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P55211

- CASP9_HUMAN

UniProt

P55211 - CASP9_HUMAN

Protein

Caspase-9

Gene

CASP9

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 166 (01 Oct 2014)
      Sequence version 3 (22 Feb 2003)
      Previous versions | rss
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    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

    1. cysteine-type endopeptidase activity Source: RefGenome
    2. enzyme activator activity Source: ProtInc
    3. peptidase activity Source: MGI
    4. protein binding Source: UniProtKB
    5. protein kinase binding Source: UniProtKB
    6. SH3 domain binding Source: UniProtKB

    GO - Biological processi

    1. activation of cysteine-type endopeptidase activity involved in apoptotic process by cytochrome c Source: Reactome
    2. aging Source: Ensembl
    3. apoptotic process Source: UniProtKB
    4. cellular response to dexamethasone stimulus Source: Ensembl
    5. cellular response to DNA damage stimulus Source: UniProtKB
    6. cellular response to UV Source: UniProtKB
    7. epidermal growth factor receptor signaling pathway Source: Reactome
    8. Fc-epsilon receptor signaling pathway Source: Reactome
    9. fibroblast growth factor receptor signaling pathway Source: Reactome
    10. glial cell apoptotic process Source: Ensembl
    11. innate immune response Source: Reactome
    12. intrinsic apoptotic signaling pathway Source: Reactome
    13. intrinsic apoptotic signaling pathway in response to DNA damage Source: UniProtKB
    14. neurotrophin TRK receptor signaling pathway Source: Reactome
    15. phosphatidylinositol-mediated signaling Source: Reactome
    16. platelet formation Source: UniProtKB
    17. positive regulation of apoptotic process Source: Reactome
    18. positive regulation of neuron apoptotic process Source: Ensembl
    19. regulation of apoptotic process Source: Reactome
    20. regulation of response to DNA damage stimulus Source: UniProtKB
    21. response to antibiotic Source: Ensembl
    22. response to cobalt ion Source: Ensembl
    23. response to estradiol Source: Ensembl
    24. response to lipopolysaccharide Source: Ensembl
    25. signal transduction in response to DNA damage Source: UniProtKB

    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_147727. Constitutive PI3K/AKT Signaling in Cancer.
    REACT_22128. Role of DCC in regulating apoptosis.
    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: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:1511. CASP9.

    Subcellular locationi

    GO - Cellular componenti

    1. apoptosome Source: UniProtKB
    2. cytosol Source: UniProtKB
    3. mitochondrion Source: Ensembl
    4. nucleus Source: Ensembl

    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.

    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.4 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

    ArrayExpressiP55211.
    BgeeiP55211.
    CleanExiHS_CASP9.
    GenevestigatoriP55211.

    Organism-specific databases

    HPAiCAB004348.
    HPA001473.

    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
    BIRC2Q134904EBI-516799,EBI-514538
    BIRC3Q134892EBI-516799,EBI-517709
    BIRC5O153922EBI-516799,EBI-518823
    BIRC7Q96CA55EBI-516799,EBI-517623
    ILKQ134182EBI-516799,EBI-747644
    XIAPP981706EBI-516799,EBI-517127

    Protein-protein interaction databases

    BioGridi107292. 29 interactions.
    DIPiDIP-27625N.
    IntActiP55211. 12 interactions.
    MINTiMINT-89165.
    STRINGi9606.ENSP00000330237.

    Structurei

    Secondary structure

    1
    416
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi3 – 119
    Helixi13 – 197
    Turni23 – 253
    Helixi26 – 316
    Helixi37 – 448
    Helixi51 – 6212
    Helixi69 – 7810
    Turni79 – 813
    Helixi83 – 9412
    Helixi143 – 1475
    Turni149 – 1513
    Beta strandi157 – 1593
    Beta strandi161 – 1677
    Helixi173 – 1753
    Helixi183 – 19614
    Beta strandi199 – 2068
    Helixi209 – 22113
    Helixi224 – 2263
    Beta strandi228 – 23912
    Beta strandi244 – 2463
    Beta strandi249 – 2513
    Beta strandi257 – 2593
    Helixi260 – 2656
    Turni269 – 2713
    Helixi273 – 2753
    Beta strandi280 – 2878
    Beta strandi317 – 3193
    Beta strandi340 – 3467
    Beta strandi351 – 3533
    Beta strandi354 – 3563
    Turni357 – 3593
    Helixi362 – 37413
    Turni375 – 3773
    Helixi380 – 39213
    Beta strandi395 – 3984
    Beta strandi402 – 4065
    Beta strandi408 – 4103

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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[»]
    ProteinModelPortaliP55211.
    SMRiP55211. Positions 1-96, 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.
    HOVERGENiHBG059022.
    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. Align

    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

    MDEADRRLLR RCRLRLVEEL QVDQLWDALL SRELFRPHMI EDIQRAGSGS    50
    RRDQARQLII DLETRGSQAL PLFISCLEDT GQDMLASFLR TNRQAAKLSK 100
    PTLENLTPVV LRPEIRKPEV LRPETPRPVD IGSGGFGDVG ALESLRGNAD 150
    LAYILSMEPC GHCLIINNVN FCRESGLRTR TGSNIDCEKL RRRFSSLHFM 200
    VEVKGDLTAK KMVLALLELA QQDHGALDCC VVVILSHGCQ ASHLQFPGAV 250
    YGTDGCPVSV EKIVNIFNGT SCPSLGGKPK LFFIQACGGE QKDHGFEVAS 300
    TSPEDESPGS NPEPDATPFQ EGLRTFDQLD AISSLPTPSD IFVSYSTFPG 350
    FVSWRDPKSG SWYVETLDDI FEQWAHSEDL QSLLLRVANA VSVKGIYKQM 400
    PGCFNFLRKK LFFKTS 416
    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. 1 PublicationCurated
    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:
    EMBL
    GenBank
    DDBJ
    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_005246014.1. [P55211-4]
    UniGeneiHs.329502.

    Genome annotation databases

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

    Polymorphism databases

    DMDMi28558771.

    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:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS158.1. [P55211-1 ]
    CCDS159.2. [P55211-4 ]
    CCDS59995.1. [P55211-2 ]
    PIRi G02635.
    RefSeqi NP_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_005246014.1. [P55211-4 ]
    UniGenei Hs.329502.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1JXQ X-ray 2.80 A/B/C/D 140-416 [» ]
    1NW9 X-ray 2.40 B 140-416 [» ]
    2AR9 X-ray 2.80 A/B/C/D 139-416 [» ]
    3D9T X-ray 1.50 C/D 316-321 [» ]
    3V3K X-ray 3.49 A/C/E/G/I/K/M/O 141-416 [» ]
    3YGS X-ray 2.50 P 1-95 [» ]
    ProteinModelPortali P55211.
    SMRi P55211. Positions 1-96, 141-416.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107292. 29 interactions.
    DIPi DIP-27625N.
    IntActi P55211. 12 interactions.
    MINTi MINT-89165.
    STRINGi 9606.ENSP00000330237.

    Chemistry

    BindingDBi P55211.
    ChEMBLi CHEMBL2273.
    GuidetoPHARMACOLOGYi 1625.

    Protein family/group databases

    MEROPSi C14.010.

    PTM databases

    PhosphoSitei P55211.

    Polymorphism databases

    DMDMi 28558771.

    Proteomic databases

    MaxQBi P55211.
    PaxDbi P55211.
    PRIDEi P55211.

    Protocols and materials databases

    DNASUi 842.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000333868 ; ENSP00000330237 ; ENSG00000132906 . [P55211-1 ]
    ENST00000348549 ; ENSP00000255256 ; ENSG00000132906 . [P55211-2 ]
    ENST00000375890 ; ENSP00000365051 ; ENSG00000132906 . [P55211-4 ]
    GeneIDi 842.
    KEGGi hsa:842.
    UCSCi uc001awn.4. human. [P55211-1 ]
    uc001awo.4. human. [P55211-2 ]

    Organism-specific databases

    CTDi 842.
    GeneCardsi GC01M015814.
    HGNCi HGNC:1511. CASP9.
    HPAi CAB004348.
    HPA001473.
    MIMi 602234. gene.
    neXtProti NX_P55211.
    PharmGKBi PA26094.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG319022.
    HOVERGENi HBG059022.
    KOi K04399.
    PhylomeDBi P55211.
    TreeFami TF102023.

    Enzyme and pathway databases

    BRENDAi 3.4.22.62. 2681.
    Reactomei REACT_12564. AKT phosphorylates targets in the cytosol.
    REACT_147727. Constitutive PI3K/AKT Signaling in Cancer.
    REACT_22128. Role of DCC in regulating apoptosis.
    REACT_607. Activation of caspases through apoptosome-mediated cleavage.
    REACT_75776. NOD1/2 Signaling Pathway.
    REACT_89. Formation of apoptosome.
    SABIO-RK P55211.

    Miscellaneous databases

    EvolutionaryTracei P55211.
    GeneWikii Caspase-9.
    GenomeRNAii 842.
    NextBioi 3524.
    PMAP-CutDB P55211.
    PROi P55211.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P55211.
    Bgeei P55211.
    CleanExi HS_CASP9.
    Genevestigatori P55211.

    Family and domain databases

    Gene3Di 1.10.533.10. 1 hit.
    3.40.50.1460. 1 hit.
    InterProi IPR001315. 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 ]
    Pfami PF00619. CARD. 1 hit.
    PF00656. Peptidase_C14. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF038001. Caspase_ICE. 1 hit.
    PRINTSi PR00376. IL1BCENZYME.
    SMARTi SM00114. CARD. 1 hit.
    SM00115. CASc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47986. SSF47986. 1 hit.
    PROSITEi PS50209. 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 ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 166 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