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O88879

- APAF_MOUSE

UniProt

O88879 - APAF_MOUSE

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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

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. forebrain development Source: MGI
  5. multicellular organismal development Source: MGI
  6. neural tube closure Source: MGI
  7. neuron apoptotic process Source: MGI
  8. positive regulation of apoptotic signaling pathway Source: MGI
  9. regulation of apoptotic DNA fragmentation Source: MGI
Complete GO annotation...

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. extracellular vesicular exosome Source: Ensembl
  4. nucleus Source: MGI
Complete GO annotation...

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

BgeeiO88879.
CleanExiMM_APAF1.
ExpressionAtlasiO88879. baseline and differential.
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 – 1168Combined sources
Helixi130 – 14112Combined sources
Turni142 – 1454Combined sources
Beta strandi148 – 1536Combined sources
Helixi160 – 1678Combined sources
Helixi171 – 1744Combined sources
Turni175 – 1773Combined sources
Beta strandi182 – 1865Combined sources
Helixi192 – 20615Combined sources
Turni207 – 2093Combined sources
Helixi220 – 23011Combined sources
Beta strandi232 – 2354Combined sources
Beta strandi239 – 2446Combined sources
Helixi248 – 2514Combined sources
Beta strandi259 – 2668Combined sources
Turni267 – 2726Combined sources
Helixi288 – 29912Combined sources
Helixi309 – 3168Combined sources
Turni317 – 3193Combined sources
Helixi321 – 33313Combined sources
Beta strandi334 – 3363Combined sources
Helixi338 – 3469Combined sources
Helixi361 – 37313Combined sources
Turni377 – 3793Combined sources
Helixi380 – 3856Combined sources
Helixi386 – 3883Combined sources
Helixi397 – 4048Combined sources
Helixi408 – 42013Combined sources
Beta strandi425 – 43612Combined sources
Helixi439 – 44810Combined sources
Helixi450 – 4523Combined sources
Helixi453 – 46513Combined sources
Turni470 – 4723Combined sources
Helixi480 – 49314Combined sources
Helixi497 – 5048Combined sources
Helixi507 – 51711Combined sources
Helixi520 – 5289Combined sources
Turni529 – 5324Combined sources
Helixi540 – 55213Combined sources
Turni553 – 5564Combined sources
Beta strandi557 – 5593Combined sources
Helixi563 – 5686Combined sources
Helixi575 – 58511Combined sources
Beta strandi589 – 5913Combined sources
Helixi598 – 6003Combined sources
Beta strandi608 – 6114Combined sources
Beta strandi618 – 6236Combined sources
Beta strandi627 – 6348Combined sources
Beta strandi639 – 6435Combined sources
Turni644 – 6463Combined sources
Beta strandi649 – 6535Combined sources
Beta strandi660 – 6656Combined sources
Beta strandi669 – 6768Combined sources
Beta strandi679 – 6857Combined sources
Turni686 – 6883Combined sources
Beta strandi691 – 6966Combined sources
Beta strandi702 – 7076Combined sources
Beta strandi709 – 7124Combined sources
Beta strandi715 – 7206Combined sources
Beta strandi725 – 7295Combined sources
Beta strandi732 – 7398Combined sources
Beta strandi746 – 7516Combined sources
Beta strandi757 – 77115Combined sources
Helixi772 – 7743Combined sources
Beta strandi777 – 7826Combined sources
Beta strandi810 – 8178Combined sources
Beta strandi820 – 8256Combined sources
Turni826 – 8283Combined sources
Beta strandi831 – 8366Combined sources
Beta strandi838 – 8414Combined sources
Beta strandi845 – 8484Combined sources
Beta strandi854 – 8585Combined sources
Beta strandi860 – 8623Combined sources
Beta strandi864 – 8685Combined sources
Turni869 – 8724Combined sources
Beta strandi873 – 8786Combined sources
Beta strandi885 – 8906Combined sources
Beta strandi894 – 9018Combined sources
Beta strandi906 – 9105Combined sources
Helixi911 – 9155Combined sources
Beta strandi919 – 93113Combined sources
Beta strandi934 – 95320Combined sources
Beta strandi956 – 9594Combined sources
Beta strandi964 – 9696Combined sources
Beta strandi973 – 9808Combined sources
Beta strandi986 – 9894Combined sources
Turni990 – 9923Combined sources
Beta strandi996 – 9983Combined sources
Beta strandi1009 – 10113Combined sources
Beta strandi1013 – 10164Combined sources
Beta strandi1018 – 10214Combined sources
Beta strandi1023 – 10308Combined sources
Turni1032 – 10343Combined sources
Beta strandi1047 – 10526Combined sources
Beta strandi1054 – 107118Combined sources
Turni1072 – 10754Combined sources
Beta strandi1079 – 10824Combined sources
Beta strandi1091 – 10933Combined sources
Beta strandi1095 – 10995Combined sources
Beta strandi1101 – 11033Combined sources
Beta strandi1114 – 11185Combined sources
Beta strandi1130 – 11356Combined sources
Beta strandi1137 – 114610Combined sources
Beta strandi1153 – 11597Combined sources
Beta strandi1183 – 11864Combined sources
Beta strandi1193 – 120311Combined sources
Beta strandi1205 – 12073Combined sources
Beta strandi1228 – 12303Combined sources
Beta strandi1233 – 12364Combined sources
Beta strandi1242 – 12454Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00770000120500.
HOVERGENiHBG018730.
InParanoidiO88879.
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.
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.
PRINTSiPR00320. 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

        10         20         30         40         50
MDAKARNCLL QHREALEKDI KTSYIMDHMI SNGVLSVIEE EKVKSQATQY
60 70 80 90 100
QRAAALIKMI LNKDNCAYIS FYNALLHEGY KDLAALLQSG LPLVSSSSGK
110 120 130 140 150
DTDGGITSFV RTVLCEGGVP QRPVIFVTRK KLVHAIQQKL WKLNGEPGWV
160 170 180 190 200
TIYGMAGCGK SVLAAEAVRD HSLLEGCFSG GVHWVSIGKQ DKSGLLMKLQ
210 220 230 240 250
NLCMRLDQEE SFSQRLPLNI EEAKDRLRVL MLRKHPRSLL ILDDVWDPWV
260 270 280 290 300
LKAFDNQCQI LLTTRDKSVT DSVMGPKHVV PVESGLGREK GLEILSLFVN
310 320 330 340 350
MKKEDLPAEA HSIIKECKGS PLVVSLIGAL LRDFPNRWAY YLRQLQNKQF
360 370 380 390 400
KRIRKSSSYD YEALDEAMSI SVEMLREDIK DYYTDLSILQ KDVKVPTKVL
410 420 430 440 450
CVLWDLETEE VEDILQEFVN KSLLFCNRNG KSFCYYLHDL QVDFLTEKNR
460 470 480 490 500
SQLQDLHRKM VTQFQRYYQP HTLSPDQEDC MYWYNFLAYH MASANMHKEL
510 520 530 540 550
CALMFSLDWI KAKTELVGPA HLIHEFVAYR HILDEKDCAV CENFQEFLSL
560 570 580 590 600
NGHLLGRQPF PNIVQLGLCE PETSEVYRQA KLQAKQEGDT GRLYLEWINK
610 620 630 640 650
KTIKNLSRLV VRPHTDAVYH ACFSQDGQRI ASCGADKTLQ VFKAETGEKL
660 670 680 690 700
LDIKAHEDEV LCCAFSSDDS YIATCSADKK VKIWDSATGK LVHTYDEHSE
710 720 730 740 750
QVNCCHFTNK SNHLLLATGS NDFFLKLWDL NQKECRNTMF GHTNSVNHCR
760 770 780 790 800
FSPDDELLAS CSADGTLRLW DVRSANERKS INVKRFFLSS EDPPEDVEVI
810 820 830 840 850
VKCCSWSADG DKIIVAAKNK VLLFDIHTSG LLAEIHTGHH STIQYCDFSP
860 870 880 890 900
YDHLAVIALS QYCVELWNID SRLKVADCRG HLSWVHGVMF SPDGSSFLTA
910 920 930 940 950
SDDQTIRVWE TKKVCKNSAI VLKQEIDVVF QENETMVLAV DNIRGLQLIA
960 970 980 990 1000
GKTGQIDYLP EAQVSCCCLS PHLEYVAFGD EDGAIKIIEL PNNRVFSSGV
1010 1020 1030 1040 1050
GHKKAVRHIQ FTADGKTLIS SSEDSVIQVW NWQTGDYVFL QAHQETVKDF
1060 1070 1080 1090 1100
RLLQDSRLLS WSFDGTVKVW NVITGRIERD FTCHQGTVLS CAISSDATKF
1110 1120 1130 1140 1150
SSTSADKTAK IWSFDLLSPL HELKGHNGCV RCSAFSLDGI LLATGDDNGE
1160 1170 1180 1190 1200
IRIWNVSDGQ LLHSCAPISV EEGTATHGGW VTDVCFSPDS KTLVSAGGYL
1210 1220 1230 1240
KWWNVATGDS SQTFYTNGTN LKKIHVSPDF RTYVTVDNLG ILYILQVLE

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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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 ENSGT00770000120500.
HOVERGENi HBG018730.
InParanoidi O88879.
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

Bgeei O88879.
CleanExi MM_APAF1.
ExpressionAtlasi O88879. baseline and differential.
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.
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 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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 129 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