dbPTM

CNN2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	CNN2_HUMAN
UniProt AC	Q99439
Protein Name	Calponin-2
Gene Name	CNN2
Organism	Homo sapiens (Human).
Sequence Length	309
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	MSSTQFNKGPSYGLSAEVKNRLLSKYDPQKEAELRTWIEGLTGLSIGPDFQKGLKDGTILCTLMNKLQPGSVPKINRSMQNWHQLENLSNFIKAMVSYGMNPVDLFEANDLFESGNMTQVQVSLLALAGKAKTKGLQSGVDIGVKYSEKQERNFDDATMKAGQCVIGLQMGTNKCASQSGMTAYGTRRHLYDPKNHILPPMDHSTISLQMGTNKCASQVGMTAPGTRRHIYDTKLGTDKCDNSSMSLQMGYTQGANQSGQVFGLGRQIYDPKYCPQGTVADGAPSGTGDCPDPGEVPEYPPYYQEEAGY

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MSSTQFNKG ------CCCCCCCCC	41.93	29514088
2	Acetylation	------MSSTQFNKG ------CCCCCCCCC	41.93	22814378
3	Phosphorylation	-----MSSTQFNKGP -----CCCCCCCCCC	25.57	26074081
4	Phosphorylation	----MSSTQFNKGPS ----CCCCCCCCCCC	29.85	26074081
8	Methylation	MSSTQFNKGPSYGLS CCCCCCCCCCCCCCC	73.76	19608861
8	Acetylation	MSSTQFNKGPSYGLS CCCCCCCCCCCCCCC	73.76	19608861
8	Ubiquitination	MSSTQFNKGPSYGLS CCCCCCCCCCCCCCC	73.76	19608861
11	Phosphorylation	TQFNKGPSYGLSAEV CCCCCCCCCCCCHHH	40.27	21945579
12	Phosphorylation	QFNKGPSYGLSAEVK CCCCCCCCCCCHHHH	25.81	21945579
15	Phosphorylation	KGPSYGLSAEVKNRL CCCCCCCCHHHHHHH	20.30	21945579
19	Sumoylation	YGLSAEVKNRLLSKY CCCCHHHHHHHHHCC	28.05	-
19	Acetylation	YGLSAEVKNRLLSKY CCCCHHHHHHHHHCC	28.05	25953088
19	Sumoylation	YGLSAEVKNRLLSKY CCCCHHHHHHHHHCC	28.05	-
19	Ubiquitination	YGLSAEVKNRLLSKY CCCCHHHHHHHHHCC	28.05	-
24	Phosphorylation	EVKNRLLSKYDPQKE HHHHHHHHCCCHHHH	33.49	24702127
25	Acetylation	VKNRLLSKYDPQKEA HHHHHHHCCCHHHHH	54.35	19608861
25	Ubiquitination	VKNRLLSKYDPQKEA HHHHHHHCCCHHHHH	54.35	21890473
25	Ubiquitination	VKNRLLSKYDPQKEA HHHHHHHCCCHHHHH	54.35	21890473
25	Ubiquitination	VKNRLLSKYDPQKEA HHHHHHHCCCHHHHH	54.35	21890473
26	Phosphorylation	KNRLLSKYDPQKEAE HHHHHHCCCHHHHHH	29.49	28152594
30	Acetylation	LSKYDPQKEAELRTW HHCCCHHHHHHHHHH	65.37	23749302
30	Ubiquitination	LSKYDPQKEAELRTW HHCCCHHHHHHHHHH	65.37	-
42	Phosphorylation	RTWIEGLTGLSIGPD HHHHHHHHCCCCCCC	47.11	21712546
45	Phosphorylation	IEGLTGLSIGPDFQK HHHHHCCCCCCCHHH	27.18	27251275
52	Ubiquitination	SIGPDFQKGLKDGTI CCCCCHHHCCCCCCE	67.23	-
55	Ubiquitination	PDFQKGLKDGTILCT CCHHHCCCCCCEEEC	63.88	-
61	S-nitrosocysteine	LKDGTILCTLMNKLQ CCCCCEEECCCHHCC	2.13	-
61	S-nitrosylation	LKDGTILCTLMNKLQ CCCCCEEECCCHHCC	2.13	22178444
64	Sulfoxidation	GTILCTLMNKLQPGS CCEEECCCHHCCCCC	1.93	21406390
66	Ubiquitination	ILCTLMNKLQPGSVP EEECCCHHCCCCCCC	34.24	-
66	Acetylation	ILCTLMNKLQPGSVP EEECCCHHCCCCCCC	34.24	26051181
71	Phosphorylation	MNKLQPGSVPKINRS CHHCCCCCCCCCCHH	41.76	29978859
74	Ubiquitination	LQPGSVPKINRSMQN CCCCCCCCCCHHHCC	50.92	-
78	Phosphorylation	SVPKINRSMQNWHQL CCCCCCHHHCCHHHH	21.89	29978859
89	Phosphorylation	WHQLENLSNFIKAMV HHHHHHHHHHHHHHH	41.08	29978859
133	Phosphorylation	ALAGKAKTKGLQSGV HHHCHHHHCCCCCCC	34.89	21130716
134	Ubiquitination	LAGKAKTKGLQSGVD HHCHHHHCCCCCCCC	57.84	-
138	Phosphorylation	AKTKGLQSGVDIGVK HHHCCCCCCCCEECC	45.91	14702039
145	Ubiquitination	SGVDIGVKYSEKQER CCCCEECCCCHHCCC	37.53	-
147	Phosphorylation	VDIGVKYSEKQERNF CCEECCCCHHCCCCC	32.38	27251275
149	Ubiquitination	IGVKYSEKQERNFDD EECCCCHHCCCCCCH	52.06	-
158	Phosphorylation	ERNFDDATMKAGQCV CCCCCHHHCHHHCEE	26.63	-
159	Sulfoxidation	RNFDDATMKAGQCVI CCCCHHHCHHHCEEE	2.76	30846556
160	Acetylation	NFDDATMKAGQCVIG CCCHHHCHHHCEEEE	45.04	26051181
160	Ubiquitination	NFDDATMKAGQCVIG CCCHHHCHHHCEEEE	45.04	-
160	Methylation	NFDDATMKAGQCVIG CCCHHHCHHHCEEEE	45.04	-
164	S-nitrosylation	ATMKAGQCVIGLQMG HHCHHHCEEEEEECC	2.05	22178444
164	Glutathionylation	ATMKAGQCVIGLQMG HHCHHHCEEEEEECC	2.05	22555962
164	S-nitrosocysteine	ATMKAGQCVIGLQMG HHCHHHCEEEEEECC	2.05	-
170	Sulfoxidation	QCVIGLQMGTNKCAS CEEEEEECCCCHHHC	9.57	21406390
172	Phosphorylation	VIGLQMGTNKCASQS EEEEECCCCHHHCCC	26.60	18212344
174	Ubiquitination	GLQMGTNKCASQSGM EEECCCCHHHCCCCC	30.89	21906983
174	Methylation	GLQMGTNKCASQSGM EEECCCCHHHCCCCC	30.89	-
177	Phosphorylation	MGTNKCASQSGMTAY CCCCHHHCCCCCCCC	34.06	26552605
179	Phosphorylation	TNKCASQSGMTAYGT CCHHHCCCCCCCCCC	28.21	26552605
181	Sulfoxidation	KCASQSGMTAYGTRR HHHCCCCCCCCCCCC	2.04	30846556
182	Phosphorylation	CASQSGMTAYGTRRH HHCCCCCCCCCCCCC	21.91	29978859
184	Phosphorylation	SQSGMTAYGTRRHLY CCCCCCCCCCCCCCC	15.18	27259358
186	Phosphorylation	SGMTAYGTRRHLYDP CCCCCCCCCCCCCCC	16.32	29978859
187	Methylation	GMTAYGTRRHLYDPK CCCCCCCCCCCCCCC	21.47	-
188	Methylation	MTAYGTRRHLYDPKN CCCCCCCCCCCCCCC	24.81	-
191	Phosphorylation	YGTRRHLYDPKNHIL CCCCCCCCCCCCCCC	24.87	-
194	Ubiquitination	RRHLYDPKNHILPPM CCCCCCCCCCCCCCC	59.25	-
204	Phosphorylation	ILPPMDHSTISLQMG CCCCCCCCCEEEECC	24.15	27251275
205	Phosphorylation	LPPMDHSTISLQMGT CCCCCCCCEEEECCC	15.92	22210691
207	Phosphorylation	PMDHSTISLQMGTNK CCCCCCEEEECCCCC	16.79	28555341
214	Ubiquitination	SLQMGTNKCASQVGM EEECCCCCCHHHCCC	30.89	-
215	S-nitrosylation	LQMGTNKCASQVGMT EECCCCCCHHHCCCC	4.83	2212679
217	Phosphorylation	MGTNKCASQVGMTAP CCCCCCHHHCCCCCC	34.56	21406692
221	Sulfoxidation	KCASQVGMTAPGTRR CCHHHCCCCCCCCCC	2.80	30846556
222	Phosphorylation	CASQVGMTAPGTRRH CHHHCCCCCCCCCCE	24.62	21406692
226	Phosphorylation	VGMTAPGTRRHIYDT CCCCCCCCCCEEEEC	24.38	21406692
231	Phosphorylation	PGTRRHIYDTKLGTD CCCCCEEEECCCCCC	16.07	28796482
233	Phosphorylation	TRRHIYDTKLGTDKC CCCEEEECCCCCCCC	15.93	29083192
234	Sumoylation	RRHIYDTKLGTDKCD CCEEEECCCCCCCCC	41.86	-
234	Sumoylation	RRHIYDTKLGTDKCD CCEEEECCCCCCCCC	41.86	-
234	Ubiquitination	RRHIYDTKLGTDKCD CCEEEECCCCCCCCC	41.86	21890473
237	Phosphorylation	IYDTKLGTDKCDNSS EEECCCCCCCCCCCC	42.60	29083192
239	Ubiquitination	DTKLGTDKCDNSSMS ECCCCCCCCCCCCEE	43.24	-
243	Phosphorylation	GTDKCDNSSMSLQMG CCCCCCCCCEEEEEC	17.73	21406692
244	Phosphorylation	TDKCDNSSMSLQMGY CCCCCCCCEEEEECC	20.74	21406692
246	Phosphorylation	KCDNSSMSLQMGYTQ CCCCCCEEEEECCCC	19.87	21406692
251	Phosphorylation	SMSLQMGYTQGANQS CEEEEECCCCCCCCC	7.19	21406692
252	Phosphorylation	MSLQMGYTQGANQSG EEEEECCCCCCCCCC	18.13	21406692
258	Phosphorylation	YTQGANQSGQVFGLG CCCCCCCCCCEEEEC	30.88	21406692
269	Phosphorylation	FGLGRQIYDPKYCPQ EEECCCCCCCCCCCC	20.18	21406692
278	Phosphorylation	PKYCPQGTVADGAPS CCCCCCCCCCCCCCC	13.79	-
299	Phosphorylation	DPGEVPEYPPYYQEE CCCCCCCCCCCCCCC	11.93	21552520
302	Phosphorylation	EVPEYPPYYQEEAGY CCCCCCCCCCCCCCC	17.18	22817900
303	Phosphorylation	VPEYPPYYQEEAGY- CCCCCCCCCCCCCC-	18.41	22817900
309	Phosphorylation	YYQEEAGY------- CCCCCCCC-------	23.56	-

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
12	Y	Phosphorylation	Kinase	SRC	P12931	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of CNN2_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 CNN2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ZYX_HUMAN	ZYX	physical	22939629
HNRH2_HUMAN	HNRNPH2	physical	22939629
TPM1_HUMAN	TPM1	physical	22939629
FSCN1_HUMAN	FSCN1	physical	22939629
MAT2B_HUMAN	MAT2B	physical	22863883
CNN3_HUMAN	CNN3	physical	26186194
ATE1_HUMAN	ATE1	physical	26186194
TPPC9_HUMAN	TRAPPC9	physical	26186194
HEM2_HUMAN	ALAD	physical	26186194
AL8A1_HUMAN	ALDH8A1	physical	26344197
MTAP_HUMAN	MTAP	physical	26344197
SF01_HUMAN	SF1	physical	26344197
CNN3_HUMAN	CNN3	physical	28514442
HSP7C_HUMAN	HSPA8	physical	28514442
ATE1_HUMAN	ATE1	physical	28514442
HEM2_HUMAN	ALAD	physical	28514442
TPPC4_HUMAN	TRAPPC4	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 CNN2_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-8 AND LYS-25, AND MASSSPECTROMETRY.	19608861 [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-184, AND MASSSPECTROMETRY.	18083107 [Abstract]