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Protein

Cell death protein hid

Gene

hid

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

Functioni

Activator of apoptosis, with grim and rpr, that acts on the effector Dredd (PubMed:9740659). Seems to act genetically upstream of baculoviral anti-apoptotic p35 (PubMed:7622034). Blocks Diap2 from binding and inactivating the effector caspase Drice (PubMed:18166655).3 Publications

GO - Molecular functioni

  • BIR domain binding Source: FlyBase
  • ubiquitin protein ligase binding Source: FlyBase

GO - Biological processi

  • antennal morphogenesis Source: FlyBase
  • apoptotic process Source: FlyBase
  • apoptotic signaling pathway Source: FlyBase
  • cell death Source: FlyBase
  • cellular response to gamma radiation Source: FlyBase
  • cellular response to starvation Source: FlyBase
  • compound eye retinal cell programmed cell death Source: FlyBase
  • dendrite morphogenesis Source: FlyBase
  • ecdysone-mediated induction of salivary gland cell autophagic cell death Source: FlyBase
  • entrainment of circadian clock by photoperiod Source: FlyBase
  • head involution Source: FlyBase
  • instar larval or pupal development Source: FlyBase
  • intrinsic apoptotic signaling pathway in response to DNA damage Source: FlyBase
  • larval midgut cell programmed cell death Source: FlyBase
  • open tracheal system development Source: FlyBase
  • positive regulation of apoptotic process Source: FlyBase
  • positive regulation of cellular response to X-ray Source: FlyBase
  • positive regulation of cysteine-type endopeptidase activity Source: FlyBase
  • positive regulation of cysteine-type endopeptidase activity involved in execution phase of apoptosis Source: FlyBase
  • positive regulation of macroautophagy Source: FlyBase
  • programmed cell death Source: FlyBase
  • regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: FlyBase
  • regulation of organ growth Source: FlyBase
  • regulation of retinal cell programmed cell death Source: FlyBase
  • response to red light Source: FlyBase
  • salivary gland cell autophagic cell death Source: FlyBase
  • sex differentiation Source: FlyBase

Keywordsi

Molecular functionDevelopmental protein
Biological processApoptosis

Names & Taxonomyi

Protein namesi
Recommended name:
Cell death protein hid
Alternative name(s):
Protein head involution defective
Protein wrinkled
Gene namesi
Name:hid
Synonyms:W
ORF Names:CG5123
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraHolometabolaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 3L

Organism-specific databases

FlyBaseiFBgn0003997. hid.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Pathology & Biotechi

Disruption phenotypei

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.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000839721 – 410Cell death protein hidAdd BLAST410

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei295Phosphoserine1 Publication1

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ24106.

PTM databases

iPTMnetiQ24106.

Expressioni

Developmental stagei

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

Gene expression databases

BgeeiFBgn0003997.
ExpressionAtlasiQ24106. differential.
GenevisibleiQ24106. DM.

Interactioni

Subunit structurei

Interacts with Diap2 (via BIR2 and BIR3 domains).1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
Diap1Q243068EBI-135509,EBI-456419

GO - Molecular functioni

  • BIR domain binding Source: FlyBase
  • ubiquitin protein ligase binding Source: FlyBase

Protein-protein interaction databases

BioGridi65293. 103 interactors.
DIPiDIP-20052N.
ELMiQ24106.
IntActiQ24106. 7 interactors.
MINTiMINT-824104.
STRINGi7227.FBpp0074899.

Structurei

Secondary structure

1410
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 6Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1JD6X-ray2.70B2-11[»]
SMRiQ24106.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi17 – 79Ser-richAdd BLAST63
Compositional biasi237 – 240Poly-Ser4
Compositional biasi332 – 340Poly-Ser9

Sequence similaritiesi

To D.melanogaster grim and rpr.Curated

Phylogenomic databases

eggNOGiENOG410KB5T. Eukaryota.
ENOG4110NM4. LUCA.
InParanoidiQ24106.
KOiK20016.
OMAiQSFTWPT.
OrthoDBiEOG091G0KX5.
PhylomeDBiQ24106.

Sequencei

Sequence statusi: Complete.

Q24106-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAVPFYLPEG GADDVASSSS GASGNSSPHN HPLPSSASSS VSSSGVSSAS
60 70 80 90 100
ASSASSSSSA SSDGASSAAS QSPNTTTSSA TQTPMQSPLP TDQVLYALYE
110 120 130 140 150
WVRMYQSQQS APQIFQYPPP SPSCNFTGGD VFFPHGHPNP NSNPHPRTPR
160 170 180 190 200
TSVSFSSGEE YNFFRQQQPQ PHPSYPAPST PQPMPPQSAP PMHCSHSYPQ
210 220 230 240 250
QSAHMMPHHS APFGMGGTYY AGYTPPPTPN TASAGTSSSS AAFGWHGHPH
260 270 280 290 300
SPFTSTSTPL SAPVAPKMRL QRSQSDAARR KRLTSTGEDE REYQSDHEAT
310 320 330 340 350
WDEFGDRYDN FTAGRERLQE FNGRIPPRKK KSSNSHSSSS NNPVCHTDSQ
360 370 380 390 400
PGGTSQAESG AIHGHISQQR QVERERQKAK AEKKKPQSFT WPTVVTVFVL
410
AMGCGFFAAR
Length:410
Mass (Da):43,877
Last modified:June 1, 2001 - v2
Checksum:i63EBF913149E27E1
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti351P → S in AAA79985 (PubMed:7622034).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti171P → S in allele A22. 1
Natural varianti261S → L in allele A206. 1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U31226 mRNA. Translation: AAA79985.1.
AE014296 Genomic DNA. Translation: AAF49270.1.
AY075188 mRNA. Translation: AAL68057.1.
RefSeqiNP_001262010.1. NM_001275081.1.
NP_524136.2. NM_079412.4.
UniGeneiDm.5624.

Genome annotation databases

EnsemblMetazoaiFBtr0075133; FBpp0074899; FBgn0003997.
FBtr0332862; FBpp0305084; FBgn0003997.
GeneIDi40009.
KEGGidme:Dmel_CG5123.

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

Entry informationi

Entry nameiHID_DROME
AccessioniPrimary (citable) accession number: Q24106
Secondary accession number(s): Q9VVP1
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: June 1, 2001
Last modified: October 25, 2017
This is version 149 of the entry and version 2 of the sequence. See 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