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Protein

Apoptotic protease-activating factor 1

Gene

Apaf1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: 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)DescriptionActionsGraphical viewLength
Binding sitei265ATP1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi154 – 161ATPSequence analysis8

GO - Molecular functioni

  • ADP binding Source: InterPro
  • ATP binding Source: UniProtKB-KW
  • cysteine-type endopeptidase activator activity involved in apoptotic process Source: MGI
  • identical protein binding Source: MGI

GO - Biological processi

  • activation of cysteine-type endopeptidase activity involved in apoptotic process Source: MGI
  • activation of cysteine-type endopeptidase activity involved in apoptotic process by cytochrome c Source: MGI
  • aging Source: Ensembl
  • brain development Source: MGI
  • cardiac muscle cell apoptotic process Source: Ensembl
  • cell differentiation Source: Ensembl
  • cellular response to transforming growth factor beta stimulus Source: Ensembl
  • forebrain development Source: MGI
  • glial cell apoptotic process Source: Ensembl
  • intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress Source: ParkinsonsUK-UCL
  • multicellular organism development Source: MGI
  • neural tube closure Source: MGI
  • neuron apoptotic process Source: MGI
  • positive regulation of apoptotic signaling pathway Source: MGI
  • protein homooligomerization Source: Ensembl
  • regulation of apoptotic DNA fragmentation Source: MGI
  • response to hypoxia Source: Ensembl
  • response to nutrient Source: Ensembl
Complete GO annotation...

Keywords - Biological processi

Apoptosis

Keywords - Ligandi

ATP-binding, Calcium, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-MMU-111458. Formation of apoptosome.
R-MMU-111459. Activation of caspases through apoptosome-mediated cleavage.
R-MMU-6798695. Neutrophil degranulation.

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
Proteomesi
  • UP000000589 Componenti: Chromosome 10

Organism-specific databases

MGIiMGI:1306796. Apaf1.

Subcellular locationi

GO - Cellular componenti

  • apoptosome Source: MGI
  • cytosol Source: MGI
  • extracellular exosome Source: MGI
  • nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi265R → S: No stimulation of CASP9 activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000508451 – 1249Apoptotic protease-activating factor 1Add BLAST1249

Proteomic databases

EPDiO88879.
MaxQBiO88879.
PaxDbiO88879.
PeptideAtlasiO88879.
PRIDEiO88879.

PTM databases

iPTMnetiO88879.
PhosphoSitePlusiO88879.

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

BgeeiENSMUSG00000019979.
CleanExiMM_APAF1.
ExpressionAtlasiO88879. baseline and differential.
GenevisibleiO88879. MM.

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

GO - Molecular functioni

  • identical protein binding Source: MGI

Protein-protein interaction databases

BioGridi198139. 1 interactor.
IntActiO88879. 1 interactor.
MINTiMINT-104429.
STRINGi10090.ENSMUSP00000020157.

Structurei

Secondary structure

11249
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi109 – 116Combined sources8
Helixi130 – 141Combined sources12
Turni142 – 145Combined sources4
Beta strandi148 – 153Combined sources6
Helixi160 – 167Combined sources8
Helixi171 – 174Combined sources4
Turni175 – 177Combined sources3
Beta strandi182 – 186Combined sources5
Helixi192 – 206Combined sources15
Turni207 – 209Combined sources3
Helixi220 – 230Combined sources11
Beta strandi232 – 235Combined sources4
Beta strandi239 – 244Combined sources6
Helixi248 – 251Combined sources4
Beta strandi259 – 266Combined sources8
Turni267 – 272Combined sources6
Helixi288 – 299Combined sources12
Helixi309 – 316Combined sources8
Turni317 – 319Combined sources3
Helixi321 – 333Combined sources13
Beta strandi334 – 336Combined sources3
Helixi338 – 346Combined sources9
Helixi361 – 373Combined sources13
Turni377 – 379Combined sources3
Helixi380 – 385Combined sources6
Helixi386 – 388Combined sources3
Helixi397 – 404Combined sources8
Helixi408 – 420Combined sources13
Beta strandi425 – 436Combined sources12
Helixi439 – 448Combined sources10
Helixi450 – 452Combined sources3
Helixi453 – 465Combined sources13
Turni470 – 472Combined sources3
Helixi480 – 493Combined sources14
Helixi497 – 504Combined sources8
Helixi507 – 517Combined sources11
Helixi520 – 528Combined sources9
Turni529 – 532Combined sources4
Helixi540 – 552Combined sources13
Turni553 – 556Combined sources4
Beta strandi557 – 559Combined sources3
Helixi563 – 568Combined sources6
Helixi575 – 585Combined sources11
Beta strandi589 – 591Combined sources3
Helixi598 – 600Combined sources3
Beta strandi608 – 611Combined sources4
Beta strandi618 – 623Combined sources6
Beta strandi627 – 634Combined sources8
Beta strandi639 – 643Combined sources5
Turni644 – 646Combined sources3
Beta strandi649 – 653Combined sources5
Beta strandi660 – 665Combined sources6
Beta strandi669 – 676Combined sources8
Beta strandi679 – 685Combined sources7
Turni686 – 688Combined sources3
Beta strandi691 – 696Combined sources6
Beta strandi702 – 707Combined sources6
Beta strandi709 – 712Combined sources4
Beta strandi715 – 720Combined sources6
Beta strandi725 – 729Combined sources5
Beta strandi732 – 739Combined sources8
Beta strandi746 – 751Combined sources6
Beta strandi757 – 771Combined sources15
Helixi772 – 774Combined sources3
Beta strandi777 – 782Combined sources6
Beta strandi810 – 817Combined sources8
Beta strandi820 – 825Combined sources6
Turni826 – 828Combined sources3
Beta strandi831 – 836Combined sources6
Beta strandi838 – 841Combined sources4
Beta strandi845 – 848Combined sources4
Beta strandi854 – 858Combined sources5
Beta strandi860 – 862Combined sources3
Beta strandi864 – 868Combined sources5
Turni869 – 872Combined sources4
Beta strandi873 – 878Combined sources6
Beta strandi885 – 890Combined sources6
Beta strandi894 – 901Combined sources8
Beta strandi906 – 910Combined sources5
Helixi911 – 915Combined sources5
Beta strandi919 – 931Combined sources13
Beta strandi934 – 953Combined sources20
Beta strandi956 – 959Combined sources4
Beta strandi964 – 969Combined sources6
Beta strandi973 – 980Combined sources8
Beta strandi986 – 989Combined sources4
Turni990 – 992Combined sources3
Beta strandi996 – 998Combined sources3
Beta strandi1009 – 1011Combined sources3
Beta strandi1013 – 1016Combined sources4
Beta strandi1018 – 1021Combined sources4
Beta strandi1023 – 1030Combined sources8
Turni1032 – 1034Combined sources3
Beta strandi1047 – 1052Combined sources6
Beta strandi1054 – 1071Combined sources18
Turni1072 – 1075Combined sources4
Beta strandi1079 – 1082Combined sources4
Beta strandi1091 – 1093Combined sources3
Beta strandi1095 – 1099Combined sources5
Beta strandi1101 – 1103Combined sources3
Beta strandi1114 – 1118Combined sources5
Beta strandi1130 – 1135Combined sources6
Beta strandi1137 – 1146Combined sources10
Beta strandi1153 – 1159Combined sources7
Beta strandi1183 – 1186Combined sources4
Beta strandi1193 – 1203Combined sources11
Beta strandi1205 – 1207Combined sources3
Beta strandi1228 – 1230Combined sources3
Beta strandi1233 – 1236Combined sources4
Beta strandi1242 – 1245Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3SFZX-ray3.00A1-1249[»]
3SHFX-ray3.55A1-1249[»]
ProteinModelPortaliO88879.
SMRiO88879.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 90CARDPROSITE-ProRule annotationAdd BLAST90
Domaini106 – 415NB-ARCAdd BLAST310
Repeati613 – 652WD 1-1PROSITE-ProRule annotation1 PublicationAdd BLAST40
Repeati655 – 694WD 1-2PROSITE-ProRule annotation1 PublicationAdd BLAST40
Repeati697 – 738WD 1-3PROSITE-ProRule annotation1 PublicationAdd BLAST42
Repeati741 – 780WD 1-4PROSITE-ProRule annotation1 PublicationAdd BLAST40
Repeati796 – 837WD 1-5PROSITE-ProRule annotation1 PublicationAdd BLAST42
Repeati838 – 877WD 1-6PROSITE-ProRule annotation1 PublicationAdd BLAST40
Repeati880 – 910WD 1-7PROSITE-ProRule annotation1 PublicationAdd BLAST31
Repeati922 – 958WD 2-1PROSITE-ProRule annotation1 PublicationAdd BLAST37
Repeati959 – 998WD 2-2PROSITE-ProRule annotation1 PublicationAdd BLAST40
Repeati1001 – 1040WD 2-3PROSITE-ProRule annotation1 PublicationAdd BLAST40
Repeati1042 – 1080WD 2-4PROSITE-ProRule annotation1 PublicationAdd BLAST39
Repeati1083 – 1122WD 2-5PROSITE-ProRule annotation1 PublicationAdd BLAST40
Repeati1125 – 1164WD 2-6PROSITE-ProRule annotation1 PublicationAdd BLAST40
Repeati1176 – 1213WD 2-7PROSITE-ProRule annotation1 PublicationAdd BLAST38
Repeati1214 – 1249WD 2-8PROSITE-ProRule annotation1 PublicationAdd BLAST36

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni910 – 921Interpropeller linkerAdd BLAST12

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

eggNOGiKOG4155. Eukaryota.
KOG4658. Eukaryota.
ENOG410XP3K. LUCA.
GeneTreeiENSGT00810000125363.
HOVERGENiHBG018730.
InParanoidiO88879.
KOiK02084.
OMAiETKKVCK.
OrthoDBiEOG091G036U.
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. Apaf-1.
IPR024977. Apc4_WD40_dom.
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]
PfamiPF12894. ANAPC4_WD40. 1 hit.
PF00619. CARD. 1 hit.
PF00931. NB-ARC. 1 hit.
PF00400. WD40. 8 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. AlignAdd to basket

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)DescriptionActionsGraphical viewLength
Sequence conflicti209E → D in AAC62458 (PubMed:9753320).Curated1
Sequence conflicti592R → P in AAC62458 (PubMed:9753320).Curated1
Sequence conflicti710K → S in AAC62458 (PubMed:9753320).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_00676399 – 110GKDTD…ITSFV → A in isoform 2. 1 PublicationAdd BLAST12

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.
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3SFZX-ray3.00A1-1249[»]
3SHFX-ray3.55A1-1249[»]
ProteinModelPortaliO88879.
SMRiO88879.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198139. 1 interactor.
IntActiO88879. 1 interactor.
MINTiMINT-104429.
STRINGi10090.ENSMUSP00000020157.

PTM databases

iPTMnetiO88879.
PhosphoSitePlusiO88879.

Proteomic databases

EPDiO88879.
MaxQBiO88879.
PaxDbiO88879.
PeptideAtlasiO88879.
PRIDEiO88879.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi317.
MGIiMGI:1306796. Apaf1.

Phylogenomic databases

eggNOGiKOG4155. Eukaryota.
KOG4658. Eukaryota.
ENOG410XP3K. LUCA.
GeneTreeiENSGT00810000125363.
HOVERGENiHBG018730.
InParanoidiO88879.
KOiK02084.
OMAiETKKVCK.
OrthoDBiEOG091G036U.
PhylomeDBiO88879.
TreeFamiTF323866.

Enzyme and pathway databases

ReactomeiR-MMU-111458. Formation of apoptosome.
R-MMU-111459. Activation of caspases through apoptosome-mediated cleavage.
R-MMU-6798695. Neutrophil degranulation.

Miscellaneous databases

ChiTaRSiApaf1. mouse.
PROiO88879.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000019979.
CleanExiMM_APAF1.
ExpressionAtlasiO88879. baseline and differential.
GenevisibleiO88879. MM.

Family and domain databases

Gene3Di1.10.533.10. 1 hit.
2.130.10.10. 2 hits.
3.40.50.300. 1 hit.
InterProiIPR017251. Apaf-1.
IPR024977. Apc4_WD40_dom.
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]
PfamiPF12894. ANAPC4_WD40. 1 hit.
PF00619. CARD. 1 hit.
PF00931. NB-ARC. 1 hit.
PF00400. WD40. 8 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]
ProtoNetiSearch...

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 30, 2016
This is version 150 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.