dbPTM

MYPC3_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	MYPC3_HUMAN
UniProt AC	Q14896
Protein Name	Myosin-binding protein C, cardiac-type
Gene Name	MYBPC3
Organism	Homo sapiens (Human).
Sequence Length	1274
Subcellular Localization
Protein Description	Thick filament-associated protein located in the crossbridge region of vertebrate striated muscle a bands. In vitro it binds MHC, F-actin and native thin filaments, and modifies the activity of actin-activated myosin ATPase. It may modulate muscle contraction or may play a more structural role..
Protein Sequence	MPEPGKKPVSAFSKKPRSVEVAAGSPAVFEAETERAGVKVRWQRGGSDISASNKYGLATEGTRHTLTVREVGPADQGSYAVIAGSSKVKFDLKVIEAEKAEPMLAPAPAPAEATGAPGEAPAPAAELGESAPSPKGSSSAALNGPTPGAPDDPIGLFVMRPQDGEVTVGGSITFSARVAGASLLKPPVVKWFKGKWVDLSSKVGQHLQLHDSYDRASKVYLFELHITDAQPAFTGSYRCEVSTKDKFDCSNFNLTVHEAMGTGDLDLLSAFRRTSLAGGGRRISDSHEDTGILDFSSLLKKRDSFRTPRDSKLEAPAEEDVWEILRQAPPSEYERIAFQYGVTDLRGMLKRLKGMRRDEKKSTAFQKKLEPAYQVSKGHKIRLTVELADHDAEVKWLKNGQEIQMSGSKYIFESIGAKRTLTISQCSLADDAAYQCVVGGEKCSTELFVKEPPVLITRPLEDQLVMVGQRVEFECEVSEEGAQVKWLKDGVELTREETFKYRFKKDGQRHHLIINEAMLEDAGHYALCTSGGQALAELIVQEKKLEVYQSIADLMVGAKDQAVFKCEVSDENVRGVWLKNGKELVPDSRIKVSHIGRVHKLTIDDVTPADEADYSFVPEGFACNLSAKLHFMEVKIDFVPRQEPPKIHLDCPGRIPDTIVVVAGNKLRLDVPISGDPAPTVIWQKAITQGNKAPARPAPDAPEDTGDSDEWVFDKKLLCETEGRVRVETTKDRSIFTVEGAEKEDEGVYTVTVKNPVGEDQVNLTVKVIDVPDAPAAPKISNVGEDSCTVQWEPPAYDGGQPILGYILERKKKKSYRWMRLNFDLIQELSHEARRMIEGVVYEMRVYAVNAIGMSRPSPASQPFMPIGPPSEPTHLAVEDVSDTTVSLKWRPPERVGAGGLDGYSVEYCPEGCSEWVAALQGLTEHTSILVKDLPTGARLLFRVRAHNMAGPGAPVTTTEPVTVQEILQRPRLQLPRHLRQTIQKKVGEPVNLLIPFQGKPRPQVTWTKEGQPLAGEEVSIRNSPTDTILFIRAARRVHSGTYQVTVRIENMEDKATLVLQVVDKPSPPQDLRVTDAWGLNVALEWKPPQDVGNTELWGYTVQKADKKTMEWFTVLEHYRRTHCVVPELIIGNGYYFRVFSQNMVGFSDRAATTKEPVFIPRPGITYEPPNYKALDFSEAPSFTQPLVNRSVIAGYTAMLCCAVRGSPKPKISWFKNGLDLGEDARFRMFSKQGVLTLEIRKPCPFDGGIYVCRATNLQGEARCECRLEVRVPQ

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MPEPGKKP -------CCCCCCCC	38.36	-
10	Phosphorylation	EPGKKPVSAFSKKPR CCCCCCCCCCCCCCC	31.93	21406692
13	Phosphorylation	KKPVSAFSKKPRSVE CCCCCCCCCCCCCEE	39.21	21406692
18	Phosphorylation	AFSKKPRSVEVAAGS CCCCCCCCEEECCCC	31.02	-
47	Phosphorylation	VRWQRGGSDISASNK EEEECCCCCCCCCCC	34.30	-
59	Phosphorylation	SNKYGLATEGTRHTL CCCCEECCCCCCCEE	39.73	-
78	Phosphorylation	VGPADQGSYAVIAGS ECCCCCCCEEEEECC	12.32	22210691
79	Phosphorylation	GPADQGSYAVIAGSS CCCCCCCEEEEECCC	16.23	22210691
85	Phosphorylation	SYAVIAGSSKVKFDL CEEEEECCCEEEEEE	20.26	22210691
86	Phosphorylation	YAVIAGSSKVKFDLK EEEEECCCEEEEEEE	40.32	22210691
133	Phosphorylation	ELGESAPSPKGSSSA HCCCCCCCCCCCCCC	38.67	-
137	Phosphorylation	SAPSPKGSSSAALNG CCCCCCCCCCCHHCC	27.52	22210691
146	Phosphorylation	SAALNGPTPGAPDDP CCHHCCCCCCCCCCC	35.43	22210691
167	Phosphorylation	RPQDGEVTVGGSITF CCCCCCEEECCEEEE	14.77	21406692
171	Phosphorylation	GEVTVGGSITFSARV CCEEECCEEEEEEEE	16.72	21406692
173	Phosphorylation	VTVGGSITFSARVAG EEECCEEEEEEEEEC	17.15	21406692
175	Phosphorylation	VGGSITFSARVAGAS ECCEEEEEEEEECHH	13.40	21406692
182	Phosphorylation	SARVAGASLLKPPVV EEEEECHHHCCCCEE	33.06	24719451
212	Phosphorylation	QHLQLHDSYDRASKV HHHEEECCCCCCCCE	20.41	-
213	Phosphorylation	HLQLHDSYDRASKVY HHEEECCCCCCCCEE	18.59	-
269	Phosphorylation	TGDLDLLSAFRRTSL CCCHHHHHHHHHHCC	32.43	24719451
274	Phosphorylation	LLSAFRRTSLAGGGR HHHHHHHHCCCCCCC	24.68	-
275	Phosphorylation	LSAFRRTSLAGGGRR HHHHHHHCCCCCCCC	17.89	20151718
284	Phosphorylation	AGGGRRISDSHEDTG CCCCCCCCCCCCCCC	31.11	22281395
286	Phosphorylation	GGRRISDSHEDTGIL CCCCCCCCCCCCCCC	23.22	-
290	Phosphorylation	ISDSHEDTGILDFSS CCCCCCCCCCCCHHH	24.12	-
297	Phosphorylation	TGILDFSSLLKKRDS CCCCCHHHHHHCCCC	37.40	24719451
304	Phosphorylation	SLLKKRDSFRTPRDS HHHHCCCCCCCCCCC	26.32	20151718
307	Phosphorylation	KKRDSFRTPRDSKLE HCCCCCCCCCCCCCC	22.21	-
311	Phosphorylation	SFRTPRDSKLEAPAE CCCCCCCCCCCCCCH	40.18	20151718
340	Phosphorylation	YERIAFQYGVTDLRG HHHHHHHHCCHHHHH	13.70	-
373	Phosphorylation	QKKLEPAYQVSKGHK HHHCCCEEECCCCCE	21.84	17322306
418	Acetylation	IFESIGAKRTLTISQ EHHHCCCCEEEEEEE	34.14	30590539
424	Phosphorylation	AKRTLTISQCSLADD CCEEEEEEECCCCCC	19.57	-
427	Phosphorylation	TLTISQCSLADDAAY EEEEEECCCCCCCEE	8.78	-
548	Phosphorylation	QEKKLEVYQSIADLM HHHHHHHHHHHHHHH	33.27	-
550	Phosphorylation	KKLEVYQSIADLMVG HHHHHHHHHHHHHCC	1.72	-
588	Phosphorylation	GKELVPDSRIKVSHI CCEECCCCCEEEEEE	39.88	-
602	Phosphorylation	IGRVHKLTIDDVTPA ECCEEEEEECCCCCC	6.53	-
607	Phosphorylation	KLTIDDVTPADEADY EEEECCCCCCCCCCC	37.25	-
708	Phosphorylation	APEDTGDSDEWVFDK CCCCCCCCCCCEECE	59.52	-
830	Phosphorylation	FDLIQELSHEARRMI HHHHHHHCHHHHHHH	45.41	-
1043	Phosphorylation	RRVHSGTYQVTVRIE HHCCCEEEEEEEEEE	25.01	-
1046	Phosphorylation	HSGTYQVTVRIENME CCEEEEEEEEEECCC	6.44	24719451
1067	Phosphorylation	LQVVDKPSPPQDLRV EEEECCCCCCCCEEE	38.81	-
1119	Phosphorylation	WFTVLEHYRRTHCVV HHHHHHHHHHHEEEE	38.64	-
1135	Phosphorylation	ELIIGNGYYFRVFSQ EEEECCCEEEEEEEC	6.06	-
1136	Phosphorylation	LIIGNGYYFRVFSQN EEECCCEEEEEEECC	3.96	-
1167	Phosphorylation	IPRPGITYEPPNYKA ECCCCCCCCCCCCCC	45.70	-
1172	Phosphorylation	ITYEPPNYKALDFSE CCCCCCCCCCCCCCC	49.46	-
1213	Phosphorylation	GSPKPKISWFKNGLD CCCCCCCCCCCCCCC	16.23	29496963
1237	Phosphorylation	FSKQGVLTLEIRKPC CCCCCEEEEEECCCC	4.50	23312004
1241	Methylation	GVLTLEIRKPCPFDG CEEEEEECCCCCCCC	57.54	-

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
133	S	Phosphorylation	Kinase	GSK3B	P49841	PSP
275	S	Phosphorylation	Kinase	PKA-FAMILY	-	GPS
275	S	Phosphorylation	Kinase	PKA_GROUP	-	PhosphoELM
275	S	Phosphorylation	Kinase	PKC	-	Uniprot
275	S	Phosphorylation	Kinase	PKA	-	Uniprot
275	S	Phosphorylation	Kinase	PRKACA	P17612	GPS
284	S	Phosphorylation	Kinase	PKA-FAMILY	-	GPS
284	S	Phosphorylation	Kinase	PKA	-	Uniprot
284	S	Phosphorylation	Kinase	PKC	-	Uniprot
284	S	Phosphorylation	Kinase	PRKACA	P17612	GPS
284	S	Phosphorylation	Kinase	PKA_GROUP	-	PhosphoELM
304	S	Phosphorylation	Kinase	PRKACA	P17612	GPS
304	S	Phosphorylation	Kinase	PRKD1	Q15139	PSP
304	S	Phosphorylation	Kinase	PKA-FAMILY	-	GPS
304	S	Phosphorylation	Kinase	GSK3B	P49841	PSP
304	S	Phosphorylation	Kinase	PKA	-	Uniprot
304	S	Phosphorylation	Kinase	PKC	-	Uniprot
304	S	Phosphorylation	Kinase	PKA_GROUP	-	PhosphoELM
311	S	Phosphorylation	Kinase	PKA-FAMILY	-	GPS
311	S	Phosphorylation	Kinase	PRKACA	P17612	GPS
311	S	Phosphorylation	Kinase	PKA_GROUP	-	PhosphoELM
-	K	Ubiquitination	E3 ubiquitin ligase	TRIM63	Q969Q1	PMID:19506036
-	K	Ubiquitination	E3 ubiquitin ligase	FBXO32	Q969P5	PMID:19850579

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of MYPC3_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 MYPC3_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
TRI63_HUMAN	TRIM63	physical	19850579

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
115197	Cardiomyopathy, familial hypertrophic 4 (CMH4)
615396	Cardiomyopathy, dilated 1MM (CMD1MM)
615396	Left ventricular non-compaction 10 (LVNC10)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of MYPC3_HUMAN

Related Literatures of Post-Translational Modification