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Reviewed, UniProtKB/Swiss-Prot Q24106 (HID_DROME)

Last modified June 16, 2009. Version 79. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Cell death protein W
Alternative name(s):
    Protein head involution defective
    Protein wrinkled
Gene names
Name: W
Synonyms: Hid
ORF Names: CG5123
OrganismDrosophila melanogaster (Fruit fly) [Complete proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length410 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Activator of apoptosis, with grim and rpr, that acts on the effector, Dredd. Seems to act genetically upstream of baculoviral anti-apoptotic p35. Ref.1 Ref.5

Developmental stage

Expression coincides with the onset of programmed cell death (PCD) at all stages of embryonic development, particularly in the head. Ref.1

Disruption phenotype

Mutants contain extra cells in the head owing to decreased levels of cell death and show a pronounced defect in the morphogenetic movements of head involution. Ectopic expression in the retina results in complete eye ablation. Ref.1

Sequence similarities

To D.melanogaster grim and rpr.

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 410410Cell death protein W
PRO_0000083972

Regions

Compositional bias17 – 7963Ser-rich
Compositional bias237 – 2404Poly-Ser
Compositional bias332 – 3409Poly-Ser

Amino acid modifications

Modified residue2951Phosphoserine Ref.6

Natural variations

Natural variant1711P → S in allele A22.
Natural variant2611S → L in allele A206.

Experimental info

Sequence conflict3511P → S in AAA79985. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q24106-1 [UniParc].

Last modified June 1, 2001. Version 2.
Checksum: 63EBF913149E27E1

FASTA41043,877
        10         20         30         40         50         60 
MAVPFYLPEG GADDVASSSS GASGNSSPHN HPLPSSASSS VSSSGVSSAS ASSASSSSSA 

        70         80         90        100        110        120 
SSDGASSAAS QSPNTTTSSA TQTPMQSPLP TDQVLYALYE WVRMYQSQQS APQIFQYPPP 

       130        140        150        160        170        180 
SPSCNFTGGD VFFPHGHPNP NSNPHPRTPR TSVSFSSGEE YNFFRQQQPQ PHPSYPAPST 

       190        200        210        220        230        240 
PQPMPPQSAP PMHCSHSYPQ QSAHMMPHHS APFGMGGTYY AGYTPPPTPN TASAGTSSSS 

       250        260        270        280        290        300 
AAFGWHGHPH SPFTSTSTPL SAPVAPKMRL QRSQSDAARR KRLTSTGEDE REYQSDHEAT 

       310        320        330        340        350        360 
WDEFGDRYDN FTAGRERLQE FNGRIPPRKK KSSNSHSSSS NNPVCHTDSQ PGGTSQAESG 

       370        380        390        400        410 
AIHGHISQQR QVERERQKAK AEKKKPQSFT WPTVVTVFVL AMGCGFFAAR 

« Hide

References

« Hide 'large scale' references
[1]"The head involution defective gene of Drosophila melanogaster functions in programmed cell death."
Grether M.E., Abrams J.M., Agapite J., White K., Steller H.
Genes Dev. 9:1694-1708(1995) [PubMed: 7622034] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE.
Strain: Canton-S.
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. expand/collapse author list , 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: 10731132] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Berkeley.
[3]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. expand/collapse author list , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed: 12537572] [Abstract]
Cited for: GENOME REANNOTATION.
[4]"A Drosophila full-length cDNA resource."
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed: 12537569] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Berkeley.
Tissue: Testis.
[5]"Dredd, a novel effector of the apoptosis activators reaper, grim, and hid in Drosophila."
Chen P., Rodriguez A., Erskine R., Thach T., Abrams J.M.
Dev. Biol. 201:202-216(1998) [PubMed: 9740659] [Abstract]
Cited for: FUNCTION.
Tissue: Embryo.
[6]"Phosphoproteome analysis of Drosophila melanogaster embryos."
Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.
J. Proteome Res. 7:1675-1682(2008) [PubMed: 18327897] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-295, MASS SPECTROMETRY.
Tissue: Embryo.
+Additional computationally mapped references.

Cross-references

Sequence databases

U31226 mRNA. Translation: AAA79985.1.
AE014296 Genomic DNA. Translation: AAF49270.1.
AY075188 mRNA. Translation: AAL68057.1.
RefSeqNP_524136.2.
UniGeneDm.5624

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

DIPDIP:20052N.
IntActQ24106. 6 interactions.

Genome annotation databases

EnsemblFBgn0003997. Drosophila melanogaster. [Contig view]
GeneID40009.
KEGGdme:Dmel_CG5123.
NMPDRfig|7227.3.peg.10409.

Organism-specific databases

FlyBaseFBgn0003997. W.

Phylogenomic databases

HOGENOMQ24106.
OMAQ24106. EDEREYQ.

Enzyme and pathway databases

BioCycDMEL-XXX-02:DMEL-XXX-02-017211-MON.

Gene expression databases

ArrayExpressQ24106.
GermOnlineCG5123. Drosophila melanogaster.

Family and domain databases

ProtoNetSearch...

Other Resources

NextBio816537.

Entry information

Entry nameHID_DROME
AccessionPrimary (citable) accession number: Q24106
Secondary accession number(s): Q9VVP1
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: June 1, 2001
Last modified: June 16, 2009
This is version 79 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectDrosophila annotation project

Relevant documents

Drosophila

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

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents