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Protein Page:
DIABLO (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
DIABLO Promotes apoptosis by activating caspases in the cytochrome c/Apaf-1/caspase-9 pathway. Acts by opposing the inhibitory activity of inhibitor of apoptosis proteins (IAP). Inhibits the activity of BIRC6/bruce by inhibiting its binding to caspases. Isoform 3 attenuates the stability and apoptosis- inhibiting activity of XIAP/BIRC4 by promoting XIAP/BIRC4 ubiquitination and degradation through the ubiquitin-proteasome pathway. Isoform 3 also disrupts XIAP/BIRC4 interacting with processed caspase-9 and promotes caspase-3 activation. Isoform 1 is defective in the capacity to down-regulate the XIAP/BIRC4 abundance. Homodimer. Interacts with NGFRAP1/BEX3. Interacts with BIRC2/c-IAP1, BIRC3/c-IAP2, XIAP/BIRC4, BIRC6/bruce and BIRC7/livin. Interacts with the monomeric and dimeric form of BIRC5/survivin. Ubiquitously expressed with highest expression in testis. Expression is also high in heart, liver, kidney, spleen, prostate and ovary. Low in brain, lung, thymus and peripheral blood leukocytes. Isoform 3 is ubiquitously expressed. 3 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB.
Protein type: Apoptosis; Mitochondrial
Cellular Component: internal side of plasma membrane; mitochondrion; mitochondrial intermembrane space; cytosol
Molecular Function: protein binding
Biological Process: caspase activation; neuron apoptosis; induction of apoptosis via death domain receptors; positive regulation of apoptosis; apoptosis; caspase activation via cytochrome c; induction of apoptosis by oxidative stress
Reference #:  Q9NR28 (UniProtKB)
Alt. Names/Synonyms: 0610041G12Rik; DBLOH; DIABLO; diablo homolog (Drosophila); Diablo homolog, mitochondrial; DIABLO-S; Direct IAP-binding protein with low pI; FLJ10537; FLJ25049; mitochondrial Smac protein; Second mitochondria-derived activator of caspase; SMAC; SMAC3
Gene Symbols: DIABLO
Molecular weight: 27,131 Da
Basal Isoelectric point: 5.68  Predict pI for various phosphorylation states
CST Pathways:  Apoptosis Regulation  |  Death Receptor Signaling  |  Inhibition of Apoptosis  |  Mitochondrial Control of Apoptosis
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
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DIABLO

Protein Structure Not Found.


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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 S6-p __MAALKsWLsRSVt
0 1 S9-p AALKsWLsRSVtSFF
0 1 T13-p sWLsRSVtSFFRYRQ
1 0 S67-p AQKSEPHsLSSEALM
0 1 Y114 VYTLTSLYRQYTSLL
0 9 K123-ub QYTSLLGkMNSEEED
0 5 K146-ub ARAEMTSkHQEYLKL
0 18 K191-ub RNHIQLVkLQVEEVH
0 2 K203-ub EVHQLSRkAETkLAE
0 1 K207 LSRkAETKLAEAQIE
0 3 K207-ub LSRkAETkLAEAQIE
0 2 E214 kLAEAQIEELRQktQ
0 6 K219-ub QIEELRQktQEEGEE
0 14 T220-p IEELRQktQEEGEER
0 1 G224 RQktQEEGEERAEsE
0 3 S230-p EGEERAEsEQEAYLR
  mouse

 
S6 __MAALRSWVTRSVC
T9 AALRSWVTRSVCSLF
C13 SWVTRSVCSLFRYRQ
S65 AQKSEPQSLSNEALM
Y112 VYTLVSLYRQYTSLL
K121 QYTSLLGKMNSQEED
K144 ARVEMTSKQQEYLKL
K189-ub RNHIQLVkSQVQEVR
K201 EVRQLSQKAETkLAE
K205-ac LSQKAETkLAEAQTk
K205 LSQKAETKLAEAQTk
K212-ub kLAEAQTkELHQkAQ
K217-ub QTkELHQkAQEVsDE
A218 TkELHQkAQEVsDEG
S222-p HQkAQEVsDEGADQE
Q228 VsDEGADQEEEAYLR
  rat

 
S6 __MAALRSWMTRSVT
T9 AALRSWMTRSVTFLF
T13 SWMTRSVTFLFRYGQ
S65 AQKSEPQSLSNEALM
Y112-p VYTLVSLyRQYTSLL
K121 QYTSLLGKMNSQEED
K144 ARVEMTSKQQEYLKL
K189 RNHIQLVKSQVQEVR
K201 EVRQLSQKAETkLAE
K205-ac LSQKAETkLAEVQTQ
K205 LSQKAETKLAEVQTQ
Q212 kLAEVQTQELRQKTQ
K217 QTQELRQKTQEAsDE
T218 TQELRQKTQEAsDEA
S222-p RQKTQEAsDEAADQE
Q228 AsDEAADQEEEAYLR
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