dbPTM

TRIP4_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	TRIP4_MOUSE
UniProt AC	Q9QXN3
Protein Name	Activating signal cointegrator 1 {ECO:0000303\|PubMed:12077347}
Gene Name	Trip4 {ECO:0000312\|MGI:MGI:1928469}
Organism	Mus musculus (Mouse).
Sequence Length	581
Subcellular Localization	Nucleus . Cytoplasm, cytosol . Cytoplasm, cytoskeleton, microtubule organizing center, centrosome . Cytoplasmic under conditions of serum deprivation. Colocalizes with NEK6 in the centrosome.
Protein Description	Transcription coactivator which associates with nuclear receptors, transcriptional coactivators including EP300, CREBBP and NCOA1, and basal transcription factors like TBP and TFIIA to facilitate nuclear receptors-mediated transcription. May thereby play an important role in establishing distinct coactivator complexes under different cellular conditions. Plays a role in thyroid hormone receptor and estrogen receptor transactivation (By similarity). Also involved in androgen receptor transactivation. [PubMed: 12077347 Plays a pivotal role in the transactivation of NF-kappa-B, SRF and AP1. Acts as a mediator of transrepression between nuclear receptor and either AP1 or NF-kappa-B. May play a role in the development of neuromuscular junction (By similarity May play a role in late myogenic differentiation]
Protein Sequence	MAVAGAAYREPLVHWCTQQLQKTFALDVSEEIIQYVLSIENAEEIREYVTDLLQGNEGKKGQFIEDLITKWQKNDQEFISDSFQQCLRKDEILDGQRSVDQLKRSRRKGRNKQEVPAFPEPDVAVEVKTPLDLAKAQESNNSVKKKTRFVNLYTREGQDKLAVLLPGRHPCDCLGQKHKLINNCLVCGRIVCEQEGSGPCLFCGSLVCTNEEQDILQRDSNKSQKLLKKLMSGAETSGKVDVSTKDLLPHQESRMKSGLEKAIKHKEKLLEFDRTSIRRTQVIDDESDYFASDSNQWLSKVEREMLQKREEELRELRHASRLSKKVTIDFAGRKILEDENPLAEYHSRLDETIQAIASGTLNQSLVTLDRSCEEPLGVLVNPNMYQASPQWVDNTGSTPQKKTSLSAGPRLEPSLHQHQLRIQDQEFQEGFDGGWCLSMHQPWASLLVRGIKRVEGRSWYTPHRGRLWIAATGKRPSPQEVSELQATYRLLRGKDVEFPNDYPSGCLLGCVDLIDCLSQKQFQEQFPDISQESDSSFVFICKNPQEMVVKFPIKGNPKIWKLDSKIHQGAKKGLMKQNKAV

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAVAGAAYR ------CCCCCCCCC	10.40	-
8	Phosphorylation	MAVAGAAYREPLVHW CCCCCCCCCCHHHHH	18.25	29514104
98	Phosphorylation	EILDGQRSVDQLKRS HHHCCCCCHHHHHHH	23.35	25338131
105	Phosphorylation	SVDQLKRSRRKGRNK CHHHHHHHHHCCCCC	34.55	29514104
129	Phosphorylation	DVAVEVKTPLDLAKA CEEEEECCHHHHHHH	33.97	20047950
139	Phosphorylation	DLAKAQESNNSVKKK HHHHHHHCCCCHHHH	29.27	30635358
142	Phosphorylation	KAQESNNSVKKKTRF HHHHCCCCHHHHHHE	39.29	30635358
160	Ubiquitination	YTREGQDKLAVLLPG EECCCCCEEEEECCC	30.38	27667366
275	Phosphorylation	KLLEFDRTSIRRTQV HHHHCCCHHCCEEEE	30.28	28285833
276	Phosphorylation	LLEFDRTSIRRTQVI HHHCCCHHCCEEEEE	18.26	29514104
289	Phosphorylation	VIDDESDYFASDSNQ EECCCCCCCCCCHHH	15.43	16141072
323	Phosphorylation	LRHASRLSKKVTIDF HHHHHHHCCCEEEEC	29.35	24719451
327	Phosphorylation	SRLSKKVTIDFAGRK HHHCCCEEEECCCCC	24.57	24719451
397	Phosphorylation	QWVDNTGSTPQKKTS HHHCCCCCCCCCCCC	34.57	-
398	Phosphorylation	WVDNTGSTPQKKTSL HHCCCCCCCCCCCCC	30.96	-
403	Phosphorylation	GSTPQKKTSLSAGPR CCCCCCCCCCCCCCC	41.77	25266776
404	Phosphorylation	STPQKKTSLSAGPRL CCCCCCCCCCCCCCC	29.25	25266776
406	Phosphorylation	PQKKTSLSAGPRLEP CCCCCCCCCCCCCCC	30.83	28066266
554	Ubiquitination	MVVKFPIKGNPKIWK EEEEEECCCCCCEEE	53.53	27667366
565	Acetylation	KIWKLDSKIHQGAKK CEEECCHHHHHHHHH	43.82	7616915

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 TRIP4_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of TRIP4_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 TRIP4_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of TRIP4_MOUSE !!

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of TRIP4_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Quantitative time-resolved phosphoproteomic analysis of mast cellsignaling."; Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,Kawakami T., Salomon A.R.; J. Immunol. 179:5864-5876(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-289, AND MASSSPECTROMETRY.	17947660 [Abstract]