dbPTM

CNN3_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	CNN3_HUMAN
UniProt AC	Q15417
Protein Name	Calponin-3
Gene Name	CNN3
Organism	Homo sapiens (Human).
Sequence Length	329
Subcellular Localization
Protein Description	Thin filament-associated protein that is implicated in the regulation and modulation of smooth muscle contraction. It is capable of binding to actin, calmodulin, troponin C and tropomyosin. The interaction of calponin with actin inhibits the actomyosin Mg-ATPase activity..
Protein Sequence	MTHFNKGPSYGLSAEVKNKIASKYDHQAEEDLRNWIEEVTGMSIGPNFQLGLKDGIILCELINKLQPGSVKKVNESSLNWPQLENIGNFIKAIQAYGMKPHDIFEANDLFENGNMTQVQTTLVALAGLAKTKGFHTTIDIGVKYAEKQTRRFDEGKLKAGQSVIGLQMGTNKCASQAGMTAYGTRRHLYDPKMQTDKPFDQTTISLQMGTNKGASQAGMLAPGTRRDIYDQKLTLQPVDNSTISLQMGTNKVASQKGMSVYGLGRQVYDPKYCAAPTEPVIHNGSQGTGTNGSEISDSDYQAEYPDEYHGEYQDDYPRDYQYSDQGIDY

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MTHFNKGPS ------CCCCCCCCC	34.86	28857561
6	Acetylation	--MTHFNKGPSYGLS --CCCCCCCCCCCCC	71.85	-
6	Acetylation	--MTHFNKGPSYGLS --CCCCCCCCCCCCC	71.85	23236377
6	Malonylation	--MTHFNKGPSYGLS --CCCCCCCCCCCCC	71.85	26320211
6	Ubiquitination	--MTHFNKGPSYGLS --CCCCCCCCCCCCC	71.85	23000965
9	Phosphorylation	THFNKGPSYGLSAEV CCCCCCCCCCCCHHH	40.27	21945579
10	Phosphorylation	HFNKGPSYGLSAEVK CCCCCCCCCCCHHHH	25.81	21945579
13	Phosphorylation	KGPSYGLSAEVKNKI CCCCCCCCHHHHHHH	20.30	21945579
17	Ubiquitination	YGLSAEVKNKIASKY CCCCHHHHHHHHHCC	43.99	-
17	Ubiquitination	YGLSAEVKNKIASKY CCCCHHHHHHHHHCC	43.99	23000965
19	Ubiquitination	LSAEVKNKIASKYDH CCHHHHHHHHHCCCH	33.65	23000965
23	Acetylation	VKNKIASKYDHQAEE HHHHHHHCCCHHHHH	45.75	-
23	Acetylation	VKNKIASKYDHQAEE HHHHHHHCCCHHHHH	45.75	25825284
23	Ubiquitination	VKNKIASKYDHQAEE HHHHHHHCCCHHHHH	45.75	23000965
30	Ubiquitination	KYDHQAEEDLRNWIE CCCHHHHHHHHHHHH	66.42	27667366
43	Phosphorylation	IEEVTGMSIGPNFQL HHHHHCCCCCCCCCC	26.24	21406692
59	S-nitrosocysteine	LKDGIILCELINKLQ CCCCCHHHHHHHHHC	2.55	-
59	S-nitrosylation	LKDGIILCELINKLQ CCCCCHHHHHHHHHC	2.55	19483679
69	Phosphorylation	INKLQPGSVKKVNES HHHHCCCCEEECCHH	37.13	27499020
71	2-Hydroxyisobutyrylation	KLQPGSVKKVNESSL HHCCCCEEECCHHHC	53.34	-
71	Ubiquitination	KLQPGSVKKVNESSL HHCCCCEEECCHHHC	53.34	27667366
97	Ubiquitination	IKAIQAYGMKPHDIF HHHHHHCCCCHHHCC	22.21	22817900
101	Ubiquitination	QAYGMKPHDIFEAND HHCCCCHHHCCCHHH	34.97	22817900
102	Ubiquitination	AYGMKPHDIFEANDL HCCCCHHHCCCHHHC	56.66	22817900
106	Ubiquitination	KPHDIFEANDLFENG CHHHCCCHHHCHHCC	12.23	22817900
110	Ubiquitination	IFEANDLFENGNMTQ CCCHHHCHHCCCCCH	8.37	23000965
112	Ubiquitination	EANDLFENGNMTQVQ CHHHCHHCCCCCHHH	39.54	23000965
115	Acetylation	DLFENGNMTQVQTTL HCHHCCCCCHHHHHH	2.69	-
115	Ubiquitination	DLFENGNMTQVQTTL HCHHCCCCCHHHHHH	2.69	23000965
117	Ubiquitination	FENGNMTQVQTTLVA HHCCCCCHHHHHHHH	17.98	-
117	Ubiquitination	FENGNMTQVQTTLVA HHCCCCCHHHHHHHH	17.98	23000965
126	Ubiquitination	QTTLVALAGLAKTKG HHHHHHHHHHHHCCC	10.96	23000965
131	Ubiquitination	ALAGLAKTKGFHTTI HHHHHHHCCCCEEEE	30.69	23000965
143	Ubiquitination	TTIDIGVKYAEKQTR EEEECCHHHHHHCCC	33.26	22817900
146	Ubiquitination	DIGVKYAEKQTRRFD ECCHHHHHHCCCCCC	42.48	23000965
147	2-Hydroxyisobutyrylation	IGVKYAEKQTRRFDE CCHHHHHHCCCCCCC	49.12	-
147	Ubiquitination	IGVKYAEKQTRRFDE CCHHHHHHCCCCCCC	49.12	22817900
151	Ubiquitination	YAEKQTRRFDEGKLK HHHHCCCCCCCCCCC	46.91	23000965
156	Acetylation	TRRFDEGKLKAGQSV CCCCCCCCCCCCCEE	44.78	-
156	Ubiquitination	TRRFDEGKLKAGQSV CCCCCCCCCCCCCEE	44.78	-
156	Acetylation	TRRFDEGKLKAGQSV CCCCCCCCCCCCCEE	44.78	23236377
156	Ubiquitination	TRRFDEGKLKAGQSV CCCCCCCCCCCCCEE	44.78	23000965
158	Methylation	RFDEGKLKAGQSVIG CCCCCCCCCCCEEEE	54.69	24129315
158	Ubiquitination	RFDEGKLKAGQSVIG CCCCCCCCCCCEEEE	54.69	23000965
162	Phosphorylation	GKLKAGQSVIGLQMG CCCCCCCEEEEEECC	18.13	27499020
166	Ubiquitination	AGQSVIGLQMGTNKC CCCEEEEEECCCCHH	1.86	23000965
168	Sulfoxidation	QSVIGLQMGTNKCAS CEEEEEECCCCHHHH	9.57	30846556
170	Phosphorylation	VIGLQMGTNKCASQA EEEEECCCCHHHHHH	26.60	22210691
171	Ubiquitination	IGLQMGTNKCASQAG EEEECCCCHHHHHHC	31.51	21890473
171	Ubiquitination	IGLQMGTNKCASQAG EEEECCCCHHHHHHC	31.51	23000965
172	Methylation	GLQMGTNKCASQAGM EEECCCCHHHHHHCC	30.89	-
172	Ubiquitination	GLQMGTNKCASQAGM EEECCCCHHHHHHCC	30.89	23000965
175	Phosphorylation	MGTNKCASQAGMTAY CCCCHHHHHHCCCCC	29.99	23532336
180	Phosphorylation	CASQAGMTAYGTRRH HHHHHCCCCCCCCCC	18.79	27251275
182	Phosphorylation	SQAGMTAYGTRRHLY HHHCCCCCCCCCCCC	15.18	24927040
184	Phosphorylation	AGMTAYGTRRHLYDP HCCCCCCCCCCCCCC	16.32	29978859
186	Ubiquitination	MTAYGTRRHLYDPKM CCCCCCCCCCCCCCC	24.81	23000965
189	Phosphorylation	YGTRRHLYDPKMQTD CCCCCCCCCCCCCCC	24.87	29759185
191	Ubiquitination	TRRHLYDPKMQTDKP CCCCCCCCCCCCCCC	22.06	21890473
191	Ubiquitination	TRRHLYDPKMQTDKP CCCCCCCCCCCCCCC	22.06	23000965
192	2-Hydroxyisobutyrylation	RRHLYDPKMQTDKPF CCCCCCCCCCCCCCC	40.52	-
192	Ubiquitination	RRHLYDPKMQTDKPF CCCCCCCCCCCCCCC	40.52	23000965
197	Acetylation	DPKMQTDKPFDQTTI CCCCCCCCCCCCCEE	51.47	23236377
197	Ubiquitination	DPKMQTDKPFDQTTI CCCCCCCCCCCCCEE	51.47	23000965
205	Phosphorylation	PFDQTTISLQMGTNK CCCCCEEEEEECCCC	15.51	27251275
205	Ubiquitination	PFDQTTISLQMGTNK CCCCCEEEEEECCCC	15.51	23000965
210	Ubiquitination	TISLQMGTNKGASQA EEEEEECCCCCCHHC	28.54	21890473
210	Ubiquitination	TISLQMGTNKGASQA EEEEEECCCCCCHHC	28.54	21890473
210	Phosphorylation	TISLQMGTNKGASQA EEEEEECCCCCCHHC	28.54	-
210	Ubiquitination	TISLQMGTNKGASQA EEEEEECCCCCCHHC	28.54	23000965
212	Ubiquitination	SLQMGTNKGASQAGM EEEECCCCCCHHCCC	56.54	23000965
215	Ubiquitination	MGTNKGASQAGMLAP ECCCCCCHHCCCCCC	29.27	-
215	Phosphorylation	MGTNKGASQAGMLAP ECCCCCCHHCCCCCC	29.27	28857561
215	Ubiquitination	MGTNKGASQAGMLAP ECCCCCCHHCCCCCC	29.27	23000965
219	Sulfoxidation	KGASQAGMLAPGTRR CCCHHCCCCCCCCCC	3.02	28465586
224	Phosphorylation	AGMLAPGTRRDIYDQ CCCCCCCCCCCCCCC	22.82	28857561
232	Ubiquitination	RRDIYDQKLTLQPVD CCCCCCCCCEEEECC	40.31	23000965
234	Phosphorylation	DIYDQKLTLQPVDNS CCCCCCCEEEECCCC	30.31	24043423
241	Phosphorylation	TLQPVDNSTISLQMG EEEECCCCEEEEEEC	23.74	29514088
242	Phosphorylation	LQPVDNSTISLQMGT EEECCCCEEEEEECC	22.34	29514088
244	Phosphorylation	PVDNSTISLQMGTNK ECCCCEEEEEECCCH	16.79	29514088
247	Sulfoxidation	NSTISLQMGTNKVAS CCEEEEEECCCHHHC	9.67	30846556
249	Phosphorylation	TISLQMGTNKVASQK EEEEEECCCHHHCCC	26.90	24173317
251	Ubiquitination	SLQMGTNKVASQKGM EEEECCCHHHCCCCC	38.73	23000965
254	Phosphorylation	MGTNKVASQKGMSVY ECCCHHHCCCCCCEE	35.10	24117733
256	Ubiquitination	TNKVASQKGMSVYGL CCHHHCCCCCCEECC	54.83	23000965
256	Ubiquitination	TNKVASQKGMSVYGL CCHHHCCCCCCEECC	54.83	21890473
258	Sulfoxidation	KVASQKGMSVYGLGR HHHCCCCCCEECCCC	2.93	30846556
259	Phosphorylation	VASQKGMSVYGLGRQ HHCCCCCCEECCCCC	22.36	27499020
261	Phosphorylation	SQKGMSVYGLGRQVY CCCCCCEECCCCCCC	10.18	27273156
272	Phosphorylation	RQVYDPKYCAAPTEP CCCCCCCCCCCCCCC	7.84	25999147
277	Phosphorylation	PKYCAAPTEPVIHNG CCCCCCCCCCEEECC	48.47	27251275
282	Phosphorylation	APTEPVIHNGSQGTG CCCCCEEECCCCCCC	32.60	32142685
285	Phosphorylation	EPVIHNGSQGTGTNG CCEEECCCCCCCCCC	30.65	23927012
288	Phosphorylation	IHNGSQGTGTNGSEI EECCCCCCCCCCCCC	32.94	25247763
290	Phosphorylation	NGSQGTGTNGSEISD CCCCCCCCCCCCCCC	35.92	23927012
293	Phosphorylation	QGTGTNGSEISDSDY CCCCCCCCCCCCCCC	33.55	28387310
296	Phosphorylation	GTNGSEISDSDYQAE CCCCCCCCCCCCCCC	27.32	23927012
298	Phosphorylation	NGSEISDSDYQAEYP CCCCCCCCCCCCCCC	31.28	25247763
300	Phosphorylation	SEISDSDYQAEYPDE CCCCCCCCCCCCCCC	17.36	28387310
304	Phosphorylation	DSDYQAEYPDEYHGE CCCCCCCCCCCCCCC	20.99	23927012
308	Phosphorylation	QAEYPDEYHGEYQDD CCCCCCCCCCCCCCC	23.62	-
316	Phosphorylation	HGEYQDDYPRDYQYS CCCCCCCCCCCCCCC	14.41	20736484
320	Phosphorylation	QDDYPRDYQYSDQGI CCCCCCCCCCCCCCC	15.61	23403867
322	Phosphorylation	DYPRDYQYSDQGIDY CCCCCCCCCCCCCCC	14.16	28152594
323	Phosphorylation	YPRDYQYSDQGIDY- CCCCCCCCCCCCCC-	14.13	21082442
329	Phosphorylation	YSDQGIDY------- CCCCCCCC-------	20.66	23403867

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
10	Y	Phosphorylation	Kinase	SRC	P12931	PSP
293	S	Phosphorylation	Kinase	ROCK2	O75116	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of CNN3_HUMAN !!

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 CNN3_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CARM1_HUMAN	CARM1	physical	26186194
C1TM_HUMAN	MTHFD1L	physical	26344197
CARM1_HUMAN	CARM1	physical	28514442

Drug and Disease Associations

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

Regulatory Network of CNN3_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry."; Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.; Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-244, AND MASSSPECTROMETRY.	17287340 [Abstract]
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-323, AND MASSSPECTROMETRY.	17081983 [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-261, AND MASSSPECTROMETRY.	18083107 [Abstract]