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P55210

- CASP7_HUMAN

UniProt

P55210 - CASP7_HUMAN

Protein

Caspase-7

Gene

CASP7

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 157 (01 Oct 2014)
      Sequence version 1 (01 Oct 1996)
      Previous versions | rss
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    Functioni

    Involved in the activation cascade of caspases responsible for apoptosis execution. Cleaves and activates sterol regulatory element binding proteins (SREBPs). Proteolytically cleaves poly(ADP-ribose) polymerase (PARP) at a '216-Asp-|-Gly-217' bond. Overexpression promotes programmed cell death.

    Catalytic activityi

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

    Enzyme regulationi

    Inhibited by isatin sulfonamides.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei144 – 1441By similarity
    Active sitei186 – 1861

    GO - Molecular functioni

    1. aspartic-type endopeptidase activity Source: Ensembl
    2. cysteine-type endopeptidase activity Source: RefGenome
    3. cysteine-type endopeptidase activity involved in apoptotic process Source: Ensembl
    4. cysteine-type peptidase activity Source: ProtInc
    5. protein 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: Reactome
    4. cellular component disassembly involved in execution phase of apoptosis Source: Reactome
    5. execution phase of apoptosis Source: RefGenome
    6. heart development Source: Ensembl
    7. intrinsic apoptotic signaling pathway Source: Reactome
    8. positive regulation of neuron apoptotic process Source: Ensembl
    9. proteolysis Source: UniProtKB
    10. release of cytochrome c from mitochondria Source: Ensembl
    11. response to UV Source: Ensembl

    Keywords - Molecular functioni

    Hydrolase, Protease, Thiol protease

    Keywords - Biological processi

    Apoptosis

    Enzyme and pathway databases

    BRENDAi3.4.22.60. 2681.
    ReactomeiREACT_107. Apoptotic cleavage of cellular proteins.
    REACT_13541. Caspase-mediated cleavage of cytoskeletal proteins.
    REACT_607. Activation of caspases through apoptosome-mediated cleavage.

    Protein family/group databases

    MEROPSiC14.004.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Caspase-7 (EC:3.4.22.60)
    Short name:
    CASP-7
    Alternative name(s):
    Apoptotic protease Mch-3
    CMH-1
    ICE-like apoptotic protease 3
    Short name:
    ICE-LAP3
    Cleaved into the following 2 chains:
    Gene namesi
    Name:CASP7
    Synonyms:MCH3
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 10

    Organism-specific databases

    HGNCiHGNC:1508. CASP7.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: ProtInc
    2. cytosol Source: UniProtKB
    3. nucleoplasm Source: Reactome
    4. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi186 – 1861C → A: No apoptotic activity.

    Organism-specific databases

    PharmGKBiPA26091.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Propeptidei2 – 2322PRO_0000004616Add
    BLAST
    Chaini24 – 198175Caspase-7 subunit p20PRO_0000004617Add
    BLAST
    Propeptidei199 – 2068PRO_0000004618
    Chaini207 – 30397Caspase-7 subunit p11PRO_0000004619Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine2 Publications

    Post-translational modificationi

    Cleavages by granzyme B or caspase-10 generate the two active subunits. Propeptide domains can also be cleaved efficiently by caspase-3. Active heterodimers between the small subunit of caspase-7 and the large subunit of caspase-3, and vice versa, also occur.1 Publication

    Keywords - PTMi

    Acetylation, Zymogen

    Proteomic databases

    MaxQBiP55210.
    PaxDbiP55210.
    PRIDEiP55210.

    PTM databases

    PhosphoSiteiP55210.

    Miscellaneous databases

    PMAP-CutDBP55210.

    Expressioni

    Tissue specificityi

    Highly expressed in lung, skeletal muscle, liver, kidney, spleen and heart, and moderately in testis. No expression in the brain.

    Gene expression databases

    ArrayExpressiP55210.
    BgeeiP55210.
    CleanExiHS_CASP7.
    GenevestigatoriP55210.

    Organism-specific databases

    HPAiCAB025563.

    Interactioni

    Subunit structurei

    Heterotetramer that consists of two anti-parallel arranged heterodimers, each one formed by a 20 kDa (p20) and a 11 kDa (p11) subunit. Interacts with BIRC6/bruce.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    BIRC2Q134902EBI-523958,EBI-514538
    PAK2Q131776EBI-523958,EBI-1045887
    SMPD1P174056EBI-523958,EBI-7095800
    XIAPP981702EBI-523958,EBI-517127

    Protein-protein interaction databases

    BioGridi107290. 46 interactions.
    DIPiDIP-29973N.
    IntActiP55210. 8 interactions.
    MINTiMINT-147084.
    STRINGi9606.ENSP00000298700.

    Structurei

    Secondary structure

    1
    303
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi56 – 583
    Beta strandi64 – 663
    Beta strandi68 – 747
    Helixi80 – 823
    Helixi90 – 10415
    Beta strandi106 – 1138
    Helixi116 – 12712
    Helixi131 – 1333
    Beta strandi137 – 1437
    Beta strandi149 – 1524
    Beta strandi155 – 1584
    Helixi159 – 1635
    Helixi164 – 1663
    Turni168 – 1703
    Helixi172 – 1743
    Beta strandi179 – 1857
    Beta strandi188 – 1903
    Turni209 – 2113
    Turni215 – 2184
    Beta strandi219 – 2257
    Beta strandi227 – 2293
    Beta strandi232 – 2343
    Turni235 – 2373
    Helixi240 – 25213
    Turni253 – 2553
    Helixi258 – 27215
    Helixi280 – 2823
    Beta strandi290 – 2934
    Beta strandi296 – 2983

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1F1JX-ray2.35A/B2-303[»]
    1GQFX-ray2.90A/B47-303[»]
    1I4OX-ray2.40A/B24-303[»]
    1I51X-ray2.45A/C51-198[»]
    B/D199-303[»]
    1K86X-ray2.60A/B51-303[»]
    1K88X-ray2.70A/B51-303[»]
    1KMCX-ray2.90A/B1-303[»]
    1MIAmodel-A57-193[»]
    B211-303[»]
    1SHJX-ray2.80A/B50-303[»]
    1SHLX-ray3.00A/B57-303[»]
    2QL5X-ray2.34A/C24-196[»]
    B/D207-303[»]
    2QL7X-ray2.40A/C24-196[»]
    B/D207-303[»]
    2QL9X-ray2.14A/C24-196[»]
    B/D207-303[»]
    2QLBX-ray2.25A/C24-196[»]
    B/D207-303[»]
    2QLFX-ray2.80A/C24-196[»]
    B/D207-303[»]
    2QLJX-ray2.60A/C24-196[»]
    B/D207-303[»]
    3EDRX-ray2.45A/C24-196[»]
    B/D207-303[»]
    3H1PX-ray2.61A/B50-303[»]
    3IBCX-ray2.75A/C24-196[»]
    B/D207-303[»]
    3IBFX-ray2.50A/C24-196[»]
    B/D207-303[»]
    3R5KX-ray2.86A/B1-303[»]
    4FDLX-ray2.80A/B2-303[»]
    4FEAX-ray3.79A/B57-303[»]
    4HQ0X-ray3.00A/B47-303[»]
    4HQRX-ray3.00A/B47-303[»]
    4JB8X-ray1.70A24-198[»]
    B207-303[»]
    4JJ8X-ray2.94A/B57-303[»]
    4JR1X-ray2.15A/B57-303[»]
    4JR2X-ray1.65A/B57-303[»]
    ProteinModelPortaliP55210.
    SMRiP55210. Positions 47-303.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP55210.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase C14A family.Curated

    Phylogenomic databases

    eggNOGiNOG279444.
    HOVERGENiHBG050802.
    InParanoidiP55210.
    KOiK04397.
    OMAiDANPRHK.
    PhylomeDBiP55210.
    TreeFamiTF102023.

    Family and domain databases

    Gene3Di3.40.50.1460. 1 hit.
    InterProiIPR029030. Caspase-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]
    PfamiPF00656. Peptidase_C14. 1 hit.
    [Graphical view]
    PRINTSiPR00376. IL1BCENZYME.
    SMARTiSM00115. CASc. 1 hit.
    [Graphical view]
    PROSITEiPS01122. 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 Alpha (identifier: P55210-1) [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

    MADDQGCIEE QGVEDSANED SVDAKPDRSS FVPSLFSKKK KNVTMRSIKT    50
    TRDRVPTYQY NMNFEKLGKC IIINNKNFDK VTGMGVRNGT DKDAEALFKC 100
    FRSLGFDVIV YNDCSCAKMQ DLLKKASEED HTNAACFACI LLSHGEENVI 150
    YGKDGVTPIK DLTAHFRGDR CKTLLEKPKL FFIQACRGTE LDDGIQADSG 200
    PINDTDANPR YKIPVEADFL FAYSTVPGYY SWRSPGRGSW FVQALCSILE 250
    EHGKDLEIMQ ILTRVNDRVA RHFESQSDDP HFHEKKQIPC VVSMLTKELY 300
    FSQ 303
    Length:303
    Mass (Da):34,277
    Last modified:October 1, 1996 - v1
    Checksum:iCD373EE54A232CA4
    GO
    Isoform Beta (identifier: P55210-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         149-303: VIYGKDGVTP...MLTKELYFSQ → MESCSVTQAG...TWKSCRSSPG

    Note: Lacks enzymatic activity.

    Show »
    Length:253
    Mass (Da):28,030
    Checksum:i514964EF3F6229E1
    GO
    Isoform Alpha' (identifier: P55210-3) [UniParc]FASTAAdd to Basket

    Also known as: Beta

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1: M → MDCVGWPPGRKWHLEKNTSCGGSSGICASYVTQM

    Note: What we call isoform Alpha' is also known as Beta.1 Publication

    Show »
    Length:336
    Mass (Da):37,815
    Checksum:i34EEFF8AF5C318A2
    GO
    Isoform 4 (identifier: P55210-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-36: MADDQGCIEEQGVEDSANEDSVDAKPDRSSFVPSLF → MQRGLFSDGDT

    Show »
    Length:278
    Mass (Da):31,614
    Checksum:iFAF2707D22D9CDE3
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti194 – 1941G → A in AAC50346. (PubMed:8576161)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti4 – 41D → E.2 Publications
    Corresponds to variant rs11593766 [ dbSNP | Ensembl ].
    VAR_048617
    Natural varianti255 – 2551D → E.
    Corresponds to variant rs2227310 [ dbSNP | Ensembl ].
    VAR_048618

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 3636MADDQ…VPSLF → MQRGLFSDGDT in isoform 4. 1 PublicationVSP_045325Add
    BLAST
    Alternative sequencei1 – 11M → MDCVGWPPGRKWHLEKNTSC GGSSGICASYVTQM in isoform Alpha'. 3 PublicationsVSP_000806
    Alternative sequencei149 – 303155VIYGK…LYFSQ → MESCSVTQAGVQRRDLGRLQ PPPPRLAEGPSLMMASRPTR GPSMTQMLILDTRSQWKLTS SSPIPRFQAITRGGAQEEAP GLCKPSAPSWRSTEKTWKSC RSSPG in isoform Beta. 1 PublicationVSP_000807Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U37448 mRNA. Translation: AAC50303.1.
    U37449 mRNA. Translation: AAC50304.1.
    U39613 mRNA. Translation: AAC50346.1.
    U40281 mRNA. Translation: AAC50352.1.
    U67319 mRNA. Translation: AAC51152.1.
    U67320 mRNA. Translation: AAC51153.1.
    U67206 mRNA. Translation: AAF21460.1.
    BT006683 mRNA. Translation: AAP35329.1.
    AB451281 mRNA. Translation: BAG70095.1.
    AB451413 mRNA. Translation: BAG70227.1.
    AK298964 mRNA. Translation: BAG61059.1.
    AL592546, AL627395 Genomic DNA. Translation: CAI12638.1.
    AL592546, AL627395 Genomic DNA. Translation: CAI12639.1.
    AL627395, AL592546 Genomic DNA. Translation: CAI16004.1.
    AL627395, AL592546 Genomic DNA. Translation: CAI16005.1.
    CH471066 Genomic DNA. Translation: EAW49494.1.
    CH471066 Genomic DNA. Translation: EAW49495.1.
    CH471066 Genomic DNA. Translation: EAW49498.1.
    CH471066 Genomic DNA. Translation: EAW49496.1.
    CH471066 Genomic DNA. Translation: EAW49497.1.
    BC015799 mRNA. Translation: AAH15799.1.
    CCDSiCCDS58096.1. [P55210-4]
    CCDS7580.1. [P55210-3]
    CCDS7581.1. [P55210-1]
    CCDS7582.1. [P55210-2]
    RefSeqiNP_001218.1. NM_001227.4. [P55210-1]
    NP_001253985.1. NM_001267056.1. [P55210-1]
    NP_001253986.1. NM_001267057.1.
    NP_001253987.1. NM_001267058.1. [P55210-4]
    NP_203124.1. NM_033338.5. [P55210-3]
    NP_203125.1. NM_033339.4. [P55210-1]
    NP_203126.1. NM_033340.3. [P55210-2]
    UniGeneiHs.9216.

    Genome annotation databases

    EnsembliENST00000345633; ENSP00000298701; ENSG00000165806. [P55210-1]
    ENST00000369315; ENSP00000358321; ENSG00000165806. [P55210-1]
    ENST00000369318; ENSP00000358324; ENSG00000165806. [P55210-1]
    ENST00000369321; ENSP00000358327; ENSG00000165806. [P55210-3]
    ENST00000369331; ENSP00000358337; ENSG00000165806. [P55210-2]
    ENST00000452490; ENSP00000398107; ENSG00000165806. [P55210-4]
    GeneIDi840.
    KEGGihsa:840.
    UCSCiuc001lam.4. human. [P55210-2]
    uc001lan.4. human. [P55210-1]
    uc001lao.4. human. [P55210-3]

    Polymorphism databases

    DMDMi1730092.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U37448 mRNA. Translation: AAC50303.1 .
    U37449 mRNA. Translation: AAC50304.1 .
    U39613 mRNA. Translation: AAC50346.1 .
    U40281 mRNA. Translation: AAC50352.1 .
    U67319 mRNA. Translation: AAC51152.1 .
    U67320 mRNA. Translation: AAC51153.1 .
    U67206 mRNA. Translation: AAF21460.1 .
    BT006683 mRNA. Translation: AAP35329.1 .
    AB451281 mRNA. Translation: BAG70095.1 .
    AB451413 mRNA. Translation: BAG70227.1 .
    AK298964 mRNA. Translation: BAG61059.1 .
    AL592546 , AL627395 Genomic DNA. Translation: CAI12638.1 .
    AL592546 , AL627395 Genomic DNA. Translation: CAI12639.1 .
    AL627395 , AL592546 Genomic DNA. Translation: CAI16004.1 .
    AL627395 , AL592546 Genomic DNA. Translation: CAI16005.1 .
    CH471066 Genomic DNA. Translation: EAW49494.1 .
    CH471066 Genomic DNA. Translation: EAW49495.1 .
    CH471066 Genomic DNA. Translation: EAW49498.1 .
    CH471066 Genomic DNA. Translation: EAW49496.1 .
    CH471066 Genomic DNA. Translation: EAW49497.1 .
    BC015799 mRNA. Translation: AAH15799.1 .
    CCDSi CCDS58096.1. [P55210-4 ]
    CCDS7580.1. [P55210-3 ]
    CCDS7581.1. [P55210-1 ]
    CCDS7582.1. [P55210-2 ]
    RefSeqi NP_001218.1. NM_001227.4. [P55210-1 ]
    NP_001253985.1. NM_001267056.1. [P55210-1 ]
    NP_001253986.1. NM_001267057.1.
    NP_001253987.1. NM_001267058.1. [P55210-4 ]
    NP_203124.1. NM_033338.5. [P55210-3 ]
    NP_203125.1. NM_033339.4. [P55210-1 ]
    NP_203126.1. NM_033340.3. [P55210-2 ]
    UniGenei Hs.9216.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1F1J X-ray 2.35 A/B 2-303 [» ]
    1GQF X-ray 2.90 A/B 47-303 [» ]
    1I4O X-ray 2.40 A/B 24-303 [» ]
    1I51 X-ray 2.45 A/C 51-198 [» ]
    B/D 199-303 [» ]
    1K86 X-ray 2.60 A/B 51-303 [» ]
    1K88 X-ray 2.70 A/B 51-303 [» ]
    1KMC X-ray 2.90 A/B 1-303 [» ]
    1MIA model - A 57-193 [» ]
    B 211-303 [» ]
    1SHJ X-ray 2.80 A/B 50-303 [» ]
    1SHL X-ray 3.00 A/B 57-303 [» ]
    2QL5 X-ray 2.34 A/C 24-196 [» ]
    B/D 207-303 [» ]
    2QL7 X-ray 2.40 A/C 24-196 [» ]
    B/D 207-303 [» ]
    2QL9 X-ray 2.14 A/C 24-196 [» ]
    B/D 207-303 [» ]
    2QLB X-ray 2.25 A/C 24-196 [» ]
    B/D 207-303 [» ]
    2QLF X-ray 2.80 A/C 24-196 [» ]
    B/D 207-303 [» ]
    2QLJ X-ray 2.60 A/C 24-196 [» ]
    B/D 207-303 [» ]
    3EDR X-ray 2.45 A/C 24-196 [» ]
    B/D 207-303 [» ]
    3H1P X-ray 2.61 A/B 50-303 [» ]
    3IBC X-ray 2.75 A/C 24-196 [» ]
    B/D 207-303 [» ]
    3IBF X-ray 2.50 A/C 24-196 [» ]
    B/D 207-303 [» ]
    3R5K X-ray 2.86 A/B 1-303 [» ]
    4FDL X-ray 2.80 A/B 2-303 [» ]
    4FEA X-ray 3.79 A/B 57-303 [» ]
    4HQ0 X-ray 3.00 A/B 47-303 [» ]
    4HQR X-ray 3.00 A/B 47-303 [» ]
    4JB8 X-ray 1.70 A 24-198 [» ]
    B 207-303 [» ]
    4JJ8 X-ray 2.94 A/B 57-303 [» ]
    4JR1 X-ray 2.15 A/B 57-303 [» ]
    4JR2 X-ray 1.65 A/B 57-303 [» ]
    ProteinModelPortali P55210.
    SMRi P55210. Positions 47-303.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107290. 46 interactions.
    DIPi DIP-29973N.
    IntActi P55210. 8 interactions.
    MINTi MINT-147084.
    STRINGi 9606.ENSP00000298700.

    Chemistry

    BindingDBi P55210.
    ChEMBLi CHEMBL3468.
    GuidetoPHARMACOLOGYi 1623.

    Protein family/group databases

    MEROPSi C14.004.

    PTM databases

    PhosphoSitei P55210.

    Polymorphism databases

    DMDMi 1730092.

    Proteomic databases

    MaxQBi P55210.
    PaxDbi P55210.
    PRIDEi P55210.

    Protocols and materials databases

    DNASUi 840.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000345633 ; ENSP00000298701 ; ENSG00000165806 . [P55210-1 ]
    ENST00000369315 ; ENSP00000358321 ; ENSG00000165806 . [P55210-1 ]
    ENST00000369318 ; ENSP00000358324 ; ENSG00000165806 . [P55210-1 ]
    ENST00000369321 ; ENSP00000358327 ; ENSG00000165806 . [P55210-3 ]
    ENST00000369331 ; ENSP00000358337 ; ENSG00000165806 . [P55210-2 ]
    ENST00000452490 ; ENSP00000398107 ; ENSG00000165806 . [P55210-4 ]
    GeneIDi 840.
    KEGGi hsa:840.
    UCSCi uc001lam.4. human. [P55210-2 ]
    uc001lan.4. human. [P55210-1 ]
    uc001lao.4. human. [P55210-3 ]

    Organism-specific databases

    CTDi 840.
    GeneCardsi GC10P115428.
    HGNCi HGNC:1508. CASP7.
    HPAi CAB025563.
    MIMi 601761. gene.
    neXtProti NX_P55210.
    PharmGKBi PA26091.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG279444.
    HOVERGENi HBG050802.
    InParanoidi P55210.
    KOi K04397.
    OMAi DANPRHK.
    PhylomeDBi P55210.
    TreeFami TF102023.

    Enzyme and pathway databases

    BRENDAi 3.4.22.60. 2681.
    Reactomei REACT_107. Apoptotic cleavage of cellular proteins.
    REACT_13541. Caspase-mediated cleavage of cytoskeletal proteins.
    REACT_607. Activation of caspases through apoptosome-mediated cleavage.

    Miscellaneous databases

    EvolutionaryTracei P55210.
    GeneWikii Caspase_7.
    GenomeRNAii 840.
    NextBioi 3500.
    PMAP-CutDB P55210.
    PROi P55210.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P55210.
    Bgeei P55210.
    CleanExi HS_CASP7.
    Genevestigatori P55210.

    Family and domain databases

    Gene3Di 3.40.50.1460. 1 hit.
    InterProi IPR029030. Caspase-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 PF00656. Peptidase_C14. 1 hit.
    [Graphical view ]
    PRINTSi PR00376. IL1BCENZYME.
    SMARTi SM00115. CASc. 1 hit.
    [Graphical view ]
    PROSITEi 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. "Mch3, a novel human apoptotic cysteine protease highly related to CPP32."
      Fernandes-Alnemri T., Takahashi A., Armstrong R.C., Krebs J., Fritz L.C., Tomaselli K.J., Wang L., Yu Z., Croce C.M., Salveson G., Earnshaw W.C., Litwack G., Alnemri E.S.
      Cancer Res. 55:6045-6052(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA AND BETA).
      Tissue: T-cell.
    2. "ICE-LAP3, a novel mammalian homologue of the Caenorhabditis elegans cell death protein Ced-3 is activated during Fas- and tumor necrosis factor-induced apoptosis."
      Duan H., Chinnaiyan A.M., Hudson P.L., Wing J.P., He W.-W., Dixit V.M.
      J. Biol. Chem. 271:1621-1625(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA).
    3. "Identification and characterization of CPP32/Mch2 homolog 1, a novel cysteine protease similar to CPP32."
      Lippke J.A., Gu Y., Sarnecki C., Caron P.R., Su M.S.-S.
      J. Biol. Chem. 271:1825-1828(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA).
      Tissue: Spleen.
    4. "Identification and mapping of Casp7, a cysteine protease resembling CPP32 beta, interleukin-1 beta converting enzyme, and CED-3."
      Juan T.S.-C., McNiece I.K., Argento J.M., Jenkins N.A., Gilbert D.J., Copeland N.G., Fletcher F.A.
      Genomics 40:86-93(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA AND ALPHA').
      Tissue: Fetal lung and Fetal spleen.
    5. "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 ALPHA), VARIANT GLU-4.
    6. "Human protein factory for converting the transcriptome into an in vitro-expressed proteome."
      Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R., Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y., Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.
      , Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S., Nomura N.
      Nat. Methods 5:1011-1017(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA').
    7. "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).
    8. "The DNA sequence and comparative analysis of human chromosome 10."
      Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
      , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
      Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    9. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    10. "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 ALPHA), VARIANT GLU-4.
      Tissue: Skin.
    11. "In vitro activation of CPP32 and Mch3 by Mch4, a novel human apoptotic cysteine protease containing two FADD-like domains."
      Fernandes-Alnemri T., Armstrong R.C., Krebs J.F., Srinivasula S.M., Wang L., Bullrich F., Fritz L.C., Trapani J.A., Tomaselli K.J., Litwack G., Alnemri E.S.
      Proc. Natl. Acad. Sci. U.S.A. 93:7464-7469(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEOLYTIC PROCESSING.
    12. "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.
    13. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "Crystal structure of a procaspase-7 zymogen: mechanisms of activation and substrate binding."
      Chai J., Wu Q., Shiozaki E., Srinivasula S.M., Alnemri E.S., Shi Y.
      Cell 107:399-407(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 51-303, SUBUNIT.

    Entry informationi

    Entry nameiCASP7_HUMAN
    AccessioniPrimary (citable) accession number: P55210
    Secondary accession number(s): B4DQU7
    , B5BU45, D3DRB8, Q13364, Q53YD5, Q5SVL0, Q5SVL3, Q96BA0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 157 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, Reference proteome

    Documents

    1. Human chromosome 10
      Human chromosome 10: 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