dbPTM

ACTS_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ACTS_MOUSE
UniProt AC	P68134
Protein Name	Actin, alpha skeletal muscle
Gene Name	Acta1
Organism	Mus musculus (Mouse).
Sequence Length	377
Subcellular Localization	Cytoplasm, cytoskeleton.
Protein Description	Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells..
Protein Sequence	MCDEDETTALVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIITNWDDMEKIWHHTFYNELRVAPEEHPTLLTEAPLNPKANREKMTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPIYEGYALPHAIMRLDLAGRDLTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFENEMATAASSSSLEKSYELPDGQVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNVMSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWITKQEYDEAGPSIVHRKCF

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MCDEDETTA ------CCCCCCCEE	8.68	-
3	Acetylation	-----MCDEDETTAL -----CCCCCCCEEE	66.15	-
7	Phosphorylation	-MCDEDETTALVCDN -CCCCCCCEEEEEEC	29.68	61997751
8	Phosphorylation	MCDEDETTALVCDNG CCCCCCCEEEEEECC	18.88	22802335
35	Phosphorylation	APRAVFPSIVGRPRH CCCCCCHHHCCCCCC	20.59	26824392
46	Oxidation	RPRHQGVMVGMGQKD CCCCCCEEEECCCCC	2.49	23911929
49	Oxidation	HQGVMVGMGQKDSYV CCCEEEECCCCCCCC	3.32	23911929
52	Acetylation	VMVGMGQKDSYVGDE EEEECCCCCCCCCCH	42.80	132713
52	Ubiquitination	VMVGMGQKDSYVGDE EEEECCCCCCCCCCH	42.80	22790023
54	Phosphorylation	VGMGQKDSYVGDEAQ EECCCCCCCCCCHHH	28.84	25521595
55	Phosphorylation	GMGQKDSYVGDEAQS ECCCCCCCCCCHHHC	20.70	26824392
62	Phosphorylation	YVGDEAQSKRGILTL CCCCHHHCCCCEEEE	31.22	27087446
63	Malonylation	VGDEAQSKRGILTLK CCCHHHCCCCEEEEE	42.43	22790023
63	Ubiquitination	VGDEAQSKRGILTLK CCCHHHCCCCEEEEE	42.43	27667366
63	N6-malonyllysine	VGDEAQSKRGILTLK CCCHHHCCCCEEEEE	42.43	-
63	Acetylation	VGDEAQSKRGILTLK CCCHHHCCCCEEEEE	42.43	130499
68	Phosphorylation	QSKRGILTLKYPIEH HCCCCEEEEECEECC	21.20	27600695
70	Ubiquitination	KRGILTLKYPIEHGI CCCEEEEECEECCCC	43.69	22790023
70	Acetylation	KRGILTLKYPIEHGI CCCEEEEECEECCCC	43.69	130495
71	Phosphorylation	RGILTLKYPIEHGII CCEEEEECEECCCCC	16.74	26239621
75	Methylation	TLKYPIEHGIITNWD EEECEECCCCCCCHH	33.21	-
79	Phosphorylation	PIEHGIITNWDDMEK EECCCCCCCHHHHHH	28.47	36012721
86	Methylation	TNWDDMEKIWHHTFY CCHHHHHHHHHHHHH	44.45	-
86	Ubiquitination	TNWDDMEKIWHHTFY CCHHHHHHHHHHHHH	44.45	22790023
86	Acetylation	TNWDDMEKIWHHTFY CCHHHHHHHHHHHHH	44.45	71089
91	O-linked_Glycosylation	MEKIWHHTFYNELRV HHHHHHHHHHCCCCC	18.22	9548379
91	Phosphorylation	MEKIWHHTFYNELRV HHHHHHHHHHCCCCC	18.22	22499769
93	Phosphorylation	KIWHHTFYNELRVAP HHHHHHHHCCCCCCC	14.64	27742792
105	Phosphorylation	VAPEEHPTLLTEAPL CCCCCCCCCCCCCCC	35.99	28542873
108	Phosphorylation	EEHPTLLTEAPLNPK CCCCCCCCCCCCCCC	32.96	22210690
115	Ubiquitination	TEAPLNPKANREKMT CCCCCCCCCCHHHHH	58.16	22790023
143	Phosphorylation	VAIQAVLSLYASGRT HHHHHHHHHHHCCCC	16.85	19060867
145	Phosphorylation	IQAVLSLYASGRTTG HHHHHHHHHCCCCEE	8.71	36642107
147	Phosphorylation	AVLSLYASGRTTGIV HHHHHHHCCCCEEEE	18.43	-
150	Phosphorylation	SLYASGRTTGIVLDS HHHHCCCCEEEEEEC	32.66	22210690
151	Phosphorylation	LYASGRTTGIVLDSG HHHCCCCEEEEEECC	24.45	22210690
157	Phosphorylation	TTGIVLDSGDGVTHN CEEEEEECCCCCCCC	34.32	28542873
168	Phosphorylation	VTHNVPIYEGYALPH CCCCCCEECCCCHHH	9.38	28464351
171	Phosphorylation	NVPIYEGYALPHAIM CCCEECCCCHHHHHH	7.94	36642093
188	Phosphorylation	DLAGRDLTDYLMKIL HCCCCCHHHHHHHHH	27.21	24899341
190	Phosphorylation	AGRDLTDYLMKILTE CCCCHHHHHHHHHHH	11.94	2001175
193	Ubiquitination	DLTDYLMKILTERGY CHHHHHHHHHHHCCC	31.78	22790023
193	Acetylation	DLTDYLMKILTERGY CHHHHHHHHHHHCCC	31.78	22646671
196	Phosphorylation	DYLMKILTERGYSFV HHHHHHHHHCCCCCE	27.40	46158553
200	Phosphorylation	KILTERGYSFVTTAE HHHHHCCCCCEEHHC	12.73	36642141
201	Phosphorylation	ILTERGYSFVTTAER HHHHCCCCCEEHHCH	18.96	35093905
204	Phosphorylation	ERGYSFVTTAEREIV HCCCCCEEHHCHHHH	20.48	24899341
205	Phosphorylation	RGYSFVTTAEREIVR CCCCCEEHHCHHHHH	22.63	24899341
215	Acetylation	REIVRDIKEKLCYVA HHHHHHHHHHHCEEE	53.75	8276001
217	Ubiquitination	IVRDIKEKLCYVALD HHHHHHHHHCEEEEE	38.56	-
220	Phosphorylation	DIKEKLCYVALDFEN HHHHHHCEEEEECCH	10.13	24351
231	Phosphorylation	DFENEMATAASSSSL ECCHHHHHHCCCCCC	22.80	23737553
234	Phosphorylation	NEMATAASSSSLEKS HHHHHHCCCCCCCHH	28.43	23737553
235	Phosphorylation	EMATAASSSSLEKSY HHHHHCCCCCCCHHE	21.15	23737553
236	Phosphorylation	MATAASSSSLEKSYE HHHHCCCCCCCHHEE	36.13	23737553
237	Phosphorylation	ATAASSSSLEKSYEL HHHCCCCCCCHHEEC	42.36	23737553
241	O-linked_Glycosylation	SSSSLEKSYELPDGQ CCCCCCHHEECCCCC	17.92	6372527
241	Phosphorylation	SSSSLEKSYELPDGQ CCCCCCHHEECCCCC	17.92	25521595
242	Phosphorylation	SSSLEKSYELPDGQV CCCCCHHEECCCCCE	32.33	24925903
251	Phosphorylation	LPDGQVITIGNERFR CCCCCEEEECCCEEC	24.79	46158343
262	Phosphorylation	ERFRCPETLFQPSFI CEECCCCHHCCCCCC	20.29	22817900
267	Phosphorylation	PETLFQPSFIGMESA CCHHCCCCCCCHHCC	20.79	46158271
281	Phosphorylation	AGIHETTYNSIMKCD CCCCCCCCHHHHCCC	17.84	15569657
293	Ubiquitination	KCDIDIRKDLYANNV CCCCEECHHHHHCCC	53.04	22790023
296	Phosphorylation	IDIRKDLYANNVMSG CEECHHHHHCCCCCC	19.88	22817900
306	Phosphorylation	NVMSGGTTMYPGIAD CCCCCCCCCCCCHHH	20.27	46158307
317	Ubiquitination	GIADRMQKEITALAP CHHHHHHHHHHHHCC	41.56	22790023
317	Acetylation	GIADRMQKEITALAP CHHHHHHHHHHHHCC	41.56	130491
320	Phosphorylation	DRMQKEITALAPSTM HHHHHHHHHHCCCCE	19.40	25521595
325	Phosphorylation	EITALAPSTMKIKII HHHHHCCCCEEEEEE	35.21	25521595
326	Phosphorylation	ITALAPSTMKIKIIA HHHHCCCCEEEEEEC	22.79	46158475
328	Acetylation	ALAPSTMKIKIIAPP HHCCCCEEEEEECCC	40.72	88091
328	Ubiquitination	ALAPSTMKIKIIAPP HHCCCCEEEEEECCC	40.72	22790023
330	Acetylation	APSTMKIKIIAPPER CCCCEEEEEECCCCC	23.65	7629329
330	Ubiquitination	APSTMKIKIIAPPER CCCCEEEEEECCCCC	23.65	22790023
360	Phosphorylation	TFQQMWITKQEYDEA HHHHHCCHHHHHCCC	15.91	51458073
364	Phosphorylation	MWITKQEYDEAGPSI HCCHHHHHCCCCCCC	19.31	7330139
370	Phosphorylation	EYDEAGPSIVHRKCF HHCCCCCCCCCCCCC	36.00	27742792

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 ACTS_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
46	M	Oxidation	23911929
Oxidation of Met-46 and Met-49 by MICALs (MICAL1, MICAL2 or MICAL3) to form methionine sulfoxide promotes actin filament depolymerization.
49	M	Oxidation	23911929
Oxidation of Met-46 and Met-49 by MICALs (MICAL1, MICAL2 or MICAL3) to form methionine sulfoxide promotes actin filament depolymerization.
75	H	Methylation	-
Methylated at His-75 by SETD3.
86	K	Methylation	-
Monomethylation at Lys-86 (K84me1) regulates actin-myosin interaction and actomyosin-dependent processes.

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 ACTS_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
SYUA_MOUSE	Snca	physical	19553474
IPP_MOUSE	Ipp	physical	11536049

Drug and Disease Associations

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

Regulatory Network of ACTS_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Large-scale identification and evolution indexing of tyrosinephosphorylation sites from murine brain."; Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.; J. Proteome Res. 7:311-318(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-55; TYR-93 AND TYR-242,AND MASS SPECTROMETRY.	18034455 [Abstract]
"Quantitative time-resolved phosphoproteomic analysis of mast cellsignaling."; Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,Kawakami T., Salomon A.R.; J. Immunol. 179:5864-5876(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-93, AND MASSSPECTROMETRY.	17947660 [Abstract]

show

show

show

show