CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-037142
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
  
Protein Name
 Calpain-5 
Protein Synonyms/Alias
  
Gene Name
 CAPN5 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
42TDDSLYYKGTPGPAVubiquitination[1, 2]
313HGLLAFFKSEKLDMIubiquitination[2, 3]
421GGGCINHKDTFFQNPubiquitination[4]
595KVRSAVQKGTSTPEYubiquitination[4]
605STPEYNVKGIFYRKKubiquitination[4]
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] 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] 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]
 [4] 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
Functional Description
  
Sequence Annotation
  
Keyword
 Complete proteome; Hydrolase; Protease; Reference proteome; Thiol protease. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 680 AA 
Protein Sequence
MFSCVKPYED QNYSALRRDC RRRKVLFEDP LFPATDDSLY YKGTPGPAVR WKRPKYSGHS 60
LAPHRPGWGD ARRMENVPRP GSSGCPSSSL RARDLGICED PRLFVDGISS HDLHQGQVGN 120
CWFVAACSSL ASRESLWQKV IPDWKEQEWD PEKPNAYAGI FHFHFWRFGE WVDVVIDDRL 180
PTVNNQLIYC HSNSRNEFWC ALVEKAYAKL AGCYQALDGG NTADALVDFT GGVSEPIDLT 240
EGDFANDETK RNQLFERMLK VHSRGGLISA SIKAVTAADM EARLACGLVK GHAYAVTDVR 300
KVRLGHGLLA FFKSEKLDMI RLRNPWGERE WNGPWSDTSE EWQKVSKSER EKMGVTVQDD 360
GEFWMTFEDV CRYFTDIIKC RVINTSHLSI HKTWEEARLH GAWTLHEDPR QNRGGGCINH 420
KDTFFQNPQY IFEVKKPEDE VLICIQQRPK RSTRREGKGE NLAIGFDIYK VEENRQYRMH 480
SLQHKAASSI YINSRSVFLR TDQPEGRYVI IPTTFEPGHT GEFLLRVFTD VPSNCRELRL 540
DEPPHTCWSS LCGYPQLVTQ VHVLGAAGLK DSPTGANSYV IIKCEGDKVR SAVQKGTSTP 600
EYNVKGIFYR KKLSQPITVQ VWNHRVLKDE FLGQVHLKAD PDNLQALHTL HLRDRNSRQP 660
SNLPGTVAVH ILSSTSLMAV 680 
Gene Ontology
 GO:0005622; C:intracellular; IEA:InterPro.
 GO:0004198; F:calcium-dependent cysteine-type endopeptidase activity; IEA:InterPro.
 GO:0006508; P:proteolysis; IEA:UniProtKB-KW. 
Interpro
 IPR000008; C2_Ca-dep.
 IPR008973; C2_Ca/lipid-bd_dom_CaLB.
 IPR022684; Calpain_cysteine_protease.
 IPR022682; Calpain_domain_III.
 IPR022683; Calpain_III.
 IPR000169; Pept_cys_AS.
 IPR001300; Peptidase_C2_calpain_cat. 
Pfam
 PF00168; C2
 PF01067; Calpain_III
 PF00648; Peptidase_C2 
SMART
 SM00239; C2
 SM00720; calpain_III
 SM00230; CysPc 
PROSITE
 PS50203; CALPAIN_CAT
 PS00139; THIOL_PROTEASE_CYS 
PRINTS
 PR00704; CALPAIN.