dbPTM

ACTG_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ACTG_HUMAN
UniProt AC	P63261
Protein Name	Actin, cytoplasmic 2
Gene Name	ACTG1
Organism	Homo sapiens (Human).
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	22223895
2	Acetylation	------MEEEIAALV ------CHHHCEEEE	65.42	29581253
14	Phosphorylation	ALVIDNGSGMCKAGF EEEEECCCCCEECCC	29.61	30108239
18	Ubiquitination	DNGSGMCKAGFAGDD ECCCCCEECCCCCCC	42.52	21906983
33	Phosphorylation	APRAVFPSIVGRPRH CCCCCCHHHCCCCCC	20.59	30266825
44	Oxidation	RPRHQGVMVGMGQKD CCCCCCEEEECCCCC	2.49	-
44	Sulfoxidation	RPRHQGVMVGMGQKD CCCCCCEEEECCCCC	2.49	30846556
47	Oxidation	HQGVMVGMGQKDSYV CCCEEEECCCCCCCC	3.32	-
47	Sulfoxidation	HQGVMVGMGQKDSYV CCCEEEECCCCCCCC	3.32	30846556
50	Acetylation	VMVGMGQKDSYVGDE EEEECCCCCCCCCCH	42.80	132715
50	Methylation	VMVGMGQKDSYVGDE EEEECCCCCCCCCCH	42.80	-
50	Ubiquitination	VMVGMGQKDSYVGDE EEEECCCCCCCCCCH	42.80	27667366
52	Phosphorylation	VGMGQKDSYVGDEAQ EECCCCCCCCCCHHH	28.84	23401153
53	Phosphorylation	GMGQKDSYVGDEAQS ECCCCCCCCCCHHHC	20.70	27273156
60	Phosphorylation	YVGDEAQSKRGILTL CCCCHHHCCCCEEEE	31.22	23401153
61	Sumoylation	VGDEAQSKRGILTLK CCCHHHCCCCEEEEE	42.43	-
61	Acetylation	VGDEAQSKRGILTLK CCCHHHCCCCEEEEE	42.43	19608861
61	Neddylation	VGDEAQSKRGILTLK CCCHHHCCCCEEEEE	42.43	32015554
61	Sumoylation	VGDEAQSKRGILTLK CCCHHHCCCCEEEEE	42.43	19608861
61	Ubiquitination	VGDEAQSKRGILTLK CCCHHHCCCCEEEEE	42.43	32142685
66	Phosphorylation	QSKRGILTLKYPIEH HCCCCEEEEECEECC	21.20	28102081
68	Methylation	KRGILTLKYPIEHGI CCCEEEEECEECCCC	43.69	-
68	Ubiquitination	KRGILTLKYPIEHGI CCCEEEEECEECCCC	43.69	23000965
69	Phosphorylation	RGILTLKYPIEHGIV CCEEEEECEECCCCC	16.74	7171283
73	Methylation	TLKYPIEHGIVTNWD EEECEECCCCCCCHH	31.81	30626964
77	Phosphorylation	PIEHGIVTNWDDMEK EECCCCCCCHHHHHH	28.77	110747731
82	Sulfoxidation	IVTNWDDMEKIWHHT CCCCHHHHHHHHHHH	5.39	30846556
84	Methylation	TNWDDMEKIWHHTFY CCHHHHHHHHHHHHH	44.45	23673617
84	Sumoylation	TNWDDMEKIWHHTFY CCHHHHHHHHHHHHH	44.45	23673617
84	Ubiquitination	TNWDDMEKIWHHTFY CCHHHHHHHHHHHHH	44.45	32015554
89	Phosphorylation	MEKIWHHTFYNELRV HHHHHHHHHHCCCCC	18.22	27273156
91	Phosphorylation	KIWHHTFYNELRVAP HHHHHHHHCCCCCCC	14.64	27273156
106	Phosphorylation	EEHPVLLTEAPLNPK CCCCEEEEECCCCCC	26.41	57405023
113	Sumoylation	TEAPLNPKANREKMT EECCCCCCCCHHHHH	58.16	-
113	Acetylation	TEAPLNPKANREKMT EECCCCCCCCHHHHH	58.16	66729129
113	Sumoylation	TEAPLNPKANREKMT EECCCCCCCCHHHHH	58.16	-
113	Ubiquitination	TEAPLNPKANREKMT EECCCCCCCCHHHHH	58.16	27667366
118	Ubiquitination	NPKANREKMTQIMFE CCCCCHHHHHHHHHH	43.97	22817900
120	Phosphorylation	KANREKMTQIMFETF CCCHHHHHHHHHHHC	26.47	-
143	Phosphorylation	IQAVLSLYASGRTTG HHHHHHHHHCCCCEE	8.71	30803939
148	Phosphorylation	SLYASGRTTGIVMDS HHHHCCCCEEEEEEC	32.66	30140170
149	Phosphorylation	LYASGRTTGIVMDSG HHHCCCCEEEEEECC	24.45	30140170
153	Sulfoxidation	GRTTGIVMDSGDGVT CCCEEEEEECCCCCE	2.99	30846556
155	Phosphorylation	TTGIVMDSGDGVTHT CEEEEEECCCCCEEE	22.23	30140170
160	Phosphorylation	MDSGDGVTHTVPIYE EECCCCCEEEEEEEC	19.84	28152594
162	Phosphorylation	SGDGVTHTVPIYEGY CCCCCEEEEEEECCC	20.72	30140170
166	Phosphorylation	VTHTVPIYEGYALPH CEEEEEEECCCCCCH	9.38	27273156
169	Phosphorylation	TVPIYEGYALPHAIL EEEEECCCCCCHHHH	7.94	21082442
186	Phosphorylation	DLAGRDLTDYLMKIL HHCCCCHHHHHHHHH	27.21	28152594
188	Phosphorylation	AGRDLTDYLMKILTE CCCCHHHHHHHHHHH	11.94	26846344
190	Sulfoxidation	RDLTDYLMKILTERG CCHHHHHHHHHHHCC	1.75	30846556
191	Acetylation	DLTDYLMKILTERGY CHHHHHHHHHHHCCC	31.78	22646699
191	Methylation	DLTDYLMKILTERGY CHHHHHHHHHHHCCC	31.78	19608861
191	Ubiquitination	DLTDYLMKILTERGY CHHHHHHHHHHHCCC	31.78	21963094
194	Phosphorylation	DYLMKILTERGYSFT HHHHHHHHHCCCCCC	27.40	19060867
198	Phosphorylation	KILTERGYSFTTTAE HHHHHCCCCCCCCHH	13.56	27273156
199	Phosphorylation	ILTERGYSFTTTAER HHHHCCCCCCCCHHH	20.95	30266825
201	Phosphorylation	TERGYSFTTTAEREI HHCCCCCCCCHHHHH	19.80	30266825
202	Phosphorylation	ERGYSFTTTAEREIV HCCCCCCCCHHHHHH	23.23	30266825
203	Phosphorylation	RGYSFTTTAEREIVR CCCCCCCCHHHHHHH	24.38	30266825
213	Acetylation	REIVRDIKEKLCYVA HHHHHHHHHHHHEEE	53.75	8276067
213	Ubiquitination	REIVRDIKEKLCYVA HHHHHHHHHHHHEEE	53.75	21906983
215	Ubiquitination	IVRDIKEKLCYVALD HHHHHHHHHHEEECC	38.56	21906983
217	S-glutathionyl cysteine	RDIKEKLCYVALDFE HHHHHHHHEEECCHH	3.68	-
217	Glutathionylation	RDIKEKLCYVALDFE HHHHHHHHEEECCHH	3.68	22833525
217	S-palmitoylation	RDIKEKLCYVALDFE HHHHHHHHEEECCHH	3.68	29575903
218	Phosphorylation	DIKEKLCYVALDFEQ HHHHHHHEEECCHHH	10.13	27461979
227	Sulfoxidation	ALDFEQEMATAASSS ECCHHHHHHHHHCCC	3.92	30846556
229	Phosphorylation	DFEQEMATAASSSSL CHHHHHHHHHCCCCC	22.80	27461979
232	Phosphorylation	QEMATAASSSSLEKS HHHHHHHCCCCCCCC	28.43	30278072
233	Phosphorylation	EMATAASSSSLEKSY HHHHHHCCCCCCCCE	21.15	30278072
234	Phosphorylation	MATAASSSSLEKSYE HHHHHCCCCCCCCEE	36.13	30278072
235	Phosphorylation	ATAASSSSLEKSYEL HHHHCCCCCCCCEEC	42.36	30278072
238	Ubiquitination	ASSSSLEKSYELPDG HCCCCCCCCEECCCC	64.73	21963094
239	Phosphorylation	SSSSLEKSYELPDGQ CCCCCCCCEECCCCC	17.92	29255136
240	Phosphorylation	SSSLEKSYELPDGQV CCCCCCCEECCCCCE	32.33	29255136
249	Phosphorylation	LPDGQVITIGNERFR CCCCCEEEECCCEEC	24.79	26846344
265	O-linked_Glycosylation	PEALFQPSFLGMESC CHHHHCCHHHCCCCC	23.48	28510447
265	Phosphorylation	PEALFQPSFLGMESC CHHHHCCHHHCCCCC	23.48	26074081
269	Sulfoxidation	FQPSFLGMESCGIHE HCCHHHCCCCCCCCC	3.59	30846556
271	O-linked_Glycosylation	PSFLGMESCGIHETT CHHHCCCCCCCCCCC	14.57	28510447
271	Phosphorylation	PSFLGMESCGIHETT CHHHCCCCCCCCCCC	14.57	26074081
272	Glutathionylation	SFLGMESCGIHETTF HHHCCCCCCCCCCCH	3.65	22555962
277	O-linked_Glycosylation	ESCGIHETTFNSIMK CCCCCCCCCHHHHHC	23.64	28510447
277	Phosphorylation	ESCGIHETTFNSIMK CCCCCCCCCHHHHHC	23.64	30140170
278	O-linked_Glycosylation	SCGIHETTFNSIMKC CCCCCCCCHHHHHCC	20.17	28510447
278	Phosphorylation	SCGIHETTFNSIMKC CCCCCCCCHHHHHCC	20.17	30140170
281	O-linked_Glycosylation	IHETTFNSIMKCDVD CCCCCHHHHHCCCCC	21.62	28510447
283	Sulfoxidation	ETTFNSIMKCDVDIR CCCHHHHHCCCCCCC	3.38	30846556
284	Ubiquitination	TTFNSIMKCDVDIRK CCHHHHHCCCCCCCC	26.13	21963094
285	Glutathionylation	TFNSIMKCDVDIRKD CHHHHHCCCCCCCCH	3.22	22555962
285	S-palmitoylation	TFNSIMKCDVDIRKD CHHHHHCCCCCCCCH	3.22	29575903
291	Sumoylation	KCDVDIRKDLYANTV CCCCCCCCHHHCCCE	53.04	-
291	Ubiquitination	KCDVDIRKDLYANTV CCCCCCCCHHHCCCE	53.04	27667366
294	Phosphorylation	VDIRKDLYANTVLSG CCCCCHHHCCCEECC	14.13	27273156
297	Phosphorylation	RKDLYANTVLSGGTT CCHHHCCCEECCCCC	18.04	27155012
300	Phosphorylation	LYANTVLSGGTTMYP HHCCCEECCCCCCCC	30.73	21712546
303	Phosphorylation	NTVLSGGTTMYPGIA CCEECCCCCCCCCHH	16.35	21712546
304	Phosphorylation	TVLSGGTTMYPGIAD CEECCCCCCCCCHHH	20.27	21712546
305	Sulfoxidation	VLSGGTTMYPGIADR EECCCCCCCCCHHHH	3.69	30846556
306	Phosphorylation	LSGGTTMYPGIADRM ECCCCCCCCCHHHHH	9.01	21712546
315	Sumoylation	GIADRMQKEITALAP CHHHHHHHHHHHHCC	41.56	-
315	Acetylation	GIADRMQKEITALAP CHHHHHHHHHHHHCC	41.56	130677
315	Neddylation	GIADRMQKEITALAP CHHHHHHHHHHHHCC	41.56	32015554
315	Sumoylation	GIADRMQKEITALAP CHHHHHHHHHHHHCC	41.56	-
315	Ubiquitination	GIADRMQKEITALAP CHHHHHHHHHHHHCC	41.56	27667366
318	Phosphorylation	DRMQKEITALAPSTM HHHHHHHHHHCCCCE	19.40	30266825
323	Phosphorylation	EITALAPSTMKIKII HHHHHCCCCEEEEEE	35.21	29255136
324	Phosphorylation	ITALAPSTMKIKIIA HHHHCCCCEEEEEEC	22.79	46158473
325	Sulfoxidation	TALAPSTMKIKIIAP HHHCCCCEEEEEECC	5.05	30846556
326	Sumoylation	ALAPSTMKIKIIAPP HHCCCCEEEEEECCC	40.72	-
326	Acetylation	ALAPSTMKIKIIAPP HHCCCCEEEEEECCC	40.72	88097
326	Methylation	ALAPSTMKIKIIAPP HHCCCCEEEEEECCC	40.72	19608861
326	Neddylation	ALAPSTMKIKIIAPP HHCCCCEEEEEECCC	40.72	32015554
326	Sumoylation	ALAPSTMKIKIIAPP HHCCCCEEEEEECCC	40.72	19608861
326	Ubiquitination	ALAPSTMKIKIIAPP HHCCCCEEEEEECCC	40.72	27667366
328	Sumoylation	APSTMKIKIIAPPER CCCCEEEEEECCCCC	23.65	-
328	Acetylation	APSTMKIKIIAPPER CCCCEEEEEECCCCC	23.65	7629387
328	Neddylation	APSTMKIKIIAPPER CCCCEEEEEECCCCC	23.65	32015554
328	Sumoylation	APSTMKIKIIAPPER CCCCEEEEEECCCCC	23.65	19608861
328	Ubiquitination	APSTMKIKIIAPPER CCCCEEEEEECCCCC	23.65	27667366
336	Sumoylation	IIAPPERKYSVWIGG EECCCCCCEEEEECH	39.97	-
336	Ubiquitination	IIAPPERKYSVWIGG EECCCCCCEEEEECH	39.97	25015289
348	Phosphorylation	IGGSILASLSTFQQM ECHHHHHHHHHHHHH	21.29	-
359	Ubiquitination	FQQMWISKQEYDESG HHHHHHHCCCCCCCC	37.71	-
362	Phosphorylation	MWISKQEYDESGPSI HHHHCCCCCCCCCCC	23.63	23401153
365	Phosphorylation	SKQEYDESGPSIVHR HCCCCCCCCCCCCCC	53.78	23401153
368	Phosphorylation	EYDESGPSIVHRKCF CCCCCCCCCCCCCCC	40.54	30266825
373	Neddylation	GPSIVHRKCF----- CCCCCCCCCC-----	25.72	32015554
373	Ubiquitination	GPSIVHRKCF----- CCCCCCCCCC-----	25.72	29967540
374	Glutathionylation	PSIVHRKCF------ CCCCCCCCC------	5.02	11684673

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_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
44	M	Oxidation	-
Oxidation of Met-44 and Met-47 by MICALs (MICAL1, MICAL2 or MICAL3) to form methionine sulfoxide promotes actin filament depolymerization.
47	M	Oxidation	-
Oxidation of Met-44 and Met-47 by MICALs (MICAL1, MICAL2 or MICAL3) to form methionine sulfoxide promotes actin filament depolymerization.
73	H	Methylation
Methylated at His-73 by SETD3.
84	K	Methylation	23673617
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_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
COF2_HUMAN	CFL2	physical	16189514
COF1_HUMAN	CFL1	physical	16189514
ACTG_HUMAN	ACTG1	physical	16189514
DEST_HUMAN	DSTN	physical	16189514
TYB4_HUMAN	TMSB4X	physical	15163409
SH3G2_HUMAN	SH3GL2	physical	16169070
PROF2_HUMAN	PFN2	physical	16169070
MLH1_HUMAN	MLH1	physical	20706999
CTBP2_HUMAN	CTBP2	physical	21988832
GIT2_HUMAN	GIT2	physical	21988832
WASL_HUMAN	WASL	physical	22847007
ACTS_HUMAN	ACTA1	physical	22863883
ACTBL_HUMAN	ACTBL2	physical	22863883
BRK1_HUMAN	BRK1	physical	22863883
CDN2A_HUMAN	CDKN2A	physical	22863883
ARF_HUMAN	CDKN2A	physical	22863883
ACTG_HUMAN	ACTG1	physical	25416956
COF1_HUMAN	CFL1	physical	25416956
COF2_HUMAN	CFL2	physical	25416956
ECHP_HUMAN	EHHADH	physical	25416956
TBA8_HUMAN	EHHADH	physical	25416956
CAP2_HUMAN	CAP2	physical	25416956
DEST_HUMAN	DSTN	physical	25416956
CCD22_HUMAN	CCDC22	physical	25416956
NTAQ1_HUMAN	WDYHV1	physical	25416956
PYR1_HUMAN	CAD	physical	26344197
EF1A1_HUMAN	EEF1A1	physical	26344197
EF1A2_HUMAN	EEF1A2	physical	26344197
NCKP1_HUMAN	NCKAP1	physical	26344197
RAN_HUMAN	RAN	physical	26344197
RUVB1_HUMAN	RUVBL1	physical	26344197
RUVB2_HUMAN	RUVBL2	physical	26344197
SYYC_HUMAN	YARS	physical	26344197
ACTG_HUMAN	ACTG1	physical	21516116

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
604717	Deafness, autosomal dominant, 20 (DFNA20)
614583	Baraitser-Winter syndrome 2 (BRWS2)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of ACTG_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Phosphoproteome of resting human platelets."; Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,Schuetz C., Walter U., Gambaryan S., Sickmann A.; J. Proteome Res. 7:526-534(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-318, AND MASSSPECTROMETRY.	18088087 [Abstract]
"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-198 AND TYR-294, ANDMASS SPECTROMETRY.	18083107 [Abstract]

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