MYSP1_DROME - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: MYSP1_DROME
• UniProt AC: P35415
• Protein Name: Paramyosin, long form
• Gene Name: Prm
• Organism: Drosophila melanogaster (Fruit fly).
• Sequence Length: 879
• Subcellular Localization: Cytoplasm, myofibril. Thick filaments of the myofibrils.
• Protein Description: Paramyosin is a major structural component of many thick filaments isolated from invertebrate muscles..
• Protein Sequence: MSSSQAVRSSKYSYRATSTGPGTADVNIEYIQDLSSLSRLEDKIRLLQDDLEVERELRQRIEREKADLSVQVIQMSERLEEAEGGAEHQFEANRKRDAELLKLRKLLEDVHLESEETTLLLKKKHNEIITDFQEQVEILTKNKARAEKDKAKFQTEVYELLSQIESYNKEKIVSEKHISKLEVSISELNVKIEELNRTVIDISSHRSRLSQENIELTKDVQDLKVQLDTVSFSKSQVISQLEDARRRLEDEDRRRSLLESSLHQVEIELDSVRNQLEEESEARIDLERQLVKANADATSWQNKWNSEVAARAEEVEEIRRKYQVRITELEEHIESLIVKVNNLEKMKTRLASEVEVLIIDLEKSNNSCRELTKSVNTLEKHNVELKSRLDETIILYETSQRDLKNKHADLVRTVHELDKVKDNNNQLTRENKKLGDDLHEAKGAINELNRRLHELELELRRLENERDELTAAYKEAEAGRKAEEQRGQRLAADFNQYRHDAERRLAEKDEEIEAIRKQTSIEIEQLNARVIEAETRLKTEVTRIKKKLQIQITELEMSLDVANKTNIDLQKVIKKQSLQLTELQAHYEDVQRQLQATLDQYAVAQRRLAGLNGELEEVRSHLDSANRAKRTVELQYEEAASRINELTTANVSLVSIKSKLEQELSVVASDYEEVSKELRISDERYQKVQVELKHVVEQVHEEQERIVKLETIKKSLEVEVKNLSIRLEEVELNAVAGSKRIISKLEARIRDLELELEEEKRRHAETIKILRKKERTVKEVLVQCEEDQKNLILLQDALDKSTAKINIYRRQLSEQEGVSQQTTTRVRRFQRELEAAEDRADTAESSLNIIRAKHRTFVTTSTVPGSQVYIQETTRTITE

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MSSSQAVRS ------CCHHHHHHH	38.40	27794539
3	Phosphorylation	-----MSSSQAVRSS -----CCHHHHHHHC	25.77	27794539
4	Phosphorylation	----MSSSQAVRSSK ----CCHHHHHHHCC	18.17	27794539
9	Phosphorylation	SSSQAVRSSKYSYRA CHHHHHHHCCCEEEE	25.28	27794539
10	Phosphorylation	SSQAVRSSKYSYRAT HHHHHHHCCCEEEEC	25.67	27794539
17	Phosphorylation	SKYSYRATSTGPGTA CCCEEEECCCCCCCC	20.16	28490779
18	Phosphorylation	KYSYRATSTGPGTAD CCEEEECCCCCCCCC	30.31	28490779
19	Phosphorylation	YSYRATSTGPGTADV CEEEECCCCCCCCCC	42.94	28490779
23	Phosphorylation	ATSTGPGTADVNIEY ECCCCCCCCCCCEEE	23.87	28490779
231	Phosphorylation	KVQLDTVSFSKSQVI HEEEEECCCCHHHHH	26.37	27794539
233	Phosphorylation	QLDTVSFSKSQVISQ EEEECCCCHHHHHHH	24.72	27794539
374	Phosphorylation	SCRELTKSVNTLEKH CHHHHHHHHHHHHHC	18.50	27794539
652	Phosphorylation	ELTTANVSLVSIKSK HHHCCCEEEEEHHHH	23.90	28490779
665	Phosphorylation	SKLEQELSVVASDYE HHHHHHHHHHHCCHH	17.50	27794539
669	Phosphorylation	QELSVVASDYEEVSK HHHHHHHCCHHHHHH	29.17	27794539

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of MYSP1_DROME !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of MYSP1_DROME !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of MYSP1_DROME !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RU17_DROME	snRNP-U1-70K	physical	14605208
MYSA_DROME	Mhc	physical	22036573
TPM2_DROME	Tm2	physical	22036573
TNNT_DROME	up	physical	22036573
TNNI_DROME	wupA	physical	22036573
TNNC1_DROME	TpnC41C	physical	22036573
ATC1_DROME	Ca-P60A	physical	22036573
ATP5J_DROME	ATPsyn-Cf6	physical	22036573
OB56D_DROME	Obp56d	physical	22036573
ICLN_DROME	icln	physical	22036573
IDH3A_DROME	l(1)G0156	physical	22036573
NPLP2_DROME	Nplp2	physical	22036573
OVO_DROME	ovo	physical	25242320
CISY_DROME	kdn	physical	22036573

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Phosphorylation

"Phosphoproteome analysis of Drosophila melanogaster embryos.";
Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
J. Proteome Res. 7:1675-1682(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18, AND MASSSPECTROMETRY.
PubMed: 18327897