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Protein Page:
CASP2 (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
CASP2 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. Heterotetramer that consists of two anti-parallel arranged heterodimers, each one formed by a p18 subunit and a p12 subunit. Interacts with LRDD. Expressed at higher levels in the embryonic lung, liver and kidney than in the heart and brain. In adults, higher level expression is seen in the placenta, lung, kidney, and pancreas than in the heart, brain, liver and skeletal muscle. Belongs to the peptidase C14A family. 2 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB.
Protein type: EC 3.4.22.55; Protease; EC 3.4.22.-; Apoptosis
Chromosomal Location of Human Ortholog: 7q34-q35
Cellular Component: membrane; mitochondrion; cytoplasm; cytosol; nucleus
Molecular Function: protein domain specific binding; protein binding; enzyme binding; cysteine-type endopeptidase activity
Biological Process: nerve growth factor receptor signaling pathway; luteolysis; apoptosis; positive regulation of apoptosis; germ cell programmed cell death; proteolysis; regulation of caspase activity; DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest; DNA damage response, signal transduction resulting in induction of apoptosis; positive regulation of neuron apoptosis; protein processing; brain development; aging
Reference #:  P42575 (UniProtKB)
Alt. Names/Synonyms: CASP-2; CASP2; caspase 2, apoptosis-related cysteine peptidase; Caspase-2; Caspase-2 subunit p12; Caspase-2 subunit p13; Caspase-2 subunit p18; ICH-1 protease; ICH-1L; ICH-1L/1S; ICH1; NEDD-2; NEDD2; NEDD2 apoptosis regulatory; Neural precursor cell expressed developmentally down-regulated protein 2; neural precursor cell expressed, developmentally down-regulated 2; Protease ICH-1
Gene Symbols: CASP2
Molecular weight: 50,685 Da
Basal Isoelectric point: 6.35  Predict pI for various phosphorylation states
CST Pathways:  Apoptosis Regulation  |  ErbB/HER Signaling  |  Mitochondrial Control of Apoptosis
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

CASP2

Protein Structure Not Found.


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Sites Implicated In
apoptosis, altered: S340‑p
cell cycle regulation: S139‑p
activity, inhibited: S157‑p
enzymatic activity, induced: S139‑p
protein conformation: S157‑p
protein processing: S139‑p

Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 1 R22 KELMAADRGRRILGV
0 1 K41 PHHQETLKKNRVVLA
1 0 K77-sm MRELIQAkVGSFSQN
0 1 K77-ub MRELIQAkVGSFSQN
0 1 K93-ub ELLNLLPkRGPQAFD
1 1 S139-p LSCDYDLsLPFPVCE
0 5 Y151-p VCESCPLyKKLRLsT
1 3 S157-p LyKKLRLsTDTVEHS
1 3 S340-p DGKNHAGsPGCEESD
0 1 Y368-p RSDMICGyACLKGtA
0 1 T374-p GyACLKGtAAMRNTK
0 1 K415-ub VKVNALIkDREGyAP
0 1 Y420-p LIkDREGyAPGTEFH
  mouse

 
R22-m1 KGLMAADrRSRILAV
K41 PDHQETLKKNRVVLA
K77 MRELIQAKGGSFSQN
K77 MRELIQAKGGSFSQN
K93 ELLNLLPKRGPQAFD
S139 LSCDYDTSLPFSVCE
H151 VCESCPPHKQLRLST
S157 PHKQLRLSTDATEHS
S340 DGKNHTQSPGCEESD
Y368 RSDMICGYACLKGNA
N374 GYACLKGNAAMRNTK
K415 VKVNALIKEREGYAP
Y420 LIKEREGYAPGTEFH
  rat

 
R22 KGLMAADRRSRILAV
K41-ub PDHQETLkKNRVVLA
K77 MRELIQAKGGSFSQN
K77 MRELIQAKGGSFSQN
K93 ELLNLLPKRGPQAFD
S139 LSCDYDSSLPFSVCE
H151 VCESCPPHKQSRLST
S157 PHKQSRLSTDTMEHS
S340 DGKNHAQSPGCEESD
Y368 RSDMICGYACLKGNA
N374 GYACLKGNAAMRNTK
K415 VKVNALIKEREGYAP
Y420 LIKEREGYAPGTEFH
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