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Protein

Death-associated inhibitor of apoptosis 1

Gene

Diap1

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Anti-apoptotic protein which functions as a caspase regulator, using its E3 ubiquitin-protein ligase activity to smother caspase activity. Binds, ubiquitinates and inactivates initiator caspase Dronc, and effector caspases Drice and Dcp-1. Acts as a Nedd8-E3 ubiquitin-protein ligase for Drice. Suppresses apoptosis by targeting the apoptosome for ubiquitination and inactivation. Plays an important role in cell motility. Overexpression suppresses rpr and hid-dependent cell death in the eye. Interaction of Diap1 with Dronc is required to suppress Dronc-mediated cell death through Diap1-mediated ubiquitination of Dronc. Acts as a positive regulator of Wnt signaling.6 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi263 – 2631ZincPROSITE-ProRule annotation
Metal bindingi266 – 2661ZincPROSITE-ProRule annotation
Metal bindingi283 – 2831ZincPROSITE-ProRule annotation
Metal bindingi290 – 2901ZincPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri391 – 42636RING-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  • caspase binding Source: FlyBase
  • cysteine-type endopeptidase inhibitor activity Source: FlyBase
  • cysteine-type endopeptidase inhibitor activity involved in apoptotic process Source: FlyBase
  • ligase activity Source: UniProtKB-KW
  • NEDD8 ligase activity Source: FlyBase
  • ubiquitin conjugating enzyme binding Source: FlyBase
  • ubiquitin-like protein conjugating enzyme binding Source: FlyBase
  • ubiquitin protein ligase activity Source: FlyBase
  • ubiquitin protein ligase binding Source: FlyBase
  • ubiquitin-protein transferase activity Source: UniProtKB
  • ubiquitin-specific protease binding Source: FlyBase
  • zinc ion binding Source: FlyBase

GO - Biological processi

  • antennal morphogenesis Source: FlyBase
  • apoptotic process Source: FlyBase
  • border follicle cell migration Source: FlyBase
  • chaeta morphogenesis Source: FlyBase
  • germ cell migration Source: FlyBase
  • inhibition of cysteine-type endopeptidase activity Source: FlyBase
  • inhibition of cysteine-type endopeptidase activity involved in apoptotic process Source: FlyBase
  • multicellular organism development Source: FlyBase
  • negative regulation of apoptotic process Source: UniProtKB
  • negative regulation of compound eye retinal cell programmed cell death Source: FlyBase
  • negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: FlyBase
  • negative regulation of cysteine-type endopeptidase activity involved in execution phase of apoptosis Source: FlyBase
  • positive regulation of canonical Wnt signaling pathway Source: UniProtKB
  • positive regulation of protein ubiquitination Source: FlyBase
  • protein autoubiquitination Source: FlyBase
  • protein K48-linked ubiquitination Source: FlyBase
  • protein neddylation Source: FlyBase
  • protein polyubiquitination Source: FlyBase
  • protein ubiquitination involved in ubiquitin-dependent protein catabolic process Source: FlyBase
  • sensory organ development Source: FlyBase
  • sensory organ precursor cell division Source: FlyBase
  • spermatid nucleus differentiation Source: FlyBase
  • spermatogenesis Source: FlyBase
  • Wnt signaling pathway Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Apoptosis, Ubl conjugation pathway, Wnt signaling pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

SignaLinkiQ24306.

Protein family/group databases

MEROPSiI32.009.

Names & Taxonomyi

Protein namesi
Recommended name:
Death-associated inhibitor of apoptosis 1 (EC:6.3.2.-)
Alternative name(s):
Apoptosis 1 inhibitor
E3 ubiquitin-protein ligase th
Inhibitor of apoptosis 1
Protein thread
Gene namesi
Name:Diap1
Synonyms:Iap1, th
ORF Names:CG12284
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 3L

Organism-specific databases

FlyBaseiFBgn0260635. Diap1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: FlyBase
  • nucleus Source: FlyBase
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi162 – 1621I → D: Destroys cleavage site. 1 Publication
Mutagenesisi165 – 1651I → D: Destroys cleavage site. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 438438Death-associated inhibitor of apoptosis 1PRO_0000122367Add
BLAST

Post-translational modificationi

Ubiquitinated and degraded by HtrA2 in apoptotic cells; proteolytic cleavage at specific sites in the BIR domain linker region generating inactive fragments. Mutation of one site reduces but does not abolish cleavage as another site is selected by the protease.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei162 – 1632Cleavage; by HtrA2
Sitei165 – 1662Cleavage; by HtrA2

Keywords - PTMi

Ubl conjugation

Proteomic databases

PaxDbiQ24306.

Miscellaneous databases

PMAP-CutDBQ24306.

Expressioni

Gene expression databases

BgeeiQ24306.
ExpressionAtlasiQ24306. differential.
GenevisibleiQ24306. DM.

Interactioni

Subunit structurei

Interacts (via BIR 2 domain) with Dronc (via residues 114-125). Rpr, hid and grim can outcompete Dronc for binding Diap1 therefore removing Diap1-mediated ubiquitination. Interacts (via BIR 2 domain) with HtrA2; this displaces any bound Dronc. Interacts with Strica (PubMed:11550090).5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
chicP258432EBI-456419,EBI-156199
DroncQ9XYF49EBI-456419,EBI-108311
hidQ241068EBI-456419,EBI-135509
IKKepsilonQ86PE73EBI-456419,EBI-987197
rprQ244756EBI-456419,EBI-106786

GO - Molecular functioni

  • caspase binding Source: FlyBase
  • ubiquitin conjugating enzyme binding Source: FlyBase
  • ubiquitin-like protein conjugating enzyme binding Source: FlyBase
  • ubiquitin protein ligase binding Source: FlyBase
  • ubiquitin-specific protease binding Source: FlyBase

Protein-protein interaction databases

BioGridi65064. 29 interactions.
IntActiQ24306. 10 interactions.
MINTiMINT-1601077.
STRINGi7227.FBpp0305795.

Structurei

Secondary structure

1
438
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi40 – 423Combined sources
Helixi44 – 485Combined sources
Turni50 – 534Combined sources
Helixi61 – 666Combined sources
Beta strandi69 – 713Combined sources
Beta strandi78 – 803Combined sources
Turni81 – 833Combined sources
Beta strandi86 – 894Combined sources
Helixi96 – 1038Combined sources
Turni108 – 1125Combined sources
Helixi122 – 1287Combined sources
Beta strandi135 – 1373Combined sources
Helixi221 – 2233Combined sources
Helixi226 – 2327Combined sources
Helixi233 – 2353Combined sources
Beta strandi240 – 2423Combined sources
Helixi244 – 2496Combined sources
Beta strandi252 – 2543Combined sources
Beta strandi261 – 2633Combined sources
Turni264 – 2663Combined sources
Beta strandi269 – 2713Combined sources
Helixi279 – 2868Combined sources
Helixi291 – 2977Combined sources
Helixi299 – 3079Combined sources
Helixi309 – 3179Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1JD4X-ray2.70A/B201-323[»]
1JD5X-ray1.90A201-323[»]
1JD6X-ray2.70A201-323[»]
1Q4QX-ray2.10A/B/C/D/E/F/G/H/I/J201-323[»]
1SDZX-ray1.78A30-145[»]
1SE0X-ray1.75A30-145[»]
3SIPX-ray3.50E/F31-145[»]
3SIQX-ray2.40A/B/C/D/E/F1-135[»]
ProteinModelPortaliQ24306.
SMRiQ24306. Positions 38-145, 214-318, 385-425.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ24306.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati44 – 11067BIR 1Add
BLAST
Repeati226 – 29368BIR 2Add
BLAST

Sequence similaritiesi

Belongs to the IAP family.Curated
Contains 2 BIR repeats.PROSITE-ProRule annotation
Contains 1 RING-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri391 – 42636RING-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiKOG1101. Eukaryota.
ENOG410YPNM. LUCA.
GeneTreeiENSGT00500000044782.
InParanoidiQ24306.
KOiK04725.
OMAiTVATHAS.
OrthoDBiEOG78H3TF.
PhylomeDBiQ24306.

Family and domain databases

Gene3Di1.10.1170.10. 2 hits.
3.30.40.10. 1 hit.
InterProiIPR001370. BIR_rpt.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF00653. BIR. 2 hits.
[Graphical view]
SMARTiSM00238. BIR. 2 hits.
SM00184. RING. 1 hit.
[Graphical view]
PROSITEiPS01282. BIR_REPEAT_1. 2 hits.
PS50143. BIR_REPEAT_2. 2 hits.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q24306-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASVVADLPS YGPIAFDQVD NNTNATQLFK NNINKTRMND LNREETRLKT
60 70 80 90 100
FTDWPLDWLD KRQLAQTGMY FTHAGDKVKC FFCGVEIGCW EQEDQPVPEH
110 120 130 140 150
QRWSPNCPLL RRRTTNNVPI NAEALDRILP PISYDICGAN DSTLEMREHA
160 170 180 190 200
YAEGVIPMSQ LIQSIGMNAV NAAGSVTGTA APQPRVTVAT HASTATQATG
210 220 230 240 250
DVQPETCRPS AASGNYFPQY PEYAIETARL RTFEAWPRNL KQKPHQLAEA
260 270 280 290 300
GFFYTGVGDR VRCFSCGGGL MDWNDNDEPW EQHALWLSQC RFVKLMKGQL
310 320 330 340 350
YIDTVAAKPV LAEEKEESSS IGGVAVASTQ ASEEEQQTSL SSEEAVSGDV
360 370 380 390 400
APSVAPTAAT RIFNKIVEAT AVATPSTNSS GSTSIPEEKL CKICYGAEYN
410 420 430
TAFLPCGHVV ACAKCASSVT KCPLCRKPFT DVMRVYFS
Length:438
Mass (Da):48,038
Last modified:November 23, 2004 - v2
Checksum:i24CA8BC13F5DEF31
GO

Sequence cautioni

The sequence AAM50178.1 differs from that shown. Reason: Erroneous translation. Wrong choice of frame.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti319 – 3191S → T in AAC41609 (PubMed:8548811).Curated
Sequence conflicti324 – 3252VA → DT in AAC41609 (PubMed:8548811).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L49440 mRNA. Translation: AAC41609.1.
AE014296 Genomic DNA. Translation: AAF49548.1.
AE014296 Genomic DNA. Translation: AAG22319.1.
AE014296 Genomic DNA. Translation: AAN11757.1.
BT031197 mRNA. Translation: ABY20438.2.
AY119524 mRNA. Translation: AAM50178.1. Sequence problems.
RefSeqiNP_001261916.1. NM_001274987.1.
NP_001261917.1. NM_001274988.1.
NP_001261918.1. NM_001274989.1.
NP_524101.2. NM_079377.3.
NP_730097.1. NM_168644.2.
NP_730098.1. NM_168645.2.
UniGeneiDm.6466.

Genome annotation databases

EnsemblMetazoaiFBtr0075499; FBpp0075254; FBgn0260635.
FBtr0075500; FBpp0075255; FBgn0260635.
FBtr0075501; FBpp0075256; FBgn0260635.
FBtr0333617; FBpp0305793; FBgn0260635.
FBtr0333618; FBpp0305794; FBgn0260635.
FBtr0333619; FBpp0305795; FBgn0260635.
GeneIDi39753.
KEGGidme:Dmel_CG12284.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L49440 mRNA. Translation: AAC41609.1.
AE014296 Genomic DNA. Translation: AAF49548.1.
AE014296 Genomic DNA. Translation: AAG22319.1.
AE014296 Genomic DNA. Translation: AAN11757.1.
BT031197 mRNA. Translation: ABY20438.2.
AY119524 mRNA. Translation: AAM50178.1. Sequence problems.
RefSeqiNP_001261916.1. NM_001274987.1.
NP_001261917.1. NM_001274988.1.
NP_001261918.1. NM_001274989.1.
NP_524101.2. NM_079377.3.
NP_730097.1. NM_168644.2.
NP_730098.1. NM_168645.2.
UniGeneiDm.6466.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1JD4X-ray2.70A/B201-323[»]
1JD5X-ray1.90A201-323[»]
1JD6X-ray2.70A201-323[»]
1Q4QX-ray2.10A/B/C/D/E/F/G/H/I/J201-323[»]
1SDZX-ray1.78A30-145[»]
1SE0X-ray1.75A30-145[»]
3SIPX-ray3.50E/F31-145[»]
3SIQX-ray2.40A/B/C/D/E/F1-135[»]
ProteinModelPortaliQ24306.
SMRiQ24306. Positions 38-145, 214-318, 385-425.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi65064. 29 interactions.
IntActiQ24306. 10 interactions.
MINTiMINT-1601077.
STRINGi7227.FBpp0305795.

Protein family/group databases

MEROPSiI32.009.

Proteomic databases

PaxDbiQ24306.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0075499; FBpp0075254; FBgn0260635.
FBtr0075500; FBpp0075255; FBgn0260635.
FBtr0075501; FBpp0075256; FBgn0260635.
FBtr0333617; FBpp0305793; FBgn0260635.
FBtr0333618; FBpp0305794; FBgn0260635.
FBtr0333619; FBpp0305795; FBgn0260635.
GeneIDi39753.
KEGGidme:Dmel_CG12284.

Organism-specific databases

CTDi39753.
FlyBaseiFBgn0260635. Diap1.

Phylogenomic databases

eggNOGiKOG1101. Eukaryota.
ENOG410YPNM. LUCA.
GeneTreeiENSGT00500000044782.
InParanoidiQ24306.
KOiK04725.
OMAiTVATHAS.
OrthoDBiEOG78H3TF.
PhylomeDBiQ24306.

Enzyme and pathway databases

SignaLinkiQ24306.

Miscellaneous databases

EvolutionaryTraceiQ24306.
GenomeRNAii39753.
NextBioi815208.
PMAP-CutDBQ24306.
PROiQ24306.

Gene expression databases

BgeeiQ24306.
ExpressionAtlasiQ24306. differential.
GenevisibleiQ24306. DM.

Family and domain databases

Gene3Di1.10.1170.10. 2 hits.
3.30.40.10. 1 hit.
InterProiIPR001370. BIR_rpt.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF00653. BIR. 2 hits.
[Graphical view]
SMARTiSM00238. BIR. 2 hits.
SM00184. RING. 1 hit.
[Graphical view]
PROSITEiPS01282. BIR_REPEAT_1. 2 hits.
PS50143. BIR_REPEAT_2. 2 hits.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Drosophila homologs of baculovirus inhibitor of apoptosis proteins function to block cell death."
    Hay B.A., Wassarman D.A., Rubin G.M.
    Cell 83:1253-1262(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
    Tissue: Eye imaginal disk.
  2. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  3. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  4. Stapleton M., Booth B., Carlson J.W., Frise E., Kapadia B., Park S., Wan K.H., Yu C., Celniker S.E.
    Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Ovary.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 39-438.
    Strain: Berkeley.
    Tissue: Head.
  6. "The Drosophila caspase DRONC is regulated by DIAP1."
    Meier P., Silke J., Leevers S.J., Evan G.I.
    EMBO J. 19:598-611(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DRONC.
    Tissue: Embryo.
  7. "STRICA, a novel Drosophila melanogaster caspase with an unusual serine/threonine-rich prodomain, interacts with DIAP1 and DIAP2."
    Doumanis J., Quinn L., Richardson H., Kumar S.
    Cell Death Differ. 8:387-394(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH STRICA.
  8. "Evolution of mitochondrial cell death pathway: Proapoptotic role of HtrA2/Omi in Drosophila."
    Igaki T., Suzuki Y., Tokushige N., Aonuma H., Takahashi R., Miura M.
    Biochem. Biophys. Res. Commun. 356:993-997(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH HTRA2, CLEAVAGE.
  9. "The interaction of DIAP1 with dOmi/HtrA2 regulates cell death in Drosophila."
    Khan F.S., Fujioka M., Datta P., Fernandes-Alnemri T., Jaynes J.B., Alnemri E.S.
    Cell Death Differ. 15:1073-1083(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH HTRA2, CLEAVAGE, MUTAGENESIS OF ILE-162 AND ILE-165.
    Strain: Berkeley.
    Tissue: Testis.
  10. "Ubiquitin-mediated regulation of apoptosis."
    Broemer M., Meier P.
    Trends Cell Biol. 19:130-140(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON FUNCTION.
  11. "Systematic in vivo RNAi analysis identifies IAPs as NEDD8-E3 ligases."
    Broemer M., Tenev T., Rigbolt K.T., Hempel S., Blagoev B., Silke J., Ditzel M., Meier P.
    Mol. Cell 40:810-822(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS AN E3 UBIQUITIN-PROTEIN LIGASE OF THE NEDD8 CONJUGATION PATHWAY.
  12. Cited for: REVIEW ON FUNCTION.
  13. "XIAP monoubiquitylates Groucho/TLE to promote canonical Wnt signaling."
    Hanson A.J., Wallace H.A., Freeman T.J., Beauchamp R.D., Lee L.A., Lee E.
    Mol. Cell 45:619-628(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  14. "Structural analysis of a functional DIAP1 fragment bound to grim and hid peptides."
    Wu J.W., Cocina A.E., Chai J., Hay B.A., Shi Y.
    Mol. Cell 8:95-104(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 215-310.
  15. "Molecular mechanism of Reaper-Grim-Hid-mediated suppression of DIAP1-dependent Dronc ubiquitination."
    Chai J., Yan N., Huh J.R., Wu J.-W., Li W., Hay B.A., Shi Y.
    Nat. Struct. Biol. 10:892-898(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 201-324 IN COMPLEX WITH DRONC, FUNCTION.

Entry informationi

Entry nameiDIAP1_DROME
AccessioniPrimary (citable) accession number: Q24306
Secondary accession number(s): A4V1Z9
, A9UN33, Q0E8E4, Q8MRM5, Q9VUX5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 23, 2004
Last modified: May 11, 2016
This is version 158 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

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 one 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.