Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P42575

- CASP2_HUMAN

UniProt

P42575 - CASP2_HUMAN

Protein

Caspase-2

Gene

CASP2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 153 (01 Oct 2014)
      Sequence version 2 (06 Dec 2005)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Involved in the activation cascade of caspases responsible for apoptosis execution. Might function by either activating some proteins required for cell death or inactivating proteins necessary for cell survival.

    Catalytic activityi

    Strict requirement for an Asp residue at P1, with 316-asp being essential for proteolytic activity and has a preferred cleavage sequence of Val-Asp-Val-Ala-Asp-|-.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei277 – 2771By similarity
    Active sitei320 – 3201By similarity

    GO - Molecular functioni

    1. cysteine-type endopeptidase activity Source: UniProtKB
    2. cysteine-type endopeptidase activity involved in apoptotic process Source: Ensembl
    3. enzyme binding Source: UniProtKB
    4. protein binding Source: IntAct
    5. protein domain specific binding Source: BHF-UCL

    GO - Biological processi

    1. aging Source: Ensembl
    2. apoptotic process Source: UniProtKB
    3. apoptotic signaling pathway Source: UniProtKB
    4. brain development Source: Ensembl
    5. cellular response to mechanical stimulus Source: UniProtKB
    6. DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest Source: UniProtKB
    7. ectopic germ cell programmed cell death Source: Ensembl
    8. execution phase of apoptosis Source: UniProtKB
    9. extrinsic apoptotic signaling pathway in absence of ligand Source: RefGenome
    10. intrinsic apoptotic signaling pathway in response to DNA damage Source: UniProtKB
    11. luteolysis Source: Ensembl
    12. neural retina development Source: Ensembl
    13. neurotrophin TRK receptor signaling pathway Source: Reactome
    14. positive regulation of apoptotic process Source: UniProtKB
    15. positive regulation of apoptotic signaling pathway Source: Ensembl
    16. positive regulation of neuron apoptotic process Source: Ensembl
    17. protein processing Source: BHF-UCL
    18. regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: Reactome

    Keywords - Molecular functioni

    Hydrolase, Protease, Thiol protease

    Keywords - Biological processi

    Apoptosis

    Enzyme and pathway databases

    BRENDAi3.4.22.55. 2681.
    ReactomeiREACT_13526. NADE modulates death signalling.
    REACT_75776. NOD1/2 Signaling Pathway.

    Protein family/group databases

    MEROPSiC14.006.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Caspase-2 (EC:3.4.22.55)
    Short name:
    CASP-2
    Alternative name(s):
    Neural precursor cell expressed developmentally down-regulated protein 2
    Short name:
    NEDD-2
    Protease ICH-1
    Cleaved into the following 3 chains:
    Gene namesi
    Name:CASP2
    Synonyms:ICH1, NEDD2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 7

    Organism-specific databases

    HGNCiHGNC:1503. CASP2.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: RefGenome
    2. cytosol Source: Reactome
    3. membrane Source: Ensembl
    4. mitochondrion Source: Ensembl
    5. nucleus Source: UniProtKB

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi320 – 3201C → S: Loss of function.
    Mutagenesisi369 – 3691A → T: Loss of function.

    Organism-specific databases

    PharmGKBiPA26086.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Propeptidei2 – 169168PRO_0000004541Add
    BLAST
    Chaini170 – 325156Caspase-2 subunit p18PRO_0000004542Add
    BLAST
    Propeptidei326 – 3338PRO_0000004543
    Chaini334 – 452119Caspase-2 subunit p13PRO_0000004544Add
    BLAST
    Chaini348 – 452105Caspase-2 subunit p12PRO_0000004545Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine1 Publication
    Modified residuei340 – 3401Phosphoserine1 Publication

    Post-translational modificationi

    The mature protease can process its own propeptide, but not that of other caspases.1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein, Zymogen

    Proteomic databases

    MaxQBiP42575.
    PaxDbiP42575.
    PeptideAtlasiP42575.
    PRIDEiP42575.

    PTM databases

    PhosphoSiteiP42575.

    Miscellaneous databases

    PMAP-CutDBP42575.

    Expressioni

    Tissue specificityi

    Expressed at higher levels in the embryonic lung, liver and kidney than in the heart and brain. In adults, higher level expression is seen in the placenta, lung, kidney, and pancreas than in the heart, brain, liver and skeletal muscle.

    Gene expression databases

    ArrayExpressiP42575.
    BgeeiP42575.
    CleanExiHS_CASP2.
    GenevestigatoriP42575.

    Organism-specific databases

    HPAiCAB012175.

    Interactioni

    Subunit structurei

    Heterotetramer that consists of two anti-parallel arranged heterodimers, each one formed by a p18 subunit and a p12 subunit. Interacts with LRDD.3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CASP2P42575-12EBI-520342,EBI-520357
    CRADDP785609EBI-520342,EBI-520375
    PRKDCP785274EBI-520342,EBI-352053

    Protein-protein interaction databases

    BioGridi107285. 30 interactions.
    IntActiP42575. 9 interactions.
    MINTiMINT-150255.
    STRINGi9606.ENSP00000312664.

    Structurei

    Secondary structure

    1
    452
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi181 – 1877
    Helixi188 – 1903
    Beta strandi197 – 20610
    Beta strandi212 – 2143
    Helixi222 – 23514
    Beta strandi238 – 2458
    Helixi248 – 25912
    Helixi262 – 2654
    Beta strandi267 – 27610
    Beta strandi282 – 2843
    Beta strandi290 – 2923
    Helixi293 – 2997
    Turni302 – 3043
    Helixi306 – 3083
    Beta strandi313 – 3197
    Beta strandi321 – 3244
    Beta strandi363 – 3708
    Beta strandi377 – 3793
    Turni380 – 3823
    Helixi385 – 39713
    Turni398 – 4003
    Helixi403 – 41513
    Turni425 – 4284
    Beta strandi434 – 4374
    Beta strandi440 – 4423

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1PYOX-ray1.65A/C167-333[»]
    B/D348-452[»]
    2P2CX-ray3.24A/C/E/G/I/K167-333[»]
    B/D/F/H/J/L348-452[»]
    3R5JX-ray1.77A/C175-333[»]
    B/D349-452[»]
    3R6GX-ray2.07A/C175-333[»]
    B/D349-452[»]
    3R6LX-ray1.90A/C175-333[»]
    B/D349-452[»]
    3R7BX-ray1.80A/C175-333[»]
    B/D349-452[»]
    3R7NX-ray2.33A/C175-333[»]
    B/D349-452[»]
    3R7SX-ray2.25A/C175-333[»]
    B/D349-452[»]
    3RJMX-ray2.55A/C167-333[»]
    B/D348-452[»]
    ProteinModelPortaliP42575.
    SMRiP42575. Positions 173-452.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP42575.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini32 – 12190CARDPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiNOG305976.
    HOVERGENiHBG103962.
    InParanoidiP42575.
    KOiK02186.
    OMAiPCLQVKP.
    OrthoDBiEOG7TTQ7K.
    PhylomeDBiP42575.
    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 (3)i

    Sequence statusi: Complete.

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

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Note: Isoforms differ in the N- and C-termini.

    Isoform 1 (identifier: P42575-1) [UniParc]FASTAAdd to Basket

    Also known as: ICH-1L

    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

    MAAPSAGSWS TFQHKELMAA DRGRRILGVC GMHPHHQETL KKNRVVLAKQ    50
    LLLSELLEHL LEKDIITLEM RELIQAKVGS FSQNVELLNL LPKRGPQAFD 100
    AFCEALRETK QGHLEDMLLT TLSGLQHVLP PLSCDYDLSL PFPVCESCPL 150
    YKKLRLSTDT VEHSLDNKDG PVCLQVKPCT PEFYQTHFQL AYRLQSRPRG 200
    LALVLSNVHF TGEKELEFRS GGDVDHSTLV TLFKLLGYDV HVLCDQTAQE 250
    MQEKLQNFAQ LPAHRVTDSC IVALLSHGVE GAIYGVDGKL LQLQEVFQLF 300
    DNANCPSLQN KPKMFFIQAC RGDETDRGVD QQDGKNHAGS PGCEESDAGK 350
    EKLPKMRLPT RSDMICGYAC LKGTAAMRNT KRGSWYIEAL AQVFSERACD 400
    MHVADMLVKV NALIKDREGY APGTEFHRCK EMSEYCSTLC RHLYLFPGHP 450
    PT 452

    Note: Acts as a positive regulator of apoptosis.

    Length:452
    Mass (Da):50,685
    Last modified:December 6, 2005 - v2
    Checksum:i6EF0ED05EF808385
    GO
    Isoform 2 (identifier: P42575-2) [UniParc]FASTAAdd to Basket

    Also known as: ICH-1S

    The sequence of this isoform differs from the canonical sequence as follows:
         1-31: Missing.
         323-452: DETDRGVDQQ...LYLFPGHPPT → GGAIGSLGHLLLFTAATASLAL

    Note: Acts as a negative regulator of apoptosis.

    Show »
    Length:313
    Mass (Da):34,923
    Checksum:iFA1E307A41B8299E
    GO
    Isoform 3 (identifier: P42575-3) [UniParc]FASTAAdd to Basket

    Also known as: Casp-2L-Pro

    The sequence of this isoform differs from the canonical sequence as follows:
         1-17: Missing.
         107-108: RE → HS
         109-452: Missing.

    Note: May function as an endogenous apoptosis inhibitor that antagonizes caspase activation and cell death.

    Show »
    Length:91
    Mass (Da):10,309
    Checksum:iE80E3D9233686A98
    GO

    Sequence cautioni

    The sequence AAA58959.1 differs from that shown. Reason: Erroneous initiation.
    The sequence AAO25653.1 differs from that shown. Reason: Erroneous initiation.
    The sequence AAP22346.1 differs from that shown. Reason: Erroneous initiation.
    The sequence AAP22349.1 differs from that shown. Reason: Erroneous initiation.
    The sequence BAD92877.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti309 – 32214QNKPK…QACRG → EEVTSLSILSAFVT in BAD92877. 1 PublicationCuratedAdd
    BLAST

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti105 – 1051A → G.
    Corresponds to variant rs4647298 [ dbSNP | Ensembl ].
    VAR_055621
    Natural varianti172 – 1721V → L.3 Publications
    Corresponds to variant rs4647297 [ dbSNP | Ensembl ].
    VAR_016334
    Natural varianti178 – 1781P → A.1 Publication
    Corresponds to variant rs4647298 [ dbSNP | Ensembl ].
    VAR_016335
    Natural varianti441 – 4411R → G.1 Publication
    Corresponds to variant rs4647338 [ dbSNP | Ensembl ].
    VAR_016336

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 3131Missing in isoform 2. 2 PublicationsVSP_000801Add
    BLAST
    Alternative sequencei1 – 1717Missing in isoform 3. 1 PublicationVSP_046280Add
    BLAST
    Alternative sequencei107 – 1082RE → HS in isoform 3. 1 PublicationVSP_046281
    Alternative sequencei109 – 452344Missing in isoform 3. 1 PublicationVSP_046282Add
    BLAST
    Alternative sequencei323 – 452130DETDR…GHPPT → GGAIGSLGHLLLFTAATASL AL in isoform 2. 2 PublicationsVSP_000802Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U13021 mRNA. Translation: AAA58959.1. Different initiation.
    U13022 mRNA. Translation: AAA58960.1.
    AF314174 mRNA. Translation: AAK00299.1.
    AF314175 mRNA. Translation: AAK00300.1.
    CR541748 mRNA. Translation: CAG46548.1.
    AK291274 mRNA. Translation: BAF83963.1.
    AY219042 Genomic DNA. Translation: AAO25653.1. Different initiation.
    AC073342 Genomic DNA. Translation: AAP22346.1. Different initiation.
    AC073342 Genomic DNA. Translation: AAP22347.1.
    AC073342 Genomic DNA. Translation: AAP22348.1.
    AC073342 Genomic DNA. Translation: AAP22349.1. Different initiation.
    CH471198 Genomic DNA. Translation: EAW51863.1.
    CH471198 Genomic DNA. Translation: EAW51867.1.
    CH471198 Genomic DNA. Translation: EAW51870.1.
    BC002427 mRNA. Translation: AAH02427.2.
    BT007240 mRNA. Translation: AAP35904.1.
    AB209640 mRNA. Translation: BAD92877.1. Different initiation.
    CCDSiCCDS5879.1. [P42575-1]
    PIRiA54821.
    RefSeqiNP_001215.1. NM_001224.4.
    NP_116764.2. NM_032982.3. [P42575-1]
    NP_116765.2. NM_032983.3.
    UniGeneiHs.368982.

    Genome annotation databases

    EnsembliENST00000310447; ENSP00000312664; ENSG00000106144. [P42575-1]
    GeneIDi835.
    KEGGihsa:835.
    UCSCiuc003wco.3. human. [P42575-1]

    Polymorphism databases

    DMDMi83300977.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U13021 mRNA. Translation: AAA58959.1 . Different initiation.
    U13022 mRNA. Translation: AAA58960.1 .
    AF314174 mRNA. Translation: AAK00299.1 .
    AF314175 mRNA. Translation: AAK00300.1 .
    CR541748 mRNA. Translation: CAG46548.1 .
    AK291274 mRNA. Translation: BAF83963.1 .
    AY219042 Genomic DNA. Translation: AAO25653.1 . Different initiation.
    AC073342 Genomic DNA. Translation: AAP22346.1 . Different initiation.
    AC073342 Genomic DNA. Translation: AAP22347.1 .
    AC073342 Genomic DNA. Translation: AAP22348.1 .
    AC073342 Genomic DNA. Translation: AAP22349.1 . Different initiation.
    CH471198 Genomic DNA. Translation: EAW51863.1 .
    CH471198 Genomic DNA. Translation: EAW51867.1 .
    CH471198 Genomic DNA. Translation: EAW51870.1 .
    BC002427 mRNA. Translation: AAH02427.2 .
    BT007240 mRNA. Translation: AAP35904.1 .
    AB209640 mRNA. Translation: BAD92877.1 . Different initiation.
    CCDSi CCDS5879.1. [P42575-1 ]
    PIRi A54821.
    RefSeqi NP_001215.1. NM_001224.4.
    NP_116764.2. NM_032982.3. [P42575-1 ]
    NP_116765.2. NM_032983.3.
    UniGenei Hs.368982.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1PYO X-ray 1.65 A/C 167-333 [» ]
    B/D 348-452 [» ]
    2P2C X-ray 3.24 A/C/E/G/I/K 167-333 [» ]
    B/D/F/H/J/L 348-452 [» ]
    3R5J X-ray 1.77 A/C 175-333 [» ]
    B/D 349-452 [» ]
    3R6G X-ray 2.07 A/C 175-333 [» ]
    B/D 349-452 [» ]
    3R6L X-ray 1.90 A/C 175-333 [» ]
    B/D 349-452 [» ]
    3R7B X-ray 1.80 A/C 175-333 [» ]
    B/D 349-452 [» ]
    3R7N X-ray 2.33 A/C 175-333 [» ]
    B/D 349-452 [» ]
    3R7S X-ray 2.25 A/C 175-333 [» ]
    B/D 349-452 [» ]
    3RJM X-ray 2.55 A/C 167-333 [» ]
    B/D 348-452 [» ]
    ProteinModelPortali P42575.
    SMRi P42575. Positions 173-452.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107285. 30 interactions.
    IntActi P42575. 9 interactions.
    MINTi MINT-150255.
    STRINGi 9606.ENSP00000312664.

    Chemistry

    BindingDBi P42575.
    ChEMBLi CHEMBL4884.
    GuidetoPHARMACOLOGYi 1618.

    Protein family/group databases

    MEROPSi C14.006.

    PTM databases

    PhosphoSitei P42575.

    Polymorphism databases

    DMDMi 83300977.

    Proteomic databases

    MaxQBi P42575.
    PaxDbi P42575.
    PeptideAtlasi P42575.
    PRIDEi P42575.

    Protocols and materials databases

    DNASUi 835.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000310447 ; ENSP00000312664 ; ENSG00000106144 . [P42575-1 ]
    GeneIDi 835.
    KEGGi hsa:835.
    UCSCi uc003wco.3. human. [P42575-1 ]

    Organism-specific databases

    CTDi 835.
    GeneCardsi GC07P142985.
    HGNCi HGNC:1503. CASP2.
    HPAi CAB012175.
    MIMi 600639. gene.
    neXtProti NX_P42575.
    PharmGKBi PA26086.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG305976.
    HOVERGENi HBG103962.
    InParanoidi P42575.
    KOi K02186.
    OMAi PCLQVKP.
    OrthoDBi EOG7TTQ7K.
    PhylomeDBi P42575.
    TreeFami TF102023.

    Enzyme and pathway databases

    BRENDAi 3.4.22.55. 2681.
    Reactomei REACT_13526. NADE modulates death signalling.
    REACT_75776. NOD1/2 Signaling Pathway.

    Miscellaneous databases

    EvolutionaryTracei P42575.
    GeneWikii Caspase_2.
    GenomeRNAii 835.
    NextBioi 3472.
    PMAP-CutDB P42575.
    PROi P42575.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P42575.
    Bgeei P42575.
    CleanExi HS_CASP2.
    Genevestigatori P42575.

    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. "Ich-1, an Ice/ced-3-related gene, encodes both positive and negative regulators of programmed cell death."
      Wang L., Miura M., Bergeron L., Zhu H., Yuan J.
      Cell 78:739-750(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE [MRNA] OF 14-452 (ISOFORM 1).
      Tissue: Fetal brain.
    2. "Identification of a caspase-2 isoform that behaves as an endogenous inhibitor of the caspase cascade."
      Droin N., Beauchemin M., Solary E., Bertrand R.
      Cancer Res. 60:7039-7047(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), NUCLEOTIDE SEQUENCE [MRNA] OF 32-108 (ISOFORMS 1/2), ALTERNATIVE SPLICING.
    3. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    4. "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 1).
    5. NIEHS SNPs program
      Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS LEU-172; ALA-178 AND GLY-441.
    6. "The DNA sequence of human chromosome 7."
      Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
      , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
      Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "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), VARIANT LEU-172.
      Tissue: Skin.
    9. "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] OF 18-452 (ISOFORM 1), VARIANT LEU-172.
    10. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
      Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 194-452.
      Tissue: Spleen.
    11. "The Caenorhabditis elegans cell-death protein CED-3 is a cysteine protease with substrate specificities similar to those of the human CPP32 protease."
      Xue D., Shaham S., Horvitz H.R.
      Genes Dev. 10:1073-1083(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: CLEAVAGE SITES.
    12. "The PIDDosome, a protein complex implicated in activation of caspase-2 in response to genotoxic stress."
      Tinel A., Tschopp J.
      Science 304:843-846(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH LRDD.
    13. "Functional connection between p53 and caspase-2 is essential for apoptosis induced by DNA damage."
      Vakifahmetoglu H., Olsson M., Orrenius S., Zhivotovsky B.
      Oncogene 25:5683-5692(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH LRDD.
    14. "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].
    15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-340, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "Crystal structure of caspase-2, apical initiator of the intrinsic apoptotic pathway."
      Schweizer A., Briand C., Grutter M.G.
      J. Biol. Chem. 278:42441-42447(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 167-452 IN COMPLEX WITH INHIBITOR, SUBUNIT, DISULFIDE BOND.

    Entry informationi

    Entry nameiCASP2_HUMAN
    AccessioniPrimary (citable) accession number: P42575
    Secondary accession number(s): A8K5F9
    , D3DXD6, E9PDN0, P42576, Q59F21, Q7KZL6, Q86UJ3, Q9BUP7, Q9BZK9, Q9BZL0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: December 6, 2005
    Last modified: October 1, 2014
    This is version 153 of the entry and version 2 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 7
      Human chromosome 7: 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