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Protein Page:
CASP7 iso2 (fruit fly)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitylation
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
CASP7 iso2 Involved in the activation cascade of caspases responsible for apoptosis execution (By similarity). Proteolytically cleaves poly(ADP-ribose) polymerase (PARP). Loss of zygotic DCP-1 function causes larval lethality and melanotic tumors.
Protein type: Apoptosis; EC 3.4.22.60; Endoplasmic reticulum; Mitochondrial; Protease
Cellular Component: cytosol; mitochondrion
Molecular Function: cysteine-type endopeptidase activity; protein binding
Biological Process: actin filament organization; apoptosis; autophagic cell death; cellular response to starvation; cytoplasmic transport, nurse cell to oocyte; multicellular organismal development; neuron remodeling; nurse cell apoptosis; oogenesis; ovarian nurse cell to oocyte transport; positive regulation of autophagy; positive regulation of macroautophagy; programmed cell death; proteolysis; salivary gland cell autophagic cell death
Reference #:  O02002 (UniProtKB)
Alt. Names/Synonyms: Caspase-1; Caspase-1 subunit p13; Caspase-1 subunit p22; CG5370; Dcp-1; Dcp1
Gene Symbols: Dcp-1
Molecular weight: 35,927 Da
Basal Isoelectric point: 7.63  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
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CASP7 iso2

Protein Structure Not Found.
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Scansite  |  Pfam  |  ENZYME  |  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


 LTP 

LTP: 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.


 HTP 

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


       fruit fly

► Hide Isoforms
 
0 17 S47 SSGLVAGSSHPYGSG
0 2 S48 SGLVAGSSHPYGSGA
0 3 H49 GLVAGSSHPYGSGAI
0 1 A60 SGAIGQLANGYSSPS
1 1 N61 GAIGQLANGYSSPSS
0 2 S65 QLANGYSSPSSSYRK
0 7 - gap
1 0 - gap
0 5 - gap
0 9 - gap
0 1 M95 MRHKNRGMALIFNHE
1 1 K110 HFEVPTLKSRAGTNV
0 1 Y182 IYAKDTQYKLDNIWS
0 1 D185 KDTQYKLDNIWSFFT
1 0 S198 FTANHCPSLAGKPKL
0 1 N260 PGFYSWRNTTRGSWF
1 0 S265 WRNTTRGSWFMQSLC
0 1 - gap
0 1 - gap
  CASP7 iso2  
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
V80 MSHKHRGVALIFNHE
K95 FFDIPSLKSRTGTNV
Y167 LYAKDTQYKLDNIWH
D170 KDTQYKLDNIWHYFT
S183 FTATFCPSLAGKPKL
N245 PGYFSWRNINNGSWY
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
K69‑ub MNFEKLGkCIIINNK
K80‑ub INNKNFDkVTGMGVR
T157‑p IYGKDGVtPIkDLTA
K160‑ub KDGVtPIkDLTAHFR
T173‑p FRGDRCKtLLEKPKL
S234‑p PGYYSWRsPGRGsWF
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
K69 MNFEKLGKCIIINNK
K80 INNKNFDKVTGMGVR
- gap
- gap
- 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
K69 MDFQKMGKCIIINNK
K80‑ub INNKNFDkATGMDVR
T157 IYGKDGVTPIKDLTA
K160 KDGVTPIKDLTAHFR
T173 FRGDRCKTLLEKPKL
N234 PGYYSWRNPGKGSWF
S239 WRNPGKGSWFVQALC
- gap
- gap
  rat

 
S16 AELEMADSSTEDGVD
S17 ELEMADSSTEDGVDA
T18 LEMADSSTEDGVDAK
S29 VDAKPDRSTIISSLL
T30 DAKPDRSTIISSLLW
S34 DRSTIISSLLWKKKK
- gap
K38 IISSLLWKKKKNASM
S44 WKKKKNASMCPVSTT
- gap
K69 MDFEKMGKCIIINNK
K80 INNKNFDKATGMDVR
T157 IYGKDGVTPIKDLTA
K160 KDGVTPIKDLTAHFR
T173 FRGDRCKTLLEKPKL
N234 PGYYSWRNPGKGSWF
S239 WRNPGKGSWFVQALC
- gap
- gap
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