Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Apoptosis regulator ced-9

Gene

ced-9

Organism
Caenorhabditis elegans
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Plays a major role in programmed cell death (PCD, apoptosis). Egl-1 binds to and directly inhibits the activity of ced-9, releasing the cell death activator ced-4 from a ced-9/ced-4 containing protein complex and allowing ced-4 to activate the cell-killing caspase ced-3.6 Publications

GO - Molecular functioni

  • GTPase activator activity Source: WormBase

GO - Biological processi

  • apoptotic process involved in development Source: UniProtKB
  • mitophagy Source: WormBase
  • negative regulation of apoptotic process Source: WormBase
  • negative regulation of programmed cell death Source: WormBase
  • positive regulation of GTPase activity Source: GOC
  • positive regulation of mitochondrial fusion Source: WormBase
Complete GO annotation...

Keywords - Biological processi

Apoptosis

Protein family/group databases

TCDBi1.A.21.2.1. the bcl-2 (bcl-2) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Apoptosis regulator ced-9
Alternative name(s):
Cell death protein 9
Gene namesi
Name:ced-9
ORF Names:T07C4.8
OrganismiCaenorhabditis elegans
Taxonomic identifieri6239 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
Proteomesi
  • UP000001940 Componenti: Chromosome III

Organism-specific databases

WormBaseiT07C4.8; CE25104; WBGene00000423; ced-9.

Subcellular locationi

GO - Cellular componenti

  • endomembrane system Source: UniProtKB-SubCell
  • membrane Source: WormBase
  • mitochondrial outer membrane Source: WormBase
  • mitochondrion Source: WormBase
  • organelle membrane Source: WormBase
  • perinuclear region of cytoplasm Source: WormBase
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi149 – 1491Y → N in N1653; lethal phenotype. 1 Publication
Mutagenesisi169 – 1691G → E in G169E; gain of function. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 280280Apoptosis regulator ced-9PRO_0000143097Add
BLAST

Proteomic databases

EPDiP41958.
PaxDbiP41958.
PRIDEiP41958.

PTM databases

iPTMnetiP41958.

Expressioni

Developmental stagei

Abundant expression is seen in embryos and adults.1 Publication

Interactioni

Subunit structurei

Interacts with ced-4 (PubMed:9027313). Interacts with egl-1 (PubMed:9604928, PubMed:12894216, PubMed:15383288). Interacts with dre-1; the interaction inhibits ced-9 activity, either directly or indirectly (PubMed:23431138).5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ced-3P425732EBI-494110,EBI-494247
ced-4P3042917EBI-494110,EBI-494118
egl-1O616676EBI-494110,EBI-495949

Protein-protein interaction databases

BioGridi533094. 4 interactions.
DIPiDIP-250N.
IntActiP41958. 3 interactions.
MINTiMINT-1526902.
STRINGi6239.T07C4.8.

Structurei

Secondary structure

1
280
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi72 – 743Combined sources
Helixi76 – 783Combined sources
Helixi80 – 9415Combined sources
Helixi111 – 13828Combined sources
Beta strandi140 – 1434Combined sources
Helixi146 – 1538Combined sources
Turni154 – 1574Combined sources
Beta strandi161 – 1633Combined sources
Helixi168 – 18518Combined sources
Turni189 – 1913Combined sources
Helixi192 – 1943Combined sources
Helixi195 – 21117Combined sources
Helixi214 – 2174Combined sources
Helixi221 – 23919Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1OHUX-ray2.03A/B68-242[»]
1TY4X-ray2.20A/B68-237[»]
2A5YX-ray2.60A48-251[»]
ProteinModelPortaliP41958.
SMRiP41958. Positions 71-236.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP41958.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi80 – 9920BH4Add
BLAST
Motifi160 – 17920BH1Add
BLAST
Motifi213 – 22917BH2Add
BLAST

Sequence similaritiesi

Belongs to the Bcl-2 family.Curated

Phylogenomic databases

eggNOGiKOG4728. Eukaryota.
ENOG41123S0. LUCA.
HOGENOMiHOG000111534.
InParanoidiP41958.
OMAiYVEVVEC.
OrthoDBiEOG764748.
PhylomeDBiP41958.

Family and domain databases

InterProiIPR002475. Bcl2-like.
IPR020717. Bcl2_BH1_motif_CS.
IPR003093. Bcl2_BH4.
IPR026298. Blc2_fam.
[Graphical view]
PANTHERiPTHR11256. PTHR11256. 1 hit.
PfamiPF00452. Bcl-2. 1 hit.
PF02180. BH4. 1 hit.
[Graphical view]
SMARTiSM00265. BH4. 1 hit.
[Graphical view]
PROSITEiPS50062. BCL2_FAMILY. 1 hit.
PS01080. BH1. 1 hit.
PS50063. BH4_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P41958-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTRCTADNSL TNPAYRRRTM ATGEMKEFLG IKGTEPTDFG INSDAQDLPS
60 70 80 90 100
PSRQASTRRM SIGESIDGKI NDWEEPRLDI EGFVVDYFTH RIRQNGMEWF
110 120 130 140 150
GAPGLPCGVQ PEHEMMRVMG TIFEKKHAEN FETFCEQLLA VPRISFSLYQ
160 170 180 190 200
DVVRTVGNAQ TDQCPMSYGR LIGLISFGGF VAAKMMESVE LQGQVRNLFV
210 220 230 240 250
YTSLFIKTRI RNNWKEHNRS WDDFMTLGKQ MKEDYERAEA EKVGRRKQNR
260 270 280
RWSMIGAGVT AGAIGIVGVV VCGRMMFSLK
Length:280
Mass (Da):31,824
Last modified:November 1, 1995 - v1
Checksum:i7603675E490DD3EB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L26545 Genomic DNA. Translation: AAA20080.1.
Z29443 Genomic DNA. Translation: CAA82573.2.
PIRiA53189.
H88578.
RefSeqiNP_499284.1. NM_066883.5.
UniGeneiCel.6305.

Genome annotation databases

EnsemblMetazoaiT07C4.8; T07C4.8; WBGene00000423.
GeneIDi3565776.
KEGGicel:CELE_T07C4.8.
UCSCiT07C4.8.1. c. elegans.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L26545 Genomic DNA. Translation: AAA20080.1.
Z29443 Genomic DNA. Translation: CAA82573.2.
PIRiA53189.
H88578.
RefSeqiNP_499284.1. NM_066883.5.
UniGeneiCel.6305.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1OHUX-ray2.03A/B68-242[»]
1TY4X-ray2.20A/B68-237[»]
2A5YX-ray2.60A48-251[»]
ProteinModelPortaliP41958.
SMRiP41958. Positions 71-236.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi533094. 4 interactions.
DIPiDIP-250N.
IntActiP41958. 3 interactions.
MINTiMINT-1526902.
STRINGi6239.T07C4.8.

Protein family/group databases

TCDBi1.A.21.2.1. the bcl-2 (bcl-2) family.

PTM databases

iPTMnetiP41958.

Proteomic databases

EPDiP41958.
PaxDbiP41958.
PRIDEiP41958.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiT07C4.8; T07C4.8; WBGene00000423.
GeneIDi3565776.
KEGGicel:CELE_T07C4.8.
UCSCiT07C4.8.1. c. elegans.

Organism-specific databases

CTDi3565776.
WormBaseiT07C4.8; CE25104; WBGene00000423; ced-9.

Phylogenomic databases

eggNOGiKOG4728. Eukaryota.
ENOG41123S0. LUCA.
HOGENOMiHOG000111534.
InParanoidiP41958.
OMAiYVEVVEC.
OrthoDBiEOG764748.
PhylomeDBiP41958.

Miscellaneous databases

EvolutionaryTraceiP41958.
NextBioi957817.
PROiP41958.

Family and domain databases

InterProiIPR002475. Bcl2-like.
IPR020717. Bcl2_BH1_motif_CS.
IPR003093. Bcl2_BH4.
IPR026298. Blc2_fam.
[Graphical view]
PANTHERiPTHR11256. PTHR11256. 1 hit.
PfamiPF00452. Bcl-2. 1 hit.
PF02180. BH4. 1 hit.
[Graphical view]
SMARTiSM00265. BH4. 1 hit.
[Graphical view]
PROSITEiPS50062. BCL2_FAMILY. 1 hit.
PS01080. BH1. 1 hit.
PS50063. BH4_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "C. elegans cell survival gene ced-9 encodes a functional homolog of the mammalian proto-oncogene bcl-2."
    Hengartner M.O., Horvitz H.R.
    Cell 76:665-676(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
    Strain: Bristol N2.
  2. "Genome sequence of the nematode C. elegans: a platform for investigating biology."
    The C. elegans sequencing consortium
    Science 282:2012-2018(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Bristol N2.
  3. "Interaction between the C. elegans cell-death regulators CED-9 and CED-4."
    Spector M.S., Desnoyers S., Hoeppner D.J., Hengartner M.O.
    Nature 385:653-656(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DEVELOPMENTAL STAGE, MUTAGENESIS OF TYR-149 AND GLY-169.
    Strain: Bristol N2.
  4. "Interaction and regulation of subcellular localization of CED-4 by CED-9."
    Wu D., Wallen H.D., Nunez G.
    Science 275:1126-1129(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CED-4.
  5. "The C. elegans protein EGL-1 is required for programmed cell death and interacts with the Bcl-2-like protein CED-9."
    Conradt B., Horvitz H.R.
    Cell 93:519-529(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH EGL-1.
  6. "Translocation of C. elegans CED-4 to nuclear membranes during programmed cell death."
    Chen F., Hersh B.M., Conradt B., Zhou Z., Riemer D., Gruenbaum Y., Horvitz H.R.
    Science 287:1485-1489(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  7. Cited for: INTERACTION WITH DRE-1.
  8. "Unique structural features of a BCL-2 family protein CED-9 and biophysical characterization of CED-9/EGL-1 interactions."
    Woo J.-S., Jung J.-S., Ha N.-C., Shin J., Kin K.-H., Lee W., Oh B.-H.
    Cell Death Differ. 10:1310-1319(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.03 ANGSTROMS) OF 68-242 IN COMPLEX WITH EGL-1.
  9. "Structural, biochemical, and functional analyses of CED-9 recognition by the proapoptotic proteins EGL-1 and CED-4."
    Yan N., Gu L., Kokel D., Chai J., Li W., Han A., Chen L., Xue D., Shi Y.
    Mol. Cell 15:999-1006(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 68-237 IN COMPLEX WITH EGL-1, FUNCTION, INTERACTION WITH EGL-1 AND CED-4.

Entry informationi

Entry nameiCED9_CAEEL
AccessioniPrimary (citable) accession number: P41958
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: May 11, 2016
This is version 128 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Caenorhabditis elegans
    Caenorhabditis elegans: entries, gene names and cross-references to WormBase
  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.