dbPTM

TPPP_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	TPPP_MOUSE
UniProt AC	Q7TQD2
Protein Name	Tubulin polymerization-promoting protein
Gene Name	Tppp
Organism	Mus musculus (Mouse).
Sequence Length	218
Subcellular Localization	Cytoplasm . Cytoplasm, cytoskeleton . Nucleus .
Protein Description	May play a role in the polymerization of tubulin into microtubules, microtubule bundling and the stabilization of existing microtubules, thus maintaining the integrity of the microtubule network. May play a role in mitotic spindle assembly and nuclear envelope breakdown..
Protein Sequence	MADSKAKPAKAANKTPPKSPGDPARAAKRLSLESEGANEGATAAPELSALEEAFRRFAVHGDTRATGKEMHGKNWSKLCKDCHVIDGKNVTVTDVDIVFSKIKGKSCRTITFEQFQEALEELAKKRFKDKSSEEAVREVHRLIEGRAPVISGVTKAVSSPTVSRLTDTSKFTGSHKERFDQSGKGKGKAGRVDLVDESGYVPGYKHAGTYDQKVQGGK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
15	Phosphorylation	PAKAANKTPPKSPGD CCCCCCCCCCCCCCC	44.63	25521595
19	Phosphorylation	ANKTPPKSPGDPARA CCCCCCCCCCCHHHH	39.63	25521595
31	Phosphorylation	ARAAKRLSLESEGAN HHHHHHHCCCCCCCC	33.84	25521595
34	Phosphorylation	AKRLSLESEGANEGA HHHHCCCCCCCCCCC	46.77	25521595
42	Phosphorylation	EGANEGATAAPELSA CCCCCCCCCCHHHHH	33.92	25521595
91	Phosphorylation	VIDGKNVTVTDVDIV EECCCCEEEEEEEEE	27.38	-
106	Phosphorylation	FSKIKGKSCRTITFE EEEECCCCCCEEEHH	19.94	-
124	Ubiquitination	EALEELAKKRFKDKS HHHHHHHHHHHCCCC	58.04	-
131	Phosphorylation	KKRFKDKSSEEAVRE HHHHCCCCHHHHHHH	53.79	29899451
132	Phosphorylation	KRFKDKSSEEAVREV HHHCCCCHHHHHHHH	45.24	29899451
151	O-linked_Glycosylation	EGRAPVISGVTKAVS CCCCCCCCCCCCCCC	27.69	26192747
151	Phosphorylation	EGRAPVISGVTKAVS CCCCCCCCCCCCCCC	27.69	25521595
154	O-linked_Glycosylation	APVISGVTKAVSSPT CCCCCCCCCCCCCCC	19.46	29977005
154	Phosphorylation	APVISGVTKAVSSPT CCCCCCCCCCCCCCC	19.46	-
155	Malonylation	PVISGVTKAVSSPTV CCCCCCCCCCCCCCC	44.37	26320211
155	Ubiquitination	PVISGVTKAVSSPTV CCCCCCCCCCCCCCC	44.37	-
158	Phosphorylation	SGVTKAVSSPTVSRL CCCCCCCCCCCCHHC	35.14	25521595
159	Phosphorylation	GVTKAVSSPTVSRLT CCCCCCCCCCCHHCC	20.28	25521595
161	Phosphorylation	TKAVSSPTVSRLTDT CCCCCCCCCHHCCCC	32.82	23335269
163	Phosphorylation	AVSSPTVSRLTDTSK CCCCCCCHHCCCCCC	24.85	28066266
182	Phosphorylation	HKERFDQSGKGKGKA CHHHCCCCCCCCCCC	44.29	22324799
184	Acetylation	ERFDQSGKGKGKAGR HHCCCCCCCCCCCCC	63.80	19860145

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 TPPP_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
31	S	Acetylation	16452087
Phosphorylation by ROCK1 at Ser-31, Ser-106 and Ser-158 inhibits interaction with HDAC6, resulting in decreased acetylation of tubulin, increased cell motility and entry into S-phase.
31	S	Phosphorylation	16452087
Phosphorylation by ROCK1 at Ser-31, Ser-106 and Ser-158 inhibits interaction with HDAC6, resulting in decreased acetylation of tubulin, increased cell motility and entry into S-phase.
106	S	Acetylation	-
Phosphorylation by ROCK1 at Ser-31, Ser-106 and Ser-158 inhibits interaction with HDAC6, resulting in decreased acetylation of tubulin, increased cell motility and entry into S-phase.
106	S	Phosphorylation	-
Phosphorylation by ROCK1 at Ser-31, Ser-106 and Ser-158 inhibits interaction with HDAC6, resulting in decreased acetylation of tubulin, increased cell motility and entry into S-phase.
158	S	Acetylation	-
Phosphorylation by ROCK1 at Ser-31, Ser-106 and Ser-158 inhibits interaction with HDAC6, resulting in decreased acetylation of tubulin, increased cell motility and entry into S-phase.
158	S	Phosphorylation	-
Phosphorylation by ROCK1 at Ser-31, Ser-106 and Ser-158 inhibits interaction with HDAC6, resulting in decreased acetylation of tubulin, increased cell motility and entry into S-phase.

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 TPPP_MOUSE !!

Protein-Protein Interaction

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

Drug and Disease Associations

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

Regulatory Network of TPPP_MOUSE

Related Literatures of Post-Translational Modification

O-linked Glycosylation
Reference	PubMed
"O-linked N-acetylglucosamine proteomics of postsynaptic densitypreparations using lectin weak affinity chromatography and massspectrometry."; Vosseller K., Trinidad J.C., Chalkley R.J., Specht C.G.,Thalhammer A., Lynn A.J., Snedecor J.O., Guan S., Medzihradszky K.F.,Maltby D.A., Schoepfer R., Burlingame A.L.; Mol. Cell. Proteomics 5:923-934(2006). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT SER-151, AND MASSSPECTROMETRY.	16452088 [Abstract]
Phosphorylation
Reference	PubMed
"Comprehensive identification of phosphorylation sites in postsynapticdensity preparations."; Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,Burlingame A.L.; Mol. Cell. Proteomics 5:914-922(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-15 AND SER-31, AND MASSSPECTROMETRY.	16452087 [Abstract]