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Protein

Diablo homolog, mitochondrial

Gene

Diablo

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 (By similarity).By similarity

GO - Biological processi

  • activation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
  • activation of cysteine-type endopeptidase activity involved in apoptotic process by cytochrome c Source: MGI
  • intrinsic apoptotic signaling pathway Source: UniProtKB
  • intrinsic apoptotic signaling pathway in response to oxidative stress Source: MGI
  • neuron apoptotic process Source: MGI
  • positive regulation of apoptotic process Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Apoptosis

Enzyme and pathway databases

ReactomeiREACT_311055. Release of apoptotic factors from the mitochondria.
REACT_311974. SMAC-mediated dissociation of IAP:caspase complexes.
REACT_350996. SMAC binds to IAPs.

Names & Taxonomyi

Protein namesi
Recommended name:
Diablo homolog, mitochondrial
Alternative name(s):
Direct IAP-binding protein with low pI
Second mitochondria-derived activator of caspase
Short name:
Smac
Gene namesi
Name:Diablo
Synonyms:Smac
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 5

Organism-specific databases

MGIiMGI:1913843. Diablo.

Subcellular locationi

GO - Cellular componenti

  • CD40 receptor complex Source: BHF-UCL
  • cytoplasm Source: MGI
  • cytoplasmic side of plasma membrane Source: BHF-UCL
  • mitochondrial intermembrane space Source: UniProtKB
  • mitochondrion Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 5353MitochondrionBy similarityAdd
BLAST
Chaini54 – 237184Diablo homolog, mitochondrialPRO_0000021073Add
BLAST

Post-translational modificationi

Ubiquitinated by BIRC7/livin.By similarity

Keywords - PTMi

Ubl conjugation

Proteomic databases

MaxQBiQ9JIQ3.
PaxDbiQ9JIQ3.
PRIDEiQ9JIQ3.

PTM databases

PhosphoSiteiQ9JIQ3.

Expressioni

Tissue specificityi

Highest expression found in heart, liver, kidney and testis.1 Publication

Gene expression databases

CleanExiMM_DIABLO.
ExpressionAtlasiQ9JIQ3. baseline and differential.
GenevestigatoriQ9JIQ3.

Interactioni

Subunit structurei

Homodimer. 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 (By similarity). Interacts with NGFRAP1/BEX3.By similarity1 Publication

Protein-protein interaction databases

BioGridi211579. 2 interactions.
IntActiQ9JIQ3. 2 interactions.
MINTiMINT-1341305.

Structurei

3D structure databases

ProteinModelPortaliQ9JIQ3.
SMRiQ9JIQ3. Positions 54-237.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi54 – 585IAP-bindingSequence Analysis

Domaini

The mature N-terminus mediates interaction with XIAP/BIRC4.By similarity

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiNOG42122.
GeneTreeiENSGT00390000007237.
HOGENOMiHOG000217916.
HOVERGENiHBG051315.
InParanoidiQ9JIQ3.
KOiK10522.
OMAiQKLEPHS.
OrthoDBiEOG7SJD66.
PhylomeDBiQ9JIQ3.
TreeFamiTF102048.

Family and domain databases

InterProiIPR015142. Smac_DIABLO.
IPR009062. Smac_DIABLO-like.
[Graphical view]
PfamiPF09057. Smac_DIABLO. 1 hit.
[Graphical view]
SUPFAMiSSF46984. SSF46984. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9JIQ3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAALRSWVTR SVCSLFRYRQ RFPVLANSKK RCFSELIKPW HKTVLTGFGM
60 70 80 90 100
TLCAVPIAQK SEPQSLSNEA LMRRAVSLVT DSTSTFLSQT TYALIEAITE
110 120 130 140 150
YTKAVYTLVS LYRQYTSLLG KMNSQEEDEV WQVIIGARVE MTSKQQEYLK
160 170 180 190 200
LETTWMTAVG LSEMAAEAAY QTGADQASIT ARNHIQLVKS QVQEVRQLSQ
210 220 230
KAETKLAEAQ TKELHQKAQE VSDEGADQEE EAYLRED
Length:237
Mass (Da):26,820
Last modified:October 3, 2012 - v2
Checksum:i6961A7E76C780AC5
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti64 – 641Q → H in AAF82190 (PubMed:10929712).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF203914 mRNA. Translation: AAF82190.1.
AK012760 mRNA. Translation: BAB28450.1.
AK002887 mRNA. No translation available.
AK077198 mRNA. Translation: BAC36676.1.
AK133194 mRNA. Translation: BAE21552.1.
AC157931 Genomic DNA. No translation available.
CCDSiCCDS39270.1.
RefSeqiNP_075721.3. NM_023232.3.
UniGeneiMm.46716.

Genome annotation databases

EnsembliENSMUST00000111587; ENSMUSP00000107214; ENSMUSG00000029433.
ENSMUST00000125652; ENSMUSP00000115045; ENSMUSG00000029433.
GeneIDi66593.
KEGGimmu:66593.
UCSCiuc008znx.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF203914 mRNA. Translation: AAF82190.1.
AK012760 mRNA. Translation: BAB28450.1.
AK002887 mRNA. No translation available.
AK077198 mRNA. Translation: BAC36676.1.
AK133194 mRNA. Translation: BAE21552.1.
AC157931 Genomic DNA. No translation available.
CCDSiCCDS39270.1.
RefSeqiNP_075721.3. NM_023232.3.
UniGeneiMm.46716.

3D structure databases

ProteinModelPortaliQ9JIQ3.
SMRiQ9JIQ3. Positions 54-237.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi211579. 2 interactions.
IntActiQ9JIQ3. 2 interactions.
MINTiMINT-1341305.

PTM databases

PhosphoSiteiQ9JIQ3.

Proteomic databases

MaxQBiQ9JIQ3.
PaxDbiQ9JIQ3.
PRIDEiQ9JIQ3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000111587; ENSMUSP00000107214; ENSMUSG00000029433.
ENSMUST00000125652; ENSMUSP00000115045; ENSMUSG00000029433.
GeneIDi66593.
KEGGimmu:66593.
UCSCiuc008znx.1. mouse.

Organism-specific databases

CTDi56616.
MGIiMGI:1913843. Diablo.

Phylogenomic databases

eggNOGiNOG42122.
GeneTreeiENSGT00390000007237.
HOGENOMiHOG000217916.
HOVERGENiHBG051315.
InParanoidiQ9JIQ3.
KOiK10522.
OMAiQKLEPHS.
OrthoDBiEOG7SJD66.
PhylomeDBiQ9JIQ3.
TreeFamiTF102048.

Enzyme and pathway databases

ReactomeiREACT_311055. Release of apoptotic factors from the mitochondria.
REACT_311974. SMAC-mediated dissociation of IAP:caspase complexes.
REACT_350996. SMAC binds to IAPs.

Miscellaneous databases

NextBioi322104.
PROiQ9JIQ3.
SOURCEiSearch...

Gene expression databases

CleanExiMM_DIABLO.
ExpressionAtlasiQ9JIQ3. baseline and differential.
GenevestigatoriQ9JIQ3.

Family and domain databases

InterProiIPR015142. Smac_DIABLO.
IPR009062. Smac_DIABLO-like.
[Graphical view]
PfamiPF09057. Smac_DIABLO. 1 hit.
[Graphical view]
SUPFAMiSSF46984. SSF46984. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of DIABLO, a mammalian protein that promotes apoptosis by binding to and antagonizing IAP proteins."
    Verhagen A.M., Ekert P.G., Pakusch M., Silke J., Connolly L.M., Reid G.E., Moritz R.L., Simpson R.J., Vaux D.L.
    Cell 102:43-53(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    Strain: BALB/c.
    Tissue: Kidney.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Testis.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  4. "Direct interaction of Smac with NADE promotes TRAIL-induced apoptosis."
    Yoon K., Jang H.D., Lee S.Y.
    Biochem. Biophys. Res. Commun. 319:649-654(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NGFRAP1.

Entry informationi

Entry nameiDBLOH_MOUSE
AccessioniPrimary (citable) accession number: Q9JIQ3
Secondary accession number(s): Q542V8, Q9CZD1, Q9DCD3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 18, 2001
Last sequence update: October 3, 2012
Last modified: April 1, 2015
This is version 117 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.