dbPTM

TPPP_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	TPPP_HUMAN
UniProt AC	O94811
Protein Name	Tubulin polymerization-promoting protein
Gene Name	TPPP
Organism	Homo sapiens (Human).
Sequence Length	219
Subcellular Localization	Cytoplasm. Cytoplasm, cytoskeleton. Nucleus. Localizes to glial Lewy bodies in the brains of individuals with synucleinopathies.
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	MADKAKPAKAANRTPPKSPGDPSKDRAAKRLSLESEGAGEGAAASPELSALEEAFRRFAVHGDARATGREMHGKNWSKLCKDCQVIDGRNVTVTDVDIVFSKIKGKSCRTITFEQFQEALEELAKKRFKDKSSEEAVREVHRLIEGKAPIISGVTKAISSPTVSRLTDTTKFTGSHKERFDPSGKGKGKAGRVDLVDESGYVSGYKHAGTYDQKVQGGK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
14	Phosphorylation	PAKAANRTPPKSPGD CCCCCCCCCCCCCCC	43.69	25463755
18	Phosphorylation	ANRTPPKSPGDPSKD CCCCCCCCCCCCCHH	39.63	25463755
23	Phosphorylation	PKSPGDPSKDRAAKR CCCCCCCCHHHHHHH	52.51	20363803
24	Acetylation	KSPGDPSKDRAAKRL CCCCCCCHHHHHHHH	57.53	7962571
32	Phosphorylation	DRAAKRLSLESEGAG HHHHHHHCCCCCCCC	33.84	25159151
35	Phosphorylation	AKRLSLESEGAGEGA HHHHCCCCCCCCCCC	46.77	22617229
45	Phosphorylation	AGEGAAASPELSALE CCCCCCCCHHHHHHH	17.74	25159151
49	Phosphorylation	AAASPELSALEEAFR CCCCHHHHHHHHHHH	29.19	29691806
78	Methylation	MHGKNWSKLCKDCQV HCCCCHHHHCCCCEE	49.90	-
78	"N6,N6-dimethyllysine"	MHGKNWSKLCKDCQV HCCCCHHHHCCCCEE	49.90	-
92	Phosphorylation	VIDGRNVTVTDVDIV EECCCCEEEEEEEEE	22.64	22817900
94	Phosphorylation	DGRNVTVTDVDIVFS CCCCEEEEEEEEEEE	22.42	24076635
94	O-linked_Glycosylation	DGRNVTVTDVDIVFS CCCCEEEEEEEEEEE	22.42	28657654
107	Phosphorylation	FSKIKGKSCRTITFE EEEECCCCCCEEEHH	19.94	23093407
152	O-linked_Glycosylation	EGKAPIISGVTKAIS CCCCCCCCCCHHHHC	28.12	UniProtKB CARBOHYD
152	Phosphorylation	EGKAPIISGVTKAIS CCCCCCCCCCHHHHC	28.12	24076635
155	Phosphorylation	APIISGVTKAISSPT CCCCCCCHHHHCCCC	20.48	-
155	O-linked_Glycosylation	APIISGVTKAISSPT CCCCCCCHHHHCCCC	20.48	28657654
159	Phosphorylation	SGVTKAISSPTVSRL CCCHHHHCCCCHHHC	34.81	28857561
159	O-linked_Glycosylation	SGVTKAISSPTVSRL CCCHHHHCCCCHHHC	34.81	28657654
160	Phosphorylation	GVTKAISSPTVSRLT CCHHHHCCCCHHHCC	20.62	23401153
162	Phosphorylation	TKAISSPTVSRLTDT HHHHCCCCHHHCCCC	32.82	30266825
164	Phosphorylation	AISSPTVSRLTDTTK HHCCCCHHHCCCCCC	24.85	30266825
167	Phosphorylation	SPTVSRLTDTTKFTG CCCHHHCCCCCCCCC	30.14	22210691
185	Acetylation	ERFDPSGKGKGKAGR CCCCCCCCCCCCCCC	62.88	19860149
187	Acetylation	FDPSGKGKGKAGRVD CCCCCCCCCCCCCEE	61.80	30586167
189	Acetylation	PSGKGKGKAGRVDLV CCCCCCCCCCCEEEE	51.67	30586173
199	Phosphorylation	RVDLVDESGYVSGYK CEEEECCCCCCCCCC	30.84	29978859
201	Phosphorylation	DLVDESGYVSGYKHA EEECCCCCCCCCCCC	10.75	29978859
203	Phosphorylation	VDESGYVSGYKHAGT ECCCCCCCCCCCCCC	28.11	29978859
205	Phosphorylation	ESGYVSGYKHAGTYD CCCCCCCCCCCCCCC	7.65	24076635

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
14	T	Phosphorylation	Kinase	CDK1	P06493	Uniprot
14	T	Phosphorylation	Kinase	CDK5	Q00535	Uniprot
18	S	Phosphorylation	Kinase	CDK1	P06493	Uniprot
18	S	Phosphorylation	Kinase	CDK5	Q00535	Uniprot
18	S	Phosphorylation	Kinase	ERK2	P28482	PSP
32	S	Phosphorylation	Kinase	PRKACA	P17612	GPS
32	S	Phosphorylation	Kinase	PKA-FAMILY	-	GPS
32	S	Phosphorylation	Kinase	ROCK1	Q13464	Uniprot
45	S	Phosphorylation	Kinase	CDK1	P06493	Uniprot
92	T	Phosphorylation	Kinase	PKA	-	Uniprot
92	T	Phosphorylation	Kinase	PKA-FAMILY	-	GPS
92	T	Phosphorylation	Kinase	PRKACA	P17612	GPS
107	S	Phosphorylation	Kinase	ROCK1	Q13464	Uniprot
159	S	Phosphorylation	Kinase	ROCK1	Q13464	Uniprot
159	S	Phosphorylation	Kinase	PKA-FAMILY	-	GPS
159	S	Phosphorylation	Kinase	PRKACA	P17612	GPS
160	S	Phosphorylation	Kinase	ERK2	P28482	PSP
160	S	Phosphorylation	Kinase	CDK5	Q00535	Uniprot
160	S	Phosphorylation	Kinase	CDK1	P06493	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
32	S	Acetylation	17693641
Phosphorylation by ROCK1 at Ser-32, Ser-107 and Ser-159 inhibits interaction with HDAC6, resulting in decreased acetylation of tubulin, increased cell motility and entry into S-phase.
32	S	Phosphorylation	17693641
Phosphorylation by ROCK1 at Ser-32, Ser-107 and Ser-159 inhibits interaction with HDAC6, resulting in decreased acetylation of tubulin, increased cell motility and entry into S-phase.
107	S	Acetylation	23093407
Phosphorylation by ROCK1 at Ser-32, Ser-107 and Ser-159 inhibits interaction with HDAC6, resulting in decreased acetylation of tubulin, increased cell motility and entry into S-phase.
107	S	Phosphorylation	23093407
Phosphorylation by ROCK1 at Ser-32, Ser-107 and Ser-159 inhibits interaction with HDAC6, resulting in decreased acetylation of tubulin, increased cell motility and entry into S-phase.
159	S	Acetylation	17693641
Phosphorylation by ROCK1 at Ser-32, Ser-107 and Ser-159 inhibits interaction with HDAC6, resulting in decreased acetylation of tubulin, increased cell motility and entry into S-phase.
159	S	Phosphorylation	17693641
Phosphorylation by ROCK1 at Ser-32, Ser-107 and Ser-159 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_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
HDAC6_HUMAN	HDAC6	physical	20308065
SYUA_HUMAN	SNCA	physical	20849899
A4_HUMAN	APP	physical	21832049

Drug and Disease Associations

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

Regulatory Network of TPPP_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-160, AND MASSSPECTROMETRY.	19413330 [Abstract]
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-14; SER-18; SER-32;SER-35; SER-45 AND SER-160, AND MASS SPECTROMETRY.	18669648 [Abstract]
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis."; Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III; J. Proteome Res. 7:1346-1351(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32, AND MASSSPECTROMETRY.	18220336 [Abstract]
"Phosphorylation blocks the activity of tubulin polymerization-promoting protein (TPPP): identification of sites targeted bydifferent kinases."; Hlavanda E., Klement E., Kokai E., Kovacs J., Vincze O., Toekesi N.,Orosz F., Medzihradszky K.F., Dombradi V., Ovadi J.; J. Biol. Chem. 282:29531-29539(2007). Cited for: FUNCTION, HOMODIMERIZATION, AND PHOSPHORYLATION AT THR-14; SER-18;SER-32; THR-92; SER-159 AND SER-160.	17693641 [Abstract]
"Phosphoproteomic analysis of synaptosomes from human cerebralcortex."; DeGiorgis J.A., Jaffe H., Moreira J.E., Carlotti C.G. Jr., Leite J.P.,Pant H.C., Dosemeci A.; J. Proteome Res. 4:306-315(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-14 AND SER-18, AND MASSSPECTROMETRY.	15822905 [Abstract]

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