CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-007569
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Caspase-2 
Protein Synonyms/Alias
 CASP-2; Neural precursor cell expressed developmentally down-regulated protein 2; NEDD-2; Protease ICH-1; Caspase-2 subunit p18; Caspase-2 subunit p13; Caspase-2 subunit p12 
Gene Name
 CASP2 
Gene Synonyms/Alias
 ICH1; NEDD2 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
15SWSTFQHKELMAADRubiquitination[1, 2]
42HHQETLKKNRVVLAKubiquitination[2]
77MRELIQAKVGSFSQNsumoylation[3]
77MRELIQAKVGSFSQNubiquitination[2, 4]
93ELLNLLPKRGPQAFDubiquitination[2, 4]
168VEHSLDNKDGPVCLQubiquitination[2]
177GPVCLQVKPCTPEFYubiquitination[2]
214NVHFTGEKELEFRSGubiquitination[2, 5]
254TAQEMQEKLQNFAQLubiquitination[2]
311NCPSLQNKPKMFFIQubiquitination[2]
350CEESDAGKEKLPKMRubiquitination[2]
352ESDAGKEKLPKMRLPubiquitination[2]
409HVADMLVKVNALIKDubiquitination[2]
415VKVNALIKDREGYAPubiquitination[2, 4]
430GTEFHRCKEMSEYCSubiquitination[1, 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] Caspase recruitment domain of procaspase-2 could be a target for SUMO-1 modification through Ubc9.
 Shirakura H, Hayashi N, Ogino S, Tsuruma K, Uehara T, Nomura Y.
 Biochem Biophys Res Commun. 2005 Jun 17;331(4):1007-15. [PMID: 15882978]
 [4] 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]
 [5] 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] 
Functional Description
 Involved in the activation cascade of caspases responsible for apoptosis execution. Might function by either activating some proteins required for cell death or inactivating proteins necessary for cell survival. 
Sequence Annotation
 DOMAIN 32 121 CARD.
 ACT_SITE 277 277 By similarity.
 ACT_SITE 320 320 By similarity.
 MOD_RES 2 2 N-acetylalanine.
 MOD_RES 340 340 Phosphoserine.  
Keyword
 3D-structure; Acetylation; Alternative splicing; Apoptosis; Complete proteome; Hydrolase; Phosphoprotein; Polymorphism; Protease; Reference proteome; Thiol protease; Zymogen. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 452 AA 
Protein Sequence
MAAPSAGSWS TFQHKELMAA DRGRRILGVC GMHPHHQETL KKNRVVLAKQ LLLSELLEHL 60
LEKDIITLEM RELIQAKVGS FSQNVELLNL LPKRGPQAFD AFCEALRETK QGHLEDMLLT 120
TLSGLQHVLP PLSCDYDLSL PFPVCESCPL YKKLRLSTDT VEHSLDNKDG PVCLQVKPCT 180
PEFYQTHFQL AYRLQSRPRG LALVLSNVHF TGEKELEFRS GGDVDHSTLV TLFKLLGYDV 240
HVLCDQTAQE MQEKLQNFAQ LPAHRVTDSC IVALLSHGVE GAIYGVDGKL LQLQEVFQLF 300
DNANCPSLQN KPKMFFIQAC RGDETDRGVD QQDGKNHAGS PGCEESDAGK EKLPKMRLPT 360
RSDMICGYAC LKGTAAMRNT KRGSWYIEAL AQVFSERACD MHVADMLVKV NALIKDREGY 420
APGTEFHRCK EMSEYCSTLC RHLYLFPGHP PT 452 
Gene Ontology
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0016020; C:membrane; IEA:Compara.
 GO:0005739; C:mitochondrion; IEA:Compara.
 GO:0005634; C:nucleus; IEA:Compara.
 GO:0004197; F:cysteine-type endopeptidase activity; IDA:UniProtKB.
 GO:0019899; F:enzyme binding; ISS:UniProtKB.
 GO:0007568; P:aging; IEA:Compara.
 GO:0097190; P:apoptotic signaling pathway; TAS:UniProtKB.
 GO:0007420; P:brain development; IEA:Compara.
 GO:0071260; P:cellular response to mechanical stimulus; IEP:UniProtKB.
 GO:0006977; P:DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest; IMP:UniProtKB.
 GO:0097194; P:execution phase of apoptosis; TAS:UniProtKB.
 GO:0006917; P:induction of apoptosis; IEA:Compara.
 GO:0001554; P:luteolysis; IEA:Compara.
 GO:0003407; P:neural retina development; IEA:Compara.
 GO:0048011; P:neurotrophin TRK receptor signaling pathway; TAS:Reactome.
 GO:0043065; P:positive regulation of apoptotic process; IDA:UniProtKB.
 GO:0043525; P:positive regulation of neuron apoptotic process; IEA:Compara.
 GO:0016485; P:protein processing; IDA:BHF-UCL.
 GO:0006508; P:proteolysis; IEA:UniProtKB-KW. 
Interpro
 IPR001315; CARD.
 IPR017350; Caspase_IL-1_beta.
 IPR011029; DEATH-like_dom.
 IPR011600; Pept_C14_cat.
 IPR001309; Pept_C14_ICE_p20.
 IPR016129; Pept_C14_ICE_p20_AS.
 IPR002138; Pept_C14_p10.
 IPR002398; Pept_C14_p45.
 IPR015917; Pept_C14_p45_core. 
Pfam
 PF00619; CARD
 PF00656; Peptidase_C14 
SMART
 SM00114; CARD
 SM00115; CASc 
PROSITE
 PS50209; CARD
 PS01122; CASPASE_CYS
 PS01121; CASPASE_HIS
 PS50207; CASPASE_P10
 PS50208; CASPASE_P20 
PRINTS
 PR00376; IL1BCENZYME.