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O14727 (APAF_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 165. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Apoptotic protease-activating factor 1

Short name=APAF-1
Gene names
Name:APAF1
Synonyms:KIAA0413
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1248 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.4 Ref.5

Subunit structure

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). Ref.4 Ref.12 Ref.14 Ref.16

Subcellular location

Cytoplasm Ref.5.

Tissue specificity

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.

Induction

By E2F and p53/TP53 in apoptotic neurons. Ref.13

Domain

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.

Miscellaneous

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

Sequence similarities

Contains 1 CARD domain.

Contains 1 NB-ARC domain.

Contains 15 WD repeats.

Sequence caution

The sequence AAK28401.1 differs from that shown. Reason: Frameshift at position 108.

The sequence BAA24843.2 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processApoptosis
   Cellular componentCytoplasm
   Coding sequence diversityAlternative splicing
   DomainRepeat
WD repeat
   LigandATP-binding
Calcium
Nucleotide-binding
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processactivation of cysteine-type endopeptidase activity involved in apoptotic process

Inferred from direct assay PubMed 21827945. Source: UniProtKB

activation of cysteine-type endopeptidase activity involved in apoptotic process by cytochrome c

Inferred from direct assay Ref.1. Source: UniProtKB

apoptotic DNA fragmentation

Inferred from electronic annotation. Source: Ensembl

apoptotic process

Traceable author statement. Source: Reactome

defense response

Inferred from electronic annotation. Source: InterPro

forebrain development

Inferred from electronic annotation. Source: Ensembl

intrinsic apoptotic signaling pathway

Traceable author statement PubMed 18309324. Source: UniProtKB

nervous system development

Traceable author statement PubMed 9753320. Source: ProtInc

neural tube closure

Inferred from electronic annotation. Source: Ensembl

neuron apoptotic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of apoptotic process

Traceable author statement PubMed 18309324. Source: UniProtKB

positive regulation of apoptotic signaling pathway

Inferred from electronic annotation. Source: Ensembl

regulation of apoptotic process

Traceable author statement Ref.2. Source: UniProtKB

response to G1 DNA damage checkpoint signaling

Traceable author statement PubMed 18309324. Source: UniProtKB

   Cellular_componentapoptosome

Inferred from direct assay PubMed 21827945. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867. Source: UniProt

nucleus

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionADP binding

Inferred from electronic annotation. Source: InterPro

ATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

cysteine-type endopeptidase activator activity involved in apoptotic process

Non-traceable author statement PubMed 15009102. Source: UniProtKB

nucleotide binding

Traceable author statement PubMed 10383829. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 6 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O14727-1)

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.
Isoform 2 (identifier: O14727-2)

Also known as: Apaf-1L;

The sequence of this isoform differs from the canonical sequence as follows:
     99-109: Missing.
Isoform 3 (identifier: O14727-3)

Also known as: Apaf-1S;

The sequence of this isoform differs from the canonical sequence as follows:
     99-109: Missing.
     824-866: Missing.
Isoform 4 (identifier: O14727-4)

Also known as: Apaf-1M;

The sequence of this isoform differs from the canonical sequence as follows:
     824-866: Missing.
Isoform 5 (identifier: O14727-5)

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.
Isoform 6 (identifier: O14727-6)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 12481248Apoptotic protease-activating factor 1
PRO_0000050844

Regions

Domain1 – 9090CARD
Domain104 – 415312NB-ARC
Repeat613 – 65240WD 1-1
Repeat655 – 69440WD 1-2
Repeat697 – 73842WD 1-3
Repeat741 – 78040WD 1-4
Repeat796 – 83641WD 1-5
Repeat838 – 87740WD 1-6
Repeat880 – 91031WD 1-7
Repeat922 – 95837WD 2-1
Repeat959 – 99840WD 2-2
Repeat1001 – 104040WD 2-3
Repeat1042 – 108039WD 2-4
Repeat1083 – 112240WD 2-5
Repeat1125 – 116440WD 2-6
Repeat1175 – 121238WD 2-7
Repeat1213 – 124836WD 2-8
Nucleotide binding154 – 1618ATP Potential
Region910 – 92112Interpropeller linker By similarity
Compositional bias95 – 984Poly-Ser

Sites

Binding site2651ATP By similarity

Natural variations

Alternative sequence99 – 10911Missing in isoform 2 and isoform 3.
VSP_006759
Alternative sequence319 – 33820GSPLV…FPNRW → VVERCHWGILTDLLHKWNQS in isoform 6.
VSP_008965
Alternative sequence339 – 1248910Missing in isoform 6.
VSP_008966
Alternative sequence5751E → ETLGFESKK in isoform 5.
VSP_006760
Alternative sequence824 – 86643Missing in isoform 3, isoform 4 and isoform 5.
VSP_006761
Alternative sequence1113 – 115442Missing in isoform 5.
VSP_006762

Experimental info

Mutagenesis1601K → R: No association with APAF-1. No binding to pro-caspase-9. Ref.4
Mutagenesis3681M → L: Activation of pro-caspase-9 independent of cytochrome c. Increased ability to induce apoptosis. Ref.4
Sequence conflict1341N → S Ref.11
Sequence conflict1451G → C in CAB55587. Ref.2
Sequence conflict1611S → F in CAB55586. Ref.2
Sequence conflict3701I → T in CAB55581. Ref.2
Sequence conflict3831Y → H in CAB55586. Ref.2
Sequence conflict5441F → L in CAB55584. Ref.2
Sequence conflict5801A → T in CAB55580. Ref.2
Sequence conflict6081R → C in CAB55585. Ref.2
Sequence conflict6201H → R in CAB55587. Ref.2
Sequence conflict6391L → F in CAB55583. Ref.2
Sequence conflict7081T → A in CAB55579. Ref.2
Sequence conflict7421H → R in CAB55584. Ref.2
Sequence conflict7461V → A in CAB55586. Ref.2
Sequence conflict7571L → P in CAB56462. Ref.2
Sequence conflict7951E → G in CAB55581. Ref.2
Sequence conflict7981E → G in CAB55587. Ref.2
Sequence conflict8251D → A in CAB55585. Ref.2
Sequence conflict8711S → L in CAB55587. Ref.2
Sequence conflict8761A → T in CAB55581. Ref.2
Sequence conflict9491I → V in CAB55585. Ref.2
Sequence conflict10081H → R in CAB55582. Ref.2
Sequence conflict10561S → P in CAB55582. Ref.2
Sequence conflict12411L → I in BAA24843. Ref.6

Secondary structure

............................................................................................. 1248
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (Apaf-1XL) [UniParc].

Last modified January 23, 2002. Version 2.
Checksum: 0750D05817AC9B3B

FASTA1,248141,840
        10         20         30         40         50         60 
MDAKARNCLL QHREALEKDI KTSYIMDHMI SDGFLTISEE EKVRNEPTQQ QRAAMLIKMI 

        70         80         90        100        110        120 
LKKDNDSYVS FYNALLHEGY KDLAALLHDG IPVVSSSSGK DSVSGITSYV RTVLCEGGVP 

       130        140        150        160        170        180 
QRPVVFVTRK KLVNAIQQKL SKLKGEPGWV TIHGMAGCGK SVLAAEAVRD HSLLEGCFPG 

       190        200        210        220        230        240 
GVHWVSVGKQ DKSGLLMKLQ NLCTRLDQDE SFSQRLPLNI EEAKDRLRIL MLRKHPRSLL 

       250        260        270        280        290        300 
ILDDVWDSWV LKAFDSQCQI LLTTRDKSVT DSVMGPKYVV PVESSLGKEK GLEILSLFVN 

       310        320        330        340        350        360 
MKKADLPEQA HSIIKECKGS PLVVSLIGAL LRDFPNRWEY YLKQLQNKQF KRIRKSSSYD 

       370        380        390        400        410        420 
YEALDEAMSI SVEMLREDIK DYYTDLSILQ KDVKVPTKVL CILWDMETEE VEDILQEFVN 

       430        440        450        460        470        480 
KSLLFCDRNG KSFRYYLHDL QVDFLTEKNC SQLQDLHKKI ITQFQRYHQP HTLSPDQEDC 

       490        500        510        520        530        540 
MYWYNFLAYH MASAKMHKEL CALMFSLDWI KAKTELVGPA HLIHEFVEYR HILDEKDCAV 

       550        560        570        580        590        600 
SENFQEFLSL NGHLLGRQPF PNIVQLGLCE PETSEVYQQA KLQAKQEVDN GMLYLEWINK 

       610        620        630        640        650        660 
KNITNLSRLV VRPHTDAVYH ACFSEDGQRI ASCGADKTLQ VFKAETGEKL LEIKAHEDEV 

       670        680        690        700        710        720 
LCCAFSTDDR FIATCSVDKK VKIWNSMTGE LVHTYDEHSE QVNCCHFTNS SHHLLLATGS 

       730        740        750        760        770        780 
SDCFLKLWDL NQKECRNTMF GHTNSVNHCR FSPDDKLLAS CSADGTLKLW DATSANERKS 

       790        800        810        820        830        840 
INVKQFFLNL EDPQEDMEVI VKCCSWSADG ARIMVAAKNK IFLFDIHTSG LLGEIHTGHH 

       850        860        870        880        890        900 
STIQYCDFSP QNHLAVVALS QYCVELWNTD SRSKVADCRG HLSWVHGVMF SPDGSSFLTS 

       910        920        930        940        950        960 
SDDQTIRLWE TKKVCKNSAV MLKQEVDVVF QENEVMVLAV DHIRRLQLIN GRTGQIDYLT 

       970        980        990       1000       1010       1020 
EAQVSCCCLS PHLQYIAFGD ENGAIEILEL VNNRIFQSRF QHKKTVWHIQ FTADEKTLIS 

      1030       1040       1050       1060       1070       1080 
SSDDAEIQVW NWQLDKCIFL RGHQETVKDF RLLKNSRLLS WSFDGTVKVW NIITGNKEKD 

      1090       1100       1110       1120       1130       1140 
FVCHQGTVLS CDISHDATKF SSTSADKTAK IWSFDLLLPL HELRGHNGCV RCSAFSVDST 

      1150       1160       1170       1180       1190       1200 
LLATGDDNGE IRIWNVSNGE LLHLCAPLSE EGAATHGGWV TDLCFSPDGK MLISAGGYIK 

      1210       1220       1230       1240 
WWNVVTGESS QTFYTNGTNL KKIHVSPDFK TYVTVDNLGI LYILQTLE 

« Hide

Isoform 2 (Apaf-1L) [UniParc].

Checksum: 0D3EF9AB2A66FFF5
Show »

FASTA1,237140,745
Isoform 3 (Apaf-1S) [UniParc].

Checksum: A675EA102DDAAFB7
Show »

FASTA1,194135,980
Isoform 4 (Apaf-1M) [UniParc].

Checksum: DA57B4E35E79D73A
Show »

FASTA1,205137,076
Isoform 5 (Apaf-1XS) [UniParc].

Checksum: CA9B14019EAB35BF
Show »

FASTA1,171133,356
Isoform 6 (Apaf-1-ALT) [UniParc].

Checksum: 29D933A65707ED92
Show »

FASTA33837,976

References

« Hide 'large scale' references
[1]"Apaf-1, a human protein homologous to C. elegans CED-4, participates in cytochrome c-dependent activation of caspase-3."
Zou H., Henzel W.J., Liu X., Lutschg A., Wang X.
Cell 90:405-413(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), PARTIAL PROTEIN SEQUENCE.
Tissue: Cervix carcinoma.
[2]"Three new types of Apaf-1 in mammalian cells."
Hahn C., Hirsch B., Jahnke D., Duerkop H., Stein H.
Biochem. Biophys. Res. Commun. 261:746-749(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 4 AND 5).
Tissue: Cervix carcinoma, Heart and Peripheral blood.
[3]"Cytochrome c and dATP-mediated oligomerization of Apaf-1 is a prerequisite for procaspase-9 activation."
Saleh A., Srinivasula S.M., Acharya S., Fishel R., Alnemri E.S.
J. Biol. Chem. 274:17941-17945(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Tissue: T-cell.
[4]"Role of cytochrome c and dATP/ATP hydrolysis in Apaf-1-mediated caspase-9 activation and apoptosis."
Hu Y., Benedict M.A., Ding L., Nunez G.
EMBO J. 18:3586-3595(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBUNIT, MUTAGENESIS OF LYS-160 AND MET-368.
Tissue: Kidney.
[5]"APAF-1-ALT, a novel alternative splicing form of APAF-1, potentially causes impeded ability of undergoing DNA damage-induced apoptosis in the LNCaP human prostate cancer cell line."
Ogawa T., Shiga K., Hashimoto S., Kobayashi T., Horii A., Furukawa T.
Biochem. Biophys. Res. Commun. 306:537-543(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 6), FUNCTION, SUBCELLULAR LOCATION.
Tissue: Prostatic carcinoma.
[6]"Prediction of the coding sequences of unidentified human genes. VIII. 78 new cDNA clones from brain which code for large proteins in vitro."
Ishikawa K., Nagase T., Nakajima D., Seki N., Ohira M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
DNA Res. 4:307-313(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Brain.
[7]"Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SEQUENCE REVISION.
[8]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]"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).
[10]"The mammalian CED4 homologue, APAF1, exists as two distinct forms in human cells."
Roberts D.L., Dalgleish R., Cohen G.M., MacFarlane M.
Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 810-864 AND 866-883.
[11]"Cloning of variant Apaf1."
Won M., Lee J.-W., Ohr H.-H., Kim D.-U., Chung K.-S., Lee M., Yoo H.-S.
Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-138 (ISOFORMS 1/4/5).
[12]"Autoactivation of procaspase-9 by Apaf-1-mediated oligomerization."
Srinivasula S.M., Ahmad M., Fernandes-Alnemri T., Alnemri E.S.
Mol. Cell 1:949-957(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: APAF-1-MEDIATED OLIGOMERIZATION.
[13]"Apaf-1 is a transcriptional target for E2F and p53."
Moroni M.C., Hickman E.S., Denchi E.L., Caprara G., Colli E., Cecconi F., Mueller H., Helin K.
Nat. Cell Biol. 3:552-558(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION BY E2F AND TP53.
[14]"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.
[15]"Calcium blocks formation of apoptosome by preventing nucleotide exchange in Apaf-1."
Bao Q., Lu W., Rabinowitz J.D., Shi Y.
Mol. Cell 25:181-192(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INHIBITION BY CALCIUM.
[16]"Integrity of ATP binding site is essential for effective inhibition of the intrinsic apoptosis pathway by NAIP."
Karimpour S., Davoodi J., Ghahremani M.H.
Biochem. Biophys. Res. Commun. 407:158-162(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NAIP/BIRC1.
[17]"Crystal structure of Apaf-1 caspase recruitment domain: an alpha-helical Greek key fold for apoptotic signaling."
Vaughn D.E., Rodriguez J., Lazebnik Y., Joshua-Tor L.
J. Mol. Biol. 293:439-447(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) OF 1-97.
[18]"Solution structure and mutagenesis of the caspase recruitment domain (CARD) from Apaf-1."
Day C.L., Dupont C., Lackmann M., Vaux D.L., Hinds M.G.
Cell Death Differ. 6:1125-1132(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 1-97.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRT03818.
RefSeqNP_001151.1. NM_001160.2.
NP_037361.1. NM_013229.2.
NP_863651.1. NM_181861.1.
NP_863658.1. NM_181868.1.
NP_863659.1. NM_181869.1.
UniGeneHs.552567.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
3YGSX-ray2.50C1-95[»]
ProteinModelPortalO14727.
SMRO14727. Positions 1-1248.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106814. 16 interactions.
DIPDIP-27624N.
IntActO14727. 6 interactions.
MINTMINT-96751.

Chemistry

BindingDBO14727.
ChEMBLCHEMBL1795093.
DrugBankDB00171. Adenosine triphosphate.

PTM databases

PhosphoSiteO14727.

Proteomic databases

PaxDbO14727.
PRIDEO14727.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000333991; 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]
GeneID317.
KEGGhsa:317.
UCSCuc001tfy.3. human. [O14727-2]
uc001tfz.3. human. [O14727-1]
uc001tga.3. human. [O14727-3]
uc001tgb.3. human. [O14727-4]
uc001tgc.3. human. [O14727-6]

Organism-specific databases

CTD317.
GeneCardsGC12P099039.
HGNCHGNC:576. APAF1.
HPAHPA031373.
MIM602233. gene.
neXtProtNX_O14727.
PharmGKBPA24868.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2319.
HOVERGENHBG018730.
InParanoidO14727.
KOK02084.
OMAKVCKNSA.
OrthoDBEOG7XWPMS.
PhylomeDBO14727.
TreeFamTF323866.

Enzyme and pathway databases

ReactomeREACT_578. Apoptosis.
SABIO-RKO14727.
SignaLinkO14727.

Gene expression databases

ArrayExpressO14727.
BgeeO14727.
GenevestigatorO14727.

Family and domain databases

Gene3D1.10.533.10. 1 hit.
2.130.10.10. 2 hits.
3.40.50.300. 1 hit.
InterProIPR017251. 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]
PfamPF00619. CARD. 1 hit.
PF00931. NB-ARC. 1 hit.
PF00400. WD40. 10 hits.
[Graphical view]
PIRSFPIRSF037646. Apop_pept_activating-1. 1 hit.
PRINTSPR00364. DISEASERSIST.
PR00320. GPROTEINBRPT.
SMARTSM00320. WD40. 13 hits.
[Graphical view]
SUPFAMSSF47986. SSF47986. 1 hit.
SSF50978. SSF50978. 2 hits.
SSF52540. SSF52540. 1 hit.
PROSITEPS50209. CARD. 1 hit.
PS00678. WD_REPEATS_1. 4 hits.
PS50082. WD_REPEATS_2. 9 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceO14727.
GeneWikiAPAF1.
GenomeRNAi317.
NextBio1287.
PMAP-CutDBO14727.
PROO14727.
SOURCESearch...

Entry information

Entry nameAPAF_HUMAN
AccessionPrimary (citable) accession number: O14727
Secondary accession number(s): B2RMX8 expand/collapse secondary AC list , O43297, Q7Z438, Q9BXZ6, Q9UBZ5, Q9UGN8, Q9UGN9, Q9UGP0, Q9UJ58, Q9UJ59, Q9UJ60, Q9UJ61, Q9UJ62, Q9UJ63, Q9UJ64, Q9UJ65, Q9UJ66, Q9UJ67, Q9UNC9
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 23, 2002
Last modified: April 16, 2014
This is version 165 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM