dbPTM

ACTG_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ACTG_MOUSE
UniProt AC	P63260
Protein Name	Actin, cytoplasmic 2
Gene Name	Actg1
Organism	Mus musculus (Mouse).
Sequence Length	375
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	MEEEIAALVIDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVMDSGDGVTHTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMATAASSSSLEKSYELPDGQVITIGNERFRCPEALFQPSFLGMESCGIHETTFNSIMKCDVDIRKDLYANTVLSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESGPSIVHRKCF

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MEEEIAAL -------CHHHCEEE	15.33	-
2	Acetylation	------MEEEIAALV ------CHHHCEEEE	65.42	213279
14	Phosphorylation	ALVIDNGSGMCKAGF EEEEECCCCCEECCC	29.61	36377615
33	Phosphorylation	APRAVFPSIVGRPRH CCCCCCHHHCCCCCC	20.59	27180971
44	Oxidation	RPRHQGVMVGMGQKD CCCCCCEEEECCCCC	2.49	23911929
47	Oxidation	HQGVMVGMGQKDSYV CCCEEEECCCCCCCC	3.32	23911929
50	Acetylation	VMVGMGQKDSYVGDE EEEECCCCCCCCCCH	42.80	132717
50	Ubiquitination	VMVGMGQKDSYVGDE EEEECCCCCCCCCCH	42.80	-
52	Phosphorylation	VGMGQKDSYVGDEAQ EECCCCCCCCCCHHH	28.84	25521595
53	Phosphorylation	GMGQKDSYVGDEAQS ECCCCCCCCCCHHHC	20.70	26824392
60	Phosphorylation	YVGDEAQSKRGILTL CCCCHHHCCCCEEEE	31.22	27087446
61	Ubiquitination	VGDEAQSKRGILTLK CCCHHHCCCCEEEEE	42.43	-
61	Acetylation	VGDEAQSKRGILTLK CCCHHHCCCCEEEEE	42.43	109301
66	Phosphorylation	QSKRGILTLKYPIEH HCCCCEEEEECEECC	21.20	22817900
69	Phosphorylation	RGILTLKYPIEHGIV CCEEEEECEECCCCC	16.74	26239621
73	Methylation	TLKYPIEHGIVTNWD EEECEECCCCCCCHH	31.81	213279
84	Methylation	TNWDDMEKIWHHTFY CCHHHHHHHHHHHHH	44.45	-
89	O-linked_Glycosylation	MEKIWHHTFYNELRV HHHHHHHHHHCCCCC	18.22	9567025
89	Phosphorylation	MEKIWHHTFYNELRV HHHHHHHHHHCCCCC	18.22	22499769
91	Phosphorylation	KIWHHTFYNELRVAP HHHHHHHHCCCCCCC	14.64	27742792
106	O-linked_Glycosylation	EEHPVLLTEAPLNPK CCCCEEEEECCCCCC	26.41	57405019
106	Phosphorylation	EEHPVLLTEAPLNPK CCCCEEEEECCCCCC	26.41	26824392
113	Ubiquitination	TEAPLNPKANREKMT EECCCCCCCCHHHHH	58.16	-
141	Phosphorylation	VAIQAVLSLYASGRT HHHHHHHHHHHCCCC	16.85	21082442
143	Phosphorylation	IQAVLSLYASGRTTG HHHHHHHHHCCCCEE	8.71	30803941
145	Phosphorylation	AVLSLYASGRTTGIV HHHHHHHCCCCEEEE	18.43	-
148	Phosphorylation	SLYASGRTTGIVMDS HHHHCCCCEEEEEEC	32.66	19060867
149	Phosphorylation	LYASGRTTGIVMDSG HHHCCCCEEEEEECC	24.45	23984901
155	Phosphorylation	TTGIVMDSGDGVTHT CEEEEEECCCCCEEE	22.23	23984901
160	Phosphorylation	MDSGDGVTHTVPIYE EECCCCCEEEEEEEC	19.84	21183079
162	Phosphorylation	SGDGVTHTVPIYEGY CCCCCEEEEEEECCC	20.72	21183079
166	Phosphorylation	VTHTVPIYEGYALPH CEEEEEEECCCCCCH	9.38	20438120
169	Phosphorylation	TVPIYEGYALPHAIL EEEEECCCCCCHHHH	7.94	40701
186	Phosphorylation	DLAGRDLTDYLMKIL HHCCCCHHHHHHHHH	27.21	24899341
188	Phosphorylation	AGRDLTDYLMKILTE CCCCHHHHHHHHHHH	11.94	2001175
191	Acetylation	DLTDYLMKILTERGY CHHHHHHHHHHHCCC	31.78	22646703
191	Ubiquitination	DLTDYLMKILTERGY CHHHHHHHHHHHCCC	31.78	-
194	Phosphorylation	DYLMKILTERGYSFT HHHHHHHHHCCCCCC	27.40	25367039
198	Phosphorylation	KILTERGYSFTTTAE HHHHHCCCCCCCCHH	13.56	25177544
199	Phosphorylation	ILTERGYSFTTTAER HHHHCCCCCCCCHHH	20.95	22499769
201	Phosphorylation	TERGYSFTTTAEREI HHCCCCCCCCHHHHH	19.80	30635358
202	Phosphorylation	ERGYSFTTTAEREIV HCCCCCCCCHHHHHH	23.23	30635358
203	Phosphorylation	RGYSFTTTAEREIVR CCCCCCCCHHHHHHH	24.38	26824392
213	Acetylation	REIVRDIKEKLCYVA HHHHHHHHHHHHEEE	53.75	8276063
215	Ubiquitination	IVRDIKEKLCYVALD HHHHHHHHHHEEECC	38.56	-
218	Phosphorylation	DIKEKLCYVALDFEQ HHHHHHHEEECCHHH	10.13	20438120
229	Phosphorylation	DFEQEMATAASSSSL CHHHHHHHHHCCCCC	22.80	55241617
232	Phosphorylation	QEMATAASSSSLEKS HHHHHHHCCCCCCCC	28.43	26745281
233	Phosphorylation	EMATAASSSSLEKSY HHHHHHCCCCCCCCE	21.15	4051811
234	Phosphorylation	MATAASSSSLEKSYE HHHHHCCCCCCCCEE	36.13	27087446
235	Phosphorylation	ATAASSSSLEKSYEL HHHHCCCCCCCCEEC	42.36	63716397
239	Phosphorylation	SSSSLEKSYELPDGQ CCCCCCCCEECCCCC	17.92	25521595
239	O-linked_Glycosylation	SSSSLEKSYELPDGQ CCCCCCCCEECCCCC	17.92	6372521
240	Phosphorylation	SSSLEKSYELPDGQV CCCCCCCEECCCCCE	32.33	24925903
249	Phosphorylation	LPDGQVITIGNERFR CCCCCEEEECCCEEC	24.79	46158343
265	Phosphorylation	PEALFQPSFLGMESC CHHHHCCHHHCCCCC	23.48	30814625
271	Phosphorylation	PSFLGMESCGIHETT CHHHCCCCCCCCCCC	14.57	26239621
277	Phosphorylation	ESCGIHETTFNSIMK CCCCCCCCCHHHHHC	23.64	23984901
278	Phosphorylation	SCGIHETTFNSIMKC CCCCCCCCHHHHHCC	20.17	23984901
281	Phosphorylation	IHETTFNSIMKCDVD CCCCCHHHHHCCCCC	21.62	23984901
291	Ubiquitination	KCDVDIRKDLYANTV CCCCCCCCHHHCCCE	53.04	-
294	Phosphorylation	VDIRKDLYANTVLSG CCCCCHHHCCCEECC	14.13	26824392
297	Phosphorylation	RKDLYANTVLSGGTT CCHHHCCCEECCCCC	18.04	9567085
300	Phosphorylation	LYANTVLSGGTTMYP HHCCCEECCCCCCCC	30.73	28833060
303	Phosphorylation	NTVLSGGTTMYPGIA CCEECCCCCCCCCHH	16.35	23984901
304	Phosphorylation	TVLSGGTTMYPGIAD CEECCCCCCCCCHHH	20.27	28833060
306	Phosphorylation	LSGGTTMYPGIADRM ECCCCCCCCCHHHHH	9.01	28833060
315	Ubiquitination	GIADRMQKEITALAP CHHHHHHHHHHHHCC	41.56	-
315	Acetylation	GIADRMQKEITALAP CHHHHHHHHHHHHCC	41.56	130679
318	Phosphorylation	DRMQKEITALAPSTM HHHHHHHHHHCCCCE	19.40	25521595
323	Phosphorylation	EITALAPSTMKIKII HHHHHCCCCEEEEEE	35.21	25521595
324	Phosphorylation	ITALAPSTMKIKIIA HHHHCCCCEEEEEEC	22.79	46158475
326	Ubiquitination	ALAPSTMKIKIIAPP HHCCCCEEEEEECCC	40.72	-
326	Acetylation	ALAPSTMKIKIIAPP HHCCCCEEEEEECCC	40.72	88099
328	Ubiquitination	APSTMKIKIIAPPER CCCCEEEEEECCCCC	23.65	-
328	Acetylation	APSTMKIKIIAPPER CCCCEEEEEECCCCC	23.65	7629383
362	Phosphorylation	MWISKQEYDESGPSI HHHHCCCCCCCCCCC	23.63	26026062
365	O-linked_Glycosylation	SKQEYDESGPSIVHR HCCCCCCCCCCCCCC	53.78	29471841
365	Phosphorylation	SKQEYDESGPSIVHR HCCCCCCCCCCCCCC	53.78	20139300
368	Phosphorylation	EYDESGPSIVHRKCF CCCCCCCCCCCCCCC	40.54	27180971

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 ACTG_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
44	M	Oxidation	23911929
Oxidation of Met-44 and Met-47 by MICALs (MICAL1, MICAL2 or MICAL3) to form methionine sulfoxide promotes actin filament depolymerization.
47	M	Oxidation	23911929
Oxidation of Met-44 and Met-47 by MICALs (MICAL1, MICAL2 or MICAL3) to form methionine sulfoxide promotes actin filament depolymerization.
73	H	Methylation	213279
Methylated at His-73 by SETD3.
84	K	Methylation	-
Monomethylation at Lys-84 (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 ACTG_MOUSE !!

Protein-Protein Interaction

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

Drug and Disease Associations

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

Regulatory Network of ACTG_MOUSE

Related Literatures of Post-Translational Modification

Methylation
Reference	PubMed
"Actin amino-acid sequences. Comparison of actins from calf thymus,bovine brain, and SV40-transformed mouse 3T3 cells with rabbitskeletal muscle actin."; Vandekerckhove J., Weber K.; Eur. J. Biochem. 90:451-462(1978). Cited for: PROTEIN SEQUENCE OF 2-375, AND METHYLATION AT HIS-73.	213279 [Abstract]
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-169, AND MASSSPECTROMETRY.	18034455 [Abstract]

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