TCP4_MOUSE - dbPTM
TCP4_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TCP4_MOUSE
UniProt AC P11031
Protein Name Activated RNA polymerase II transcriptional coactivator p15
Gene Name Sub1
Organism Mus musculus (Mouse).
Sequence Length 127
Subcellular Localization Nucleus.
Protein Description General coactivator that functions cooperatively with TAFs and mediates functional interactions between upstream activators and the general transcriptional machinery. May be involved in stabilizing the multiprotein transcription complex. Binds single-stranded DNA. Also binds, in vitro, non-specifically to double-stranded DNA (ds DNA)..
Protein Sequence MPKSKELVSSSSSGSDSDSEVEKKLKRKKQAVPEKPVKKQKPGETSRALASSKQSSSSRDDNMFQIGKMRYVSVRDFKGKILIDIREYWMDSEGEMKPGRKGISLNMEQWSQLKEQISDIDDAVRKL
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
3Acetylation-----MPKSKELVSS
-----CCCCHHHHCC
73.2422826441
4Phosphorylation----MPKSKELVSSS
----CCCCHHHHCCC
26.03-
5Acetylation---MPKSKELVSSSS
---CCCCHHHHCCCC
62.2822826441
9PhosphorylationPKSKELVSSSSSGSD
CCCHHHHCCCCCCCC
36.8125619855
10PhosphorylationKSKELVSSSSSGSDS
CCHHHHCCCCCCCCC
27.1025619855
11PhosphorylationSKELVSSSSSGSDSD
CHHHHCCCCCCCCCH
22.4825619855
12PhosphorylationKELVSSSSSGSDSDS
HHHHCCCCCCCCCHH
40.4425293948
13PhosphorylationELVSSSSSGSDSDSE
HHHCCCCCCCCCHHH
44.2423984901
15PhosphorylationVSSSSSGSDSDSEVE
HCCCCCCCCCHHHHH
35.5726824392
17PhosphorylationSSSSGSDSDSEVEKK
CCCCCCCCHHHHHHH
44.7425521595
19PhosphorylationSSGSDSDSEVEKKLK
CCCCCCHHHHHHHHH
47.7122942356
35AcetylationKKQAVPEKPVKKQKP
HHCCCCCCCCCCCCC
49.3823201123
45PhosphorylationKKQKPGETSRALASS
CCCCCCHHHHHHHHH
29.4525338131
51PhosphorylationETSRALASSKQSSSS
HHHHHHHHHCCCCCC
38.6326643407
52PhosphorylationTSRALASSKQSSSSR
HHHHHHHHCCCCCCC
29.1626643407
53SuccinylationSRALASSKQSSSSRD
HHHHHHHCCCCCCCC
52.2623806337
53UbiquitinationSRALASSKQSSSSRD
HHHHHHHCCCCCCCC
52.26-
53AcetylationSRALASSKQSSSSRD
HHHHHHHCCCCCCCC
52.2623806337
55PhosphorylationALASSKQSSSSRDDN
HHHHHCCCCCCCCCC
35.6025521595
56PhosphorylationLASSKQSSSSRDDNM
HHHHCCCCCCCCCCC
29.8225521595
57PhosphorylationASSKQSSSSRDDNMF
HHHCCCCCCCCCCCE
34.3425521595
58PhosphorylationSSKQSSSSRDDNMFQ
HHCCCCCCCCCCCEE
41.5024453211
68UbiquitinationDNMFQIGKMRYVSVR
CCCEEECCEEEEEEE
23.1022790023
68AcetylationDNMFQIGKMRYVSVR
CCCEEECCEEEEEEE
23.1023236377
71PhosphorylationFQIGKMRYVSVRDFK
EEECCEEEEEEECCC
8.1229514104
80MalonylationSVRDFKGKILIDIRE
EEECCCCCEEEEEHH
34.6226320211
92PhosphorylationIREYWMDSEGEMKPG
EHHHEECCCCCCCCC
31.2525266776
104PhosphorylationKPGRKGISLNMEQWS
CCCCCCCCCCHHHHH
23.5126643407
118PhosphorylationSQLKEQISDIDDAVR
HHHHHHHHCHHHHHH
28.3625521595

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 TCP4_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TCP4_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 TCP4_MOUSE !!

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

Oops, there are no PPI records of TCP4_MOUSE !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TCP4_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A differential phosphoproteomic analysis of retinoic acid-treated P19cells.";
Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.;
J. Proteome Res. 6:3174-3186(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9; SER-10; SER-11;SER-12; SER-13; SER-15; SER-17 AND SER-19, AND MASS SPECTROMETRY.

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