CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-000148
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Calpain-2 catalytic subunit 
Protein Synonyms/Alias
 80 kDa M-calpain subunit; CALP80; Calcium-activated neutral proteinase 2; CANP 2; Calpain M-type; Calpain-2 large subunit; Millimolar-calpain; M-calpain 
Gene Name
 Capn2 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
7*MAGIAIKLAKDREAacetylation[1]
26GSHERAIKYLNQDYEacetylation[2]
76KTRGIEWKRPTEICAacetylation[2]
226KPPPNLFKIIQKALEacetylation[2]
230NLFKIIQKALEKGSLacetylation[2]
260VTYQKLVKGHAYSVTacetylation[1, 2]
260VTYQKLVKGHAYSVTubiquitination[3]
280ESSGSLQKLIRIRNPubiquitination[3]
360YKKWKLTKMDGNWRRacetylation[2]
414FLVGLIQKHRRRQRKacetylation[2]
637ALEEAGFKLPCQLHQacetylation[2]
674VRLETLFKIFKQLDPubiquitination[3]
Reference
 [1] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [2] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441]
 [3] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023] 
Functional Description
 Calcium-regulated non-lysosomal thiol-protease which catalyze limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction (By similarity). 
Sequence Annotation
 DOMAIN 45 344 Calpain catalytic.
 DOMAIN 572 605 EF-hand 1.
 DOMAIN 602 637 EF-hand 2.
 REGION 345 514 Domain III.
 REGION 515 529 Linker.
 REGION 530 700 Domain IV.
 ACT_SITE 105 105 By similarity.
 ACT_SITE 262 262 By similarity.
 ACT_SITE 286 286 By similarity.
 METAL 89 89 Calcium 3; via carbonyl oxygen (By
 METAL 91 91 Calcium 3; via carbonyl oxygen (By
 METAL 96 96 Calcium 3 (By similarity).
 METAL 175 175 Calcium 3 (By similarity).
 METAL 229 229 Calcium 2 (By similarity).
 METAL 230 230 Calcium 2 (By similarity).
 METAL 292 292 Calcium 4 (By similarity).
 METAL 299 299 Calcium 4 (By similarity).
 METAL 319 319 Calcium 4; via carbonyl oxygen (By
 METAL 323 323 Calcium 4; via carbonyl oxygen (By
 METAL 542 542 Calcium 5; via carbonyl oxygen (By
 METAL 545 545 Calcium 5 (By similarity).
 METAL 547 547 Calcium 5; via carbonyl oxygen (By
 METAL 552 552 Calcium 5 (By similarity).
 METAL 585 585 Calcium 6 (By similarity).
 METAL 587 587 Calcium 6 (By similarity).
 METAL 589 589 Calcium 6; via carbonyl oxygen (By
 METAL 591 591 Calcium 6; via carbonyl oxygen (By
 METAL 596 596 Calcium 6 (By similarity).
 METAL 615 615 Calcium 7 (By similarity).
 METAL 617 617 Calcium 7 (By similarity).
 METAL 619 619 Calcium 7; via carbonyl oxygen (By
 METAL 621 621 Calcium 7; via carbonyl oxygen (By
 METAL 626 626 Calcium 7 (By similarity).
 METAL 658 658 Calcium 1 (By similarity).
 METAL 661 661 Calcium 1 (By similarity).  
Keyword
 Calcium; Cell membrane; Complete proteome; Cytoplasm; Hydrolase; Membrane; Metal-binding; Protease; Reference proteome; Repeat; Thiol protease. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 700 AA 
Protein Sequence
MAGIAIKLAK DREAAEGLGS HERAIKYLNQ DYETLRNECL EAGALFQDPS FPALPSSLGY 60
KELGPYSSKT RGIEWKRPTE ICADPQFIIG GATRTDICQG ALGDCWLLAA IASLTLNEEI 120
LARVVPPDQS FQENYAGIFH FQFWQYGEWV EVVVDDRLPT KDGELLFVHS AEGSEFWSAL 180
LEKAYAKING CYEALSGGAT TEGFEDFTGG IAEWYELRKP PPNLFKIIQK ALEKGSLLGC 240
SIDITSAADS EAVTYQKLVK GHAYSVTGAE EVESSGSLQK LIRIRNPWGQ VEWTGKWNDN 300
CPSWNTVDPE VRANLTERQE DGEFWMSFSD FLRHYSRLEI CNLTPDTLTC DSYKKWKLTK 360
MDGNWRRGST AGGCRNYPNT FWMNPQYLIK LEEEDEDEED GERGCTFLVG LIQKHRRRQR 420
KMGEDMHTIG FGIYEVPEEL TGQTNIHLGK NFFLTTRARE RSDTFINLRE VLNRFKLPPG 480
EYVLVPSTFE PHKDGDFCIR VFSEKKADYQ AVDDEIEANI EEIDANEEDI DDGFRRLFVQ 540
LAGEDAEISA FELQTILRRV LAKRQDIKSD GFSIETCKIM VDMLDEDGSG KLGLKEFYIL 600
WTKIQKYQKI YREIDVDRSG TMNSYEMRKA LEEAGFKLPC QLHQVIVARF ADDELIIDFD 660
NFVRCLVRLE TLFKIFKQLD PENTGTIQLN LASWLSFSVL 700 
Gene Ontology
 GO:0000785; C:chromatin; IDA:MGI.
 GO:0005737; C:cytoplasm; IDA:MGI.
 GO:0005634; C:nucleus; IDA:MGI.
 GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
 GO:0005509; F:calcium ion binding; IEA:Compara.
 GO:0004198; F:calcium-dependent cysteine-type endopeptidase activity; TAS:MGI.
 GO:0001824; P:blastocyst development; IMP:MGI.
 GO:0007520; P:myoblast fusion; IMP:MGI.
 GO:0016540; P:protein autoprocessing; IEA:Compara.
 GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
 GO:0001666; P:response to hypoxia; 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
 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.