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Protein

Caspase-9

Gene

CASP9

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the activation cascade of caspases responsible for apoptosis execution. Binding of caspase-9 to Apaf-1 leads to activation of the protease which then cleaves and activates caspase-3. Promotes DNA damage-induced apoptosis in a ABL1/c-Abl-dependent manner. Proteolytically cleaves poly(ADP-ribose) polymerase (PARP).
Isoform 2 lacks activity is an dominant-negative inhibitor of caspase-9.

Catalytic activityi

Strict requirement for an Asp residue at position P1 and with a marked preference for His at position P2. It has a preferred cleavage sequence of Leu-Gly-His-Asp-|-Xaa.1 Publication

Enzyme regulationi

Inhibited by the effector protein NleF that is produced by pathogenic E.coli; this inhibits apoptosis.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei237 – 2371By similarity
Active sitei287 – 2871By similarity

GO - Molecular functioni

  • cysteine-type endopeptidase activity Source: ProtInc
  • cysteine-type endopeptidase activity involved in apoptotic signaling pathway Source: GO_Central
  • enzyme activator activity Source: ProtInc
  • peptidase activity Source: MGI
  • protein kinase binding Source: UniProtKB
  • SH3 domain binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease

Keywords - Biological processi

Apoptosis

Enzyme and pathway databases

BRENDAi3.4.22.62. 2681.
ReactomeiREACT_12564. AKT phosphorylates targets in the cytosol.
REACT_1767. SMAC-mediated dissociation of IAP:caspase complexes.
REACT_2190. SMAC binds to IAPs.
REACT_22128. Ligand-independent caspase activation via DCC.
REACT_355468. Constitutive Signaling by AKT1 E17K in Cancer.
REACT_607. Activation of caspases through apoptosome-mediated cleavage.
REACT_75776. NOD1/2 Signaling Pathway.
REACT_89. Formation of apoptosome.
SABIO-RKP55211.

Protein family/group databases

MEROPSiC14.010.

Names & Taxonomyi

Protein namesi
Recommended name:
Caspase-9 (EC:3.4.22.62)
Short name:
CASP-9
Alternative name(s):
Apoptotic protease Mch-6
Apoptotic protease-activating factor 3
Short name:
APAF-3
ICE-like apoptotic protease 6
Short name:
ICE-LAP6
Cleaved into the following 2 chains:
Gene namesi
Name:CASP9
Synonyms:MCH6
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:1511. CASP9.

Subcellular locationi

GO - Cellular componenti

  • apoptosome Source: UniProtKB
  • cytoplasm Source: GO_Central
  • cytosol Source: UniProtKB
  • mitochondrion Source: Ensembl
  • nucleus Source: Ensembl
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi153 – 1531Y → F: Inhibits tyrosine phosphorylation. Reduces caspase-9 subunit p35 formation in response to genotoxic stress. Attenuates ABL1/c-Abl-mediated caspase-3 activation, DNA fragmentation and UV irradiation-induced apoptosis. 1 Publication

Organism-specific databases

PharmGKBiPA26094.

Polymorphism and mutation databases

DMDMi28558771.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 315Caspase-9 subunit p35PRO_0000004641
Propeptidei1 – ?Sequence AnalysisPRO_0000004640
Propeptidei316 – 33015PRO_0000004642Add
BLAST
Chaini331 – 41686Caspase-9 subunit p10PRO_0000004643Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei125 – 1251Phosphothreonine; by MAPK12 Publications
Modified residuei153 – 1531Phosphotyrosine; by ABL11 Publication
Modified residuei302 – 3021Phosphoserine1 Publication
Modified residuei307 – 3071Phosphoserine2 Publications

Post-translational modificationi

Cleavages at Asp-315 by granzyme B and at Asp-330 by caspase-3 generate the two active subunits. Caspase-8 and -10 can also be involved in these processing events.
Phosphorylated at Thr-125 by MAPK1/ERK2. Phosphorylation at Thr-125 is sufficient to block caspase-9 processing and subsequent caspase-3 activation. Phosphorylation on Tyr-153 by ABL1/c-Abl; occurs in the response of cells to DNA damage.2 Publications

Keywords - PTMi

Phosphoprotein, Zymogen

Proteomic databases

MaxQBiP55211.
PaxDbiP55211.
PRIDEiP55211.

PTM databases

PhosphoSiteiP55211.

Miscellaneous databases

PMAP-CutDBP55211.

Expressioni

Tissue specificityi

Ubiquitous, with highest expression in the heart, moderate expression in liver, skeletal muscle, and pancreas. Low levels in all other tissues. Within the heart, specifically expressed in myocytes.1 Publication

Developmental stagei

Expressed at low levels in fetal heart, at moderate levels in neonate heart, and at high levels in adult heart.1 Publication

Gene expression databases

BgeeiP55211.
CleanExiHS_CASP9.
ExpressionAtlasiP55211. baseline and differential.
GenevisibleiP55211. HS.

Organism-specific databases

HPAiCAB004348.
HPA001473.
HPA046488.

Interactioni

Subunit structurei

Heterotetramer that consists of two anti-parallel arranged heterodimers, each one formed by a 35 kDa (p35) and a 10 kDa (p10) subunit. Caspase-9 and APAF1 bind to each other via their respective NH2-terminal CED-3 homologous domains in the presence of cytochrome C and ATP. Interacts (inactive form) with EFHD2. Interacts with HAX1. Interacts with BIRC2/c-IAP1, XIAP/BIRC4, BIRC5/survivin, BIRC6/bruce and BIRC7/livin. Interacts with ABL1 (via SH3 domain); the interaction is direct and increases in the response of cells to genotoxic stress and ABL1/c-Abl activation. Interacts with NleF from pathogenic E.coli.7 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
APAF1O1472718EBI-516799,EBI-446492
BIRC2Q134907EBI-516799,EBI-514538
BIRC3Q134892EBI-516799,EBI-517709
BIRC5O153922EBI-516799,EBI-518823
BIRC7Q96CA58EBI-516799,EBI-517623
BIRC8Q6PIA03EBI-516799,EBI-2129837
ILKQ134182EBI-516799,EBI-747644
XIAPP981709EBI-516799,EBI-517127

Protein-protein interaction databases

BioGridi107292. 32 interactions.
DIPiDIP-27625N.
IntActiP55211. 14 interactions.
MINTiMINT-89165.
STRINGi9606.ENSP00000330237.

Structurei

Secondary structure

1
416
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 119Combined sources
Helixi13 – 197Combined sources
Turni23 – 253Combined sources
Helixi26 – 316Combined sources
Helixi37 – 448Combined sources
Helixi51 – 6212Combined sources
Helixi69 – 7911Combined sources
Helixi83 – 9311Combined sources
Helixi143 – 1475Combined sources
Turni149 – 1513Combined sources
Beta strandi157 – 1593Combined sources
Beta strandi161 – 1677Combined sources
Helixi173 – 1753Combined sources
Helixi183 – 19614Combined sources
Beta strandi199 – 2068Combined sources
Helixi209 – 22113Combined sources
Helixi224 – 2263Combined sources
Beta strandi228 – 23912Combined sources
Beta strandi244 – 2463Combined sources
Beta strandi249 – 2513Combined sources
Beta strandi257 – 2593Combined sources
Helixi260 – 2656Combined sources
Turni269 – 2713Combined sources
Helixi273 – 2753Combined sources
Beta strandi280 – 2878Combined sources
Beta strandi317 – 3193Combined sources
Beta strandi340 – 3467Combined sources
Beta strandi351 – 3533Combined sources
Beta strandi354 – 3563Combined sources
Turni357 – 3593Combined sources
Helixi362 – 37413Combined sources
Turni375 – 3773Combined sources
Helixi380 – 39213Combined sources
Beta strandi395 – 3984Combined sources
Beta strandi402 – 4065Combined sources
Beta strandi408 – 4103Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1JXQX-ray2.80A/B/C/D140-416[»]
1NW9X-ray2.40B140-416[»]
2AR9X-ray2.80A/B/C/D139-416[»]
3D9TX-ray1.50C/D316-321[»]
3V3KX-ray3.49A/C/E/G/I/K/M/O141-416[»]
3YGSX-ray2.50P1-95[»]
4RHWX-ray2.10E/F1-100[»]
ProteinModelPortaliP55211.
SMRiP55211. Positions 1-95, 141-416.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP55211.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 9292CARDPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the peptidase C14A family.Curated
Contains 1 CARD domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG319022.
GeneTreeiENSGT00760000118912.
HOVERGENiHBG059022.
InParanoidiP55211.
KOiK04399.
PhylomeDBiP55211.
TreeFamiTF102023.

Family and domain databases

Gene3Di1.10.533.10. 1 hit.
3.40.50.1460. 1 hit.
InterProiIPR001315. CARD.
IPR029030. Caspase-like_dom.
IPR017350. Caspase_ICE-type.
IPR011029. DEATH-like_dom.
IPR011600. Pept_C14_caspase.
IPR001309. Pept_C14_ICE_p20.
IPR016129. Pept_C14_ICE_p20_AS.
IPR002138. Pept_C14_p10.
IPR015917. Pept_C14A_p45_core.
[Graphical view]
PfamiPF00619. CARD. 1 hit.
PF00656. Peptidase_C14. 1 hit.
[Graphical view]
PIRSFiPIRSF038001. Caspase_ICE. 1 hit.
PRINTSiPR00376. IL1BCENZYME.
SMARTiSM00114. CARD. 1 hit.
SM00115. CASc. 1 hit.
[Graphical view]
SUPFAMiSSF47986. SSF47986. 1 hit.
PROSITEiPS50209. CARD. 1 hit.
PS01122. CASPASE_CYS. 1 hit.
PS01121. CASPASE_HIS. 1 hit.
PS50207. CASPASE_P10. 1 hit.
PS50208. CASPASE_P20. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P55211-1) [UniParc]FASTAAdd to basket

Also known as: 9L, Alpha

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MDEADRRLLR RCRLRLVEEL QVDQLWDALL SRELFRPHMI EDIQRAGSGS
60 70 80 90 100
RRDQARQLII DLETRGSQAL PLFISCLEDT GQDMLASFLR TNRQAAKLSK
110 120 130 140 150
PTLENLTPVV LRPEIRKPEV LRPETPRPVD IGSGGFGDVG ALESLRGNAD
160 170 180 190 200
LAYILSMEPC GHCLIINNVN FCRESGLRTR TGSNIDCEKL RRRFSSLHFM
210 220 230 240 250
VEVKGDLTAK KMVLALLELA QQDHGALDCC VVVILSHGCQ ASHLQFPGAV
260 270 280 290 300
YGTDGCPVSV EKIVNIFNGT SCPSLGGKPK LFFIQACGGE QKDHGFEVAS
310 320 330 340 350
TSPEDESPGS NPEPDATPFQ EGLRTFDQLD AISSLPTPSD IFVSYSTFPG
360 370 380 390 400
FVSWRDPKSG SWYVETLDDI FEQWAHSEDL QSLLLRVANA VSVKGIYKQM
410
PGCFNFLRKK LFFKTS
Length:416
Mass (Da):46,281
Last modified:February 22, 2003 - v3
Checksum:i78E0180DF2A3BDD2
GO
Isoform 2 (identifier: P55211-2) [UniParc]FASTAAdd to basket

Also known as: 9S, Beta

The sequence of this isoform differs from the canonical sequence as follows:
     140-289: Missing.

Show »
Length:266
Mass (Da):30,184
Checksum:iA12848BEBDC35A64
GO
Isoform 3 (identifier: P55211-3) [UniParc]FASTAAdd to basket

Also known as: Gamma

The sequence of this isoform differs from the canonical sequence as follows:
     152-154: AYI → TVL
     155-416: Missing.

Note: May function as an endogenous apoptotic inhibitor, inhibits the BAX-mediated cleavage of procaspase-3.
Show »
Length:154
Mass (Da):17,397
Checksum:iB23A46C92AC6AA11
GO
Isoform 4 (identifier: P55211-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-83: Missing.

Show »
Length:333
Mass (Da):36,564
Checksum:i2B62F8CFD1FF3145
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti32 – 321R → S in AAC50776 (PubMed:8900201).Curated
Sequence conflicti32 – 321R → S in BAA82697 (PubMed:10384055).Curated
Sequence conflicti32 – 321R → S in BAA87905 (Ref. 6) Curated
Sequence conflicti96 – 961A → G in AAC50640 (PubMed:8663294).Curated
Sequence conflicti197 – 1971L → P in AAC50776 (PubMed:8900201).Curated
Sequence conflicti197 – 1971L → P in BAA82697 (PubMed:10384055).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti28 – 281A → V.4 Publications
Corresponds to variant rs1052571 [ dbSNP | Ensembl ].
VAR_015415
Natural varianti99 – 991S → L.1 Publication
Corresponds to variant rs4646008 [ dbSNP | Ensembl ].
VAR_015416
Natural varianti102 – 1021T → I.1 Publication
Corresponds to variant rs2308941 [ dbSNP | Ensembl ].
VAR_015417
Natural varianti106 – 1061L → V.1 Publication
Corresponds to variant rs2308938 [ dbSNP | Ensembl ].
VAR_015418
Natural varianti114 – 1141E → D.1 Publication
Corresponds to variant rs2020897 [ dbSNP | Ensembl ].
VAR_015419
Natural varianti136 – 1361F → L.
Corresponds to variant rs1820204 [ dbSNP | Ensembl ].
VAR_059198
Natural varianti173 – 1731R → H.1 Publication
Corresponds to variant rs2308950 [ dbSNP | Ensembl ].
VAR_015420
Natural varianti176 – 1761G → R.
Corresponds to variant rs2308949 [ dbSNP | Ensembl ].
VAR_016131
Natural varianti185 – 1851I → M.
Corresponds to variant rs9282624 [ dbSNP | Ensembl ].
VAR_022053
Natural varianti192 – 1921R → C.
Corresponds to variant rs2308939 [ dbSNP | Ensembl ].
VAR_016132
Natural varianti221 – 2211Q → R.2 Publications
Corresponds to variant rs1052576 [ dbSNP | Ensembl ].
VAR_015421

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 8383Missing in isoform 4. 1 PublicationVSP_044256Add
BLAST
Alternative sequencei140 – 289150Missing in isoform 2. 4 PublicationsVSP_000818Add
BLAST
Alternative sequencei152 – 1543AYI → TVL in isoform 3. 1 PublicationVSP_043910
Alternative sequencei155 – 416262Missing in isoform 3. 1 PublicationVSP_043911Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U56390 mRNA. Translation: AAC50640.1.
U60521 mRNA. Translation: AAC50776.1.
AB019205 Genomic DNA. Translation: BAA82697.1.
AF093130 mRNA. Translation: AAD12248.1.
AB015653 mRNA. Translation: BAA78780.1.
AB020979 mRNA. Translation: BAA87905.1.
AF110376 mRNA. Translation: AAD13615.1.
AY732490 mRNA. Translation: AAV33129.1.
AY214168 Genomic DNA. Translation: AAO21133.1.
BT006911 mRNA. Translation: AAP35557.1.
AK303743 mRNA. Translation: BAG64715.1.
AL512883 Genomic DNA. Translation: CAC42423.1.
AL512883 Genomic DNA. Translation: CAI12973.1.
CH471167 Genomic DNA. Translation: EAW51730.1.
CH471167 Genomic DNA. Translation: EAW51731.1.
BC002452 mRNA. Translation: AAH02452.1.
BC006463 mRNA. Translation: AAH06463.1.
CCDSiCCDS158.1. [P55211-1]
CCDS159.2. [P55211-4]
CCDS59995.1. [P55211-2]
PIRiG02635.
RefSeqiNP_001220.2. NM_001229.4. [P55211-1]
NP_001264983.1. NM_001278054.1. [P55211-2]
NP_127463.2. NM_032996.3. [P55211-4]
XP_005246071.1. XM_005246014.2. [P55211-4]
XP_011540573.1. XM_011542271.1. [P55211-4]
XP_011540574.1. XM_011542272.1. [P55211-4]
UniGeneiHs.329502.

Genome annotation databases

EnsembliENST00000333868; ENSP00000330237; ENSG00000132906.
ENST00000348549; ENSP00000255256; ENSG00000132906. [P55211-2]
ENST00000375890; ENSP00000365051; ENSG00000132906. [P55211-4]
GeneIDi842.
KEGGihsa:842.
UCSCiuc001awn.4. human. [P55211-1]
uc001awo.4. human. [P55211-2]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology
NIEHS-SNPs
Wikipedia

Caspase-9 entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U56390 mRNA. Translation: AAC50640.1.
U60521 mRNA. Translation: AAC50776.1.
AB019205 Genomic DNA. Translation: BAA82697.1.
AF093130 mRNA. Translation: AAD12248.1.
AB015653 mRNA. Translation: BAA78780.1.
AB020979 mRNA. Translation: BAA87905.1.
AF110376 mRNA. Translation: AAD13615.1.
AY732490 mRNA. Translation: AAV33129.1.
AY214168 Genomic DNA. Translation: AAO21133.1.
BT006911 mRNA. Translation: AAP35557.1.
AK303743 mRNA. Translation: BAG64715.1.
AL512883 Genomic DNA. Translation: CAC42423.1.
AL512883 Genomic DNA. Translation: CAI12973.1.
CH471167 Genomic DNA. Translation: EAW51730.1.
CH471167 Genomic DNA. Translation: EAW51731.1.
BC002452 mRNA. Translation: AAH02452.1.
BC006463 mRNA. Translation: AAH06463.1.
CCDSiCCDS158.1. [P55211-1]
CCDS159.2. [P55211-4]
CCDS59995.1. [P55211-2]
PIRiG02635.
RefSeqiNP_001220.2. NM_001229.4. [P55211-1]
NP_001264983.1. NM_001278054.1. [P55211-2]
NP_127463.2. NM_032996.3. [P55211-4]
XP_005246071.1. XM_005246014.2. [P55211-4]
XP_011540573.1. XM_011542271.1. [P55211-4]
XP_011540574.1. XM_011542272.1. [P55211-4]
UniGeneiHs.329502.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1JXQX-ray2.80A/B/C/D140-416[»]
1NW9X-ray2.40B140-416[»]
2AR9X-ray2.80A/B/C/D139-416[»]
3D9TX-ray1.50C/D316-321[»]
3V3KX-ray3.49A/C/E/G/I/K/M/O141-416[»]
3YGSX-ray2.50P1-95[»]
4RHWX-ray2.10E/F1-100[»]
ProteinModelPortaliP55211.
SMRiP55211. Positions 1-95, 141-416.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107292. 32 interactions.
DIPiDIP-27625N.
IntActiP55211. 14 interactions.
MINTiMINT-89165.
STRINGi9606.ENSP00000330237.

Chemistry

BindingDBiP55211.
ChEMBLiCHEMBL2273.
GuidetoPHARMACOLOGYi1625.

Protein family/group databases

MEROPSiC14.010.

PTM databases

PhosphoSiteiP55211.

Polymorphism and mutation databases

DMDMi28558771.

Proteomic databases

MaxQBiP55211.
PaxDbiP55211.
PRIDEiP55211.

Protocols and materials databases

DNASUi842.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000333868; ENSP00000330237; ENSG00000132906.
ENST00000348549; ENSP00000255256; ENSG00000132906. [P55211-2]
ENST00000375890; ENSP00000365051; ENSG00000132906. [P55211-4]
GeneIDi842.
KEGGihsa:842.
UCSCiuc001awn.4. human. [P55211-1]
uc001awo.4. human. [P55211-2]

Organism-specific databases

CTDi842.
GeneCardsiGC01M015814.
HGNCiHGNC:1511. CASP9.
HPAiCAB004348.
HPA001473.
HPA046488.
MIMi602234. gene.
neXtProtiNX_P55211.
PharmGKBiPA26094.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG319022.
GeneTreeiENSGT00760000118912.
HOVERGENiHBG059022.
InParanoidiP55211.
KOiK04399.
PhylomeDBiP55211.
TreeFamiTF102023.

Enzyme and pathway databases

BRENDAi3.4.22.62. 2681.
ReactomeiREACT_12564. AKT phosphorylates targets in the cytosol.
REACT_1767. SMAC-mediated dissociation of IAP:caspase complexes.
REACT_2190. SMAC binds to IAPs.
REACT_22128. Ligand-independent caspase activation via DCC.
REACT_355468. Constitutive Signaling by AKT1 E17K in Cancer.
REACT_607. Activation of caspases through apoptosome-mediated cleavage.
REACT_75776. NOD1/2 Signaling Pathway.
REACT_89. Formation of apoptosome.
SABIO-RKP55211.

Miscellaneous databases

EvolutionaryTraceiP55211.
GeneWikiiCaspase-9.
GenomeRNAii842.
NextBioi3524.
PMAP-CutDBP55211.
PROiP55211.
SOURCEiSearch...

Gene expression databases

BgeeiP55211.
CleanExiHS_CASP9.
ExpressionAtlasiP55211. baseline and differential.
GenevisibleiP55211. HS.

Family and domain databases

Gene3Di1.10.533.10. 1 hit.
3.40.50.1460. 1 hit.
InterProiIPR001315. CARD.
IPR029030. Caspase-like_dom.
IPR017350. Caspase_ICE-type.
IPR011029. DEATH-like_dom.
IPR011600. Pept_C14_caspase.
IPR001309. Pept_C14_ICE_p20.
IPR016129. Pept_C14_ICE_p20_AS.
IPR002138. Pept_C14_p10.
IPR015917. Pept_C14A_p45_core.
[Graphical view]
PfamiPF00619. CARD. 1 hit.
PF00656. Peptidase_C14. 1 hit.
[Graphical view]
PIRSFiPIRSF038001. Caspase_ICE. 1 hit.
PRINTSiPR00376. IL1BCENZYME.
SMARTiSM00114. CARD. 1 hit.
SM00115. CASc. 1 hit.
[Graphical view]
SUPFAMiSSF47986. SSF47986. 1 hit.
PROSITEiPS50209. CARD. 1 hit.
PS01122. CASPASE_CYS. 1 hit.
PS01121. CASPASE_HIS. 1 hit.
PS50207. CASPASE_P10. 1 hit.
PS50208. CASPASE_P20. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "ICE-LAP6, a novel member of the ICE/Ced-3 gene family, is activated by the cytotoxic T cell protease granzyme B."
    Duan H., Orth K., Chinnaiyan A.M., Poirier G.G., Froelich C.J., He W.-W., Dixit V.M.
    J. Biol. Chem. 271:16720-16724(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS VAL-28 AND ARG-221.
  2. "The Ced-3/interleukin 1beta converting enzyme-like homolog Mch6 and the lamin-cleaving enzyme Mch2alpha are substrates for the apoptotic mediator CPP32."
    Srinivasula S.M., Fernandes-Alnemri T., Zangrilli J., Robertson N., Armstrong R.C., Wang L., Trapani J.A., Tomaselli K.J., Litwack G., Alnemri E.S.
    J. Biol. Chem. 271:27099-27106(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEOLYTIC PROCESSING.
    Tissue: T-cell.
  3. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "Identification of an endogenous dominant-negative short isoform of caspase-9 that can regulate apoptosis."
    Srinivasula S.M., Ahmad M., Guo Y., Zhan Y., Lazebnik Y., Fernandes-Alnemri T., Alnemri E.S.
    Cancer Res. 59:999-1002(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
  5. "Molecular cloning and sequencing of a cDNA predicting an alternative form of pro-caspase-9 from human gastric cancer cell lines."
    Izawa M., Mori T., Ito H., Sairenji T.
    Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    Tissue: Stomach cancer.
  6. "A novel splicing product of human caspase-9 lacking protease activity."
    Miho Y., Momoi T., Fujita E.
    Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
  7. "A caspase-9 variant missing the catalytic site is an endogenous inhibitor of apoptosis."
    Seol D.W., Billiar T.R.
    J. Biol. Chem. 274:2072-2076(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANT VAL-28.
  8. "Cloning of a novel human caspase-9 splice variant containing only the CARD domain."
    Wang P., Shi T., Ma D.
    Life Sci. 79:934-940(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), VARIANT VAL-28.
  9. NIEHS SNPs program
    Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS VAL-28; LEU-99; ILE-102; VAL-106; ASP-114; HIS-173 AND ARG-221.
  10. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  11. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
    Tissue: Kidney.
  12. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  13. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  14. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Eye and Lymph.
  15. "Inhibition of caspase-9 through phosphorylation at Thr 125 by ERK MAPK."
    Allan L.A., Morrice N., Brady S., Magee G., Pathak S., Clarke P.R.
    Nat. Cell Biol. 5:647-654(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT THR-125.
  16. "Dual role of BRUCE as an antiapoptotic IAP and a chimeric E2/E3 ubiquitin ligase."
    Bartke T., Pohl C., Pyrowolakis G., Jentsch S.
    Mol. Cell 14:801-811(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH BIRC6/BRUCE.
  17. "c-Abl tyrosine kinase regulates caspase-9 autocleavage in the apoptotic response to DNA damage."
    Raina D., Pandey P., Ahmad R., Bharti A., Ren J., Kharbanda S., Weichselbaum R., Kufe D.
    J. Biol. Chem. 280:11147-11151(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN APOPTOSIS, INTERACTION WITH ABL1, PROTEOLYTIC PROCESSING, PHOSPHORYLATION AT TYR-153 BY ABL1, MUTAGENESIS OF TYR-153.
  18. "Overexpression of HAX-1 protects cardiac myocytes from apoptosis through caspase-9 inhibition."
    Han Y., Chen Y.S., Liu Z., Bodyak N., Rigor D., Bisping E., Pu W.T., Kang P.M.
    Circ. Res. 99:415-423(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HAX1, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
  19. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-125; SER-302 AND SER-307, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  20. "Comparative proteomics analysis of caspase-9-protein complexes in untreated and cytochrome c/dATP stimulated lysates of NSCLC cells."
    Checinska A., Giaccone G., Rodriguez J.A., Kruyt F.A.E., Jimenez C.R.
    J. Proteomics 72:575-585(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH EFHD2.
  21. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-307, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  22. "Dimer formation drives the activation of the cell death protease caspase 9."
    Renatus M., Stennicke H.R., Scott F.L., Liddington R.C., Salvesen G.S.
    Proc. Natl. Acad. Sci. U.S.A. 98:14250-14255(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 140-416, SUBUNIT.
  23. Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 140-416 IN COMPLEX WITH BIRC4/XIAP.
  24. "The E.coli effector protein NleF is a caspase inhibitor."
    Blasche S., Moertl M., Steuber H., Siszler G., Nisa S., Schwarz F., Lavrik I., Gronewold T.M.A., Maskos K., Donnenberg M.S., Ullmann D., Uetz P., Koegl M.
    PLoS ONE 0:0-0(2013)
    Cited for: X-RAY CRYSTALLOGRAPHY (3.49 ANGSTROMS) OF 140-416 IN COMPLEX WITH E.COLI NLEF, INTERACTION WITH E.COLI NLEF, SUBUNIT, CATALYTIC ACTIVITY, FUNCTION, ENZYME REGULATION.

Entry informationi

Entry nameiCASP9_HUMAN
AccessioniPrimary (citable) accession number: P55211
Secondary accession number(s): B4E1A3
, O95348, Q53Y70, Q5JRU9, Q5UGI1, Q92852, Q9BQ62, Q9UEQ3, Q9UIJ8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: February 22, 2003
Last modified: July 22, 2015
This is version 176 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Peptidase families
    Classification of peptidase families and list of entries
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.