dbPTM

TCTP_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	TCTP_HUMAN
UniProt AC	P13693
Protein Name	Translationally-controlled tumor protein
Gene Name	TPT1
Organism	Homo sapiens (Human).
Sequence Length	172
Subcellular Localization	Cytoplasm .
Protein Description	Involved in calcium binding and microtubule stabilization..
Protein Sequence	MIIYRDLISHDEMFSDIYKIREIADGLCLEVEGKMVSRTEGNIDDSLIGGNASAEGPEGEGTESTVITGVDIVMNHHLQETSFTKEAYKKYIKDYMKSIKGKLEEQRPERVKPFMTGAAEQIKHILANFKNYQFFIGENMNPDGMVALLDYREDGVTPYMIFFKDGLEMEKC

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
4	Phosphorylation	----MIIYRDLISHD ----CCCCCCCCCCH	6.27	21406692
9	Phosphorylation	IIYRDLISHDEMFSD CCCCCCCCCHHHHHH	31.98	21406692
13	Sulfoxidation	DLISHDEMFSDIYKI CCCCCHHHHHHHHHH	4.92	21406390
15	Phosphorylation	ISHDEMFSDIYKIRE CCCHHHHHHHHHHHH	23.07	21406692
18	Phosphorylation	DEMFSDIYKIREIAD HHHHHHHHHHHHHHC	12.83	21406692
19	Acetylation	EMFSDIYKIREIADG HHHHHHHHHHHHHCC	35.30	23236377
19	2-Hydroxyisobutyrylation	EMFSDIYKIREIADG HHHHHHHHHHHHHCC	35.30	-
19	Ubiquitination	EMFSDIYKIREIADG HHHHHHHHHHHHHCC	35.30	21890473
28	Glutathionylation	REIADGLCLEVEGKM HHHHCCCEEEEECEE	3.58	22555962
37	Phosphorylation	EVEGKMVSRTEGNID EEECEEEECCCCCCC	29.95	26074081
39	Phosphorylation	EGKMVSRTEGNIDDS ECEEEECCCCCCCCC	40.51	30175587
46	Phosphorylation	TEGNIDDSLIGGNAS CCCCCCCCCCCCCCC	20.38	30175587
53	Phosphorylation	SLIGGNASAEGPEGE CCCCCCCCCCCCCCC	30.74	28674151
62	Phosphorylation	EGPEGEGTESTVITG CCCCCCCCCCEEEEE	23.59	24732914
64	Phosphorylation	PEGEGTESTVITGVD CCCCCCCCEEEEECC	28.01	24732914
65	O-linked_Glycosylation	EGEGTESTVITGVDI CCCCCCCEEEEECCC	15.08	OGP
65	Phosphorylation	EGEGTESTVITGVDI CCCCCCCEEEEECCC	15.08	24732914
68	Phosphorylation	GTESTVITGVDIVMN CCCCEEEEECCCHHC	27.15	24732914
78	Ubiquitination	DIVMNHHLQETSFTK CCHHCCCCCCCCCCH	3.70	21890473
81	Phosphorylation	MNHHLQETSFTKEAY HCCCCCCCCCCHHHH	19.04	27251275
82	Phosphorylation	NHHLQETSFTKEAYK CCCCCCCCCCHHHHH	30.11	24732914
84	Phosphorylation	HLQETSFTKEAYKKY CCCCCCCCHHHHHHH	27.95	27251275
88	Phosphorylation	TSFTKEAYKKYIKDY CCCCHHHHHHHHHHH	14.76	22817900
90	Malonylation	FTKEAYKKYIKDYMK CCHHHHHHHHHHHHH	39.26	26320211
91	Phosphorylation	TKEAYKKYIKDYMKS CHHHHHHHHHHHHHH	14.73	28152594
93	Ubiquitination	EAYKKYIKDYMKSIK HHHHHHHHHHHHHHC	39.45	19608861
93	Acetylation	EAYKKYIKDYMKSIK HHHHHHHHHHHHHHC	39.45	23749302
93	Malonylation	EAYKKYIKDYMKSIK HHHHHHHHHHHHHHC	39.45	26320211
95	Phosphorylation	YKKYIKDYMKSIKGK HHHHHHHHHHHHCCH	11.05	28152594
97	2-Hydroxyisobutyrylation	KYIKDYMKSIKGKLE HHHHHHHHHHCCHHH	42.68	-
97	Malonylation	KYIKDYMKSIKGKLE HHHHHHHHHHCCHHH	42.68	26320211
97	Ubiquitination	KYIKDYMKSIKGKLE HHHHHHHHHHCCHHH	42.68	19608861
97	Acetylation	KYIKDYMKSIKGKLE HHHHHHHHHHCCHHH	42.68	23749302
102	Sumoylation	YMKSIKGKLEEQRPE HHHHHCCHHHHHCCH	47.96	-
102	Acetylation	YMKSIKGKLEEQRPE HHHHHCCHHHHHCCH	47.96	23749302
102	Ubiquitination	YMKSIKGKLEEQRPE HHHHHCCHHHHHCCH	47.96	-
102	Sumoylation	YMKSIKGKLEEQRPE HHHHHCCHHHHHCCH	47.96	-
112	Sumoylation	EQRPERVKPFMTGAA HHCCHHCCCCHHCHH	38.47	-
112	2-Hydroxyisobutyrylation	EQRPERVKPFMTGAA HHCCHHCCCCHHCHH	38.47	-
112	Sumoylation	EQRPERVKPFMTGAA HHCCHHCCCCHHCHH	38.47	19608861
112	Malonylation	EQRPERVKPFMTGAA HHCCHHCCCCHHCHH	38.47	26320211
112	Ubiquitination	EQRPERVKPFMTGAA HHCCHHCCCCHHCHH	38.47	19608861
112	Acetylation	EQRPERVKPFMTGAA HHCCHHCCCCHHCHH	38.47	23954790
115	Sulfoxidation	PERVKPFMTGAAEQI CHHCCCCHHCHHHHH	4.60	28465586
116	Phosphorylation	ERVKPFMTGAAEQIK HHCCCCHHCHHHHHH	24.85	20068231
123	Acetylation	TGAAEQIKHILANFK HCHHHHHHHHHHHCC	25.04	21466224
123	Ubiquitination	TGAAEQIKHILANFK HCHHHHHHHHHHHCC	25.04	-
130	Sumoylation	KHILANFKNYQFFIG HHHHHHCCCCEEEEE	55.33	-
130	Methylation	KHILANFKNYQFFIG HHHHHHCCCCEEEEE	55.33	-
130	Ubiquitination	KHILANFKNYQFFIG HHHHHHCCCCEEEEE	55.33	21890473
159	Phosphorylation	REDGVTPYMIFFKDG CCCCCCEEEEEECCC	8.09	20393185
164	Sumoylation	TPYMIFFKDGLEMEK CEEEEEECCCCCEEC	39.89	-
164	Ubiquitination	TPYMIFFKDGLEMEK CEEEEEECCCCCEEC	39.89	21890473
169	Sulfoxidation	FFKDGLEMEKC---- EECCCCCEECC----	7.78	30846556
171	Ubiquitination	KDGLEMEKC------ CCCCCEECC------	43.89	-

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
46	S	Phosphorylation	Kinase	PLK1	P53350	Uniprot
64	S	Phosphorylation	Kinase	PLK1	P53350	Uniprot

Functions of PTM Sites

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

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 TCTP_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
DREB_HUMAN	DBN1	physical	21900206
RLA1_HUMAN	RPLP1	physical	21900206
P53_HUMAN	TP53	physical	22157679
MDM2_HUMAN	MDM2	physical	22912717
A4_HUMAN	APP	physical	21832049
B2CL1_HUMAN	BCL2L1	physical	15870695
MCL1_HUMAN	MCL1	physical	15870695
TBB2A_HUMAN	TUBB2A	physical	15870695
VHL_HUMAN	VHL	physical	23387829
PCH2_HUMAN	TRIP13	physical	25416956
CALR_HUMAN	CALR	physical	26344197
PEPL1_HUMAN	NPEPL1	physical	26344197
SAMD9_HUMAN	SAMD9	physical	26344197
LACC1_HUMAN	LACC1	physical	28514442
CYTF_HUMAN	CST7	physical	28514442
EF1A2_HUMAN	EEF1A2	physical	28514442

Drug and Disease Associations

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

Regulatory Network of TCTP_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-93, AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"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 SER-46 AND SER-53, AND MASSSPECTROMETRY.	18669648 [Abstract]
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry."; Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.; Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-46, AND MASSSPECTROMETRY.	17287340 [Abstract]
"Plk phosphorylation regulates the microtubule-stabilizing proteinTCTP."; Yarm F.R.; Mol. Cell. Biol. 22:6209-6221(2002). Cited for: PHOSPHORYLATION AT SER-46 AND SER-64.	12167714 [Abstract]