CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-012557
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Calponin-3 
Protein Synonyms/Alias
 Calponin, acidic isoform 
Gene Name
 CNN3 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
6**MTHFNKGPSYGLSubiquitination[1]
17YGLSAEVKNKIASKYubiquitination[2]
23VKNKIASKYDHQAEEubiquitination[1]
158RFDEGKLKAGQSVIGubiquitination[1, 2]
172GLQMGTNKCASQAGMubiquitination[1]
197DPKMQTDKPFDQTTIubiquitination[1, 2]
212SLQMGTNKGASQAGMubiquitination[1, 2, 3]
232RRDIYDQKLTLQPVDubiquitination[1, 2, 3]
251SLQMGTNKVASQKGMubiquitination[1, 2, 3]
256TNKVASQKGMSVYGLubiquitination[1, 2, 4]
Reference
 [1] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [2] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [3] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [4] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473] 
Functional 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. 
Sequence Annotation
 DOMAIN 26 129 CH.
 REPEAT 164 189 Calponin-like 1.
 REPEAT 204 229 Calponin-like 2.
 REPEAT 243 268 Calponin-like 3.
 MOD_RES 323 323 Phosphoserine.  
Keyword
 Actin-binding; Calmodulin-binding; Complete proteome; Direct protein sequencing; Phosphoprotein; Reference proteome; Repeat. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 329 AA 
Protein Sequence
MTHFNKGPSY GLSAEVKNKI ASKYDHQAEE DLRNWIEEVT GMSIGPNFQL GLKDGIILCE 60
LINKLQPGSV KKVNESSLNW PQLENIGNFI KAIQAYGMKP HDIFEANDLF ENGNMTQVQT 120
TLVALAGLAK TKGFHTTIDI GVKYAEKQTR RFDEGKLKAG QSVIGLQMGT NKCASQAGMT 180
AYGTRRHLYD PKMQTDKPFD QTTISLQMGT NKGASQAGML APGTRRDIYD QKLTLQPVDN 240
STISLQMGTN KVASQKGMSV YGLGRQVYDP KYCAAPTEPV IHNGSQGTGT NGSEISDSDY 300
QAEYPDEYHG EYQDDYPRDY QYSDQGIDY 329 
Gene Ontology
 GO:0003779; F:actin binding; NAS:UniProtKB.
 GO:0005516; F:calmodulin binding; NAS:UniProtKB.
 GO:0005523; F:tropomyosin binding; NAS:UniProtKB.
 GO:0030172; F:troponin C binding; NAS:UniProtKB.
 GO:0031032; P:actomyosin structure organization; IEA:InterPro.
 GO:0006939; P:smooth muscle contraction; NAS:UniProtKB. 
Interpro
 IPR001997; Calponin.
 IPR000557; Calponin_repeat.
 IPR001715; CH-domain.
 IPR003096; SM22_calponin. 
Pfam
 PF00402; Calponin
 PF00307; CH 
SMART
 SM00033; CH 
PROSITE
 PS01052; CALPONIN_1
 PS51122; CALPONIN_2
 PS50021; CH 
PRINTS
 PR00889; CALPONIN.
 PR00888; SM22CALPONIN.