CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-024038
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Calpain-7 
Protein Synonyms/Alias
 PalB homolog; PalBH 
Gene Name
 CAPN7 
Gene Synonyms/Alias
 PALBH 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
74LHSAVQSKSADPLKSubiquitination[1, 2, 3]
82SADPLKSKHQLDLERubiquitination[3]
130TSYETADKVLQNKLKubiquitination[4, 5]
135ADKVLQNKLKQLARQubiquitination[3]
137KVLQNKLKQLARQALubiquitination[3]
156ALSEPLTKPVGKISSacetylation[6]
156ALSEPLTKPVGKISSubiquitination[1, 3, 7]
167KISSTSVKPKPPPVRubiquitination[2]
217EVLRTTSKINGIEYVubiquitination[2, 3, 7, 8]
247PFCDRWGKLPLSPKQubiquitination[3, 4, 5]
253GKLPLSPKQKTTFSKubiquitination[7]
309YERRFNKKLITGIIYubiquitination[3]
320GIIYPQNKDGEPEYNubiquitination[3]
331PEYNPCGKYMVKLHLubiquitination[3]
335PCGKYMVKLHLNGVPubiquitination[3]
344HLNGVPRKVIIDDQLubiquitination[3]
419SDSQTFSKDNSFRMLubiquitination[1, 3, 4, 5, 9]
477GLRFIQLKNPWSHLRubiquitination[3]
495RYSENDVKNWTPELQubiquitination[1, 3, 8]
503NWTPELQKYLNFDPRubiquitination[1, 3, 4, 5, 8]
561DAKQGPVKDAYSLANubiquitination[2]
596LSRHITDKDDFANNRubiquitination[1, 7]
641NSPHYLTKIKLTTPGubiquitination[2]
723IYQFHIEKTGPLLIEubiquitination[3]
Reference
 [1] 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]
 [2] 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]
 [3] 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]
 [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]
 [5] 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]
 [6] 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]
 [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] 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]
 [9] 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
Functional Description
 Calcium-regulated non-lysosomal thiol-protease (By similarity). 
Sequence Annotation
 DOMAIN 232 540 Calpain catalytic.
 REGION 541 701 Domain III.
 REGION 702 813 Domain N.
 ACT_SITE 290 290 By similarity.
 ACT_SITE 458 458 By similarity.
 ACT_SITE 578 578 By similarity.
 MOD_RES 95 95 Phosphothreonine.  
Keyword
 3D-structure; Complete proteome; Hydrolase; Nucleus; Phosphoprotein; Protease; Reference proteome; Repeat; Thiol protease. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 813 AA 
Protein Sequence
MDATALERDA VQFARLAVQR DHEGRYSEAV FYYKEAAQAL IYAEMAGSSL ENIQEKITEY 60
LERVQALHSA VQSKSADPLK SKHQLDLERA HFLVTQAFDE DEKENVEDAI ELYTEAVDLC 120
LKTSYETADK VLQNKLKQLA RQALDRAEAL SEPLTKPVGK ISSTSVKPKP PPVRAHFPLG 180
ANPFLERPQS FISPQSCDAQ GQRYTAEEIE VLRTTSKING IEYVPFMNVD LRERFAYPMP 240
FCDRWGKLPL SPKQKTTFSK WVRPEDLTNN PTMIYTVSSF SIKQTIVSDC SFVASLAISA 300
AYERRFNKKL ITGIIYPQNK DGEPEYNPCG KYMVKLHLNG VPRKVIIDDQ LPVDHKGELL 360
CSYSNNKSEL WVSLIEKAYM KVMGGYDFPG SNSNIDLHAL TGWIPERIAM HSDSQTFSKD 420
NSFRMLYQRF HKGDVLITAS TGMMTEAEGE KWGLVPTHAY AVLDIREFKG LRFIQLKNPW 480
SHLRWKGRYS ENDVKNWTPE LQKYLNFDPR TAQKIDNGIF WISWDDLCQY YDVIYLSWNP 540
GLFKESTCIH STWDAKQGPV KDAYSLANNP QYKLEVQCPQ GGAAVWVLLS RHITDKDDFA 600
NNREFITMVV YKTDGKKVYY PADPPPYIDG IRINSPHYLT KIKLTTPGTH TFTLVVSQYE 660
KQNTIHYTVR VYSACSFTFS KIPSPYTLSK RINGKWSGQS AGGCGNFQET HKNNPIYQFH 720
IEKTGPLLIE LRGPRQYSVG FEVVTVSTLG DPGPHGFLRK SSGDYRCGFC YLELENIPSG 780
IFNIIPSTFL PKQEGPFFLD FNSIIPIKIT QLQ 813 
Gene Ontology
 GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
 GO:0004198; F:calcium-dependent cysteine-type endopeptidase activity; IEA:InterPro.
 GO:0097264; P:self proteolysis; IDA:UniProtKB. 
Interpro
 IPR022684; Calpain_cysteine_protease.
 IPR022682; Calpain_domain_III.
 IPR022683; Calpain_III.
 IPR007330; MIT.
 IPR001300; Peptidase_C2_calpain_cat. 
Pfam
 PF01067; Calpain_III
 PF04212; MIT
 PF00648; Peptidase_C2 
SMART
 SM00720; calpain_III
 SM00230; CysPc
 SM00745; MIT 
PROSITE
 PS50203; CALPAIN_CAT
 PS00640; THIOL_PROTEASE_ASN
 PS00139; THIOL_PROTEASE_CYS
 PS00639; THIOL_PROTEASE_HIS 
PRINTS
 PR00704; CALPAIN.