CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-002501
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Calpain-1 catalytic subunit 
Protein Synonyms/Alias
 Calcium-activated neutral proteinase 1; CANP 1; Calpain mu-type; Calpain-1 large subunit; Cell proliferation-inducing gene 30 protein; Micromolar-calpain; muCANP 
Gene Name
 CAPN1 
Gene Synonyms/Alias
 CANPL1; PIG30 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
20GVSAQVQKQRARELGubiquitination[1, 2]
36GRHENAIKYLGQDYEubiquitination[1, 2, 3, 4]
71VPQSLGYKDLGPNSSubiquitination[3]
79DLGPNSSKTYGIKWKubiquitination[2, 3]
84SSKTYGIKWKRPTELacetylation[5]
84SSKTYGIKWKRPTELubiquitination[2, 3, 4]
86KTYGIKWKRPTELLSubiquitination[2, 3]
193FWSALLEKAYAKVNGubiquitination[3, 4]
229TEWYELRKAPSDLYQubiquitination[2, 3]
240DLYQIILKALERGSLubiquitination[4]
270ITFKKLVKGHAYSVTubiquitination[2, 3]
280AYSVTGAKQVNYRGQubiquitination[2, 3, 4]
328ERDQLRVKMEDGEFWubiquitination[2, 3]
359NLTPDALKSRTIRKWubiquitination[1, 3, 6, 7]
365LKSRTIRKWNTTLYEubiquitination[2, 3, 7, 8, 9]
398FWVNPQFKIRLDETDubiquitination[2, 4, 7, 8, 9, 10]
461GQPAVHLKRDFFLANubiquitination[3, 4, 11]
505PSTFEPNKEGDFVLRubiquitination[3, 4]
564EDMEISVKELRTILNubiquitination[2, 3]
583KHKDLRTKGFSLESCubiquitination[2]
Reference
 [1] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [2] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [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] 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]
 [5] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [6] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
 [7] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [8] 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]
 [9] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [10] 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]
 [11] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094
Functional Description
 Calcium-regulated non-lysosomal thiol-protease which catalyze limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction. 
Sequence Annotation
 DOMAIN 55 354 Calpain catalytic.
 DOMAIN 541 576 EF-hand 1.
 DOMAIN 585 618 EF-hand 2.
 DOMAIN 615 650 EF-hand 3.
 DOMAIN 680 714 EF-hand 4.
 REGION 355 526 Domain III.
 REGION 527 542 Linker.
 REGION 543 713 Domain IV.
 ACT_SITE 115 115 By similarity.
 ACT_SITE 272 272 By similarity.
 ACT_SITE 296 296 By similarity.
 MOD_RES 2 2 N-acetylserine.  
Keyword
 3D-structure; Acetylation; Autocatalytic cleavage; Calcium; Cell membrane; Complete proteome; Cytoplasm; Hydrolase; Membrane; Metal-binding; Polymorphism; Protease; Reference proteome; Repeat; Thiol protease. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 714 AA 
Protein Sequence
MSEEIITPVY CTGVSAQVQK QRARELGLGR HENAIKYLGQ DYEQLRVRCL QSGTLFRDEA 60
FPPVPQSLGY KDLGPNSSKT YGIKWKRPTE LLSNPQFIVD GATRTDICQG ALGDCWLLAA 120
IASLTLNDTL LHRVVPHGQS FQNGYAGIFH FQLWQFGEWV DVVVDDLLPI KDGKLVFVHS 180
AEGNEFWSAL LEKAYAKVNG SYEALSGGST SEGFEDFTGG VTEWYELRKA PSDLYQIILK 240
ALERGSLLGC SIDISSVLDM EAITFKKLVK GHAYSVTGAK QVNYRGQVVS LIRMRNPWGE 300
VEWTGAWSDS SSEWNNVDPY ERDQLRVKME DGEFWMSFRD FMREFTRLEI CNLTPDALKS 360
RTIRKWNTTL YEGTWRRGST AGGCRNYPAT FWVNPQFKIR LDETDDPDDY GDRESGCSFV 420
LALMQKHRRR ERRFGRDMET IGFAVYEVPP ELVGQPAVHL KRDFFLANAS RARSEQFINL 480
REVSTRFRLP PGEYVVVPST FEPNKEGDFV LRFFSEKSAG TVELDDQIQA NLPDEQVLSE 540
EEIDENFKAL FRQLAGEDME ISVKELRTIL NRIISKHKDL RTKGFSLESC RSMVNLMDRD 600
GNGKLGLVEF NILWNRIRNY LSIFRKFDLD KSGSMSAYEM RMAIESAGFK LNKKLYELII 660
TRYSEPDLAV DFDNFVCCLV RLETMFRFFK TLDTDLDGVV TFDLFKWLQL TMFA 714 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:HPA.
 GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
 GO:0005509; F:calcium ion binding; IEA:InterPro.
 GO:0004198; F:calcium-dependent cysteine-type endopeptidase activity; IEA:InterPro.
 GO:0008284; P:positive regulation of cell proliferation; TAS:ProtInc.
 GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
 GO:0032801; P:receptor catabolic process; IEA:Compara. 
Interpro
 IPR022684; Calpain_cysteine_protease.
 IPR022682; Calpain_domain_III.
 IPR022683; Calpain_III.
 IPR011992; EF-hand-like_dom.
 IPR018247; EF_Hand_1_Ca_BS.
 IPR002048; EF_hand_dom.
 IPR000169; Pept_cys_AS.
 IPR001300; Peptidase_C2_calpain_cat. 
Pfam
 PF01067; Calpain_III
 PF13405; EF_hand_4
 PF00648; Peptidase_C2 
SMART
 SM00720; calpain_III
 SM00230; CysPc
 SM00054; EFh 
PROSITE
 PS50203; CALPAIN_CAT
 PS00018; EF_HAND_1
 PS50222; EF_HAND_2
 PS00640; THIOL_PROTEASE_ASN
 PS00139; THIOL_PROTEASE_CYS
 PS00639; THIOL_PROTEASE_HIS 
PRINTS
 PR00704; CALPAIN.