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Protein

Diablo homolog, mitochondrial

Gene

DIABLO

Organism
Homo sapiens (Human)
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. 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.3 Publications

GO - Biological processi

  1. activation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
  2. activation of cysteine-type endopeptidase activity involved in apoptotic process by cytochrome c Source: ProtInc
  3. apoptotic process Source: Reactome
  4. extrinsic apoptotic signaling pathway via death domain receptors Source: ProtInc
  5. intrinsic apoptotic signaling pathway Source: UniProtKB
  6. intrinsic apoptotic signaling pathway in response to oxidative stress Source: Ensembl
  7. neuron apoptotic process Source: Ensembl
  8. positive regulation of apoptotic process Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Apoptosis

Enzyme and pathway databases

ReactomeiREACT_1322. Release of apoptotic factors from the mitochondria.
REACT_1767. SMAC-mediated dissociation of IAP:caspase complexes.
REACT_2190. 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
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:21528. DIABLO.

Subcellular locationi

  1. Mitochondrion 1 Publication

  2. Note: Released into the cytosol when cells undergo apoptosis.

GO - Cellular componenti

  1. CD40 receptor complex Source: BHF-UCL
  2. cytoplasmic side of plasma membrane Source: BHF-UCL
  3. cytosol Source: Reactome
  4. mitochondrial intermembrane space Source: UniProtKB
  5. mitochondrion Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Involvement in diseasei

Deafness, autosomal dominant, 64 (DFNA64)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA form of non-syndromic sensorineural hearing loss. Sensorineural deafness results from damage to the neural receptors of the inner ear, the nerve pathways to the brain, or the area of the brain that receives sound information.

See also OMIM:614152
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti126 – 1261S → L in DFNA64; does not increase apoptotic activity compared to wild-type; enhances the degradation of mutant and wild-type protein via heterodimerization; cells expressing the mutant protein show increased susceptibility to calcium-induced loss of mitochondrial potential compared to wild-type, indicating increased sensitivity to mitochondrial stress and suggestive of mitochondrial dysfunction. 1 Publication
VAR_066487

Keywords - Diseasei

Deafness, Disease mutation, Non-syndromic deafness

Organism-specific databases

MIMi614152. phenotype.
Orphaneti90635. Autosomal dominant non-syndromic sensorineural deafness type DFNA.
PharmGKBiPA134945044.

Polymorphism and mutation databases

DMDMi18203316.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 5555MitochondrionAdd
BLAST
Chaini56 – 239184Diablo homolog, mitochondrialPRO_0000021072Add
BLAST

Post-translational modificationi

Ubiquitinated by BIRC7/livin.1 Publication

Keywords - PTMi

Ubl conjugation

Proteomic databases

MaxQBiQ9NR28.
PaxDbiQ9NR28.
PRIDEiQ9NR28.

PTM databases

PhosphoSiteiQ9NR28.

Miscellaneous databases

PMAP-CutDBQ9NR28.

Expressioni

Tissue specificityi

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.2 Publications

Gene expression databases

BgeeiQ9NR28.
CleanExiHS_DIABLO.
ExpressionAtlasiQ9NR28. baseline.
GenevestigatoriQ9NR28.

Organism-specific databases

HPAiCAB003857.
CAB016688.
HPA001825.

Interactioni

Subunit structurei

Homodimer. Interacts with NGFRAP1/BEX3 (By similarity). 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 similarity4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ARL6IP1Q150413EBI-517508,EBI-714543
BIRC2Q134905EBI-517508,EBI-514538
BIRC5O153922EBI-517508,EBI-518823
BIRC7Q96CA56EBI-517508,EBI-517623
PRKCDQ056554EBI-517508,EBI-704279
XIAPP981709EBI-517508,EBI-517127

Protein-protein interaction databases

BioGridi121157. 41 interactions.
DIPiDIP-27627N.
IntActiQ9NR28. 22 interactions.
MINTiMINT-141675.
STRINGi9606.ENSP00000267169.

Structurei

Secondary structure

1
239
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi57 – 593Combined sources
Helixi69 – 11951Combined sources
Turni120 – 1234Combined sources
Helixi127 – 17347Combined sources
Helixi177 – 21135Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FEWX-ray2.20A56-239[»]
1G3FNMR-B56-64[»]
1G73X-ray2.00A/B56-217[»]
1OXQX-ray2.30F56-64[»]
1TW6X-ray1.71C/D56-64[»]
1XB0X-ray2.20G/H/I/J/K/L56-62[»]
1XB1X-ray2.70G/H/I/J/K/L56-62[»]
3D9UX-ray2.30B56-61[»]
3UIHX-ray2.40P/Q56-70[»]
3UIJX-ray2.70P/Q56-70[»]
ProteinModelPortaliQ9NR28.
SMRiQ9NR28. Positions 67-239.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9NR28.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi56 – 605IAP-binding

Domaini

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

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiNOG42122.
GeneTreeiENSGT00390000007237.
HOGENOMiHOG000217916.
HOVERGENiHBG051315.
InParanoidiQ9NR28.
KOiK10522.
OMAiQKLEPHS.
OrthoDBiEOG7SJD66.
PhylomeDBiQ9NR28.
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.

Sequences (3)i

Sequence statusi: Complete.

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

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9NR28-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAALKSWLSR SVTSFFRYRQ CLCVPVVANF KKRCFSELIR PWHKTVTIGF
60 70 80 90 100
GVTLCAVPIA QKSEPHSLSS EALMRRAVSL VTDSTSTFLS QTTYALIEAI
110 120 130 140 150
TEYTKAVYTL TSLYRQYTSL LGKMNSEEED EVWQVIIGAR AEMTSKHQEY
160 170 180 190 200
LKLETTWMTA VGLSEMAAEA AYQTGADQAS ITARNHIQLV KLQVEEVHQL
210 220 230
SRKAETKLAE AQIEELRQKT QEEGEERAES EQEAYLRED
Length:239
Mass (Da):27,131
Last modified:October 1, 2000 - v1
Checksum:i70C2AE0DC654D031
GO
Isoform 2 (identifier: Q9NR28-2) [UniParc]FASTAAdd to basket

Also known as: Diablo-S

The sequence of this isoform differs from the canonical sequence as follows:
     1-60: MAALKSWLSRSVTSFFRYRQCLCVPVVANFKKRCFSELIRPWHKTVTIGFGVTLCAVPIA → MKSDFYF

Show »
Length:186
Mass (Da):21,233
Checksum:iFF567F7827AB6108
GO
Isoform 3 (identifier: Q9NR28-3) [UniParc]FASTAAdd to basket

Also known as: SMAC3

The sequence of this isoform differs from the canonical sequence as follows:
     62-105: Missing.

Show »
Length:195
Mass (Da):22,284
Checksum:iB344087CF2A87C05
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti32 – 321K → E in BAB71568 (PubMed:14702039).Curated
Sequence conflicti44 – 441K → R in BAB14994 (PubMed:14702039).Curated
Sequence conflicti165 – 1651E → K in BAB71568 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti126 – 1261S → L in DFNA64; does not increase apoptotic activity compared to wild-type; enhances the degradation of mutant and wild-type protein via heterodimerization; cells expressing the mutant protein show increased susceptibility to calcium-induced loss of mitochondrial potential compared to wild-type, indicating increased sensitivity to mitochondrial stress and suggestive of mitochondrial dysfunction. 1 Publication
VAR_066487

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 6060MAALK…AVPIA → MKSDFYF in isoform 2. 1 PublicationVSP_004397Add
BLAST
Alternative sequencei62 – 10544Missing in isoform 3. 1 PublicationVSP_042785Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF262240 mRNA. Translation: AAF87716.1.
AY313210 mRNA. Translation: AAQ86939.1.
AK024768 mRNA. Translation: BAB14994.1.
AK057778 mRNA. Translation: BAB71568.1.
AK315629 mRNA. Translation: BAG37997.1.
AF298770 mRNA. Translation: AAG22077.1.
AC048338 Genomic DNA. No translation available.
BC004417 mRNA. Translation: AAH04417.1.
BC011909 mRNA. Translation: AAH11909.1.
CCDSiCCDS9228.1. [Q9NR28-1]
CCDS9229.1. [Q9NR28-3]
RefSeqiNP_001265231.1. NM_001278302.1.
NP_001265232.1. NM_001278303.1.
NP_001265233.1. NM_001278304.1. [Q9NR28-2]
NP_001265271.1. NM_001278342.1. [Q9NR28-3]
NP_063940.1. NM_019887.5. [Q9NR28-1]
NP_620308.1. NM_138930.3. [Q9NR28-2]
UniGeneiHs.169611.

Genome annotation databases

EnsembliENST00000267169; ENSP00000267169; ENSG00000184047. [Q9NR28-2]
ENST00000353548; ENSP00000320343; ENSG00000184047. [Q9NR28-3]
ENST00000443649; ENSP00000398495; ENSG00000184047. [Q9NR28-1]
ENST00000464942; ENSP00000442360; ENSG00000184047. [Q9NR28-2]
GeneIDi56616.
KEGGihsa:56616.
UCSCiuc010tab.2. human. [Q9NR28-1]
uc010tad.2. human. [Q9NR28-3]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF262240 mRNA. Translation: AAF87716.1.
AY313210 mRNA. Translation: AAQ86939.1.
AK024768 mRNA. Translation: BAB14994.1.
AK057778 mRNA. Translation: BAB71568.1.
AK315629 mRNA. Translation: BAG37997.1.
AF298770 mRNA. Translation: AAG22077.1.
AC048338 Genomic DNA. No translation available.
BC004417 mRNA. Translation: AAH04417.1.
BC011909 mRNA. Translation: AAH11909.1.
CCDSiCCDS9228.1. [Q9NR28-1]
CCDS9229.1. [Q9NR28-3]
RefSeqiNP_001265231.1. NM_001278302.1.
NP_001265232.1. NM_001278303.1.
NP_001265233.1. NM_001278304.1. [Q9NR28-2]
NP_001265271.1. NM_001278342.1. [Q9NR28-3]
NP_063940.1. NM_019887.5. [Q9NR28-1]
NP_620308.1. NM_138930.3. [Q9NR28-2]
UniGeneiHs.169611.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FEWX-ray2.20A56-239[»]
1G3FNMR-B56-64[»]
1G73X-ray2.00A/B56-217[»]
1OXQX-ray2.30F56-64[»]
1TW6X-ray1.71C/D56-64[»]
1XB0X-ray2.20G/H/I/J/K/L56-62[»]
1XB1X-ray2.70G/H/I/J/K/L56-62[»]
3D9UX-ray2.30B56-61[»]
3UIHX-ray2.40P/Q56-70[»]
3UIJX-ray2.70P/Q56-70[»]
ProteinModelPortaliQ9NR28.
SMRiQ9NR28. Positions 67-239.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi121157. 41 interactions.
DIPiDIP-27627N.
IntActiQ9NR28. 22 interactions.
MINTiMINT-141675.
STRINGi9606.ENSP00000267169.

PTM databases

PhosphoSiteiQ9NR28.

Polymorphism and mutation databases

DMDMi18203316.

Proteomic databases

MaxQBiQ9NR28.
PaxDbiQ9NR28.
PRIDEiQ9NR28.

Protocols and materials databases

DNASUi56616.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000267169; ENSP00000267169; ENSG00000184047. [Q9NR28-2]
ENST00000353548; ENSP00000320343; ENSG00000184047. [Q9NR28-3]
ENST00000443649; ENSP00000398495; ENSG00000184047. [Q9NR28-1]
ENST00000464942; ENSP00000442360; ENSG00000184047. [Q9NR28-2]
GeneIDi56616.
KEGGihsa:56616.
UCSCiuc010tab.2. human. [Q9NR28-1]
uc010tad.2. human. [Q9NR28-3]

Organism-specific databases

CTDi56616.
GeneCardsiGC12M122692.
HGNCiHGNC:21528. DIABLO.
HPAiCAB003857.
CAB016688.
HPA001825.
MIMi605219. gene.
614152. phenotype.
neXtProtiNX_Q9NR28.
Orphaneti90635. Autosomal dominant non-syndromic sensorineural deafness type DFNA.
PharmGKBiPA134945044.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG42122.
GeneTreeiENSGT00390000007237.
HOGENOMiHOG000217916.
HOVERGENiHBG051315.
InParanoidiQ9NR28.
KOiK10522.
OMAiQKLEPHS.
OrthoDBiEOG7SJD66.
PhylomeDBiQ9NR28.
TreeFamiTF102048.

Enzyme and pathway databases

ReactomeiREACT_1322. Release of apoptotic factors from the mitochondria.
REACT_1767. SMAC-mediated dissociation of IAP:caspase complexes.
REACT_2190. SMAC binds to IAPs.

Miscellaneous databases

ChiTaRSiDIABLO. human.
EvolutionaryTraceiQ9NR28.
GeneWikiiDiablo_homolog.
GenomeRNAii56616.
NextBioi62059.
PMAP-CutDBQ9NR28.
PROiQ9NR28.
SOURCEiSearch...

Gene expression databases

BgeeiQ9NR28.
CleanExiHS_DIABLO.
ExpressionAtlasiQ9NR28. baseline.
GenevestigatoriQ9NR28.

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. "Smac, a mitochondrial protein that promotes cytochrome c-dependent caspase activation by eliminating IAP inhibition."
    Du C., Fang M., Li Y., Li L., Wang X.
    Cell 102:33-42(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE, FUNCTION, TISSUE SPECIFICITY.
  2. "Molecular determinants of the caspase-promoting activity of Smac/DIABLO and its role in the death receptor pathway."
    Srinivasula S.M., Datta P., Fan X.J., Fernandes-Alnemri T., Huang Z., Alnemri E.S.
    J. Biol. Chem. 275:36152-36157(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), CHARACTERIZATION.
  3. "Smac3, a novel Smac/DIABLO splicing variant, attenuates the stability and apoptosis-inhibiting activity of X-linked inhibitor of apoptosis protein."
    Fu J., Jin Y., Arend L.J.
    J. Biol. Chem. 278:52660-52672(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Stomach.
  5. "The finished DNA sequence of human chromosome 12."
    Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
    , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
    Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Muscle and Uterus.
  7. "Dual role of BRUCE as an antiapoptotic IAP and a chimeric E2/E3 ubiquitin ligase."
    Bartke T., Pohl C., Pyrowolakis G., Jentsch S.
    Mol. Cell 14:801-811(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH BIRC6/BRUCE.
  8. "Livin promotes Smac/DIABLO degradation by ubiquitin-proteasome pathway."
    Ma L., Huang Y., Song Z., Feng S., Tian X., Du W., Qiu X., Heese K., Wu M.
    Cell Death Differ. 13:2079-2088(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION BY BIRC7/LIVIN, INTERACTION WITH BIRC7/LIVIN.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. Cited for: INTERACTION WITH BIRC5/SURVIVIN.
  11. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  12. "Structural and biochemical basis of apoptotic activation by Smac/DIABLO."
    Chai J., Du C., Wu J.W., Kyin S., Wang X., Shi Y.
    Nature 406:855-862(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 56-239.
  13. "Structural basis for binding of Smac/DIABLO to the XIAP BIR3 domain."
    Liu Z., Sun C., Olejniczak E.T., Meadows R.P., Betz S.F., Oost T., Herrmann J., Wu J.C., Fesik S.W.
    Nature 408:1004-1008(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 56-64 IN COMPLEX WITH XIAP.
  14. "Functional mutation of SMAC/DIABLO, encoding a mitochondrial proapoptotic protein, causes human progressive hearing loss DFNA64."
    Cheng J., Zhu Y., He S., Lu Y., Chen J., Han B., Petrillo M., Wrzeszczynski K.O., Yang S., Dai P., Zhai S., Han D., Zhang M.Q., Li W., Liu X., Li H., Chen Z.Y., Yuan H.
    Am. J. Hum. Genet. 89:56-66(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT DFNA64 LEU-126, CHARACTERIZATION OF DFNA64 LEU-126.

Entry informationi

Entry nameiDBLOH_HUMAN
AccessioniPrimary (citable) accession number: Q9NR28
Secondary accession number(s): B2RDQ0
, Q6W3F3, Q96LV0, Q9BT11, Q9HAV6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 18, 2001
Last sequence update: October 1, 2000
Last modified: April 29, 2015
This is version 148 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references

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.