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O88879

- APAF_MOUSE

UniProt

O88879 - APAF_MOUSE

Protein

Apoptotic protease-activating factor 1

Gene

Apaf1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 127 (01 Oct 2014)
      Sequence version 3 (27 Jul 2011)
      Previous versions | rss
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    Functioni

    Oligomeric Apaf-1 mediates the cytochrome c-dependent autocatalytic activation of pro-caspase 9 (Apaf-3), leading to the activation of caspase-3 and apoptosis. This activation requires ATP By similarity.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei265 – 2651ATP

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi154 – 1618ATPSequence Analysis

    GO - Molecular functioni

    1. ADP binding Source: InterPro
    2. ATP binding Source: UniProtKB-KW
    3. cysteine-type endopeptidase activator activity involved in apoptotic process Source: MGI
    4. identical protein binding Source: MGI

    GO - Biological processi

    1. activation of cysteine-type endopeptidase activity involved in apoptotic process Source: MGI
    2. activation of cysteine-type endopeptidase activity involved in apoptotic process by cytochrome c Source: RefGenome
    3. brain development Source: MGI
    4. defense response Source: InterPro
    5. forebrain development Source: MGI
    6. multicellular organismal development Source: MGI
    7. neural tube closure Source: MGI
    8. neuron apoptotic process Source: MGI
    9. positive regulation of apoptotic signaling pathway Source: MGI
    10. regulation of apoptotic DNA fragmentation Source: MGI

    Keywords - Biological processi

    Apoptosis

    Keywords - Ligandi

    ATP-binding, Calcium, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_206522. Formation of apoptosome.
    REACT_225157. Activation of caspases through apoptosome-mediated cleavage.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Apoptotic protease-activating factor 1
    Short name:
    APAF-1
    Gene namesi
    Name:Apaf1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 10

    Organism-specific databases

    MGIiMGI:1306796. Apaf1.

    Subcellular locationi

    Cytoplasm By similarity

    GO - Cellular componenti

    1. apoptosome Source: RefGenome
    2. cytosol Source: MGI
    3. Golgi apparatus Source: Ensembl
    4. nucleus Source: MGI

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi265 – 2651R → S: No stimulation of CASP9 activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 12491249Apoptotic protease-activating factor 1PRO_0000050845Add
    BLAST

    Proteomic databases

    MaxQBiO88879.
    PaxDbiO88879.
    PRIDEiO88879.

    PTM databases

    PhosphoSiteiO88879.

    Expressioni

    Tissue specificityi

    Highly expressed in lung and spleen, weakly in brain and kidney and not detectable in liver.

    Developmental stagei

    High levels in embryonic brain and liver from E11.5 to E17.5 day.

    Gene expression databases

    ArrayExpressiO88879.
    BgeeiO88879.
    CleanExiMM_APAF1.
    GenevestigatoriO88879.

    Interactioni

    Subunit structurei

    Monomer. Oligomerizes to a heptameric ring, known as the apoptosome, upon binding of cytochrome c and dATP. Oligomeric Apaf-1 and pro-caspase-9 bind to each other via their respective NH2-terminal CARD domains and consecutively mature caspase-9 is released from the complex By similarity. Interacts with UACA. It may also interact with Bcl-XL. Interacts with APIP. Interacts (via CARD and NACHT domains) with NAIP/BIRC1 (via NACHT domain) By similarity.By similarity

    Protein-protein interaction databases

    BioGridi198139. 1 interaction.
    IntActiO88879. 1 interaction.
    MINTiMINT-104429.

    Structurei

    Secondary structure

    1
    1249
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi109 – 1168
    Helixi130 – 14112
    Turni142 – 1454
    Beta strandi148 – 1536
    Helixi160 – 1678
    Helixi171 – 1744
    Turni175 – 1773
    Beta strandi182 – 1865
    Helixi192 – 20615
    Turni207 – 2093
    Helixi220 – 23011
    Beta strandi232 – 2354
    Beta strandi239 – 2446
    Helixi248 – 2514
    Beta strandi259 – 2668
    Turni267 – 2726
    Helixi288 – 29912
    Helixi309 – 3168
    Turni317 – 3193
    Helixi321 – 33313
    Beta strandi334 – 3363
    Helixi338 – 3469
    Helixi361 – 37313
    Turni377 – 3793
    Helixi380 – 3856
    Helixi386 – 3883
    Helixi397 – 4048
    Helixi408 – 42013
    Beta strandi425 – 43612
    Helixi439 – 44810
    Helixi450 – 4523
    Helixi453 – 46513
    Turni470 – 4723
    Helixi480 – 49314
    Helixi497 – 5048
    Helixi507 – 51711
    Helixi520 – 5289
    Turni529 – 5324
    Helixi540 – 55213
    Turni553 – 5564
    Beta strandi557 – 5593
    Helixi563 – 5686
    Helixi575 – 58511
    Beta strandi589 – 5913
    Helixi598 – 6003
    Beta strandi608 – 6114
    Beta strandi618 – 6236
    Beta strandi627 – 6348
    Beta strandi639 – 6435
    Turni644 – 6463
    Beta strandi649 – 6535
    Beta strandi660 – 6656
    Beta strandi669 – 6768
    Beta strandi679 – 6857
    Turni686 – 6883
    Beta strandi691 – 6966
    Beta strandi702 – 7076
    Beta strandi709 – 7124
    Beta strandi715 – 7206
    Beta strandi725 – 7295
    Beta strandi732 – 7398
    Beta strandi746 – 7516
    Beta strandi757 – 77115
    Helixi772 – 7743
    Beta strandi777 – 7826
    Beta strandi810 – 8178
    Beta strandi820 – 8256
    Turni826 – 8283
    Beta strandi831 – 8366
    Beta strandi838 – 8414
    Beta strandi845 – 8484
    Beta strandi854 – 8585
    Beta strandi860 – 8623
    Beta strandi864 – 8685
    Turni869 – 8724
    Beta strandi873 – 8786
    Beta strandi885 – 8906
    Beta strandi894 – 9018
    Beta strandi906 – 9105
    Helixi911 – 9155
    Beta strandi919 – 93113
    Beta strandi934 – 95320
    Beta strandi956 – 9594
    Beta strandi964 – 9696
    Beta strandi973 – 9808
    Beta strandi986 – 9894
    Turni990 – 9923
    Beta strandi996 – 9983
    Beta strandi1009 – 10113
    Beta strandi1013 – 10164
    Beta strandi1018 – 10214
    Beta strandi1023 – 10308
    Turni1032 – 10343
    Beta strandi1047 – 10526
    Beta strandi1054 – 107118
    Turni1072 – 10754
    Beta strandi1079 – 10824
    Beta strandi1091 – 10933
    Beta strandi1095 – 10995
    Beta strandi1101 – 11033
    Beta strandi1114 – 11185
    Beta strandi1130 – 11356
    Beta strandi1137 – 114610
    Beta strandi1153 – 11597
    Beta strandi1183 – 11864
    Beta strandi1193 – 120311
    Beta strandi1205 – 12073
    Beta strandi1228 – 12303
    Beta strandi1233 – 12364
    Beta strandi1242 – 12454

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3SFZX-ray3.00A1-1249[»]
    3SHFX-ray3.55A1-1249[»]
    ProteinModelPortaliO88879.
    SMRiO88879. Positions 1-586.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 9090CARDPROSITE-ProRule annotationAdd
    BLAST
    Domaini106 – 415310NB-ARCAdd
    BLAST
    Repeati613 – 65240WD 1-11 PublicationPROSITE-ProRule annotationAdd
    BLAST
    Repeati655 – 69440WD 1-21 PublicationPROSITE-ProRule annotationAdd
    BLAST
    Repeati697 – 73842WD 1-31 PublicationPROSITE-ProRule annotationAdd
    BLAST
    Repeati741 – 78040WD 1-41 PublicationPROSITE-ProRule annotationAdd
    BLAST
    Repeati796 – 83742WD 1-51 PublicationPROSITE-ProRule annotationAdd
    BLAST
    Repeati838 – 87740WD 1-61 PublicationPROSITE-ProRule annotationAdd
    BLAST
    Repeati880 – 91031WD 1-71 PublicationPROSITE-ProRule annotationAdd
    BLAST
    Repeati922 – 95837WD 2-11 PublicationPROSITE-ProRule annotationAdd
    BLAST
    Repeati959 – 99840WD 2-21 PublicationPROSITE-ProRule annotationAdd
    BLAST
    Repeati1001 – 104040WD 2-31 PublicationPROSITE-ProRule annotationAdd
    BLAST
    Repeati1042 – 108039WD 2-41 PublicationPROSITE-ProRule annotationAdd
    BLAST
    Repeati1083 – 112240WD 2-51 PublicationPROSITE-ProRule annotationAdd
    BLAST
    Repeati1125 – 116440WD 2-61 PublicationPROSITE-ProRule annotationAdd
    BLAST
    Repeati1176 – 121338WD 2-71 PublicationPROSITE-ProRule annotationAdd
    BLAST
    Repeati1214 – 124936WD 2-81 PublicationPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni910 – 92112Interpropeller linkerAdd
    BLAST

    Domaini

    The CARD domain mediates interaction with APIP.1 Publication
    The monomeric form is autoinhibited in a closed conformation through a bound ADP at the nucleotide binding site. Exchange of ADP for ATP and binding of cytochrome c trigger a large conformational change where the first WD repeat region swings out, allowing the NB-ARC domain to rotate and expose the contact areas for oligomerization.1 Publication

    Sequence similaritiesi

    Contains 1 CARD domain.PROSITE-ProRule annotation
    Contains 1 NB-ARC domain.Curated
    Contains 15 WD repeats.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, WD repeat

    Phylogenomic databases

    eggNOGiCOG2319.
    GeneTreeiENSGT00750000117677.
    HOVERGENiHBG018730.
    InParanoidiA2RRK8.
    KOiK02084.
    OMAiETKKVCK.
    OrthoDBiEOG7XWPMS.
    PhylomeDBiO88879.
    TreeFamiTF323866.

    Family and domain databases

    Gene3Di1.10.533.10. 1 hit.
    2.130.10.10. 2 hits.
    3.40.50.300. 1 hit.
    InterProiIPR017251. Apoptotic_pept-activating_1.
    IPR001315. CARD.
    IPR011029. DEATH-like_dom.
    IPR000767. Disease_R.
    IPR020472. G-protein_beta_WD-40_rep.
    IPR002182. NB-ARC.
    IPR027417. P-loop_NTPase.
    IPR015943. WD40/YVTN_repeat-like_dom.
    IPR001680. WD40_repeat.
    IPR019775. WD40_repeat_CS.
    IPR017986. WD40_repeat_dom.
    [Graphical view]
    PfamiPF00619. CARD. 1 hit.
    PF00931. NB-ARC. 1 hit.
    PF00400. WD40. 10 hits.
    [Graphical view]
    PIRSFiPIRSF037646. Apop_pept_activating-1. 1 hit.
    PRINTSiPR00364. DISEASERSIST.
    PR00320. GPROTEINBRPT.
    SMARTiSM00320. WD40. 13 hits.
    [Graphical view]
    SUPFAMiSSF47986. SSF47986. 1 hit.
    SSF50978. SSF50978. 2 hits.
    SSF52540. SSF52540. 1 hit.
    PROSITEiPS50209. CARD. 1 hit.
    PS00678. WD_REPEATS_1. 4 hits.
    PS50082. WD_REPEATS_2. 9 hits.
    PS50294. WD_REPEATS_REGION. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O88879-1) [UniParc]FASTAAdd to Basket

    Also known as: Apaf-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

    MDAKARNCLL QHREALEKDI KTSYIMDHMI SNGVLSVIEE EKVKSQATQY     50
    QRAAALIKMI LNKDNCAYIS FYNALLHEGY KDLAALLQSG LPLVSSSSGK 100
    DTDGGITSFV RTVLCEGGVP QRPVIFVTRK KLVHAIQQKL WKLNGEPGWV 150
    TIYGMAGCGK SVLAAEAVRD HSLLEGCFSG GVHWVSIGKQ DKSGLLMKLQ 200
    NLCMRLDQEE SFSQRLPLNI EEAKDRLRVL MLRKHPRSLL ILDDVWDPWV 250
    LKAFDNQCQI LLTTRDKSVT DSVMGPKHVV PVESGLGREK GLEILSLFVN 300
    MKKEDLPAEA HSIIKECKGS PLVVSLIGAL LRDFPNRWAY YLRQLQNKQF 350
    KRIRKSSSYD YEALDEAMSI SVEMLREDIK DYYTDLSILQ KDVKVPTKVL 400
    CVLWDLETEE VEDILQEFVN KSLLFCNRNG KSFCYYLHDL QVDFLTEKNR 450
    SQLQDLHRKM VTQFQRYYQP HTLSPDQEDC MYWYNFLAYH MASANMHKEL 500
    CALMFSLDWI KAKTELVGPA HLIHEFVAYR HILDEKDCAV CENFQEFLSL 550
    NGHLLGRQPF PNIVQLGLCE PETSEVYRQA KLQAKQEGDT GRLYLEWINK 600
    KTIKNLSRLV VRPHTDAVYH ACFSQDGQRI ASCGADKTLQ VFKAETGEKL 650
    LDIKAHEDEV LCCAFSSDDS YIATCSADKK VKIWDSATGK LVHTYDEHSE 700
    QVNCCHFTNK SNHLLLATGS NDFFLKLWDL NQKECRNTMF GHTNSVNHCR 750
    FSPDDELLAS CSADGTLRLW DVRSANERKS INVKRFFLSS EDPPEDVEVI 800
    VKCCSWSADG DKIIVAAKNK VLLFDIHTSG LLAEIHTGHH STIQYCDFSP 850
    YDHLAVIALS QYCVELWNID SRLKVADCRG HLSWVHGVMF SPDGSSFLTA 900
    SDDQTIRVWE TKKVCKNSAI VLKQEIDVVF QENETMVLAV DNIRGLQLIA 950
    GKTGQIDYLP EAQVSCCCLS PHLEYVAFGD EDGAIKIIEL PNNRVFSSGV 1000
    GHKKAVRHIQ FTADGKTLIS SSEDSVIQVW NWQTGDYVFL QAHQETVKDF 1050
    RLLQDSRLLS WSFDGTVKVW NVITGRIERD FTCHQGTVLS CAISSDATKF 1100
    SSTSADKTAK IWSFDLLSPL HELKGHNGCV RCSAFSLDGI LLATGDDNGE 1150
    IRIWNVSDGQ LLHSCAPISV EEGTATHGGW VTDVCFSPDS KTLVSAGGYL 1200
    KWWNVATGDS SQTFYTNGTN LKKIHVSPDF RTYVTVDNLG ILYILQVLE 1249

    Note: Major isoform.

    Length:1,249
    Mass (Da):141,003
    Last modified:July 27, 2011 - v3
    Checksum:iAA639E407F9ABC24
    GO
    Isoform 2 (identifier: O88879-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         99-110: GKDTDGGITSFV → A

    Show »
    Length:1,238
    Mass (Da):139,896
    Checksum:iCC9BE41A95B20ADF
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti209 – 2091E → D in AAC62458. (PubMed:9753320)Curated
    Sequence conflicti592 – 5921R → P in AAC62458. (PubMed:9753320)Curated
    Sequence conflicti710 – 7101K → S in AAC62458. (PubMed:9753320)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei99 – 11012GKDTD…ITSFV → A in isoform 2. 1 PublicationVSP_006763Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF064071 mRNA. Translation: AAC62458.1.
    BC131683 mRNA. Translation: AAI31684.1.
    BC131684 mRNA. Translation: AAI31685.1.
    CCDSiCCDS36030.1. [O88879-1]
    CCDS70095.1. [O88879-2]
    RefSeqiNP_001036023.1. NM_001042558.1. [O88879-1]
    NP_033814.2. NM_009684.2. [O88879-1]
    UniGeneiMm.220289.

    Genome annotation databases

    EnsembliENSMUST00000020157; ENSMUSP00000020157; ENSMUSG00000019979. [O88879-1]
    ENSMUST00000159110; ENSMUSP00000125291; ENSMUSG00000019979. [O88879-1]
    GeneIDi11783.
    KEGGimmu:11783.
    UCSCiuc007gtg.1. mouse. [O88879-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF064071 mRNA. Translation: AAC62458.1 .
    BC131683 mRNA. Translation: AAI31684.1 .
    BC131684 mRNA. Translation: AAI31685.1 .
    CCDSi CCDS36030.1. [O88879-1 ]
    CCDS70095.1. [O88879-2 ]
    RefSeqi NP_001036023.1. NM_001042558.1. [O88879-1 ]
    NP_033814.2. NM_009684.2. [O88879-1 ]
    UniGenei Mm.220289.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3SFZ X-ray 3.00 A 1-1249 [» ]
    3SHF X-ray 3.55 A 1-1249 [» ]
    ProteinModelPortali O88879.
    SMRi O88879. Positions 1-586.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 198139. 1 interaction.
    IntActi O88879. 1 interaction.
    MINTi MINT-104429.

    PTM databases

    PhosphoSitei O88879.

    Proteomic databases

    MaxQBi O88879.
    PaxDbi O88879.
    PRIDEi O88879.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000020157 ; ENSMUSP00000020157 ; ENSMUSG00000019979 . [O88879-1 ]
    ENSMUST00000159110 ; ENSMUSP00000125291 ; ENSMUSG00000019979 . [O88879-1 ]
    GeneIDi 11783.
    KEGGi mmu:11783.
    UCSCi uc007gtg.1. mouse. [O88879-1 ]

    Organism-specific databases

    CTDi 317.
    MGIi MGI:1306796. Apaf1.

    Phylogenomic databases

    eggNOGi COG2319.
    GeneTreei ENSGT00750000117677.
    HOVERGENi HBG018730.
    InParanoidi A2RRK8.
    KOi K02084.
    OMAi ETKKVCK.
    OrthoDBi EOG7XWPMS.
    PhylomeDBi O88879.
    TreeFami TF323866.

    Enzyme and pathway databases

    Reactomei REACT_206522. Formation of apoptosome.
    REACT_225157. Activation of caspases through apoptosome-mediated cleavage.

    Miscellaneous databases

    ChiTaRSi APAF1. mouse.
    NextBioi 279591.
    PROi O88879.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O88879.
    Bgeei O88879.
    CleanExi MM_APAF1.
    Genevestigatori O88879.

    Family and domain databases

    Gene3Di 1.10.533.10. 1 hit.
    2.130.10.10. 2 hits.
    3.40.50.300. 1 hit.
    InterProi IPR017251. Apoptotic_pept-activating_1.
    IPR001315. CARD.
    IPR011029. DEATH-like_dom.
    IPR000767. Disease_R.
    IPR020472. G-protein_beta_WD-40_rep.
    IPR002182. NB-ARC.
    IPR027417. P-loop_NTPase.
    IPR015943. WD40/YVTN_repeat-like_dom.
    IPR001680. WD40_repeat.
    IPR019775. WD40_repeat_CS.
    IPR017986. WD40_repeat_dom.
    [Graphical view ]
    Pfami PF00619. CARD. 1 hit.
    PF00931. NB-ARC. 1 hit.
    PF00400. WD40. 10 hits.
    [Graphical view ]
    PIRSFi PIRSF037646. Apop_pept_activating-1. 1 hit.
    PRINTSi PR00364. DISEASERSIST.
    PR00320. GPROTEINBRPT.
    SMARTi SM00320. WD40. 13 hits.
    [Graphical view ]
    SUPFAMi SSF47986. SSF47986. 1 hit.
    SSF50978. SSF50978. 2 hits.
    SSF52540. SSF52540. 1 hit.
    PROSITEi PS50209. CARD. 1 hit.
    PS00678. WD_REPEATS_1. 4 hits.
    PS50082. WD_REPEATS_2. 9 hits.
    PS50294. WD_REPEATS_REGION. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Apaf1 (CED-4 homolog) regulates programmed cell death in mammalian development."
      Cecconi F., Alvarez-Bolado G., Meyer B.I., Roth K.A., Gruss P.
      Cell 94:727-737(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Strain: Swiss Webster / NIH.
      Tissue: Embryo.
    2. "A comparison of the expression and properties of Apaf-1 and Apaf-1L."
      Walke D.W., Morgan J.I.
      Brain Res. 886:73-81(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
      Tissue: Spleen.
    3. "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).
    4. "Induced inhibition of ischemic/hypoxic injury by APIP, a novel Apaf-1-interacting protein."
      Cho D.-H., Hong Y.-M., Lee H.-J., Woo H.-N., Pyo J.-O., Mak T.W., Jung Y.-K.
      J. Biol. Chem. 279:39942-39950(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH APIP, DOMAIN.
    5. "Nucling recruits Apaf-1/pro-caspase-9 complex for the induction of stress-induced apoptosis."
      Sakai T., Liu L., Teng X., Mukai-Sakai R., Shimada H., Kaji R., Mitani T., Matsumoto M., Toida K., Ishimura K., Shishido Y., Mak T.W., Fukui K.
      J. Biol. Chem. 279:41131-41140(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH UACA.
    6. "Crystal structure of full-length Apaf-1: how the death signal is relayed in the mitochondrial pathway of apoptosis."
      Reubold T.F., Wohlgemuth S., Eschenburg S.
      Structure 19:1074-1083(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS), WD REPEATS, SUBUNIT, MUTAGENESIS OF ARG-265.

    Entry informationi

    Entry nameiAPAF_MOUSE
    AccessioniPrimary (citable) accession number: O88879
    Secondary accession number(s): A2RRK8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 23, 2002
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 127 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Physiological concentrations of calcium ions negatively affect the assembly of apoptosome by inhibiting nucleotide exchange in the monomeric form.By similarity

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3