dbPTM

TTC4_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	TTC4_HUMAN
UniProt AC	O95801
Protein Name	Tetratricopeptide repeat protein 4
Gene Name	TTC4
Organism	Homo sapiens (Human).
Sequence Length	387
Subcellular Localization
Protein Description
Protein Sequence	MEQPGQDPTSDDVMDSFLEKFQSQPYRGGFHEDQWEKEFEKVPLFMSRAPSEIDPRENPDLACLQSIIFDEERSPEEQAKTYKDEGNDYFKEKDYKKAVISYTEGLKKKCADPDLNAVLYTNRAAAQYYLGNFRSALNDVTAARKLKPCHLKAIIRGALCHLELKHFAEAVNWCDEGLQIDAKEKKLLEMRAKADKLKRIEQRDVRKANLKEKKERNQNEALLQAIKARNIRLSEAACEDEDSASEGLGELFLDGLSTENPHGARLSLDGQGRLSWPVLFLYPEYAQSDFISAFHEDSRFIDHLMVMFGETPSWDLEQKYCPDNLEVYFEDEDRAELYRVPAKSTLLQVLQHQRYFVKALTPAFLVCVGSSPFCKNFLRGRKVYQIR

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MEQPGQDP -------CCCCCCCC	11.02	19413330
9	Phosphorylation	EQPGQDPTSDDVMDS CCCCCCCCCHHHHHH	53.75	26074081
10	Phosphorylation	QPGQDPTSDDVMDSF CCCCCCCCHHHHHHH	36.88	26074081
16	Phosphorylation	TSDDVMDSFLEKFQS CCHHHHHHHHHHHHC	17.40	25072903
23	Phosphorylation	SFLEKFQSQPYRGGF HHHHHHHCCCCCCCC	35.93	23917254
27	Methylation	KFQSQPYRGGFHEDQ HHHCCCCCCCCCHHH	45.50	115919097
37	Ubiquitination	FHEDQWEKEFEKVPL CCHHHHHHHHHCCCC	65.82	21890473
41	Ubiquitination	QWEKEFEKVPLFMSR HHHHHHHCCCCEECC	55.24	29967540
46	Sulfoxidation	FEKVPLFMSRAPSEI HHCCCCEECCCCCCC	3.32	21406390
47	Phosphorylation	EKVPLFMSRAPSEID HCCCCEECCCCCCCC	20.25	30576142
51	Phosphorylation	LFMSRAPSEIDPREN CEECCCCCCCCCCCC	46.31	23401153
63	Glutathionylation	RENPDLACLQSIIFD CCCCCHHHHHHHHHC	4.64	22555962
74	Phosphorylation	IIFDEERSPEEQAKT HHHCCCCCHHHHHHH	39.69	28348404
80	Ubiquitination	RSPEEQAKTYKDEGN CCHHHHHHHHHCCCC	52.67	29967540
83	Ubiquitination	EEQAKTYKDEGNDYF HHHHHHHHCCCCHHH	55.31	29967540
89	Phosphorylation	YKDEGNDYFKEKDYK HHCCCCHHHCHHHHH	22.13	29978859
97	Ubiquitination	FKEKDYKKAVISYTE HCHHHHHHHHHHHCH	41.47	29967540
107	Acetylation	ISYTEGLKKKCADPD HHHCHHHHHHCCCCC	62.13	26051181
107	Ubiquitination	ISYTEGLKKKCADPD HHHCHHHHHHCCCCC	62.13	29967540
128	Phosphorylation	TNRAAAQYYLGNFRS CCHHHHHHHHHCHHH	8.91	28152594
129	Phosphorylation	NRAAAQYYLGNFRSA CHHHHHHHHHCHHHH	8.96	28152594
160	Glutathionylation	AIIRGALCHLELKHF HHHHHHHHHHHHHHH	3.22	22555962
174	Glutathionylation	FAEAVNWCDEGLQID HHHHHHHHHHCCCCC	2.62	22555962
198	Ubiquitination	RAKADKLKRIEQRDV HHHHHHHHHHHHHHH	58.01	24816145
213	Ubiquitination	RKANLKEKKERNQNE HHHHHHHHHHHCHHH	59.35	24816145
227	Ubiquitination	EALLQAIKARNIRLS HHHHHHHHHHCCCHH	44.29	21963094
227	Acetylation	EALLQAIKARNIRLS HHHHHHHHHHCCCHH	44.29	19608861
234	Phosphorylation	KARNIRLSEAACEDE HHHCCCHHHHHHCCC	18.49	28464451
238	Glutathionylation	IRLSEAACEDEDSAS CCHHHHHHCCCCHHC	9.74	22555962
243	Phosphorylation	AACEDEDSASEGLGE HHHCCCCHHCCCCHH	31.48	25159151
245	Phosphorylation	CEDEDSASEGLGELF HCCCCHHCCCCHHHH	35.83	21712546
257	Phosphorylation	ELFLDGLSTENPHGA HHHHHCCCCCCCCCC	38.92	20873877
258	Phosphorylation	LFLDGLSTENPHGAR HHHHCCCCCCCCCCC	44.84	20873877
267	Phosphorylation	NPHGARLSLDGQGRL CCCCCCCCCCCCCCC	20.89	25159151
334	Methylation	VYFEDEDRAELYRVP EEECCCCHHHHEECC	28.10	115919101
343	Ubiquitination	ELYRVPAKSTLLQVL HHEECCCHHHHHHHH	37.59	-
367	S-nitrosylation	LTPAFLVCVGSSPFC HCHHHEEECCCCHHH	2.89	19483679
367	S-nitrosocysteine	LTPAFLVCVGSSPFC HCHHHEEECCCCHHH	2.89	-
374	S-nitrosylation	CVGSSPFCKNFLRGR ECCCCHHHHHHHCCC	3.90	19483679
374	S-nitrosocysteine	CVGSSPFCKNFLRGR ECCCCHHHHHHHCCC	3.90	-

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 TTC4_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of TTC4_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 TTC4_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RN219_HUMAN	RNF219	physical	17353931
VPS35_HUMAN	VPS35	physical	22939629
VIGLN_HUMAN	HDLBP	physical	22939629
VPS36_HUMAN	VPS36	physical	22939629
VP26A_HUMAN	VPS26A	physical	22939629
UBE2S_HUMAN	UBE2S	physical	22939629
CHAP1_HUMAN	CHAMP1	physical	22939629
TXLNG_HUMAN	TXLNG	physical	22939629
VPS29_HUMAN	VPS29	physical	22939629
HGS_HUMAN	HGS	physical	22863883
SLK_HUMAN	SLK	physical	22863883
HS90A_HUMAN	HSP90AA1	physical	25036637
CHRD1_HUMAN	CHORDC1	physical	25036637
HS90B_HUMAN	HSP90AB1	physical	25036637
CDC37_HUMAN	CDC37	physical	25036637
ACD11_HUMAN	ACAD11	physical	25036637
HGH1_HUMAN	HGH1	physical	25036637
EDRF1_HUMAN	EDRF1	physical	25036637
TMOD4_HUMAN	TMOD4	physical	25036637
AHSA1_HUMAN	AHSA1	physical	25036637
GCC2_HUMAN	GCC2	physical	26186194
EDRF1_HUMAN	EDRF1	physical	26186194
HGH1_HUMAN	HGH1	physical	26186194
PYRG1_HUMAN	CTPS1	physical	26344197
HAT1_HUMAN	HAT1	physical	26344197
PCID2_HUMAN	PCID2	physical	26344197
TLN2_HUMAN	TLN2	physical	26344197
UBE4B_HUMAN	UBE4B	physical	26344197
VP26A_HUMAN	VPS26A	physical	26344197
VPS29_HUMAN	VPS29	physical	26344197
VPS35_HUMAN	VPS35	physical	26344197
GCC2_HUMAN	GCC2	physical	28514442
EDRF1_HUMAN	EDRF1	physical	28514442
HGH1_HUMAN	HGH1	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 TTC4_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.	19413330 [Abstract]
"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-227, 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-243 AND SER-267, ANDMASS SPECTROMETRY.	18669648 [Abstract]