dbPTM

TTC1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	TTC1_HUMAN
UniProt AC	Q99614
Protein Name	Tetratricopeptide repeat protein 1
Gene Name	TTC1
Organism	Homo sapiens (Human).
Sequence Length	292
Subcellular Localization
Protein Description
Protein Sequence	MGEKSENCGVPEDLLNGLKVTDTQEAECAGPPVPDPKNQHSQSKLLRDDEAHLQEDQGEEECFHDCSASFEEEPGADKVENKSNEDVNSSELDEEYLIELEKNMSDEEKQKRREESTRLKEEGNEQFKKGDYIEAESSYSRALEMCPSCFQKERSILFSNRAAARMKQDKKEMAINDCSKAIQLNPSYIRAILRRAELYEKTDKLDEALEDYKSILEKDPSIHQAREACMRLPKQIEERNERLKEEMLGKLKDLGNLVLRPFGLSTENFQIKQDSSTGSYSINFVQNPNNNR

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
19	Acetylation	EDLLNGLKVTDTQEA HHHHCCCCCCCCCCC	44.48	26051181
21	Phosphorylation	LLNGLKVTDTQEAEC HHCCCCCCCCCCCHH	31.57	23663014
23	Phosphorylation	NGLKVTDTQEAECAG CCCCCCCCCCCHHCC	20.95	23663014
28	Glutathionylation	TDTQEAECAGPPVPD CCCCCCHHCCCCCCC	7.36	22555962
37	Ubiquitination	GPPVPDPKNQHSQSK CCCCCCCCCCCCHHH	76.30	29967540
41	Phosphorylation	PDPKNQHSQSKLLRD CCCCCCCCHHHHHHC	26.78	20068231
43	Phosphorylation	PKNQHSQSKLLRDDE CCCCCCHHHHHHCHH	28.43	20068231
44	Acetylation	KNQHSQSKLLRDDEA CCCCCHHHHHHCHHH	43.85	25953088
44	Ubiquitination	KNQHSQSKLLRDDEA CCCCCHHHHHHCHHH	43.85	29967540
67	Phosphorylation	EECFHDCSASFEEEP HHHCCCCCCCCCCCC	32.76	23898821
69	Phosphorylation	CFHDCSASFEEEPGA HCCCCCCCCCCCCCC	19.52	23898821
78	Ubiquitination	EEEPGADKVENKSNE CCCCCCCCCCCCCCC	51.41	29967540
83	Phosphorylation	ADKVENKSNEDVNSS CCCCCCCCCCCCCHH	57.97	30266825
89	Phosphorylation	KSNEDVNSSELDEEY CCCCCCCHHHCCHHH	25.66	30266825
90	O-linked_Glycosylation	SNEDVNSSELDEEYL CCCCCCHHHCCHHHH	36.65	23301498
90	Phosphorylation	SNEDVNSSELDEEYL CCCCCCHHHCCHHHH	36.65	30266825
96	Phosphorylation	SSELDEEYLIELEKN HHHCCHHHHHHHHHH	15.78	30266825
102	Ubiquitination	EYLIELEKNMSDEEK HHHHHHHHHCCHHHH	71.25	21906983
105	Phosphorylation	IELEKNMSDEEKQKR HHHHHHCCHHHHHHH	51.79	28258704
109	Acetylation	KNMSDEEKQKRREES HHCCHHHHHHHHHHH	60.10	23954790
120	Ubiquitination	REESTRLKEEGNEQF HHHHHHHHHHHHHHH	50.89	-
128	2-Hydroxyisobutyrylation	EEGNEQFKKGDYIEA HHHHHHHHCCCCEEE	56.38	-
128	Ubiquitination	EEGNEQFKKGDYIEA HHHHHHHHCCCCEEE	56.38	21906983
128	Acetylation	EEGNEQFKKGDYIEA HHHHHHHHCCCCEEE	56.38	23749302
129	Ubiquitination	EGNEQFKKGDYIEAE HHHHHHHCCCCEEEC	59.30	22817900
132	Phosphorylation	EQFKKGDYIEAESSY HHHHCCCCEEECCHH	14.88	28796482
137	Phosphorylation	GDYIEAESSYSRALE CCCEEECCHHHHHHH	41.44	28796482
138	Phosphorylation	DYIEAESSYSRALEM CCEEECCHHHHHHHH	20.73	28796482
139	Phosphorylation	YIEAESSYSRALEMC CEEECCHHHHHHHHC	16.08	28796482
140	Phosphorylation	IEAESSYSRALEMCP EEECCHHHHHHHHCH	17.02	28796482
145	Sulfoxidation	SYSRALEMCPSCFQK HHHHHHHHCHHHHHH	4.18	21406390
152	Ubiquitination	MCPSCFQKERSILFS HCHHHHHHHHHHHHH	34.54	23000965
152	Acetylation	MCPSCFQKERSILFS HCHHHHHHHHHHHHH	34.54	25953088
155	Phosphorylation	SCFQKERSILFSNRA HHHHHHHHHHHHHHH	25.41	23911959
173	Sulfoxidation	MKQDKKEMAINDCSK HHHHHHHHHHHHHHH	6.61	30846556
180	Ubiquitination	MAINDCSKAIQLNPS HHHHHHHHHHHCCHH	56.70	29967540
187	Phosphorylation	KAIQLNPSYIRAILR HHHHCCHHHHHHHHH	31.92	28152594
188	Phosphorylation	AIQLNPSYIRAILRR HHHCCHHHHHHHHHH	8.83	28152594
188	Nitration	AIQLNPSYIRAILRR HHHCCHHHHHHHHHH	8.83	-
204	2-Hydroxyisobutyrylation	ELYEKTDKLDEALED HHHHHCCHHHHHHHH	64.17	-
212	Phosphorylation	LDEALEDYKSILEKD HHHHHHHHHHHHHHC	9.39	-
213	Ubiquitination	DEALEDYKSILEKDP HHHHHHHHHHHHHCC	43.26	29967540
214	Phosphorylation	EALEDYKSILEKDPS HHHHHHHHHHHHCCC	26.61	24719451
218	Ubiquitination	DYKSILEKDPSIHQA HHHHHHHHCCCHHHH	72.06	29967540
218	2-Hydroxyisobutyrylation	DYKSILEKDPSIHQA HHHHHHHHCCCHHHH	72.06	-
221	Phosphorylation	SILEKDPSIHQAREA HHHHHCCCHHHHHHH	42.72	25159151
234	Ubiquitination	EACMRLPKQIEERNE HHHHHCHHHHHHHHH	69.38	24816145
244	Ubiquitination	EERNERLKEEMLGKL HHHHHHHHHHHHHHH	58.82	29967540
250	Acetylation	LKEEMLGKLKDLGNL HHHHHHHHHHHHHHH	48.69	25953088
250	Ubiquitination	LKEEMLGKLKDLGNL HHHHHHHHHHHHHHH	48.69	23000965
252	Ubiquitination	EEMLGKLKDLGNLVL HHHHHHHHHHHHHEE	55.16	23000965
265	Phosphorylation	VLRPFGLSTENFQIK EEEECCCCCCCEEEE	33.77	22496350
266	Phosphorylation	LRPFGLSTENFQIKQ EEECCCCCCCEEEEE	39.74	29514088
272	Ubiquitination	STENFQIKQDSSTGS CCCCEEEEECCCCCC	36.95	23503661
275	Phosphorylation	NFQIKQDSSTGSYSI CEEEEECCCCCCEEE	27.57	28555341
276	Phosphorylation	FQIKQDSSTGSYSIN EEEEECCCCCCEEEE	45.11	21945579
277	Phosphorylation	QIKQDSSTGSYSINF EEEECCCCCCEEEEE	33.81	21945579
279	Phosphorylation	KQDSSTGSYSINFVQ EECCCCCCEEEEEEE	18.78	21945579
280	Phosphorylation	QDSSTGSYSINFVQN ECCCCCCEEEEEEEC	18.21	21945579
281	Phosphorylation	DSSTGSYSINFVQNP CCCCCCEEEEEEECC	16.86	21945579

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 TTC1_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of TTC1_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 TTC1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
GNA15_HUMAN	GNA15	physical	12748287
GNAQ_HUMAN	GNAQ	physical	12748287
GNAS3_HUMAN	GNAS	physical	12748287
GNAS2_HUMAN	GNAS	physical	12748287
ALEX_HUMAN	GNAS	physical	12748287
GNAS1_HUMAN	GNAS	physical	12748287
GNAI2_HUMAN	GNAI2	physical	12748287
RASH_HUMAN	HRAS	physical	12748287
UBXN1_HUMAN	UBXN1	physical	22939629
ANCHR_HUMAN	ZFYVE19	physical	22939629
ZRAB2_HUMAN	ZRANB2	physical	22939629
UBE2B_HUMAN	UBE2B	physical	22939629
UFM1_HUMAN	UFM1	physical	22939629
TTL12_HUMAN	TTLL12	physical	22939629
UB2D2_HUMAN	UBE2D2	physical	22939629
UBQL2_HUMAN	UBQLN2	physical	22939629
UCHL3_HUMAN	UCHL3	physical	22939629
AASD1_HUMAN	AARSD1	physical	22863883
SYCC_HUMAN	CARS	physical	22863883
U5S1_HUMAN	EFTUD2	physical	22863883
GFPT1_HUMAN	GFPT1	physical	22863883
SYHC_HUMAN	HARS	physical	22863883
RUSD2_HUMAN	RPUSD2	physical	22863883
SYSC_HUMAN	SARS	physical	22863883
SH3G1_HUMAN	SH3GL1	physical	22863883
GLYC_HUMAN	SHMT1	physical	22863883
SNF8_HUMAN	SNF8	physical	22863883
XPO7_HUMAN	XPO7	physical	22863883
VAPB_HUMAN	VAPB	physical	25036637
HS74L_HUMAN	HSPA4L	physical	25036637
VAPA_HUMAN	VAPA	physical	25036637
RNF41_HUMAN	RNF41	physical	25036637
TBA1A_HUMAN	TUBA1A	physical	25036637
BAG2_HUMAN	BAG2	physical	25036637
RNF41_HUMAN	RNF41	physical	25416956
VAPA_HUMAN	VAPA	physical	26186194
VAPB_HUMAN	VAPB	physical	26186194
RNF41_HUMAN	RNF41	physical	26186194
PDIA6_HUMAN	PDIA6	physical	26344197
RNF41_HUMAN	RNF41	physical	28514442
ST1A3_HUMAN	SULT1A3	physical	28514442
ST1A4_HUMAN	SULT1A3	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 TTC1_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-67; SER-69; SER-83 ANDSER-90, AND MASS SPECTROMETRY.	18669648 [Abstract]