Javascript is not enabled on this browser. This site will not work properly without Javascript.
PhosphoSitePlus Homepage Cell Signaling Technology
PhosphoSitePlus
HomeAbout PhosphoSiteUsing PhosphoSiteCuration ProcessContact
NIH-logos NIGMS Logo NIAAA Logo NCI Logo NIH Logo
Protein Page:
CASP7 (fruit fly)
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
CASP7 Involved in the activation cascade of caspases responsible for apoptosis execution. Acts downstream of rpr. Cleaves baculovirus p35 and lamin DmO in vitro.
Protein type: Protease; EC 3.4.22.-; EC 3.4.22.60; Apoptosis; Mitochondrial; Endoplasmic reticulum
Molecular Function: cysteine-type endopeptidase activity
Biological Process: sterol regulatory element binding protein cleavage; spermatid differentiation; apoptosis; programmed cell death; regulation of retinal cell programmed cell death; nurse cell apoptosis; proteolysis; salivary gland histolysis; positive regulation of compound eye retinal cell programmed cell death; neuron remodeling; response to X-ray
Reference #:  O01382 (UniProtKB)
Alt. Names/Synonyms: Caspase; Caspase subunit p12; Caspase subunit p21; CG7788; drICE
Gene Symbols: Ice
Molecular weight: 37,363 Da
Basal Isoelectric point: 6.59  Predict pI for various phosphorylation states
CST Pathways:  Apoptosis Regulation  |  Death Receptor Signaling  |  ErbB/HER Signaling  |  Inhibition of Apoptosis
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

CASP7

Protein Structure Not Found.


STRING  |  Scansite  |  Pfam  |  RCSB PDB  |  ENZYME  |  Phospho.ELM  |  Source  |  GeneCards  |  UniProtKB  |  Entrez-Gene


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.


       fruit fly

► Hide Isoforms
 
0 6 - gap
0 1 - gap
0 2 - gap
0 1 - gap
1 1 - gap
0 1 - gap
0 4 - gap
1 0 - gap
0 5 - gap
0 6 - gap
1 1 K110 HFEVPTLKSRAGTNV
0 1 Y182 IYAKDTQYKLDNIWS
1 0 S198 FTANHCPSLAGKPKL
1 0 S265 WRNTTRGSWFMQSLC
0 1 - gap
0 1 - gap
  CASP7 iso2  
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
K95 FFDIPSLKSRTGTNV
Y167 LYAKDTQYKLDNIWH
S183 FTATFCPSLAGKPKL
S250 WRNINNGSWYMQSLI
- gap
- gap
  human

► Hide Isoforms
 
S16-p EEQGVEDsANEDSVD
A17 EQGVEDsANEDSVDA
N18 QGVEDsANEDSVDAK
S29-p VDAKPDRssFVPsLF
S30-p DAKPDRssFVPsLFs
S34-p DRssFVPsLFskKKK
S37-p sFVPsLFskKKKNVt
K38-ub FVPsLFskKKKNVtM
T44-p skKKKNVtMRsIKTT
S47-p KKNVtMRsIKTTRDR
K80-ub INNKNFDkVTGMGVR
T157-p IYGKDGVtPIKDLTA
T173-p FRGDRCKtLLEKPKL
S239-p WRSPGRGsWFVQALC
- gap
- gap
  CASP7 iso2  
S16 EEQGVEDSANEDSVD
A17 EQGVEDSANEDSVDA
N18 QGVEDSANEDSVDAK
S29 VDAKPDRSSFVPSLF
S30 DAKPDRSSFVPSLFS
S34 DRSSFVPSLFSKKKK
S37 SFVPSLFSKKKKNVT
K38 FVPSLFSKKKKNVTM
T44 SKKKKNVTMRSIKTT
S47 KKNVTMRSIKTTRDR
K80 INNKNFDKVTGMGVR
- gap
- gap
- gap
T193-p PTRGPSMtQMLILDt
T200-p tQMLILDtRSQWKLT
  mouse

 
S16-p AELEKVDsssEDGVD
S17-p ELEKVDsssEDGVDA
S18-p LEKVDsssEDGVDAK
S29 VDAKPDRSSIISSIL
S30 DAKPDRSSIISSILL
S34 DRSSIISSILLKKKR
- gap
K38 IISSILLKKKRNASA
S44 LKKKRNASAGPVRTG
- gap
K80-ub INNKNFDkATGMDVR
T157 IYGKDGVTPIKDLTA
T173 FRGDRCKTLLEKPKL
S239 WRNPGKGSWFVQALC
- gap
- gap
  rat

 
S16 AELEMADSSTEDGVD
S17 ELEMADSSTEDGVDA
T18 LEMADSSTEDGVDAK
S29 VDAKPDRSTIISSLL
T30 DAKPDRSTIISSLLW
S34 DRSTIISSLLWKKKK
- gap
K38 IISSLLWKKKKNASM
S44 WKKKKNASMCPVSTT
- gap
K80 INNKNFDKATGMDVR
T157 IYGKDGVTPIKDLTA
T173 FRGDRCKTLLEKPKL
S239 WRNPGKGSWFVQALC
- gap
- gap
Home  |  Curator Login With enhanced literature mining using Linguamatics I2E I2E Logo Produced by 3rd Millennium  |  Design by Digizyme
©2003-2013 Cell Signaling Technology, Inc.