dbPTM

TNNI3_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	TNNI3_HUMAN
UniProt AC	P19429
Protein Name	Troponin I, cardiac muscle
Gene Name	TNNI3
Organism	Homo sapiens (Human).
Sequence Length	210
Subcellular Localization
Protein Description	Troponin I is the inhibitory subunit of troponin, the thin filament regulatory complex which confers calcium-sensitivity to striated muscle actomyosin ATPase activity..
Protein Sequence	MADGSSDAAREPRPAPAPIRRRSSNYRAYATEPHAKKKSKISASRKLQLKTLLLQIAKQELEREAEERRGEKGRALSTRCQPLELAGLGFAELQDLCRQLHARVDKVDEERYDIEAKVTKNITEIADLTQKIFDLRGKFKRPTLRRVRISADAMMQALLGARAKESLDLRAHLKQVKKEDTEKENREVGDWRKNIDALSGMEGRKKKFES

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MADGSSDAA ------CCCCCCCCC	29.85	2226863
5	Phosphorylation	---MADGSSDAAREP ---CCCCCCCCCCCC	26.12	22972900
6	Phosphorylation	--MADGSSDAAREPR --CCCCCCCCCCCCC	36.48	22972900
23	Phosphorylation	PAPIRRRSSNYRAYA CCCCCCCCCCCCEEC	22.56	9346285
24	Phosphorylation	APIRRRSSNYRAYAT CCCCCCCCCCCEECC	35.75	9346285
26	Phosphorylation	IRRRSSNYRAYATEP CCCCCCCCCEECCCC	9.89	22972900
29	Phosphorylation	RSSNYRAYATEPHAK CCCCCCEECCCCCCC	12.69	-
31	Phosphorylation	SNYRAYATEPHAKKK CCCCEECCCCCCCCC	37.06	22817900
31	O-linked_Glycosylation	SNYRAYATEPHAKKK CCCCEECCCCCCCCC	37.06	30379171
39	Phosphorylation	EPHAKKKSKISASRK CCCCCCCCCCCHHHH	44.06	22817900
40	Methylation	PHAKKKSKISASRKL CCCCCCCCCCHHHHH	49.95	-
40	Trimethylation	PHAKKKSKISASRKL CCCCCCCCCCHHHHH	49.95	-
42	Phosphorylation	AKKKSKISASRKLQL CCCCCCCCHHHHHHH	24.75	2584239
44	Phosphorylation	KKSKISASRKLQLKT CCCCCCHHHHHHHHH	24.13	2584239
51	Phosphorylation	SRKLQLKTLLLQIAK HHHHHHHHHHHHHHH	31.09	22817900
72	Acetylation	AEERRGEKGRALSTR HHHHHCHHHHHHHHC	57.42	30593035
77	Phosphorylation	GEKGRALSTRCQPLE CHHHHHHHHCCCHHH	16.90	2584239
78	Phosphorylation	EKGRALSTRCQPLEL HHHHHHHHCCCHHHH	35.99	22817900
112	Phosphorylation	DKVDEERYDIEAKVT HCCCHHHHCHHHHHC	25.26	22985185
119	Phosphorylation	YDIEAKVTKNITEIA HCHHHHHCCCHHHHH	20.05	22985185
129	Phosphorylation	ITEIADLTQKIFDLR HHHHHHHHHHHHHHC	28.50	22817900
143	Phosphorylation	RGKFKRPTLRRVRIS CCCCCCCCHHHHEEC	36.61	2584239
150	Phosphorylation	TLRRVRISADAMMQA CHHHHEECHHHHHHH	14.99	12242269
166	Phosphorylation	LGARAKESLDLRAHL HHHHHHHHHHHHHHH	26.86	22817900
177	Acetylation	RAHLKQVKKEDTEKE HHHHHHHHHHHHHHH	48.20	7297799
178	Acetylation	AHLKQVKKEDTEKEN HHHHHHHHHHHHHHH	63.06	7297815
181	Phosphorylation	KQVKKEDTEKENREV HHHHHHHHHHHHHCH	50.47	22972900
199	Phosphorylation	RKNIDALSGMEGRKK HHHHHHHCCCCCHHH	37.50	9241277

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
23	S	Phosphorylation	Kinase	PRKAA1	Q13131	GPS
23	S	Phosphorylation	Kinase	PKA_GROUP	-	PhosphoELM
23	S	Phosphorylation	Kinase	PKA	-	Uniprot
23	S	Phosphorylation	Kinase	PKD-FAMILY	-	GPS
23	S	Phosphorylation	Kinase	PRKACA	P17612	GPS
23	S	Phosphorylation	Kinase	PKA-FAMILY	-	GPS
23	S	Phosphorylation	Kinase	PRKD1	Q15139	Uniprot
23	S	Phosphorylation	Kinase	PRKCA	P17252	GPS
23	S	Phosphorylation	Kinase	PRKCD	Q05655	GPS
24	S	Phosphorylation	Kinase	PRKAA1	Q13131	GPS
24	S	Phosphorylation	Kinase	PKA_GROUP	-	PhosphoELM
24	S	Phosphorylation	Kinase	PKA	-	Uniprot
24	S	Phosphorylation	Kinase	PKD-FAMILY	-	GPS
24	S	Phosphorylation	Kinase	PKA-FAMILY	-	GPS
24	S	Phosphorylation	Kinase	PRKD1	Q15139	Uniprot
24	S	Phosphorylation	Kinase	PRKCD	Q05655	GPS
24	S	Phosphorylation	Kinase	PRKCA	P17252	GPS
24	S	Phosphorylation	Kinase	PRKACA	P17612	GPS
26	Y	Phosphorylation	Kinase	PKA-FAMILY	-	GPS
31	T	Phosphorylation	Kinase	MST1	P26927	Uniprot
31	T	Phosphorylation	Kinase	STK4	Q13043	GPS
39	S	Phosphorylation	Kinase	PRKACA	P17612	GPS
42	S	Phosphorylation	Kinase	PRKCA	P17252	GPS
42	S	Phosphorylation	Kinase	PRKCE	Q02156	Uniprot
44	S	Phosphorylation	Kinase	PRKCA	P17252	GPS
44	S	Phosphorylation	Kinase	KPCE	Q02156	PhosphoELM
51	T	Phosphorylation	Kinase	STK4	Q13043	GPS
51	T	Phosphorylation	Kinase	MST1	P26927	Uniprot
129	T	Phosphorylation	Kinase	MST1	P26927	Uniprot
129	T	Phosphorylation	Kinase	STK4	Q13043	GPS
143	T	Phosphorylation	Kinase	MST1	P26927	Uniprot
143	T	Phosphorylation	Kinase	STK4	Q13043	GPS
143	T	Phosphorylation	Kinase	PRKCD	Q05655	GPS
143	T	Phosphorylation	Kinase	PRKCA	P17252	GPS
150	S	Phosphorylation	Kinase	PRKAA1	Q13131	GPS
150	S	Phosphorylation	Kinase	PAK3	O75914	Uniprot
166	S	Phosphorylation	Kinase	PRKACA	P17612	GPS
199	S	Phosphorylation	Kinase	PKD-FAMILY	-	GPS
199	S	Phosphorylation	Kinase	PRKCA	P17252	GPS
-	K	Ubiquitination	E3 ubiquitin ligase	TRIM63	Q969Q1	PMID:15601779
-	K	Ubiquitination	E3 ubiquitin ligase	FBXO32	Q969P5	PMID:22199232

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
23	S	Phosphorylation	2226863
Phosphorylated at Ser-23 and Ser-24 by PRKD1; phosphorylation reduces myofilament calcium sensitivity.
24	S	Phosphorylation	2226863
Phosphorylated at Ser-23 and Ser-24 by PRKD1; phosphorylation reduces myofilament calcium sensitivity.
31	T	Phosphorylation	18986304
Phosphorylated preferentially at Thr-31.
42	S	Phosphorylation	22972900
Phosphorylated at Ser-42 and Ser-44 by PRKCE; phosphorylation increases myocardium contractile dysfunction (By similarity).
44	S	Phosphorylation	22972900
Phosphorylated at Ser-42 and Ser-44 by PRKCE; phosphorylation increases myocardium contractile dysfunction (By similarity).

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 TNNI3_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
TNNC1_HUMAN	TNNC1	physical	15134451
TNNC1_HUMAN	TNNC1	physical	15049709
TNI3K_HUMAN	TNNI3K	physical	12721663
PKD2_HUMAN	PKD2	physical	12525172
TNNT2_HUMAN	TNNT2	physical	11904166
IFNA4_HUMAN	IFNA4	physical	28514442
HGFL_HUMAN	MST1	physical	18986304
TNNC1_HUMAN	TNNC1	physical	18986304
TNNT2_HUMAN	TNNT2	physical	18986304

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
613690	Cardiomyopathy, familial hypertrophic 7 (CMH7)
115210	Cardiomyopathy, familial restrictive 1 (RCM1)
611880	Cardiomyopathy, dilated 2A (CMD2A)
613286	Cardiomyopathy, dilated 1FF (CMD1FF)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of TNNI3_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"A common motif of two adjacent phosphoserines in bovine, rabbit andhuman cardiac troponin I."; Mittmann K., Jaquet K., Heilmeyer L.M.G. Jr.; FEBS Lett. 273:41-45(1990). Cited for: PROTEIN SEQUENCE OF 11-36, ACETYLATION AT ALA-2, AND PHOSPHORYLATIONAT SER-23 AND SER-24.	2226863 [Abstract]
Phosphorylation
Reference	PubMed
"Protein kinase D is a novel mediator of cardiac troponin Iphosphorylation and regulates myofilament function."; Haworth R.S., Cuello F., Herron T.J., Franzen G., Kentish J.C.,Gautel M., Avkiran M.; Circ. Res. 95:1091-1099(2004). Cited for: PHOSPHORYLATION AT SER-23 AND SER-24.	15514163 [Abstract]
"p21-activated kinase increases the calcium sensitivity of rat triton-skinned cardiac muscle fiber bundles via a mechanism potentiallyinvolving novel phosphorylation of troponin I."; Buscemi N., Foster D.B., Neverova I., Van Eyk J.E.; Circ. Res. 91:509-516(2002). Cited for: PHOSPHORYLATION AT SER-150 BY PAK3.	12242269 [Abstract]
"The ordered phosphorylation of cardiac troponin I by the cAMP-dependent protein kinase -- structural consequences and functionalimplications."; Keane N.E., Quirk P.G., Gao Y., Patchell V.B., Perry S.V.,Levine B.A.; Eur. J. Biochem. 248:329-337(1997). Cited for: PHOSPHORYLATION AT SER-23 AND SER-24.	9346285 [Abstract]
"A common motif of two adjacent phosphoserines in bovine, rabbit andhuman cardiac troponin I."; Mittmann K., Jaquet K., Heilmeyer L.M.G. Jr.; FEBS Lett. 273:41-45(1990). Cited for: PROTEIN SEQUENCE OF 11-36, ACETYLATION AT ALA-2, AND PHOSPHORYLATIONAT SER-23 AND SER-24.	2226863 [Abstract]
"Phosphorylation of cardiac troponin I by mammalian sterile 20-likekinase 1."; You B., Yan G., Zhang Z., Yan L., Li J., Ge Q., Jin J.P., Sun J.; Biochem. J. 418:93-101(2009). Cited for: INTERACTION WITH STK4/MST1, AND PHOSPHORYLATION AT THR-31; THR-51;THR-129 AND THR-143.	18986304 [Abstract]

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