CNN1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: CNN1_HUMAN
• UniProt AC: P51911
• Protein Name: Calponin-1
• Gene Name: CNN1
• Organism: Homo sapiens (Human).
• Sequence Length: 297
• 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 (By similarity)..
• Protein Sequence: MSSAHFNRGPAYGLSAEVKNKLAQKYDHQREQELREWIEGVTGRRIGNNFMDGLKDGIILCEFINKLQPGSVKKINESTQNWHQLENIGNFIKAITKYGVKPHDIFEANDLFENTNHTQVQSTLLALASMAKTKGNKVNVGVKYAEKQERKFEPGKLREGRNIIGLQMGTNKFASQQGMTAYGTRRHLYDPKLGTDQPLDQATISLQMGTNKGASQAGMTAPGTKRQIFEPGLGMEHCDTLNVSLQMGSNKGASQRGMTVYGLPRQVYDPKYCLTPEYPELGEPAHNHHAHNYYNSA

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MSSAHFNRG ------CCCCCCCCC	35.91	23663014
3	Phosphorylation	-----MSSAHFNRGP -----CCCCCCCCCC	25.19	23663014
12	Phosphorylation	HFNRGPAYGLSAEVK CCCCCCCCCCCHHHH	23.02	23663014
15	Phosphorylation	RGPAYGLSAEVKNKL CCCCCCCCHHHHHHH	20.30	26657352
25	Acetylation	VKNKLAQKYDHQREQ HHHHHHHHCCHHHHH	47.22	27178108
26	Phosphorylation	KNKLAQKYDHQREQE HHHHHHHCCHHHHHH	13.43	-
71	Phosphorylation	INKLQPGSVKKINES HHHCCCCCCEECCHH	37.13	27499020
78	Phosphorylation	SVKKINESTQNWHQL CCEECCHHHCCHHHH	30.70	26657352
170	Phosphorylation	IIGLQMGTNKFASQQ EEEEECCCCHHHHHC	29.87	21082442
175	Phosphorylation	MGTNKFASQQGMTAY CCCCHHHHHCCCCCC	26.60	26657352
180	Phosphorylation	FASQQGMTAYGTRRH HHHHCCCCCCCCCCC	24.45	23090842
182	Phosphorylation	SQQGMTAYGTRRHLY HHCCCCCCCCCCCCC	15.18	21253578
184	Phosphorylation	QGMTAYGTRRHLYDP CCCCCCCCCCCCCCC	16.32	23090842
189	Phosphorylation	YGTRRHLYDPKLGTD CCCCCCCCCCCCCCC	24.87	-
195	Phosphorylation	LYDPKLGTDQPLDQA CCCCCCCCCCCCCCE	41.73	21406692
203	Phosphorylation	DQPLDQATISLQMGT CCCCCCEEEEEECCC	12.88	21406692
205	Phosphorylation	PLDQATISLQMGTNK CCCCEEEEEECCCCC	14.27	21406692
210	Phosphorylation	TISLQMGTNKGASQA EEEEECCCCCCCHHC	28.54	21406692
212	Ubiquitination	SLQMGTNKGASQAGM EEECCCCCCCHHCCC	56.54	21906983
215	Phosphorylation	MGTNKGASQAGMTAP CCCCCCCHHCCCCCC	29.27	26657352
219	Sulfoxidation	KGASQAGMTAPGTKR CCCHHCCCCCCCCCC	3.03	30846556
225	Acetylation	GMTAPGTKRQIFEPG CCCCCCCCCCCCCCC	48.50	7618967
254	Phosphorylation	MGSNKGASQRGMTVY CCCCCCCHHCCCEEE	29.13	25332170
259	Phosphorylation	GASQRGMTVYGLPRQ CCHHCCCEEECCCCC	17.25	19060867
261	Phosphorylation	SQRGMTVYGLPRQVY HHCCCEEECCCCCCC	12.09	22461510
278	Phosphorylation	KYCLTPEYPELGEPA CCCCCCCCCCCCCCC	11.83	27251275
293	Phosphorylation	HNHHAHNYYNSA--- CCCCCCCCCCCC---	8.31	28857561
294	Phosphorylation	NHHAHNYYNSA---- CCCCCCCCCCC----	14.14	28857561
296	Phosphorylation	HAHNYYNSA------ CCCCCCCCC------	21.16	28857561

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
170	T	Phosphorylation	Kinase	ROCK2	O75116	Uniprot
175	S	Phosphorylation	Kinase	ROCK2	O75116	Uniprot
180	T	Phosphorylation	Kinase	ROCK2	O75116	Uniprot
184	T	Phosphorylation	Kinase	ROCK2	O75116	Uniprot
259	T	Phosphorylation	Kinase	ROCK2	O75116	Uniprot

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of CNN1_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of CNN1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
TPM1_HUMAN	TPM1	physical	2161834
ACTS_HUMAN	ACTA1	physical	2161834
MYO1A_HUMAN	MYO1A	physical	2161834
C1TC_HUMAN	MTHFD1	physical	26344197
C1TM_HUMAN	MTHFD1L	physical	26344197

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.