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P29466

- CASP1_HUMAN

UniProt

P29466 - CASP1_HUMAN

Protein

Caspase-1

Gene

CASP1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 168 (01 Oct 2014)
      Sequence version 1 (01 Apr 1993)
      Previous versions | rss
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    Functioni

    Thiol protease that cleaves IL-1 beta between an Asp and an Ala, releasing the mature cytokine which is involved in a variety of inflammatory processes. Important for defense against pathogens. Cleaves and activates sterol regulatory element binding proteins (SREBPs). Can also promote apoptosis.2 Publications

    Catalytic activityi

    Strict requirement for an Asp residue at position P1 and has a preferred cleavage sequence of Tyr-Val-Ala-Asp-|-.

    Enzyme regulationi

    Specifically inhibited by the cowpox virus Crma protein.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei237 – 23711 Publication
    Active sitei285 – 28511 Publication

    GO - Molecular functioni

    1. cysteine-type endopeptidase activator activity involved in apoptotic process Source: ProtInc
    2. cysteine-type endopeptidase activity Source: RefGenome
    3. endopeptidase activity Source: ParkinsonsUK-UCL
    4. protein binding Source: IntAct

    GO - Biological processi

    1. activation of cysteine-type endopeptidase activity involved in apoptotic process Source: GOC
    2. apoptotic process Source: ProtInc
    3. cellular response to mechanical stimulus Source: UniProtKB
    4. cellular response to organic substance Source: MGI
    5. execution phase of apoptosis Source: RefGenome
    6. innate immune response Source: Reactome
    7. interleukin-1 beta production Source: Ensembl
    8. membrane hyperpolarization Source: Ensembl
    9. mitochondrial depolarization Source: Ensembl
    10. nucleotide-binding domain, leucine rich repeat containing receptor signaling pathway Source: Reactome
    11. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
    12. positive regulation of interleukin-1 alpha secretion Source: Ensembl
    13. positive regulation of interleukin-1 beta secretion Source: Ensembl
    14. proteolysis Source: UniProtKB
    15. pyroptosis Source: Ensembl
    16. regulation of inflammatory response Source: RefGenome
    17. response to ATP Source: Ensembl
    18. response to hypoxia Source: Ensembl
    19. response to lipopolysaccharide Source: Ensembl
    20. signal transduction Source: ProtInc

    Keywords - Molecular functioni

    Hydrolase, Protease, Thiol protease

    Keywords - Biological processi

    Apoptosis

    Enzyme and pathway databases

    BRENDAi3.4.22.36. 2681.
    ReactomeiREACT_23950. Interleukin-1 processing.
    REACT_75776. NOD1/2 Signaling Pathway.
    REACT_75777. The AIM2 inflammasome.
    REACT_75808. The NLRP3 inflammasome.
    REACT_75892. The IPAF inflammasome.
    SABIO-RKP29466.
    SignaLinkiP29466.

    Protein family/group databases

    MEROPSiC14.001.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Caspase-1 (EC:3.4.22.36)
    Short name:
    CASP-1
    Alternative name(s):
    Interleukin-1 beta convertase
    Short name:
    IL-1BC
    Interleukin-1 beta-converting enzyme
    Short name:
    ICE
    Short name:
    IL-1 beta-converting enzyme
    p45
    Cleaved into the following 2 chains:
    Gene namesi
    Name:CASP1
    Synonyms:IL1BC, IL1BCE
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:1499. CASP1.

    Subcellular locationi

    GO - Cellular componenti

    1. AIM2 inflammasome complex Source: UniProtKB
    2. cytoplasm Source: RefGenome
    3. cytosol Source: Reactome
    4. extracellular region Source: Ensembl
    5. IPAF inflammasome complex Source: UniProtKB
    6. NLRP1 inflammasome complex Source: UniProtKB
    7. NLRP3 inflammasome complex Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi285 – 2851C → A or S: Loss of activity. 1 Publication

    Organism-specific databases

    PharmGKBiPA26083.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Propeptidei1 – 119119PRO_0000004521Add
    BLAST
    Chaini120 – 297178Caspase-1 subunit p20PRO_0000004522Add
    BLAST
    Propeptidei298 – 31619PRO_0000004523Add
    BLAST
    Chaini317 – 40488Caspase-1 subunit p10PRO_0000004524Add
    BLAST

    Post-translational modificationi

    The two subunits are derived from the precursor sequence by an autocatalytic mechanism.

    Keywords - PTMi

    Zymogen

    Proteomic databases

    MaxQBiP29466.
    PaxDbiP29466.
    PRIDEiP29466.

    PTM databases

    PhosphoSiteiP29466.

    Miscellaneous databases

    PMAP-CutDBP29466.

    Expressioni

    Tissue specificityi

    Expressed in larger amounts in spleen and lung. Detected in liver, heart, small intestine, colon, thymus, prostate, skeletal muscle, peripheral blood leukocytes, kidney and testis. No expression in the brain.1 Publication

    Gene expression databases

    ArrayExpressiP29466.
    BgeeiP29466.
    CleanExiHS_CASP1.
    GenevestigatoriP29466.

    Organism-specific databases

    HPAiCAB002685.
    HPA003056.

    Interactioni

    Subunit structurei

    Heterotetramer that consists of two anti-parallel arranged heterodimers, each one formed by a 20 kDa (p20) and a 10 kDa (p10) subunit. The p20 subunit can also form a heterodimer with the epsilon isoform which then has an inhibitory effect. May be a component of the inflammasome, a protein complex which also includes PYCARD, CARD8 and NALP2 and whose function would be the activation of proinflammatory caspases. Both the p10 and p20 subunits interact with MEFV. Interacts with CARD17/INCA and CARD18.5 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    FGF2P090382EBI-516667,EBI-977447
    IL1AP015833EBI-516667,EBI-1749782
    NLRC4Q9NPP44EBI-516667,EBI-1222527

    Protein-protein interaction databases

    BioGridi107284. 24 interactions.
    DIPiDIP-175N.
    IntActiP29466. 6 interactions.
    MINTiMINT-201196.
    STRINGi9606.ENSP00000410076.

    Structurei

    Secondary structure

    1
    404
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni129 – 1324
    Helixi138 – 14710
    Beta strandi148 – 1503
    Turni158 – 1603
    Beta strandi164 – 1696
    Beta strandi174 – 1763
    Helixi182 – 19514
    Beta strandi199 – 2057
    Helixi208 – 21912
    Helixi222 – 2265
    Beta strandi230 – 2367
    Beta strandi242 – 2443
    Beta strandi250 – 2523
    Beta strandi255 – 2573
    Helixi258 – 2658
    Turni267 – 2693
    Helixi271 – 2733
    Beta strandi278 – 2836
    Beta strandi287 – 2893
    Beta strandi291 – 2988
    Helixi316 – 3194
    Beta strandi326 – 3338
    Beta strandi340 – 3423
    Turni343 – 3453
    Helixi348 – 36013
    Turni361 – 3633
    Helixi366 – 37611
    Beta strandi381 – 3833
    Beta strandi388 – 3914
    Beta strandi395 – 3973

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1BMQX-ray2.50A131-297[»]
    B317-404[»]
    1IBCX-ray2.73A104-297[»]
    B317-404[»]
    1ICEX-ray2.60A131-297[»]
    B317-404[»]
    1RWKX-ray2.30A120-297[»]
    B317-404[»]
    1RWMX-ray2.70A120-297[»]
    B317-404[»]
    1RWNX-ray2.00A120-297[»]
    B317-404[»]
    1RWOX-ray2.10A120-297[»]
    B317-404[»]
    1RWPX-ray2.20A120-297[»]
    B317-404[»]
    1RWVX-ray2.10A120-297[»]
    B317-404[»]
    1RWWX-ray2.80A120-297[»]
    B317-404[»]
    1RWXX-ray1.85A120-297[»]
    B317-404[»]
    1SC1X-ray2.60A120-297[»]
    B317-404[»]
    1SC3X-ray1.80A120-297[»]
    B317-404[»]
    1SC4X-ray2.10A120-297[»]
    B317-404[»]
    2FQQX-ray3.30A120-297[»]
    B317-404[»]
    2H48X-ray2.20A120-297[»]
    B317-404[»]
    2H4WX-ray2.00A120-297[»]
    B317-404[»]
    2H4YX-ray1.90A120-297[»]
    B317-404[»]
    2H51X-ray2.10A120-297[»]
    B317-404[»]
    2H54X-ray1.80A120-297[»]
    B317-404[»]
    2HBQX-ray1.80A120-297[»]
    B317-404[»]
    2HBRX-ray2.20A120-297[»]
    B317-404[»]
    2HBYX-ray2.10A120-297[»]
    B317-404[»]
    2HBZX-ray1.90A120-297[»]
    B317-404[»]
    3D6FX-ray1.90A120-297[»]
    B317-404[»]
    3D6HX-ray2.00A120-297[»]
    B317-404[»]
    3D6MX-ray1.80A120-297[»]
    B317-404[»]
    3E4CX-ray2.05A/B104-404[»]
    3NS7X-ray2.60A136-297[»]
    B317-404[»]
    ProteinModelPortaliP29466.
    SMRiP29466. Positions 2-89, 125-404.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP29466.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 9191CARDPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiNOG274219.
    HOVERGENiHBG076981.
    InParanoidiP29466.
    KOiK01370.
    OMAiKSAEIYP.
    PhylomeDBiP29466.
    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 (5)i

    Sequence statusi: Complete.

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

    This entry describes 5 isoformsi produced by alternative splicing. Align

    Note: Additional isoforms seem to exist.

    Isoform Alpha (identifier: P29466-1) [UniParc]FASTAAdd to Basket

    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

    MADKVLKEKR KLFIRSMGEG TINGLLDELL QTRVLNKEEM EKVKRENATV    50
    MDKTRALIDS VIPKGAQACQ ICITYICEED SYLAGTLGLS ADQTSGNYLN 100
    MQDSQGVLSS FPAPQAVQDN PAMPTSSGSE GNVKLCSLEE AQRIWKQKSA 150
    EIYPIMDKSS RTRLALIICN EEFDSIPRRT GAEVDITGMT MLLQNLGYSV 200
    DVKKNLTASD MTTELEAFAH RPEHKTSDST FLVFMSHGIR EGICGKKHSE 250
    QVPDILQLNA IFNMLNTKNC PSLKDKPKVI IIQACRGDSP GVVWFKDSVG 300
    VSGNLSLPTT EEFEDDAIKK AHIEKDFIAF CSSTPDNVSW RHPTMGSVFI 350
    GRLIEHMQEY ACSCDVEEIF RKVRFSFEQP DGRAQMPTTE RVTLTRCFYL 400
    FPGH 404
    Length:404
    Mass (Da):45,159
    Last modified:April 1, 1993 - v1
    Checksum:iABF33CF33CC71584
    GO
    Isoform Beta (identifier: P29466-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         92-112: Missing.

    Show »
    Length:383
    Mass (Da):42,888
    Checksum:iC8D92A9B235B2E6F
    GO
    Isoform Gamma (identifier: P29466-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         20-112: Missing.

    Show »
    Length:311
    Mass (Da):35,019
    Checksum:i902A4384E49282C8
    GO
    Isoform Delta (identifier: P29466-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         20-112: Missing.
         288-335: Missing.

    Note: Apoptosis inactive.

    Show »
    Length:263
    Mass (Da):29,821
    Checksum:i5ED98AC7864EB0BA
    GO
    Isoform Epsilon (identifier: P29466-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         20-335: Missing.

    Note: Apoptosis inactive.

    Show »
    Length:88
    Mass (Da):10,417
    Checksum:iF3D811149FCDF159
    GO

    Sequence cautioni

    The sequence AAT72297.1 differs from that shown. Reason: Probable cloning artifact.
    The sequence AAT72297.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti319 – 3191K → R in BAD97223. 1 PublicationCurated
    Sequence conflicti402 – 4021P → L in BAD97223. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti15 – 151R → H.
    Corresponds to variant rs1042743 [ dbSNP | Ensembl ].
    VAR_048615

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei20 – 335316Missing in isoform Epsilon. 1 PublicationVSP_000797Add
    BLAST
    Alternative sequencei20 – 11293Missing in isoform Gamma and isoform Delta. 2 PublicationsVSP_000799Add
    BLAST
    Alternative sequencei92 – 11221Missing in isoform Beta. 2 PublicationsVSP_000798Add
    BLAST
    Alternative sequencei288 – 33548Missing in isoform Delta. 1 PublicationVSP_000800Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X65019 mRNA. Translation: CAA46153.1.
    M87507 mRNA. Translation: AAA66942.1.
    U13697 mRNA. Translation: AAC50107.1.
    U13698 mRNA. Translation: AAC50108.1.
    U13699 mRNA. Translation: AAC50109.1.
    U13700 mRNA. Translation: AAC50110.1.
    AK223503 mRNA. Translation: BAD97223.1.
    AP001153 Genomic DNA. No translation available.
    BC041689 mRNA. Translation: AAH41689.1.
    BC062327 mRNA. Translation: AAH62327.1.
    AY660536 mRNA. Translation: AAT72297.1. Sequence problems.
    CCDSiCCDS53704.1. [P29466-3]
    CCDS8329.1. [P29466-2]
    CCDS8330.1. [P29466-1]
    CCDS8331.1. [P29466-4]
    CCDS8332.1. [P29466-5]
    PIRiA54263. A42677.
    A56084.
    B56084.
    C56084.
    D56084.
    RefSeqiNP_001214.1. NM_001223.4. [P29466-2]
    NP_001244047.1. NM_001257118.2. [P29466-1]
    NP_001244048.1. NM_001257119.2. [P29466-2]
    NP_150634.1. NM_033292.3. [P29466-1]
    NP_150635.1. NM_033293.3. [P29466-3]
    NP_150636.1. NM_033294.3. [P29466-4]
    NP_150637.1. NM_033295.3. [P29466-5]
    UniGeneiHs.2490.

    Genome annotation databases

    EnsembliENST00000353247; ENSP00000344132; ENSG00000137752. [P29466-5]
    ENST00000436863; ENSP00000410076; ENSG00000137752. [P29466-1]
    ENST00000446369; ENSP00000403260; ENSG00000137752. [P29466-4]
    ENST00000525825; ENSP00000434779; ENSG00000137752. [P29466-2]
    ENST00000526568; ENSP00000434250; ENSG00000137752. [P29466-3]
    ENST00000531166; ENSP00000434303; ENSG00000137752. [P29466-5]
    ENST00000533400; ENSP00000433138; ENSG00000137752. [P29466-1]
    ENST00000534497; ENSP00000436875; ENSG00000137752. [P29466-4]
    GeneIDi834.
    KEGGihsa:834.
    UCSCiuc001pig.4. human. [P29466-3]
    uc001pim.5. human. [P29466-1]
    uc009yxi.4. human. [P29466-2]
    uc021qpr.2. human. [P29466-4]
    uc021qps.2. human. [P29466-5]

    Polymorphism databases

    DMDMi266321.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X65019 mRNA. Translation: CAA46153.1 .
    M87507 mRNA. Translation: AAA66942.1 .
    U13697 mRNA. Translation: AAC50107.1 .
    U13698 mRNA. Translation: AAC50108.1 .
    U13699 mRNA. Translation: AAC50109.1 .
    U13700 mRNA. Translation: AAC50110.1 .
    AK223503 mRNA. Translation: BAD97223.1 .
    AP001153 Genomic DNA. No translation available.
    BC041689 mRNA. Translation: AAH41689.1 .
    BC062327 mRNA. Translation: AAH62327.1 .
    AY660536 mRNA. Translation: AAT72297.1 . Sequence problems.
    CCDSi CCDS53704.1. [P29466-3 ]
    CCDS8329.1. [P29466-2 ]
    CCDS8330.1. [P29466-1 ]
    CCDS8331.1. [P29466-4 ]
    CCDS8332.1. [P29466-5 ]
    PIRi A54263. A42677.
    A56084.
    B56084.
    C56084.
    D56084.
    RefSeqi NP_001214.1. NM_001223.4. [P29466-2 ]
    NP_001244047.1. NM_001257118.2. [P29466-1 ]
    NP_001244048.1. NM_001257119.2. [P29466-2 ]
    NP_150634.1. NM_033292.3. [P29466-1 ]
    NP_150635.1. NM_033293.3. [P29466-3 ]
    NP_150636.1. NM_033294.3. [P29466-4 ]
    NP_150637.1. NM_033295.3. [P29466-5 ]
    UniGenei Hs.2490.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1BMQ X-ray 2.50 A 131-297 [» ]
    B 317-404 [» ]
    1IBC X-ray 2.73 A 104-297 [» ]
    B 317-404 [» ]
    1ICE X-ray 2.60 A 131-297 [» ]
    B 317-404 [» ]
    1RWK X-ray 2.30 A 120-297 [» ]
    B 317-404 [» ]
    1RWM X-ray 2.70 A 120-297 [» ]
    B 317-404 [» ]
    1RWN X-ray 2.00 A 120-297 [» ]
    B 317-404 [» ]
    1RWO X-ray 2.10 A 120-297 [» ]
    B 317-404 [» ]
    1RWP X-ray 2.20 A 120-297 [» ]
    B 317-404 [» ]
    1RWV X-ray 2.10 A 120-297 [» ]
    B 317-404 [» ]
    1RWW X-ray 2.80 A 120-297 [» ]
    B 317-404 [» ]
    1RWX X-ray 1.85 A 120-297 [» ]
    B 317-404 [» ]
    1SC1 X-ray 2.60 A 120-297 [» ]
    B 317-404 [» ]
    1SC3 X-ray 1.80 A 120-297 [» ]
    B 317-404 [» ]
    1SC4 X-ray 2.10 A 120-297 [» ]
    B 317-404 [» ]
    2FQQ X-ray 3.30 A 120-297 [» ]
    B 317-404 [» ]
    2H48 X-ray 2.20 A 120-297 [» ]
    B 317-404 [» ]
    2H4W X-ray 2.00 A 120-297 [» ]
    B 317-404 [» ]
    2H4Y X-ray 1.90 A 120-297 [» ]
    B 317-404 [» ]
    2H51 X-ray 2.10 A 120-297 [» ]
    B 317-404 [» ]
    2H54 X-ray 1.80 A 120-297 [» ]
    B 317-404 [» ]
    2HBQ X-ray 1.80 A 120-297 [» ]
    B 317-404 [» ]
    2HBR X-ray 2.20 A 120-297 [» ]
    B 317-404 [» ]
    2HBY X-ray 2.10 A 120-297 [» ]
    B 317-404 [» ]
    2HBZ X-ray 1.90 A 120-297 [» ]
    B 317-404 [» ]
    3D6F X-ray 1.90 A 120-297 [» ]
    B 317-404 [» ]
    3D6H X-ray 2.00 A 120-297 [» ]
    B 317-404 [» ]
    3D6M X-ray 1.80 A 120-297 [» ]
    B 317-404 [» ]
    3E4C X-ray 2.05 A/B 104-404 [» ]
    3NS7 X-ray 2.60 A 136-297 [» ]
    B 317-404 [» ]
    ProteinModelPortali P29466.
    SMRi P29466. Positions 2-89, 125-404.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107284. 24 interactions.
    DIPi DIP-175N.
    IntActi P29466. 6 interactions.
    MINTi MINT-201196.
    STRINGi 9606.ENSP00000410076.

    Chemistry

    BindingDBi P29466.
    ChEMBLi CHEMBL4801.
    DrugBanki DB01017. Minocycline.
    DB00859. Penicillamine.
    GuidetoPHARMACOLOGYi 1617.

    Protein family/group databases

    MEROPSi C14.001.

    PTM databases

    PhosphoSitei P29466.

    Polymorphism databases

    DMDMi 266321.

    Proteomic databases

    MaxQBi P29466.
    PaxDbi P29466.
    PRIDEi P29466.

    Protocols and materials databases

    DNASUi 834.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000353247 ; ENSP00000344132 ; ENSG00000137752 . [P29466-5 ]
    ENST00000436863 ; ENSP00000410076 ; ENSG00000137752 . [P29466-1 ]
    ENST00000446369 ; ENSP00000403260 ; ENSG00000137752 . [P29466-4 ]
    ENST00000525825 ; ENSP00000434779 ; ENSG00000137752 . [P29466-2 ]
    ENST00000526568 ; ENSP00000434250 ; ENSG00000137752 . [P29466-3 ]
    ENST00000531166 ; ENSP00000434303 ; ENSG00000137752 . [P29466-5 ]
    ENST00000533400 ; ENSP00000433138 ; ENSG00000137752 . [P29466-1 ]
    ENST00000534497 ; ENSP00000436875 ; ENSG00000137752 . [P29466-4 ]
    GeneIDi 834.
    KEGGi hsa:834.
    UCSCi uc001pig.4. human. [P29466-3 ]
    uc001pim.5. human. [P29466-1 ]
    uc009yxi.4. human. [P29466-2 ]
    uc021qpr.2. human. [P29466-4 ]
    uc021qps.2. human. [P29466-5 ]

    Organism-specific databases

    CTDi 834.
    GeneCardsi GC11M104898.
    HGNCi HGNC:1499. CASP1.
    HPAi CAB002685.
    HPA003056.
    MIMi 147678. gene.
    neXtProti NX_P29466.
    PharmGKBi PA26083.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG274219.
    HOVERGENi HBG076981.
    InParanoidi P29466.
    KOi K01370.
    OMAi KSAEIYP.
    PhylomeDBi P29466.
    TreeFami TF102023.

    Enzyme and pathway databases

    BRENDAi 3.4.22.36. 2681.
    Reactomei REACT_23950. Interleukin-1 processing.
    REACT_75776. NOD1/2 Signaling Pathway.
    REACT_75777. The AIM2 inflammasome.
    REACT_75808. The NLRP3 inflammasome.
    REACT_75892. The IPAF inflammasome.
    SABIO-RK P29466.
    SignaLinki P29466.

    Miscellaneous databases

    ChiTaRSi CASP1. human.
    EvolutionaryTracei P29466.
    GeneWikii Caspase_1.
    GenomeRNAii 834.
    NextBioi 3460.
    PMAP-CutDB P29466.
    PROi P29466.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P29466.
    Bgeei P29466.
    CleanExi HS_CASP1.
    Genevestigatori P29466.

    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. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA), PARTIAL PROTEIN SEQUENCE, ACTIVE SITE.
    2. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA), PROTEIN SEQUENCE OF 120-142.
    3. "Cloning and expression of four novel isoforms of human interleukin-1 beta converting enzyme with different apoptotic activities."
      Alnemri E.S., Fernandes-Alnemri T., Litwack G.
      J. Biol. Chem. 270:4312-4317(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS BETA; DELTA; EPSILON AND GAMMA), ALTERNATIVE SPLICING, FUNCTION.
    4. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
      Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA).
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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 GAMMA), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 4-404 (ISOFORM BETA).
      Tissue: Testis.
    7. "Caspase-1 zeta, a new splice variant of caspase-1 gene."
      Feng Q., Li P., Leung P.C.K., Auersperg N.
      Genomics 84:587-591(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 32-404 (ISOFORM ALPHA), FUNCTION, MUTAGENESIS OF CYS-285, ALTERNATIVE SPLICING, TISSUE SPECIFICITY.
    8. "Purification of interleukin-1 beta converting enzyme, the protease that cleaves the interleukin-1 beta precursor."
      Kronheim S.R., Mumma A., Greenstreet T., Glackin P.J., Van Ness K., March C.J., Black R.A.
      Arch. Biochem. Biophys. 296:698-703(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 120-142.
    9. "ICEBERG: a novel inhibitor of interleukin-1beta generation."
      Humke E.W., Shriver S.K., Starovasnik M.A., Fairbrother W.J., Dixit V.M.
      Cell 103:99-111(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CARD18.
    10. "NALP3 forms an IL-1beta-processing inflammasome with increased activity in Muckle-Wells autoinflammatory disorder."
      Agostini L., Martinon F., Burns K., McDermott M.F., Hawkins P.N., Tschopp J.
      Immunity 20:319-325(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: COMPONENT OF THE INFLAMMASOME.
    11. "INCA, a novel human caspase recruitment domain protein that inhibits interleukin-1beta generation."
      Lamkanfi M., Denecker G., Kalai M., D'hondt K., Meeus A., Declercq W., Saelens X., Vandenabeele P.
      J. Biol. Chem. 279:51729-51738(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CARD17.
    12. "The B30.2 domain of pyrin, the familial Mediterranean fever protein, interacts directly with caspase-1 to modulate IL-1beta production."
      Chae J.J., Wood G., Masters S.L., Richard K., Park G., Smith B.J., Kastner D.L.
      Proc. Natl. Acad. Sci. U.S.A. 103:9982-9987(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MEFV.
    13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), SUBUNIT.
    15. "A combinatorial approach for determining protease specificities: application to interleukin-1beta converting enzyme (ICE)."
      Rano T.A., Timkey T., Peterson E.P., Rotonda J., Nicholson D.W., Becker J.W., Chapman K.T., Thornberry N.A.
      Chem. Biol. 4:149-155(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.73 ANGSTROMS).
    16. "Peptide based interleukin-1 beta converting enzyme (ICE) inhibitors: synthesis, structure activity relationships and crystallographic study of the ICE-inhibitor complex."
      Okamoto Y., Anan H., Nakai E., Morihira K., Yonetoku Y., Kurihara H., Sakashita H., Terai Y., Takeuchi M., Shibanuma T., Isomura Y.
      Chem. Pharm. Bull. 47:11-21(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH INHIBITORS.
    17. "Crystal structures of a ligand-free and malonate-bound human caspase-1: implications for the mechanism of substrate binding."
      Romanowski M.J., Scheer J.M., O'Brien T., McDowell R.S.
      Structure 12:1361-1371(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 120-404 OF MUTANT ALA-285.

    Entry informationi

    Entry nameiCASP1_HUMAN
    AccessioniPrimary (citable) accession number: P29466
    Secondary accession number(s): B5MDZ1
    , Q53EY6, Q6DMQ1, Q6GSS3, Q6PI75, Q9UCN3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1993
    Last sequence update: April 1, 1993
    Last modified: October 1, 2014
    This is version 168 of the entry and version 1 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, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 11
      Human chromosome 11: 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