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Protein

Apoptosis inhibitor 5 homolog

Gene

Aac11

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Antiapoptotic factor. Also known to efficiently suppress E2F1-induced apoptosis.1 Publication

GO - Biological processi

  • apoptotic process Source: UniProtKB-KW
  • negative regulation of apoptotic process Source: UniProtKB
  • neurogenesis Source: FlyBase
  • sensory perception of pain Source: FlyBase
Complete GO annotation...

Keywords - Biological processi

Apoptosis

Names & Taxonomyi

Protein namesi
Recommended name:
Apoptosis inhibitor 5 homolog
Short name:
API-5
Alternative name(s):
Antiapoptosis clone 11 protein homolog
Short name:
AAC-11
Gene namesi
Name:Aac11
Synonyms:LD09852
ORF Names:CG6582
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 2L

Organism-specific databases

FlyBaseiFBgn0027885. Aac11.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Disruption phenotypei

Enhanced E2f1-induced apoptosis.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 536536Apoptosis inhibitor 5 homologPRO_0000378097Add
BLAST

Proteomic databases

PaxDbiQ9V431.
PRIDEiQ9V431.

Expressioni

Gene expression databases

BgeeiQ9V431.
GenevisibleiQ9V431. DM.

Interactioni

Protein-protein interaction databases

BioGridi61049. 2 interactions.
IntActiQ9V431. 2 interactions.
MINTiMINT-304850.
STRINGi7227.FBpp0080554.

Structurei

3D structure databases

ProteinModelPortaliQ9V431.
SMRiQ9V431. Positions 4-447.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the API5 family.Curated

Phylogenomic databases

eggNOGiKOG2213. Eukaryota.
ENOG410XSH0. LUCA.
GeneTreeiENSGT00390000010991.
InParanoidiQ9V431.
OMAiWHPEDPE.
OrthoDBiEOG7XSTDC.
PhylomeDBiQ9V431.

Family and domain databases

Gene3Di1.25.10.10. 2 hits.
InterProiIPR008383. API5.
IPR011989. ARM-like.
IPR016024. ARM-type_fold.
[Graphical view]
PfamiPF05918. API5. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 2 hits.

Sequencei

Sequence statusi: Complete.

Q9V431-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDNIERLYKC YEILSEAGDK ISEHVDEYKE ILKAVKGTSK EKRLASQFIG
60 70 80 90 100
NFFKHFPDLA DTAIDAQFDL CEDDDTQIRR QAIKDLPKLC QGNADATIRV
110 120 130 140 150
GDTLAQLLIL DDPTELQQVN NSLLAIIKLD TKSSIAGLFQ QISTGDETTR
160 170 180 190 200
ERCLKFIATK LLTMGPTVIT KEIEDYIVEE IKKALQDVTA DEFHLCMTIL
210 220 230 240 250
GATKLGSTIT GHAELVKLAT EQAELNNTDA DIIAVDDEVV ERFIQCASAA
260 270 280 290 300
APYFSKTIKS TAFVAHVCDK LLPIKTWNMI ATAVSQDQIQ LRLLKVFAEM
310 320 330 340 350
ITNTDKLDNA SERINAVYNV LLEYMPLPKL SDEDLGDTPP SFQFSHAECL
360 370 380 390 400
LYALHTLGKN HPNSLSFVED AEKLKDFRAR LQYLARGTQG YIKKLEESLK
410 420 430 440 450
GKTGEELKTE ENQLKQTALK TTSNINILIR DLFHSPPIFK HDIVLSWIVP
460 470 480 490 500
KNNKLGKRHA PITFGEKAAA NGKDKDQEPE KKSRPSNDQK FYSPPSGKYS
510 520 530
NKVNQSYGNN NRTRQRGGGG GGGSGGGYRN RRFNKY
Length:536
Mass (Da):59,930
Last modified:May 1, 2000 - v1
Checksum:i207BCC1F52BB69BF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF160921 mRNA. Translation: AAD46861.1.
AE014134 Genomic DNA. Translation: AAF53618.1.
RefSeqiNP_477454.1. NM_058106.5.
UniGeneiDm.445.

Genome annotation databases

EnsemblMetazoaiFBtr0081001; FBpp0080554; FBgn0027885.
GeneIDi35053.
KEGGidme:Dmel_CG6582.
UCSCiCG6582-RA. d. melanogaster.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF160921 mRNA. Translation: AAD46861.1.
AE014134 Genomic DNA. Translation: AAF53618.1.
RefSeqiNP_477454.1. NM_058106.5.
UniGeneiDm.445.

3D structure databases

ProteinModelPortaliQ9V431.
SMRiQ9V431. Positions 4-447.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi61049. 2 interactions.
IntActiQ9V431. 2 interactions.
MINTiMINT-304850.
STRINGi7227.FBpp0080554.

Proteomic databases

PaxDbiQ9V431.
PRIDEiQ9V431.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0081001; FBpp0080554; FBgn0027885.
GeneIDi35053.
KEGGidme:Dmel_CG6582.
UCSCiCG6582-RA. d. melanogaster.

Organism-specific databases

CTDi35053.
FlyBaseiFBgn0027885. Aac11.

Phylogenomic databases

eggNOGiKOG2213. Eukaryota.
ENOG410XSH0. LUCA.
GeneTreeiENSGT00390000010991.
InParanoidiQ9V431.
OMAiWHPEDPE.
OrthoDBiEOG7XSTDC.
PhylomeDBiQ9V431.

Miscellaneous databases

GenomeRNAii35053.
NextBioi791582.
PROiQ9V431.

Gene expression databases

BgeeiQ9V431.
GenevisibleiQ9V431. DM.

Family and domain databases

Gene3Di1.25.10.10. 2 hits.
InterProiIPR008383. API5.
IPR011989. ARM-like.
IPR016024. ARM-type_fold.
[Graphical view]
PfamiPF05918. API5. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 2 hits.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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.
  2. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  3. "Functional identification of Api5 as a suppressor of E2F-dependent apoptosis in vivo."
    Morris E.J., Michaud W.A., Ji J.Y., Moon N.S., Rocco J.W., Dyson N.J.
    PLoS Genet. 2:E196-E196(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.

Entry informationi

Entry nameiAPI5_DROME
AccessioniPrimary (citable) accession number: Q9V431
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 16, 2009
Last sequence update: May 1, 2000
Last modified: May 11, 2016
This is version 104 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. 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.