dbPTM

TRIP6_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	TRIP6_HUMAN
UniProt AC	Q15654
Protein Name	Thyroid receptor-interacting protein 6
Gene Name	TRIP6
Organism	Homo sapiens (Human).
Sequence Length	476
Subcellular Localization	Cytoplasm, cytoskeleton . Cell junction, focal adhesion . Nucleus . Cytoplasm . Shuttles between nucleus and cytoplasm (PubMed:16624523). Colocalizes with actin (PubMed:10826496).
Protein Description	Relays signals from the cell surface to the nucleus to weaken adherens junction and promote actin cytoskeleton reorganization and cell invasiveness. Involved in lysophosphatidic acid-induced cell adhesion and migration. Acts as a transcriptional coactivator for NF-kappa-B and JUN, and mediates the transrepression of these transcription factors induced by glucocorticoid receptor..
Protein Sequence	MSGPTWLPPKQPEPARAPQGRAIPRGTPGPPPAHGAALQPHPRVNFCPLPSEQCYQAPGGPEDRGPAWVGSHGVLQHTQGLPADRGGLRPGSLDAEIDLLSSTLAELNGGRGHASRRPDRQAYEPPPPPAYRTGSLKPNPASPLPASPYGGPTPASYTTASTPAGPAFPVQVKVAQPVRGCGPPRRGASQASGPLPGPHFPLPGRGEVWGPGYRSQREPGPGAKEEAAGVSGPAGRGRGGEHGPQVPLSQPPEDELDRLTKKLVHDMNHPPSGEYFGQCGGCGEDVVGDGAGVVALDRVFHVGCFVCSTCRAQLRGQHFYAVERRAYCEGCYVATLEKCATCSQPILDRILRAMGKAYHPGCFTCVVCHRGLDGIPFTVDATSQIHCIEDFHRKFAPRCSVCGGAIMPEPGQEETVRIVALDRSFHIGCYKCEECGLLLSSEGECQGCYPLDGHILCKACSAWRIQELSATVTTDC

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MSGPTWLPP ------CCCCCCCCC	54.18	28348404
5	Phosphorylation	---MSGPTWLPPKQP ---CCCCCCCCCCCC	43.06	24719451
16	Methylation	PKQPEPARAPQGRAI CCCCCCCCCCCCCCC	58.47	115386627
21	Methylation	PARAPQGRAIPRGTP CCCCCCCCCCCCCCC	24.89	97816441
25	Methylation	PQGRAIPRGTPGPPP CCCCCCCCCCCCCCC	56.35	24129315
25	Asymmetric dimethylarginine	PQGRAIPRGTPGPPP CCCCCCCCCCCCCCC	56.35	-
27	Phosphorylation	GRAIPRGTPGPPPAH CCCCCCCCCCCCCCC	26.76	25159151
43	Methylation	AALQPHPRVNFCPLP CCCCCCCCCCCCCCC	32.74	82797053
51	Phosphorylation	VNFCPLPSEQCYQAP CCCCCCCHHHHCCCC	48.24	21945579
55	Phosphorylation	PLPSEQCYQAPGGPE CCCHHHHCCCCCCCC	13.85	21945579
64	Methylation	APGGPEDRGPAWVGS CCCCCCCCCCCCCCC	51.86	115919001
71	Phosphorylation	RGPAWVGSHGVLQHT CCCCCCCCCHHHHHC	13.88	24719451
85	Methylation	TQGLPADRGGLRPGS CCCCCCCCCCCCCCC	43.09	115919005
89	Methylation	PADRGGLRPGSLDAE CCCCCCCCCCCCHHH	36.49	115919009
92	Phosphorylation	RGGLRPGSLDAEIDL CCCCCCCCCHHHHHH	26.26	25159151
101	Phosphorylation	DAEIDLLSSTLAELN HHHHHHHHHHHHHHC	28.68	23663014
102	Phosphorylation	AEIDLLSSTLAELNG HHHHHHHHHHHHHCC	27.66	23663014
103	Phosphorylation	EIDLLSSTLAELNGG HHHHHHHHHHHHCCC	26.98	23663014
111	Methylation	LAELNGGRGHASRRP HHHHCCCCCCCCCCC	34.81	24129315
116	Methylation	GGRGHASRRPDRQAY CCCCCCCCCCCCCCC	55.74	12019283
120	Methylation	HASRRPDRQAYEPPP CCCCCCCCCCCCCCC	26.22	115918989
123	Phosphorylation	RRPDRQAYEPPPPPA CCCCCCCCCCCCCCC	22.19	21945579
131	Phosphorylation	EPPPPPAYRTGSLKP CCCCCCCCCCCCCCC	17.93	21945579
133	Phosphorylation	PPPPAYRTGSLKPNP CCCCCCCCCCCCCCC	20.60	21945579
135	Phosphorylation	PPAYRTGSLKPNPAS CCCCCCCCCCCCCCC	32.38	21945579
137	Acetylation	AYRTGSLKPNPASPL CCCCCCCCCCCCCCC	44.43	26051181
142	Phosphorylation	SLKPNPASPLPASPY CCCCCCCCCCCCCCC	28.38	21945579
147	Phosphorylation	PASPLPASPYGGPTP CCCCCCCCCCCCCCC	19.40	21945579
149	Phosphorylation	SPLPASPYGGPTPAS CCCCCCCCCCCCCCC	32.02	21945579
153	Phosphorylation	ASPYGGPTPASYTTA CCCCCCCCCCCCEEC	34.46	21945579
156	Phosphorylation	YGGPTPASYTTASTP CCCCCCCCCEECCCC	24.98	21945579
157	Phosphorylation	GGPTPASYTTASTPA CCCCCCCCEECCCCC	15.37	21945579
158	Phosphorylation	GPTPASYTTASTPAG CCCCCCCEECCCCCC	17.25	21945579
159	Phosphorylation	PTPASYTTASTPAGP CCCCCCEECCCCCCC	15.46	21945579
161	Phosphorylation	PASYTTASTPAGPAF CCCCEECCCCCCCCC	32.60	21945579
162	Phosphorylation	ASYTTASTPAGPAFP CCCEECCCCCCCCCC	18.07	21945579
179	Methylation	VKVAQPVRGCGPPRR EEECCCCCCCCCCCC	41.17	24129315
179	Dimethylation	VKVAQPVRGCGPPRR EEECCCCCCCCCCCC	41.17	-
185	Methylation	VRGCGPPRRGASQAS CCCCCCCCCCCCCCC	53.45	115386633
186	Methylation	RGCGPPRRGASQASG CCCCCCCCCCCCCCC	51.29	24129315
186	Dimethylation	RGCGPPRRGASQASG CCCCCCCCCCCCCCC	51.29	-
189	Phosphorylation	GPPRRGASQASGPLP CCCCCCCCCCCCCCC	29.15	28857561
192	Phosphorylation	RRGASQASGPLPGPH CCCCCCCCCCCCCCC	33.05	26434776
205	Methylation	PHFPLPGRGEVWGPG CCCCCCCCCCCCCCC	35.84	24129315
213	Phosphorylation	GEVWGPGYRSQREPG CCCCCCCCCCCCCCC	15.38	27642862
214	Methylation	EVWGPGYRSQREPGP CCCCCCCCCCCCCCC	32.03	12019323
215	Phosphorylation	VWGPGYRSQREPGPG CCCCCCCCCCCCCCC	25.71	24670416
217	Methylation	GPGYRSQREPGPGAK CCCCCCCCCCCCCCH	54.01	58854985
224	Methylation	REPGPGAKEEAAGVS CCCCCCCHHHHCCCC	63.10	115918985
236	Dimethylation	GVSGPAGRGRGGEHG CCCCCCCCCCCCCCC	33.47	-
236	Methylation	GVSGPAGRGRGGEHG CCCCCCCCCCCCCCC	33.47	24129315
238	Methylation	SGPAGRGRGGEHGPQ CCCCCCCCCCCCCCC	48.89	24129315
249	Phosphorylation	HGPQVPLSQPPEDEL CCCCCCCCCCCHHHH	34.27	23917254
258	Methylation	PPEDELDRLTKKLVH CCHHHHHHHHHHHHH	57.81	24394759
261	Methylation	DELDRLTKKLVHDMN HHHHHHHHHHHHHCC	49.02	115368145
272	Phosphorylation	HDMNHPPSGEYFGQC HHCCCCCCCCCCCCC	49.02	24719451
275	Phosphorylation	NHPPSGEYFGQCGGC CCCCCCCCCCCCCCC	19.28	22817900
315	Methylation	STCRAQLRGQHFYAV HHHHHHHCCCCEEEE	30.55	115918993
320	Phosphorylation	QLRGQHFYAVERRAY HHCCCCEEEEEEEEE	13.96	27642862
332	Phosphorylation	RAYCEGCYVATLEKC EEECCCCEEEEHHHH	12.18	-
335	Phosphorylation	CEGCYVATLEKCATC CCCCEEEEHHHHCCC	25.96	28857561
400	Phosphorylation	RKFAPRCSVCGGAIM HHHCCCCCCCCCCCC	23.01	28857561
423	Methylation	VRIVALDRSFHIGCY EEEEEEECCEEEECE	41.91	115918997
424	Phosphorylation	RIVALDRSFHIGCYK EEEEEECCEEEECEE	22.35	28450419
458	Ubiquitination	LDGHILCKACSAWRI CCCCEEEHHHCCCCE	49.32	21963094
469	Phosphorylation	AWRIQELSATVTTDC CCCEEEEECEEECCC	22.57	27251275
471	Phosphorylation	RIQELSATVTTDC-- CEEEEECEEECCC--	18.27	28555341
473	Phosphorylation	QELSATVTTDC---- EEEECEEECCC----	16.74	27251275

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
55	Y	Phosphorylation	Kinase	SRC	P12931	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of TRIP6_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 TRIP6_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
LPAR2_HUMAN	LPAR2	physical	14688263
F124B_HUMAN	FAM124B	physical	16189514
P121A_HUMAN	POM121	physical	16189514
FA46C_HUMAN	FAM46C	physical	16189514
CTSR1_HUMAN	CATSPER1	physical	16189514
NCK2_HUMAN	NCK2	physical	16189514
PP16A_HUMAN	PPP1R16A	physical	16189514
K1683_HUMAN	KIAA1683	physical	16189514
EXAS1_HUMAN	EXOC3-AS1	physical	16189514
VINC_HUMAN	VCL	physical	16189514
PDIA1_HUMAN	P4HB	physical	17353931
MOB1A_HUMAN	MOB1A	physical	17353931
STOM_HUMAN	STOM	physical	17353931
KCTD5_HUMAN	KCTD5	physical	17353931
TR150_HUMAN	THRAP3	physical	17353931
AF1L1_HUMAN	AFAP1L1	physical	17353931
RS14_HUMAN	RPS14	physical	17353931
MRM3_HUMAN	RNMTL1	physical	17353931
BCAR1_HUMAN	BCAR1	physical	14688263
FAK1_HUMAN	PTK2	physical	14688263
PAXI_HUMAN	PXN	physical	14688263
SRC_HUMAN	SRC	physical	14688263
CASL_HUMAN	NEDD9	physical	11782456
PO210_HUMAN	NUP210	physical	11782456
TPM4_HUMAN	TPM4	physical	11782456
BCAR1_HUMAN	BCAR1	physical	11782456
LPAR2_HUMAN	LPAR2	physical	19293149
NHRF2_HUMAN	SLC9A3R2	physical	19293149
EGLN2_HUMAN	EGLN2	physical	22286099
UBE2C_HUMAN	UBE2C	physical	22939629
TTL12_HUMAN	TTLL12	physical	22939629
UNK_HUMAN	UNK	physical	22939629
UFM1_HUMAN	UFM1	physical	22939629
UBE4B_HUMAN	UBE4B	physical	22939629
TTC1_HUMAN	TTC1	physical	22939629
DPP3_HUMAN	DPP3	physical	22863883
GGH_HUMAN	GGH	physical	22863883
PA1B2_HUMAN	PAFAH1B2	physical	22863883
NCK2_HUMAN	NCK2	physical	25416956
STK16_HUMAN	STK16	physical	25416956
CREB5_HUMAN	CREB5	physical	25416956
TCAF1_HUMAN	FAM115A	physical	25416956
ABI2_HUMAN	ABI2	physical	25416956
CIKS_HUMAN	TRAF3IP2	physical	25416956
FRS3_HUMAN	FRS3	physical	25416956
MS18B_HUMAN	OIP5	physical	25416956
MABP1_HUMAN	MAPKBP1	physical	25416956
GSE1_HUMAN	GSE1	physical	25416956
SIK3_HUMAN	SIK3	physical	25416956
RHOQ_HUMAN	RHOQ	physical	25416956
TRI29_HUMAN	TRIM29	physical	25416956
THIOM_HUMAN	TXN2	physical	25416956
CTAG2_HUMAN	CTAG2	physical	25416956
MEMO1_HUMAN	MEMO1	physical	25416956
S15A3_HUMAN	SLC15A3	physical	25416956
TPC2L_HUMAN	TRAPPC2L	physical	25416956
ATL4_HUMAN	ADAMTSL4	physical	25416956
KLK15_HUMAN	KLK15	physical	25416956
DHX37_HUMAN	DHX37	physical	25416956
RN213_HUMAN	RNF213	physical	25416956
DMRT3_HUMAN	DMRT3	physical	25416956
MET17_HUMAN	METTL17	physical	25416956
OTUB2_HUMAN	OTUB2	physical	25416956
ZBP1_HUMAN	ZBP1	physical	25416956
GDPD5_HUMAN	GDPD5	physical	25416956
TXND5_HUMAN	TXNDC5	physical	25416956
YPEL3_HUMAN	YPEL3	physical	25416956
ATP23_HUMAN	XRCC6BP1	physical	25416956
DTX2_HUMAN	DTX2	physical	25416956
EXAS1_HUMAN	EXOC3-AS1	physical	25416956
CTSR1_HUMAN	CATSPER1	physical	25416956
HYKK_HUMAN	HYKK	physical	25416956
NEUR4_HUMAN	NEU4	physical	25416956
TEKT4_HUMAN	TEKT4	physical	25416956
SAXO1_HUMAN	FAM154A	physical	25416956
MSRB3_HUMAN	MSRB3	physical	25416956
TTL10_HUMAN	TTLL10	physical	25416956
RN214_HUMAN	RNF214	physical	25416956
CE57L_HUMAN	CEP57L1	physical	25416956
INCA1_HUMAN	INCA1	physical	25416956
KR261_HUMAN	KRTAP26-1	physical	25416956
AAPK2_HUMAN	PRKAA2	physical	16624523
LPAR2_HUMAN	LPAR2	physical	16624523
CASL_HUMAN	NEDD9	physical	16624523
LIMD1_HUMAN	LIMD1	physical	26186194
WTIP_HUMAN	WTIP	physical	26186194
G3PT_HUMAN	GAPDHS	physical	26186194
KIF5C_HUMAN	KIF5C	physical	26186194
KINH_HUMAN	KIF5B	physical	26186194
KIF5A_HUMAN	KIF5A	physical	26186194
EFL1_HUMAN	EFTUD1	physical	26186194
KLC1_HUMAN	KLC1	physical	26186194
KLC4_HUMAN	KLC4	physical	26186194
TB10B_HUMAN	TBC1D10B	physical	26186194
PDLI7_HUMAN	PDLIM7	physical	26186194
AJUBA_HUMAN	AJUBA	physical	26186194
PCBP1_HUMAN	PCBP1	physical	26344197
PCBP2_HUMAN	PCBP2	physical	26344197
PGK1_HUMAN	PGK1	physical	26344197
PYGO2_HUMAN	PYGO2	physical	26344197
SNX3_HUMAN	SNX3	physical	26344197
STIP1_HUMAN	STIP1	physical	26344197
VINC_HUMAN	VCL	physical	21516116
TCAF1_HUMAN	FAM115A	physical	21516116
AJUBA_HUMAN	AJUBA	physical	28514442
KLC4_HUMAN	KLC4	physical	28514442
EFL1_HUMAN	EFTUD1	physical	28514442
WTIP_HUMAN	WTIP	physical	28514442
KLC1_HUMAN	KLC1	physical	28514442
KIF5A_HUMAN	KIF5A	physical	28514442
KIF5C_HUMAN	KIF5C	physical	28514442
KINH_HUMAN	KIF5B	physical	28514442
LIMD1_HUMAN	LIMD1	physical	28514442
G3PT_HUMAN	GAPDHS	physical	28514442

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 TRIP6_HUMAN

Related Literatures of Post-Translational Modification

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-142 AND SER-147, ANDMASS SPECTROMETRY.	18669648 [Abstract]
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-92, AND MASSSPECTROMETRY.	17081983 [Abstract]
"An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells."; Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.; J. Proteome Res. 8:3852-3861(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-123, AND MASSSPECTROMETRY.	19534553 [Abstract]
"PTPL1/FAP-1 negatively regulates TRIP6 function in lysophosphatidicacid-induced cell migration."; Lai Y.-J., Lin W.-C., Lin F.-T.; J. Biol. Chem. 282:24381-24387(2007). Cited for: INTERACTION WITH PTPN13, AND PHOSPHORYLATION AT TYR-55.	17591779 [Abstract]
"c-Src-mediated phosphorylation of TRIP6 regulates its function inlysophosphatidic acid-induced cell migration."; Lai Y.-J., Chen C.-S., Lin W.-C., Lin F.-T.; Mol. Cell. Biol. 25:5859-5868(2005). Cited for: PHOSPHORYLATION AT TYR-55.	15988003 [Abstract]