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Protein

Apoptotic protease-activating factor 1

Gene

APAF1

Organism
Homo sapiens (Human)
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. Isoform 6 is less effective in inducing apoptosis.2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei265ATPBy similarity1

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: UniProtKB
  • nucleotide binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Apoptosis

Keywords - Ligandi

ATP-binding, Calcium, Nucleotide-binding

Enzyme and pathway databases

BioCyciZFISH:ENSG00000120868-MONOMER.
ReactomeiR-HSA-111458. Formation of apoptosome.
R-HSA-111459. Activation of caspases through apoptosome-mediated cleavage.
R-HSA-6798695. Neutrophil degranulation.
R-HSA-6803207. TP53 Regulates Transcription of Caspase Activators and Caspases.
SABIO-RKO14727.
SignaLinkiO14727.
SIGNORiO14727.

Names & Taxonomyi

Protein namesi
Recommended name:
Apoptotic protease-activating factor 1
Short name:
APAF-1
Gene namesi
Name:APAF1
Synonyms:KIAA0413
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:576. APAF1.

Subcellular locationi

GO - Cellular componenti

  • apoptosome Source: UniProtKB
  • cytosol Source: Reactome
  • extracellular exosome Source: UniProtKB
  • nucleus Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi160K → R: No association with APAF-1. No binding to pro-caspase-9. 1 Publication1
Mutagenesisi368M → L: Activation of pro-caspase-9 independent of cytochrome c. Increased ability to induce apoptosis. 1 Publication1

Organism-specific databases

DisGeNETi317.
OpenTargetsiENSG00000120868.
PharmGKBiPA24868.

Chemistry databases

ChEMBLiCHEMBL1795093.
DrugBankiDB00171. Adenosine triphosphate.

Polymorphism and mutation databases

BioMutaiAPAF1.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000508441 – 1248Apoptotic protease-activating factor 1Add BLAST1248

Proteomic databases

EPDiO14727.
MaxQBiO14727.
PaxDbiO14727.
PeptideAtlasiO14727.
PRIDEiO14727.

PTM databases

iPTMnetiO14727.
PhosphoSitePlusiO14727.

Miscellaneous databases

PMAP-CutDBO14727.

Expressioni

Tissue specificityi

Ubiquitous. Highest levels of expression in adult spleen and peripheral blood leukocytes, and in fetal brain, kidney and lung. Isoform 1 is expressed in heart, kidney and liver.

Inductioni

By E2F and p53/TP53 in apoptotic neurons.1 Publication

Gene expression databases

BgeeiENSG00000120868.
ExpressionAtlasiO14727. baseline and differential.
GenevisibleiO14727. HS.

Organism-specific databases

HPAiCAB069399.
HPA031373.

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. Pro-caspase-3 is recruited into the Apaf-1-pro-caspase-9 complex via interaction with pro-caspase-9. Interacts with APIP. Interacts (via CARD and NACHT domains) with NAIP/BIRC1 (via NACHT domain).3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CASP9P5521118EBI-446492,EBI-516799
CYCSP999996EBI-446492,EBI-446479
PPP1CAP621362EBI-446492,EBI-357253
YWHAEP622582EBI-446492,EBI-356498

Protein-protein interaction databases

BioGridi106814. 27 interactors.
DIPiDIP-27624N.
IntActiO14727. 7 interactors.
MINTiMINT-96751.
STRINGi9606.ENSP00000448165.

Chemistry databases

BindingDBiO14727.

Structurei

Secondary structure

11248
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi3 – 11Combined sources9
Helixi13 – 19Combined sources7
Helixi22 – 32Combined sources11
Helixi37 – 44Combined sources8
Beta strandi46 – 48Combined sources3
Helixi49 – 61Combined sources13
Helixi65 – 77Combined sources13
Helixi81 – 87Combined sources7
Helixi88 – 90Combined sources3
Helixi99 – 104Combined sources6
Helixi108 – 116Combined sources9
Helixi130 – 140Combined sources11
Beta strandi148 – 153Combined sources6
Helixi160 – 168Combined sources9
Helixi171 – 177Combined sources7
Beta strandi182 – 189Combined sources8
Helixi192 – 206Combined sources15
Helixi220 – 233Combined sources14
Beta strandi239 – 245Combined sources7
Helixi248 – 252Combined sources5
Beta strandi259 – 265Combined sources7
Helixi267 – 270Combined sources4
Beta strandi277 – 281Combined sources5
Helixi288 – 299Combined sources12
Helixi303 – 305Combined sources3
Helixi309 – 316Combined sources8
Turni317 – 319Combined sources3
Helixi321 – 333Combined sources13
Helixi338 – 346Combined sources9
Helixi362 – 373Combined sources12
Turni377 – 379Combined sources3
Helixi380 – 385Combined sources6
Helixi386 – 388Combined sources3
Helixi397 – 404Combined sources8
Helixi408 – 420Combined sources13
Beta strandi423 – 429Combined sources7
Beta strandi432 – 436Combined sources5
Helixi439 – 448Combined sources10
Helixi450 – 452Combined sources3
Helixi453 – 464Combined sources12
Turni465 – 467Combined sources3
Helixi470 – 472Combined sources3
Helixi480 – 493Combined sources14
Helixi497 – 504Combined sources8
Helixi507 – 517Combined sources11
Helixi520 – 528Combined sources9
Helixi530 – 532Combined sources3
Helixi535 – 550Combined sources16
Turni551 – 556Combined sources6
Helixi563 – 567Combined sources5
Helixi575 – 585Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1C15NMR-A1-97[»]
1CWWNMR-A1-97[»]
1CY5X-ray1.30A1-97[»]
1Z6TX-ray2.21A/B/C/D1-591[»]
2P1HX-ray1.59A1-92[»]
2YGSX-ray1.60A1-92[»]
3J2Telectron microscopy9.5A/B/C/D/E/F/G1-1248[»]
3JBTelectron microscopy3.80A/C/E/G/I/K/M1-1248[»]
3YGSX-ray2.50C1-95[»]
4RHWX-ray2.10A/B/C/D1-97[»]
5JUYelectron microscopy4.10A/B/C/D/E/F/G1-1248[»]
ProteinModelPortaliO14727.
SMRiO14727.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO14727.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 90CARDPROSITE-ProRule annotationAdd BLAST90
Domaini104 – 415NB-ARCAdd BLAST312
Repeati613 – 652WD 1-1Add BLAST40
Repeati655 – 694WD 1-2Add BLAST40
Repeati697 – 738WD 1-3Add BLAST42
Repeati741 – 780WD 1-4Add BLAST40
Repeati796 – 836WD 1-5Add BLAST41
Repeati838 – 877WD 1-6Add BLAST40
Repeati880 – 910WD 1-7Add BLAST31
Repeati922 – 958WD 2-1Add BLAST37
Repeati959 – 998WD 2-2Add BLAST40
Repeati1001 – 1040WD 2-3Add BLAST40
Repeati1042 – 1080WD 2-4Add BLAST39
Repeati1083 – 1122WD 2-5Add BLAST40
Repeati1125 – 1164WD 2-6Add BLAST40
Repeati1175 – 1212WD 2-7Add BLAST38
Repeati1213 – 1248WD 2-8Add BLAST36

Region

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

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi95 – 98Poly-Ser4

Domaini

The CARD domain mediates interaction with APIP.
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 (By similarity).By similarity

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.
InParanoidiO14727.
KOiK02084.
OMAiETKKVCK.
OrthoDBiEOG091G036U.
PhylomeDBiO14727.
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.
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. 9 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 (6)i

Sequence statusi: Complete.

This entry describes 6 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: O14727-1) [UniParc]FASTAAdd to basket
Also known as: Apaf-1XL

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 SDGFLTISEE EKVRNEPTQQ
60 70 80 90 100
QRAAMLIKMI LKKDNDSYVS FYNALLHEGY KDLAALLHDG IPVVSSSSGK
110 120 130 140 150
DSVSGITSYV RTVLCEGGVP QRPVVFVTRK KLVNAIQQKL SKLKGEPGWV
160 170 180 190 200
TIHGMAGCGK SVLAAEAVRD HSLLEGCFPG GVHWVSVGKQ DKSGLLMKLQ
210 220 230 240 250
NLCTRLDQDE SFSQRLPLNI EEAKDRLRIL MLRKHPRSLL ILDDVWDSWV
260 270 280 290 300
LKAFDSQCQI LLTTRDKSVT DSVMGPKYVV PVESSLGKEK GLEILSLFVN
310 320 330 340 350
MKKADLPEQA HSIIKECKGS PLVVSLIGAL LRDFPNRWEY YLKQLQNKQF
360 370 380 390 400
KRIRKSSSYD YEALDEAMSI SVEMLREDIK DYYTDLSILQ KDVKVPTKVL
410 420 430 440 450
CILWDMETEE VEDILQEFVN KSLLFCDRNG KSFRYYLHDL QVDFLTEKNC
460 470 480 490 500
SQLQDLHKKI ITQFQRYHQP HTLSPDQEDC MYWYNFLAYH MASAKMHKEL
510 520 530 540 550
CALMFSLDWI KAKTELVGPA HLIHEFVEYR HILDEKDCAV SENFQEFLSL
560 570 580 590 600
NGHLLGRQPF PNIVQLGLCE PETSEVYQQA KLQAKQEVDN GMLYLEWINK
610 620 630 640 650
KNITNLSRLV VRPHTDAVYH ACFSEDGQRI ASCGADKTLQ VFKAETGEKL
660 670 680 690 700
LEIKAHEDEV LCCAFSTDDR FIATCSVDKK VKIWNSMTGE LVHTYDEHSE
710 720 730 740 750
QVNCCHFTNS SHHLLLATGS SDCFLKLWDL NQKECRNTMF GHTNSVNHCR
760 770 780 790 800
FSPDDKLLAS CSADGTLKLW DATSANERKS INVKQFFLNL EDPQEDMEVI
810 820 830 840 850
VKCCSWSADG ARIMVAAKNK IFLFDIHTSG LLGEIHTGHH STIQYCDFSP
860 870 880 890 900
QNHLAVVALS QYCVELWNTD SRSKVADCRG HLSWVHGVMF SPDGSSFLTS
910 920 930 940 950
SDDQTIRLWE TKKVCKNSAV MLKQEVDVVF QENEVMVLAV DHIRRLQLIN
960 970 980 990 1000
GRTGQIDYLT EAQVSCCCLS PHLQYIAFGD ENGAIEILEL VNNRIFQSRF
1010 1020 1030 1040 1050
QHKKTVWHIQ FTADEKTLIS SSDDAEIQVW NWQLDKCIFL RGHQETVKDF
1060 1070 1080 1090 1100
RLLKNSRLLS WSFDGTVKVW NIITGNKEKD FVCHQGTVLS CDISHDATKF
1110 1120 1130 1140 1150
SSTSADKTAK IWSFDLLLPL HELRGHNGCV RCSAFSVDST LLATGDDNGE
1160 1170 1180 1190 1200
IRIWNVSNGE LLHLCAPLSE EGAATHGGWV TDLCFSPDGK MLISAGGYIK
1210 1220 1230 1240
WWNVVTGESS QTFYTNGTNL KKIHVSPDFK TYVTVDNLGI LYILQTLE
Length:1,248
Mass (Da):141,840
Last modified:January 23, 2002 - v2
Checksum:i0750D05817AC9B3B
GO
Isoform 2 (identifier: O14727-2) [UniParc]FASTAAdd to basket
Also known as: Apaf-1L

The sequence of this isoform differs from the canonical sequence as follows:
     99-109: Missing.

Show »
Length:1,237
Mass (Da):140,745
Checksum:i0D3EF9AB2A66FFF5
GO
Isoform 3 (identifier: O14727-3) [UniParc]FASTAAdd to basket
Also known as: Apaf-1S

The sequence of this isoform differs from the canonical sequence as follows:
     99-109: Missing.
     824-866: Missing.

Show »
Length:1,194
Mass (Da):135,980
Checksum:iA675EA102DDAAFB7
GO
Isoform 4 (identifier: O14727-4) [UniParc]FASTAAdd to basket
Also known as: Apaf-1M

The sequence of this isoform differs from the canonical sequence as follows:
     824-866: Missing.

Show »
Length:1,205
Mass (Da):137,076
Checksum:iDA57B4E35E79D73A
GO
Isoform 5 (identifier: O14727-5) [UniParc]FASTAAdd to basket
Also known as: Apaf-1XS

The sequence of this isoform differs from the canonical sequence as follows:
     575-575: E → ETLGFESKK
     824-866: Missing.
     1113-1154: Missing.

Show »
Length:1,171
Mass (Da):133,356
Checksum:iCA9B14019EAB35BF
GO
Isoform 6 (identifier: O14727-6) [UniParc]FASTAAdd to basket
Also known as: Apaf-1-ALT

The sequence of this isoform differs from the canonical sequence as follows:
     319-338: GSPLVVSLIGALLRDFPNRW → VVERCHWGILTDLLHKWNQS
     339-1248: Missing.

Show »
Length:338
Mass (Da):37,976
Checksum:i29D933A65707ED92
GO

Sequence cautioni

The sequence AAK28401 differs from that shown. Reason: Frameshift at position 108.Curated
The sequence BAA24843 differs from that shown. Reason: Erroneous initiation.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti134N → S (Ref. 11) Curated1
Sequence conflicti145G → C in CAB55587 (PubMed:10441496).Curated1
Sequence conflicti161S → F in CAB55586 (PubMed:10441496).Curated1
Sequence conflicti370I → T in CAB55581 (PubMed:10441496).Curated1
Sequence conflicti383Y → H in CAB55586 (PubMed:10441496).Curated1
Sequence conflicti544F → L in CAB55584 (PubMed:10441496).Curated1
Sequence conflicti580A → T in CAB55580 (PubMed:10441496).Curated1
Sequence conflicti608R → C in CAB55585 (PubMed:10441496).Curated1
Sequence conflicti620H → R in CAB55587 (PubMed:10441496).Curated1
Sequence conflicti639L → F in CAB55583 (PubMed:10441496).Curated1
Sequence conflicti708T → A in CAB55579 (PubMed:10441496).Curated1
Sequence conflicti742H → R in CAB55584 (PubMed:10441496).Curated1
Sequence conflicti746V → A in CAB55586 (PubMed:10441496).Curated1
Sequence conflicti757L → P in CAB56462 (PubMed:10441496).Curated1
Sequence conflicti795E → G in CAB55581 (PubMed:10441496).Curated1
Sequence conflicti798E → G in CAB55587 (PubMed:10441496).Curated1
Sequence conflicti825D → A in CAB55585 (PubMed:10441496).Curated1
Sequence conflicti871S → L in CAB55587 (PubMed:10441496).Curated1
Sequence conflicti876A → T in CAB55581 (PubMed:10441496).Curated1
Sequence conflicti949I → V in CAB55585 (PubMed:10441496).Curated1
Sequence conflicti1008H → R in CAB55582 (PubMed:10441496).Curated1
Sequence conflicti1056S → P in CAB55582 (PubMed:10441496).Curated1
Sequence conflicti1241L → I in BAA24843 (PubMed:9455477).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_00675999 – 109Missing in isoform 2 and isoform 3. 3 PublicationsAdd BLAST11
Alternative sequenceiVSP_008965319 – 338GSPLV…FPNRW → VVERCHWGILTDLLHKWNQS in isoform 6. 1 PublicationAdd BLAST20
Alternative sequenceiVSP_008966339 – 1248Missing in isoform 6. 1 PublicationAdd BLAST910
Alternative sequenceiVSP_006760575E → ETLGFESKK in isoform 5. 1 Publication1
Alternative sequenceiVSP_006761824 – 866Missing in isoform 3, isoform 4 and isoform 5. 2 PublicationsAdd BLAST43
Alternative sequenceiVSP_0067621113 – 1154Missing in isoform 5. 1 PublicationAdd BLAST42

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF013263 mRNA. Translation: AAC51678.1.
AJ243003 mRNA. Translation: CAB55579.1.
AJ243004 mRNA. Translation: CAB55580.1.
AJ243005 mRNA. Translation: CAB55581.1.
AJ243006 mRNA. Translation: CAB55582.1.
AJ243007 mRNA. Translation: CAB55583.1.
AJ243008 mRNA. Translation: CAB55584.1.
AJ243009 mRNA. Translation: CAB55585.1.
AJ243010 mRNA. Translation: CAB55586.1.
AJ243011 mRNA. Translation: CAB55587.1.
AJ243048 mRNA. Translation: CAB55588.1.
AJ243107 mRNA. Translation: CAB56462.1.
AF134397 mRNA. Translation: AAD38344.1.
AF149794 mRNA. Translation: AAD34016.1.
AB007873 mRNA. Translation: BAA24843.2. Different initiation.
AB103079 mRNA. Translation: BAC77343.1.
CH471054 Genomic DNA. Translation: EAW97606.1.
BC136531 mRNA. Translation: AAI36532.1.
BC136532 mRNA. Translation: AAI36533.1.
AJ133643 Genomic DNA. Translation: CAB65085.1.
AJ133644 Genomic DNA. Translation: CAB65086.1.
AJ133645 Genomic DNA. Translation: CAB65087.1.
AF248734 mRNA. Translation: AAK28401.1. Frameshift.
CCDSiCCDS55862.1. [O14727-2]
CCDS55863.1. [O14727-3]
CCDS9069.1. [O14727-1]
CCDS9070.1. [O14727-4]
CCDS9071.1. [O14727-6]
PIRiT03818.
RefSeqiNP_001151.1. NM_001160.2. [O14727-3]
NP_037361.1. NM_013229.2. [O14727-2]
NP_863651.1. NM_181861.1. [O14727-1]
NP_863658.1. NM_181868.1. [O14727-4]
NP_863659.1. NM_181869.1. [O14727-6]
UniGeneiHs.552567.

Genome annotation databases

EnsembliENST00000333991; ENSP00000334558; ENSG00000120868. [O14727-6]
ENST00000357310; ENSP00000349862; ENSG00000120868. [O14727-4]
ENST00000359972; ENSP00000353059; ENSG00000120868. [O14727-3]
ENST00000547045; ENSP00000449791; ENSG00000120868. [O14727-4]
ENST00000550527; ENSP00000448449; ENSG00000120868. [O14727-2]
ENST00000551964; ENSP00000448165; ENSG00000120868. [O14727-1]
ENST00000552268; ENSP00000448826; ENSG00000120868. [O14727-6]
GeneIDi317.
KEGGihsa:317.
UCSCiuc001tfz.4. human. [O14727-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF013263 mRNA. Translation: AAC51678.1.
AJ243003 mRNA. Translation: CAB55579.1.
AJ243004 mRNA. Translation: CAB55580.1.
AJ243005 mRNA. Translation: CAB55581.1.
AJ243006 mRNA. Translation: CAB55582.1.
AJ243007 mRNA. Translation: CAB55583.1.
AJ243008 mRNA. Translation: CAB55584.1.
AJ243009 mRNA. Translation: CAB55585.1.
AJ243010 mRNA. Translation: CAB55586.1.
AJ243011 mRNA. Translation: CAB55587.1.
AJ243048 mRNA. Translation: CAB55588.1.
AJ243107 mRNA. Translation: CAB56462.1.
AF134397 mRNA. Translation: AAD38344.1.
AF149794 mRNA. Translation: AAD34016.1.
AB007873 mRNA. Translation: BAA24843.2. Different initiation.
AB103079 mRNA. Translation: BAC77343.1.
CH471054 Genomic DNA. Translation: EAW97606.1.
BC136531 mRNA. Translation: AAI36532.1.
BC136532 mRNA. Translation: AAI36533.1.
AJ133643 Genomic DNA. Translation: CAB65085.1.
AJ133644 Genomic DNA. Translation: CAB65086.1.
AJ133645 Genomic DNA. Translation: CAB65087.1.
AF248734 mRNA. Translation: AAK28401.1. Frameshift.
CCDSiCCDS55862.1. [O14727-2]
CCDS55863.1. [O14727-3]
CCDS9069.1. [O14727-1]
CCDS9070.1. [O14727-4]
CCDS9071.1. [O14727-6]
PIRiT03818.
RefSeqiNP_001151.1. NM_001160.2. [O14727-3]
NP_037361.1. NM_013229.2. [O14727-2]
NP_863651.1. NM_181861.1. [O14727-1]
NP_863658.1. NM_181868.1. [O14727-4]
NP_863659.1. NM_181869.1. [O14727-6]
UniGeneiHs.552567.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1C15NMR-A1-97[»]
1CWWNMR-A1-97[»]
1CY5X-ray1.30A1-97[»]
1Z6TX-ray2.21A/B/C/D1-591[»]
2P1HX-ray1.59A1-92[»]
2YGSX-ray1.60A1-92[»]
3J2Telectron microscopy9.5A/B/C/D/E/F/G1-1248[»]
3JBTelectron microscopy3.80A/C/E/G/I/K/M1-1248[»]
3YGSX-ray2.50C1-95[»]
4RHWX-ray2.10A/B/C/D1-97[»]
5JUYelectron microscopy4.10A/B/C/D/E/F/G1-1248[»]
ProteinModelPortaliO14727.
SMRiO14727.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi106814. 27 interactors.
DIPiDIP-27624N.
IntActiO14727. 7 interactors.
MINTiMINT-96751.
STRINGi9606.ENSP00000448165.

Chemistry databases

BindingDBiO14727.
ChEMBLiCHEMBL1795093.
DrugBankiDB00171. Adenosine triphosphate.

PTM databases

iPTMnetiO14727.
PhosphoSitePlusiO14727.

Polymorphism and mutation databases

BioMutaiAPAF1.

Proteomic databases

EPDiO14727.
MaxQBiO14727.
PaxDbiO14727.
PeptideAtlasiO14727.
PRIDEiO14727.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000333991; ENSP00000334558; ENSG00000120868. [O14727-6]
ENST00000357310; ENSP00000349862; ENSG00000120868. [O14727-4]
ENST00000359972; ENSP00000353059; ENSG00000120868. [O14727-3]
ENST00000547045; ENSP00000449791; ENSG00000120868. [O14727-4]
ENST00000550527; ENSP00000448449; ENSG00000120868. [O14727-2]
ENST00000551964; ENSP00000448165; ENSG00000120868. [O14727-1]
ENST00000552268; ENSP00000448826; ENSG00000120868. [O14727-6]
GeneIDi317.
KEGGihsa:317.
UCSCiuc001tfz.4. human. [O14727-1]

Organism-specific databases

CTDi317.
DisGeNETi317.
GeneCardsiAPAF1.
HGNCiHGNC:576. APAF1.
HPAiCAB069399.
HPA031373.
MIMi602233. gene.
neXtProtiNX_O14727.
OpenTargetsiENSG00000120868.
PharmGKBiPA24868.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4155. Eukaryota.
KOG4658. Eukaryota.
ENOG410XP3K. LUCA.
GeneTreeiENSGT00810000125363.
HOVERGENiHBG018730.
InParanoidiO14727.
KOiK02084.
OMAiETKKVCK.
OrthoDBiEOG091G036U.
PhylomeDBiO14727.
TreeFamiTF323866.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000120868-MONOMER.
ReactomeiR-HSA-111458. Formation of apoptosome.
R-HSA-111459. Activation of caspases through apoptosome-mediated cleavage.
R-HSA-6798695. Neutrophil degranulation.
R-HSA-6803207. TP53 Regulates Transcription of Caspase Activators and Caspases.
SABIO-RKO14727.
SignaLinkiO14727.
SIGNORiO14727.

Miscellaneous databases

EvolutionaryTraceiO14727.
GeneWikiiAPAF1.
GenomeRNAii317.
PMAP-CutDBO14727.
PROiO14727.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000120868.
ExpressionAtlasiO14727. baseline and differential.
GenevisibleiO14727. HS.

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.
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. 9 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_HUMAN
AccessioniPrimary (citable) accession number: O14727
Secondary accession number(s): B2RMX8
, O43297, Q7Z438, Q9BXZ6, Q9UBZ5, Q9UGN8, Q9UGN9, Q9UGP0, Q9UJ58, Q9UJ59, Q9UJ60, Q9UJ61, Q9UJ62, Q9UJ63, Q9UJ64, Q9UJ65, Q9UJ66, Q9UJ67, Q9UNC9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 23, 2002
Last modified: November 30, 2016
This is version 194 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

Miscellaneous

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

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.