dbPTM

MYPC2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	MYPC2_HUMAN
UniProt AC	Q14324
Protein Name	Myosin-binding protein C, fast-type
Gene Name	MYBPC2
Organism	Homo sapiens (Human).
Sequence Length	1141
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	MPEAKPAAKKAPKGKDAPKGAPKEAPPKEAPAEAPKEAPPEDQSPTAEEPTGVFLKKPDSVSVETGKDAVVVAKVNGKELPDKPTIKWFKGKWLELGSKSGARFSFKESHNSASNVYTVELHIGKVVLGDRGYYRLEVKAKDTCDSCGFNIDVEAPRQDASGQSLESFKRTSEKKSDTAGELDFSGLLKKREVVEEEKKKKKKDDDDLGIPPEIWELLKGAKKSEYEKIAFQYGITDLRGMLKRLKKAKVEVKKSAAFTKKLDPAYQVDRGNKIKLMVEISDPDLTLKWFKNGQEIKPSSKYVFENVGKKRILTINKCTLADDAAYEVAVKDEKCFTELFVKEPPVLIVTPLEDQQVFVGDRVEMAVEVSEEGAQVMWMKDGVELTREDSFKARYRFKKDGKRHILIFSDVVQEDRGRYQVITNGGQCEAELIVEEKQLEVLQDIADLTVKASEQAVFKCEVSDEKVTGKWYKNGVEVRPSKRITISHVGRFHKLVIDDVRPEDEGDYTFVPDGYALSLSAKLNFLEIKVEYVPKQEPPKIHLDCSGKTSENAIVVVAGNKLRLDVSITGEPPPVATWLKGDEVFTTTEGRTRIEKRVDCSSFVIESAQREDEGRYTIKVTNPVGEDVASIFLQVVDVPDPPEAVRITSVGEDWAILVWEPPMYDGGKPVTGYLVERKKKGSQRWMKLNFEVFTETTYESTKMIEGILYEMRVFAVNAIGVSQPSMNTKPFMPIAPTSEPLHLIVEDVTDTTTTLKWRPPNRIGAGGIDGYLVEYCLEGSEEWVPANTEPVERCGFTVKNLPTGARILFRVVGVNIAGRSEPATLAQPVTIREIAEPPKIRLPRHLRQTYIRKVGEQLNLVVPFQGKPRPQVVWTKGGAPLDTSRVHVRTSDFDTVFFVRQAARSDSGEYELSVQIENMKDTATIRIRVVEKAGPPINVMVKEVWGTNALVEWQAPKDDGNSEIMGYFVQKADKKTMEWFNVYERNRHTSCTVSDLIVGNEYYFRVYTENICGLSDSPGVSKNTARILKTGITFKPFEYKEHDFRMAPKFLTPLIDRVVVAGYSAALNCAVRGHPKPKVVWMKNKMEIREDPKFLITNYQGVLTLNIRRPSPFDAGTYTCRAVNELGEALAECKLEVRVPQ

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
44	Phosphorylation	EAPPEDQSPTAEEPT CCCCCCCCCCCCCCC	36.22	19764811
46	Phosphorylation	PPEDQSPTAEEPTGV CCCCCCCCCCCCCEE	52.53	19764811
60	Phosphorylation	VFLKKPDSVSVETGK EEECCCCCEEEEECC	25.48	26437602
62	Phosphorylation	LKKPDSVSVETGKDA ECCCCCEEEEECCCE	20.42	26437602
98	Phosphorylation	GKWLELGSKSGARFS CCEEECCCCCCCEEE	35.95	26437602
105	Phosphorylation	SKSGARFSFKESHNS CCCCCEEEEECCCCC	29.83	23927012
112	Phosphorylation	SFKESHNSASNVYTV EEECCCCCCCCEEEE	27.87	26437602
114	Phosphorylation	KESHNSASNVYTVEL ECCCCCCCCEEEEEE	27.01	26437602
118	Phosphorylation	NSASNVYTVELHIGK CCCCCEEEEEEEEEE	11.83	26437602
167	Phosphorylation	ASGQSLESFKRTSEK CCCCCHHHHHCCCCC	41.16	26437602
223	Acetylation	ELLKGAKKSEYEKIA HHHHCCCHHHHHHHH	48.24	30590527
228	Acetylation	AKKSEYEKIAFQYGI CCHHHHHHHHHHHCC	38.13	30590533
249	Acetylation	LKRLKKAKVEVKKSA HHHHHHCCCEECCCH	48.05	19813251
300	Phosphorylation	GQEIKPSSKYVFENV CEECCCCCCEEEEEC	36.21	26437602
409	Phosphorylation	KRHILIFSDVVQEDR CEEEEEEECCEECCC	23.62	22673903
468	Phosphorylation	EVSDEKVTGKWYKNG EECCCCCCCEEEECC	44.08	26437602
472	Phosphorylation	EKVTGKWYKNGVEVR CCCCCEEEECCEEEC	9.69	-
481	Phosphorylation	NGVEVRPSKRITISH CCEEECCCCCEEECC	24.81	26437602
487	Phosphorylation	PSKRITISHVGRFHK CCCCEEECCCCCEEE	11.94	24719451
546	Phosphorylation	PKIHLDCSGKTSENA CCEEEECCCCCCCCE	42.88	26437602
587	Phosphorylation	KGDEVFTTTEGRTRI CCCEEEECCCCCCEE	16.04	26437602
722	Phosphorylation	AVNAIGVSQPSMNTK EEEEECCCCCCCCCC	31.03	-
820	Phosphorylation	GVNIAGRSEPATLAQ CEECCCCCCCCCCCC	47.19	26437602
830	Phosphorylation	ATLAQPVTIREIAEP CCCCCCEEHHHHCCC	22.47	26437602
849	Phosphorylation	LPRHLRQTYIRKVGE CCHHHHHHHHHHHHH	17.93	24719451
850	Phosphorylation	PRHLRQTYIRKVGEQ CHHHHHHHHHHHHHH	7.15	26437602
883	Phosphorylation	KGGAPLDTSRVHVRT ECCCCCCCCEEEEEC	26.56	26437602
884	Phosphorylation	GGAPLDTSRVHVRTS CCCCCCCCEEEEECC	31.78	26437602
924	Phosphorylation	ENMKDTATIRIRVVE ECCCCCEEEEEEEEE	16.93	26437602
962	Phosphorylation	APKDDGNSEIMGYFV CCCCCCCCCEEEEEE	33.75	-
967	Phosphorylation	GNSEIMGYFVQKADK CCCCEEEEEEEECCH	5.34	-
989	Phosphorylation	VYERNRHTSCTVSDL HHHHCCCCCCCHHHE	23.43	26437602
1003	Phosphorylation	LIVGNEYYFRVYTEN EEECCEEEEEEEECC	4.44	-
1007	Phosphorylation	NEYYFRVYTENICGL CEEEEEEEECCCCCC	12.22	-
1015	Phosphorylation	TENICGLSDSPGVSK ECCCCCCCCCCCCCH	22.71	-
1017	Phosphorylation	NICGLSDSPGVSKNT CCCCCCCCCCCCHHH	21.85	26437602
1078	Ubiquitination	VRGHPKPKVVWMKNK HCCCCCCCEEEECCC	56.39	-
1085	"N6,N6-dimethyllysine"	KVVWMKNKMEIREDP CEEEECCCEECCCCC	32.18	-
1085	Methylation	KVVWMKNKMEIREDP CEEEECCCEECCCCC	32.18	-
1099	Phosphorylation	PKFLITNYQGVLTLN CCEEEECCCCEEEEE	9.67	-
1104	Phosphorylation	TNYQGVLTLNIRRPS ECCCCEEEEEECCCC	18.49	-
1111	Phosphorylation	TLNIRRPSPFDAGTY EEEECCCCCCCCCCC	36.07	26437602
1117	Phosphorylation	PSPFDAGTYTCRAVN CCCCCCCCCCHHHHH	19.85	24043423
1118	Phosphorylation	SPFDAGTYTCRAVNE CCCCCCCCCHHHHHH	11.70	24043423
1119	Phosphorylation	PFDAGTYTCRAVNEL CCCCCCCCHHHHHHH	8.71	24043423

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
-	K	Ubiquitination	E3 ubiquitin ligase	TRIM63	Q969Q1	PMID:17314137

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of MYPC2_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 MYPC2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of MYPC2_HUMAN !!

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 MYPC2_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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-105, AND MASSSPECTROMETRY.	17081983 [Abstract]