dbPTM

ACTS_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ACTS_HUMAN
UniProt AC	P68133
Protein Name	Actin, alpha skeletal muscle
Gene Name	ACTA1
Organism	Homo sapiens (Human).
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	-
35	Phosphorylation	APRAVFPSIVGRPRH CCCCCCHHHCCCCCC	20.59	30266825
46	Oxidation	RPRHQGVMVGMGQKD CCCCCCEEEECCCCC	2.49	-
49	Oxidation	HQGVMVGMGQKDSYV CCCEEEECCCCCCCC	3.32	-
52	Acetylation	VMVGMGQKDSYVGDE EEEECCCCCCCCCCH	42.80	132711
52	Methylation	VMVGMGQKDSYVGDE EEEECCCCCCCCCCH	42.80	-
52	Ubiquitination	VMVGMGQKDSYVGDE EEEECCCCCCCCCCH	42.80	21906983
54	Phosphorylation	VGMGQKDSYVGDEAQ EECCCCCCCCCCHHH	28.84	23401153
55	Phosphorylation	GMGQKDSYVGDEAQS ECCCCCCCCCCHHHC	20.70	27273156
62	Phosphorylation	YVGDEAQSKRGILTL CCCCHHHCCCCEEEE	31.22	23401153
63	N6-malonyllysine	VGDEAQSKRGILTLK CCCHHHCCCCEEEEE	42.43	-
63	Acetylation	VGDEAQSKRGILTLK CCCHHHCCCCEEEEE	42.43	130497
63	Malonylation	VGDEAQSKRGILTLK CCCHHHCCCCEEEEE	42.43	21908771
63	Neddylation	VGDEAQSKRGILTLK CCCHHHCCCCEEEEE	42.43	32015554
63	Sumoylation	VGDEAQSKRGILTLK CCCHHHCCCCEEEEE	42.43	-
63	Ubiquitination	VGDEAQSKRGILTLK CCCHHHCCCCEEEEE	42.43	32142685
68	Phosphorylation	QSKRGILTLKYPIEH HCCCCEEEEECEECC	21.20	22617229
70	Acetylation	KRGILTLKYPIEHGI CCCEEEEECEECCCC	43.69	130493
70	Methylation	KRGILTLKYPIEHGI CCCEEEEECEECCCC	43.69	-
70	Ubiquitination	KRGILTLKYPIEHGI CCCEEEEECEECCCC	43.69	23000965
71	Phosphorylation	RGILTLKYPIEHGII CCEEEEECEECCCCC	16.74	18180459
75	Methylation	TLKYPIEHGIITNWD EEECEECCCCCCCHH	33.21	30626964
79	Phosphorylation	PIEHGIITNWDDMEK EECCCCCCCHHHHHH	28.47	36012735
86	Acetylation	TNWDDMEKIWHHTFY CCHHHHHHHHHHHHH	44.45	71087
86	Methylation	TNWDDMEKIWHHTFY CCHHHHHHHHHHHHH	44.45	23673617
86	Sumoylation	TNWDDMEKIWHHTFY CCHHHHHHHHHHHHH	44.45	23673617
86	Ubiquitination	TNWDDMEKIWHHTFY CCHHHHHHHHHHHHH	44.45	21906983
91	Phosphorylation	MEKIWHHTFYNELRV HHHHHHHHHHCCCCC	18.22	27273156
93	Phosphorylation	KIWHHTFYNELRVAP HHHHHHHHCCCCCCC	14.64	27273156
105	Phosphorylation	VAPEEHPTLLTEAPL CCCCCCCCCCCCCCC	35.99	26437602
108	Phosphorylation	EEHPTLLTEAPLNPK CCCCCCCCCCCCCCC	32.96	21406692
115	Acetylation	TEAPLNPKANREKMT CCCCCCCCCCHHHHH	58.16	30583639
115	Ubiquitination	TEAPLNPKANREKMT CCCCCCCCCCHHHHH	58.16	21906983
120	Ubiquitination	NPKANREKMTQIMFE CCCCCHHHHHHHHHH	43.97	22817900
122	Phosphorylation	KANREKMTQIMFETF CCCHHHHHHHHHHHC	26.47	-
128	Phosphorylation	MTQIMFETFNVPAMY HHHHHHHHCCHHHHH	14.83	-
145	Phosphorylation	IQAVLSLYASGRTTG HHHHHHHHHCCCCEE	8.71	30803931
150	Phosphorylation	SLYASGRTTGIVLDS HHHHCCCCEEEEEEC	32.66	26657352
151	Phosphorylation	LYASGRTTGIVLDSG HHHCCCCEEEEEECC	24.45	26437602
157	Phosphorylation	TTGIVLDSGDGVTHN CEEEEEECCCCCCCC	34.32	10632791
162	Phosphorylation	LDSGDGVTHNVPIYE EECCCCCCCCCCEEC	17.17	26437602
168	Phosphorylation	VTHNVPIYEGYALPH CCCCCCEECCCCHHH	9.38	7561247
171	Phosphorylation	NVPIYEGYALPHAIM CCCEECCCCHHHHHH	7.94	7330091
188	Phosphorylation	DLAGRDLTDYLMKIL HCCCCCHHHHHHHHH	27.21	28152594
190	Phosphorylation	AGRDLTDYLMKILTE CCCCHHHHHHHHHHH	11.94	26846344
192	Sulfoxidation	RDLTDYLMKILTERG CCHHHHHHHHHHHCC	1.75	31801345
193	Acetylation	DLTDYLMKILTERGY CHHHHHHHHHHHCCC	31.78	22646667
193	Methylation	DLTDYLMKILTERGY CHHHHHHHHHHHCCC	31.78	-
193	Ubiquitination	DLTDYLMKILTERGY CHHHHHHHHHHHCCC	31.78	21906983
196	Phosphorylation	DYLMKILTERGYSFV HHHHHHHHHCCCCCE	27.40	46158449
198	Methylation	LMKILTERGYSFVTT HHHHHHHCCCCCEEH	44.08	-
200	Phosphorylation	KILTERGYSFVTTAE HHHHHCCCCCEEHHC	12.73	54893
201	O-linked_Glycosylation	ILTERGYSFVTTAER HHHHCCCCCEEHHCH	18.96	5142853
201	Phosphorylation	ILTERGYSFVTTAER HHHHCCCCCEEHHCH	18.96	36642193
204	Phosphorylation	ERGYSFVTTAEREIV HCCCCCEEHHCHHHH	20.48	26657352
205	Phosphorylation	RGYSFVTTAEREIVR CCCCCEEHHCHHHHH	22.63	28857561
215	Acetylation	REIVRDIKEKLCYVA HHHHHHHHHHHCEEE	53.75	8276007
215	Ubiquitination	REIVRDIKEKLCYVA HHHHHHHHHHHCEEE	53.75	21906983
217	Acetylation	IVRDIKEKLCYVALD HHHHHHHHHCEEEEE	38.56	155931
217	Methylation	IVRDIKEKLCYVALD HHHHHHHHHCEEEEE	38.56	-
217	Ubiquitination	IVRDIKEKLCYVALD HHHHHHHHHCEEEEE	38.56	22817900
219	Glutathionylation	RDIKEKLCYVALDFE HHHHHHHCEEEEECC	3.68	22555962
220	Phosphorylation	DIKEKLCYVALDFEN HHHHHHCEEEEECCH	10.13	29396449
231	Phosphorylation	DFENEMATAASSSSL ECCHHHHHHCCCCCC	22.80	26657352
234	Phosphorylation	NEMATAASSSSLEKS HHHHHHCCCCCCCHH	28.43	26657352
235	Phosphorylation	EMATAASSSSLEKSY HHHHHCCCCCCCHHE	21.15	35096073
236	Phosphorylation	MATAASSSSLEKSYE HHHHCCCCCCCHHEE	36.13	26657352
237	Phosphorylation	ATAASSSSLEKSYEL HHHCCCCCCCHHEEC	42.36	29396449
240	Ubiquitination	ASSSSLEKSYELPDG CCCCCCCHHEECCCC	64.73	22817900
241	Phosphorylation	SSSSLEKSYELPDGQ CCCCCCHHEECCCCC	17.92	29255136
242	Phosphorylation	SSSLEKSYELPDGQV CCCCCHHEECCCCCE	32.33	29255136
251	Phosphorylation	LPDGQVITIGNERFR CCCCCEEEECCCEEC	24.79	26846344
262	O-linked_Glycosylation	ERFRCPETLFQPSFI CEECCCCHHCCCCCC	20.29	23301498
262	Phosphorylation	ERFRCPETLFQPSFI CEECCCCHHCCCCCC	20.29	-
267	O-linked_Glycosylation	PETLFQPSFIGMESA CCHHCCCCCCCHHCC	20.79	23301498
267	Phosphorylation	PETLFQPSFIGMESA CCHHCCCCCCCHHCC	20.79	46158533
273	O-linked_Glycosylation	PSFIGMESAGIHETT CCCCCHHCCCCCCCC	23.93	23301498
273	Phosphorylation	PSFIGMESAGIHETT CCCCCHHCCCCCCCC	23.93	22210691
280	O-linked_Glycosylation	SAGIHETTYNSIMKC CCCCCCCCCHHHHCC	20.09	23301498
280	Phosphorylation	SAGIHETTYNSIMKC CCCCCCCCCHHHHCC	20.09	-
281	Phosphorylation	AGIHETTYNSIMKCD CCCCCCCCHHHHCCC	17.84	3828983
283	Phosphorylation	IHETTYNSIMKCDID CCCCCCHHHHCCCCE	17.41	-
293	Ubiquitination	KCDIDIRKDLYANNV CCCCEECHHHHHCCC	53.04	33845483
296	Phosphorylation	IDIRKDLYANNVMSG CEECHHHHHCCCCCC	19.88	19702290
302	Phosphorylation	LYANNVMSGGTTMYP HHHCCCCCCCCCCCC	29.77	22210691
305	Phosphorylation	NNVMSGGTTMYPGIA CCCCCCCCCCCCCHH	16.35	22210691
306	Phosphorylation	NVMSGGTTMYPGIAD CCCCCCCCCCCCHHH	20.27	25394399
308	Phosphorylation	MSGGTTMYPGIADRM CCCCCCCCCCHHHHH	9.01	25884760
317	Sumoylation	GIADRMQKEITALAP CHHHHHHHHHHHHCC	41.56	-
317	Acetylation	GIADRMQKEITALAP CHHHHHHHHHHHHCC	41.56	130489
317	Neddylation	GIADRMQKEITALAP CHHHHHHHHHHHHCC	41.56	32015554
317	Sumoylation	GIADRMQKEITALAP CHHHHHHHHHHHHCC	41.56	-
317	Ubiquitination	GIADRMQKEITALAP CHHHHHHHHHHHHCC	41.56	21906983
320	Phosphorylation	DRMQKEITALAPSTM HHHHHHHHHHCCCCE	19.40	30266825
325	Phosphorylation	EITALAPSTMKIKII HHHHHCCCCEEEEEE	35.21	23401153
326	Phosphorylation	ITALAPSTMKIKIIA HHHHCCCCEEEEEEC	22.79	46158473
328	Sumoylation	ALAPSTMKIKIIAPP HHCCCCEEEEEECCC	40.72	-
328	Acetylation	ALAPSTMKIKIIAPP HHCCCCEEEEEECCC	40.72	88089
328	Methylation	ALAPSTMKIKIIAPP HHCCCCEEEEEECCC	40.72	-
328	Neddylation	ALAPSTMKIKIIAPP HHCCCCEEEEEECCC	40.72	32015554
328	Sumoylation	ALAPSTMKIKIIAPP HHCCCCEEEEEECCC	40.72	-
328	Ubiquitination	ALAPSTMKIKIIAPP HHCCCCEEEEEECCC	40.72	27667366
330	Sumoylation	APSTMKIKIIAPPER CCCCEEEEEECCCCC	23.65	-
330	Acetylation	APSTMKIKIIAPPER CCCCEEEEEECCCCC	23.65	7629335
330	Neddylation	APSTMKIKIIAPPER CCCCEEEEEECCCCC	23.65	32015554
330	Sumoylation	APSTMKIKIIAPPER CCCCEEEEEECCCCC	23.65	-
330	Ubiquitination	APSTMKIKIIAPPER CCCCEEEEEECCCCC	23.65	21906983
338	Sumoylation	IIAPPERKYSVWIGG EECCCCCCEEEEECH	39.97	-
338	Ubiquitination	IIAPPERKYSVWIGG EECCCCCCEEEEECH	39.97	25015289
339	Phosphorylation	IAPPERKYSVWIGGS ECCCCCCEEEEECHH	18.06	29978859
340	Phosphorylation	APPERKYSVWIGGSI CCCCCCEEEEECHHH	17.63	29978859
346	Phosphorylation	YSVWIGGSILASLST EEEEECHHHHHHHHH	14.82	29978859
350	Phosphorylation	IGGSILASLSTFQQM ECHHHHHHHHHHHHH	21.29	29978859
352	Phosphorylation	GSILASLSTFQQMWI HHHHHHHHHHHHHCC	25.36	29978859
353	Phosphorylation	SILASLSTFQQMWIT HHHHHHHHHHHHCCH	30.65	29978859
360	Phosphorylation	TFQQMWITKQEYDEA HHHHHCCHHHHHCCC	15.91	29978859
364	Phosphorylation	MWITKQEYDEAGPSI HCCHHHHHCCCCCCC	19.31	20068231
370	Phosphorylation	EYDEAGPSIVHRKCF HHCCCCCCCCCCCCC	36.00	26657352
375	Ubiquitination	GPSIVHRKCF----- CCCCCCCCCC-----	25.72	-

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:21764995

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
46	M	Oxidation	-
Oxidation of Met-46 and Met-49 by MICALs (MICAL1, MICAL2 or MICAL3) to form methionine sulfoxide promotes actin filament depolymerization.
49	M	Oxidation	-
Oxidation of Met-46 and Met-49 by MICALs (MICAL1, MICAL2 or MICAL3) to form methionine sulfoxide promotes actin filament depolymerization.
75	H	Methylation	30626964
Methylated at His-75 by SETD3.
86	K	Methylation	23673617
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_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
TRIP6_HUMAN	TRIP6	physical	14688263
ERD10_ARATH	ERD10	physical	17010111
KS6B1_HUMAN	RPS6KB1	physical	15149849
NRAP_HUMAN	NRAP	physical	10320340
VTDB_HUMAN	GC	physical	12554937
TYB4Y_HUMAN	TMSB4Y	physical	8416954
TYB4_HUMAN	TMSB4X	physical	9153421
TCPD_HUMAN	CCT4	physical	11580270
PCY1B_HUMAN	PCYT1B	physical	11580270
TCPE_HUMAN	CCT5	physical	11580270
DMD_HUMAN	DMD	physical	1544421
HDAC8_HUMAN	HDAC8	physical	15772115
DHX9_HUMAN	DHX9	physical	11687588
HDAC4_HUMAN	HDAC4	physical	21464227
COF1_HUMAN	CFL1	physical	21723825
DNAS1_HUMAN	DNASE1	physical	2395459
ABLM3_HUMAN	ABLIM3	physical	17194709
ABLM2_HUMAN	ABLIM2	physical	17194709
RPA2_HUMAN	POLR1B	physical	15558034
ACTBL_HUMAN	ACTBL2	physical	22863883
BRK1_HUMAN	BRK1	physical	22863883
CDN2A_HUMAN	CDKN2A	physical	22863883
ARF_HUMAN	CDKN2A	physical	22863883
NCKP1_HUMAN	NCKAP1	physical	22863883
AMOT_HUMAN	AMOT	physical	24106267
ABL1_HUMAN	ABL1	physical	16109371
MYO1C_HUMAN	MYO1C	physical	15558034
SRC_HUMAN	SRC	physical	23353701
P85A_HUMAN	PIK3R1	physical	23353701
AKT1_HUMAN	AKT1	physical	23353701
SPTA1_HUMAN	SPTA1	physical	16889989

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
161800	Nemaline myopathy 3 (NEM3)
161800	Myopathy, actin, congenital, with excess of thin myofilaments (MPCETM)
255310	Myopathy, congenital, with fiber-type disproportion (CFTD)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of ACTS_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-63; LYS-70; LYS-193; LYS-328AND LYS-330, AND MASS SPECTROMETRY.	19608861 [Abstract]
"Substrate and functional diversity of lysine acetylation revealed bya proteomics survey."; Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T.,Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.; Mol. Cell 23:607-618(2006). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-63, AND MASS SPECTROMETRY.	16916647 [Abstract]
Malonylation
Reference	PubMed
"The first identification of lysine malonylation substrates and itsregulatory enzyme."; Peng C., Lu Z., Xie Z., Cheng Z., Chen Y., Tan M., Luo H., Zhang Y.,He W., Yang K., Zwaans B.M., Tishkoff D., Ho L., Lombard D., He T.C.,Dai J., Verdin E., Ye Y., Zhao Y.; Mol. Cell. Proteomics 10:M111.012658.01-M111.012658.12(2011). Cited for: MALONYLATION AT LYS-63.	21908771 [Abstract]
N6-malonyllysine
Reference	PubMed
"The first identification of lysine malonylation substrates and itsregulatory enzyme."; Peng C., Lu Z., Xie Z., Cheng Z., Chen Y., Tan M., Luo H., Zhang Y.,He W., Yang K., Zwaans B.M., Tishkoff D., Ho L., Lombard D., He T.C.,Dai J., Verdin E., Ye Y., Zhao Y.; Mol. Cell. Proteomics 10:M111.012658.01-M111.012658.12(2011). Cited for: MALONYLATION AT LYS-63.	21908771 [Abstract]
Phosphorylation
Reference	PubMed
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer."; Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.; Cell 131:1190-1203(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-55 AND TYR-93, AND MASSSPECTROMETRY.	18083107 [Abstract]

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