CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-001264
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Calpain-15 
Protein Synonyms/Alias
 Small optic lobes homolog 
Gene Name
 SOLH 
Gene Synonyms/Alias
 CAPN15 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
32ICEAPRHKPDLNHILubiquitination[1]
293LAELLSGKRLSVLEEubiquitination[1, 2, 3, 4]
404GRVSSAQKAARVLPEubiquitination[5]
430LLNALRAKHCAACHTubiquitination[1]
471QTDEGEAKALWENIVubiquitination[1, 3]
618LFSQAQRKQLWVALIubiquitination[1]
627LWVALIEKALAKLHGubiquitination[1]
681DTDLIWAKMLSSKEAubiquitination[1, 2, 3]
686WAKMLSSKEAGFLMGubiquitination[1, 3]
702SCGGGNMKVDDSAYEubiquitination[1]
791FDSVDICKVHSDWQEubiquitination[1, 3]
1053THRLAHRKAAQAFLSubiquitination[1]
1066LSDWTASKGTHSPPLubiquitination[1, 3, 6, 7]
Reference
 [1] 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]
 [2] 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]
 [3] 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]
 [4] 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]
 [5] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
 Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
 J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931]
 [6] 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]
 [7] 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
Functional Description
  
Sequence Annotation
 DOMAIN 487 793 Calpain catalytic.
 ZN_FING 3 32 RanBP2-type 1.
 ZN_FING 44 73 RanBP2-type 2.
 ZN_FING 143 172 RanBP2-type 3.
 ZN_FING 338 369 RanBP2-type 4.
 ZN_FING 412 441 RanBP2-type 5.
 ACT_SITE 552 552 By similarity.
 ACT_SITE 717 717 By similarity.
 ACT_SITE 737 737 By similarity.  
Keyword
 Alternative splicing; Complete proteome; Hydrolase; Metal-binding; Protease; Reference proteome; Repeat; Thiol protease; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1086 AA 
Protein Sequence
MATVGEWSCV RCTFLNPAGQ RQCSICEAPR HKPDLNHILR LSVEEQKWPC ARCTFRNFLG 60
KEACEVCGFT PEPAPGAAFL PVLNGVLPKP PAILGEPKGS CQEEAGPVRT AGLVATEPAR 120
GQCEDKDEEE KEEQEEEEGA AEPRGGWACP RCTLHNTPVA SSCSVCGGPR RLSLPRIPPE 180
ALVVPEVVAP AGFHVVPAAP PPGLPGEGAE ANPPATSQGP AAEPEPPRVP PFSPFSSTLQ 240
NNPVPRSRRE VPPQLQPPVP EAAQPSPSAG CRGAPQGSGW AGASRLAELL SGKRLSVLEE 300
EATEGGTSRV EAGSSTSGSD IIDLAGDTVR YTPASPSSPD FTTWSCAKCT LRNPTVAPRC 360
SACGCSKLHG FQEHGEPPTH CPDCGADKPS PCGRSCGRVS SAQKAARVLP ERPGQWACPA 420
CTLLNALRAK HCAACHTPQL LVAQRRGAAP LRRRESMHVE QRRQTDEGEA KALWENIVAF 480
CRENNVSFVD DSFPPGPESV GFPAGDSVQQ RVRQWLRPQE INCSVFRDHR ATWSVFHTLR 540
PSDILQGLLG NCWFLSALAV LAERPDLVER VMVTRSLCAE GAYQVRLCKD GTWTTVLVDD 600
MLPCDEAGCL LFSQAQRKQL WVALIEKALA KLHGSYFALQ AGRAIEGLAT LTGAPCESLA 660
LQLSSTNPRE EPVDTDLIWA KMLSSKEAGF LMGASCGGGN MKVDDSAYES LGLRPRHAYS 720
ILDVRDVQGT RLLRLRNPWG RFSWNGSWSD EWPHWPGHLR GELMPHGSSE GVFWMEYGDF 780
VRYFDSVDIC KVHSDWQEAR VQGCFPSSAS APVGVTALTV LERASLEFAL FQEGSRRSDA 840
VDSHLLDLCI LVFRATFGSG GHLSLGRLLA HSKRAVKKFV SCDVMLEPGE YAVVCCAFNH 900
WGPPLPGTPA PQASSPSAGV PRASPEPPGH VLAVYSSRLV MVEPVEAQPT TLADAIILLT 960
ESRGERHEGR EGMTCYYLTH GWAGLIVVVE NRHPKAYLHV QCDCTDSFNV VSTRGSLRTQ 1020
DSVPPLHRQV LVILSQLEGN AGFSITHRLA HRKAAQAFLS DWTASKGTHS PPLTPEVAGL 1080
HGPRPL 1086 
Gene Ontology
 GO:0005622; C:intracellular; IEA:InterPro.
 GO:0004198; F:calcium-dependent cysteine-type endopeptidase activity; TAS:ProtInc.
 GO:0003700; F:sequence-specific DNA binding transcription factor activity; TAS:ProtInc.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0006508; P:proteolysis; IEA:UniProtKB-KW. 
Interpro
 IPR022684; Calpain_cysteine_protease.
 IPR000169; Pept_cys_AS.
 IPR001300; Peptidase_C2_calpain_cat.
 IPR001876; Znf_RanBP2. 
Pfam
 PF00648; Peptidase_C2
 PF00641; zf-RanBP 
SMART
 SM00230; CysPc
 SM00547; ZnF_RBZ 
PROSITE
 PS50203; CALPAIN_CAT
 PS00640; THIOL_PROTEASE_ASN
 PS00139; THIOL_PROTEASE_CYS
 PS00639; THIOL_PROTEASE_HIS
 PS01358; ZF_RANBP2_1
 PS50199; ZF_RANBP2_2 
PRINTS
 PR00704; CALPAIN.