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UniProtKB/Swiss-Prot entry Q16611


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name BAK_HUMAN
Primary accession number Q16611
Secondary accession number Q92533
Integrated into Swiss-Prot on November 1, 1997
Sequence was last modified on November 1, 1996 (Sequence version 1)
Annotations were last modified on    June 16, 2009 (Entry version 107)
Name and origin of the protein
Protein name Bcl-2 homologous antagonist/killer
Synonyms Apoptosis regulator BAK
Bcl-2-like protein 7
Bcl2-L-7
Gene name
Name: BAK1
Synonyms: BAK, BCL2L7, CDN1
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=B-cell;
DOI=10.1038/374731a0; PubMed=7715729 [NCBI, ExPASy, EBI, Israel, Japan]
Farrow S.N., White J.H.M., Martinou I., Raven T., Pun K.-T., Grinham C.J., Martinou J.-C., Brown R.;
"Cloning of a bcl-2 homologue by interaction with adenovirus E1B 19K.";
Nature 374:731-733(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1038/374733a0; PubMed=7715730 [NCBI, ExPASy, EBI, Israel, Japan]
Chittenden T., Harrington E.A., O'Connor R., Flemington C., Lutz R.J., Evan G.I., Guild B.C.;
"Induction of apoptosis by the Bcl-2 homologue Bak.";
Nature 374:733-736(1995).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1038/374736a0; PubMed=7715731 [NCBI, ExPASy, EBI, Israel, Japan]
Kiefer M.C., Brauer M.J., Powers V.C., Wu J.J., Umansky S.R., Tomei L.D., Barr P.J.;
"Modulation of apoptosis by the widely distributed Bcl-2 homologue Bak.";
Nature 374:736-739(1995).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS VAL-28 AND ARG-69.
NIEHS SNPs program;
Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature02055; PubMed=14574404 [NCBI, ExPASy, EBI, Israel, Japan]
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lung;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 96-206.
Eguchi H., Hayashi S.;
"Estrogen alters expression of apoptosis-regulators, Bcl-2, Bcl-xL and Bak, as well as susceptibility to therapeutic agents of human breast cancer cells.";
Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases.
[8]
MUTAGENESIS, AND FUNCTION OF BH3 MOTIF.
PubMed=8521816 [NCBI, ExPASy, EBI, Israel, Japan]
Chittenden T., Flemington C., Houghton A.B., Ebb R.G., Gallo G.J., Elangovan B., Chinnadurai G., Lutz R.J.;
"A conserved domain in Bak, distinct from BH1 and BH2, mediates cell death and protein binding functions.";
EMBO J. 14:5589-5596(1995).
[9]
STRUCTURE BY NMR OF 72-87 IN COMPLEX WITH BCL2L1 ISOFORM BCL-X(L).
DOI=10.1126/science.275.5302.983; PubMed=9020082 [NCBI, ExPASy, EBI, Israel, Japan]
Sattler M., Liang H., Nettesheim D., Meadows R.P., Harlan J.E., Eberstadt M., Yoon H.S., Shuker S.B., Chang B.S., Minn A.J., Thompson C.B., Fesik S.W.;
"Structure of Bcl-xL-Bak peptide complex: recognition between regulators of apoptosis.";
Science 275:983-986(1997).
[10]
X-RAY CRYSTALLOGRAPHY (1.48 ANGSTROMS) OF 16-186, FUNCTION, SUBUNIT, MUTAGENESIS OF HIS-164, AND ZINC BINDING.
DOI=10.1016/j.molcel.2006.10.014; PubMed=17157251 [NCBI, ExPASy, EBI, Israel, Japan]
Moldoveanu T., Liu Q., Tocilj A., Watson M., Shore G., Gehring K.;
"The X-ray structure of a BAK homodimer reveals an inhibitory zinc binding site.";
Mol. Cell 24:677-688(2006).
[11]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RIKEN structural genomics initiative (RSGI);
"Crystal structure of MS0836.";
Submitted (APR-2008) to the PDB data bank.
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X84213; CAA58997.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U23765; AAA93066.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U16811; AAA74466.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY260471; AAO74828.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z93017; CAB65626.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC004431; AAH04431.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
D88397; BAA13606.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00011420; -.
PIR S58873; S58873.
RefSeq NP_001179.1; -.
UniGene Hs.485139
3D structure databases
PDB
1BXL; NMR; -; B=72-87.[ExPASy / RCSB / EBI]
2IMS; X-ray; 1.48 A; A=16-186.[ExPASy / RCSB / EBI]
2IMT; X-ray; 1.49 A; A=16-186.[ExPASy / RCSB / EBI]
2JCN; X-ray; 1.80 A; A=21-190.[ExPASy / RCSB / EBI]
2YV6; X-ray; 2.50 A; A=23-185.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1BXL; -.
2IMS; -.
2IMT; -.
2JCN; -.
2YV6; -.
ModBase Q16611.
Protein-protein interaction databases
DIP DIP:935N; -.
IntAct Q16611; 18.
Enzyme and pathway databases
Reactome REACT_578; Apoptosis.
Organism-specific databases
GeneCards GC06M033648; -.
H-InvDB HIX0005780; -.
HIX0040824; -.
HIX0058969; -.
HGNC HGNC:949; BAK1.
GenAtlas BAK1.
HPA CAB005029; -.
MIM 600516; gene. [NCBI / EBI]
PharmGKB PA25253; -.
Gene expression databases
Bgee Q16611; -.
CleanEx HS_BAK1; -.
GermOnline ENSG00000030110; Homo sapiens.
Ontologies
GO
GO:0005741; Cellular component: mitochondrial outer membrane (inferred from experiment from Reactome).
GO:0046930; Cellular component: pore complex (inferred from direct assay from HGNC).
GO:0042802; Molecular function: identical protein binding (inferred from physical interaction from IntAct).
GO:0046982; Molecular function: protein heterodimerization activity (inferred from physical interaction from UniProtKB).
GO:0008270; Molecular function: zinc ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0010248; Biological process: establishment or maintenance of transmembrane electrochemical gradient (inferred from direct assay from HGNC).
GO:0006917; Biological process: induction of apoptosis (traceable author statement from UniProtKB).
GO:0046902; Biological process: regulation of mitochondrial membrane permeability (inferred from direct assay from HGNC).
GO:0051881; Biological process: regulation of mitochondrial membrane potential (inferred from direct assay from HGNC).
GO:0043497; Biological process: regulation of protein heterodimerization activity (inferred from direct assay from HGNC).
GO:0043496; Biological process: regulation of protein homodimerization activity (inferred from direct assay from HGNC).
GO:0001836; Biological process: release of cytochrome c from mitochondria (inferred from direct assay from HGNC).
QuickGo view.
Family and domain databases
InterPro IPR002475; BCL2_apoptsis.
IPR000712; Bcl2_BH.
Graphical view of domain structure.
Pfam PF00452; Bcl-2; 1.
Pfam graphical view of domain structure.
PRINTS PR01862; BCL2FAMILY.
SMART SM00337; BCL; 1.
SMART graphical view of domain structure.
PROSITE PS50062; BCL2_FAMILY; 1.
PS01080; BH1; 1.
PS01258; BH2; 1.
PS01259; BH3; 1.
PROSITE graphical view of domain structure (profiles).
Proteomic databases
PRIDE Q16611; -.
Genome annotation databases
Ensembl ENSG00000030110; Homo sapiens. [Contig view]
GeneID 578; -.
KEGG hsa:578; -.
Phylogenomic databases
HOVERGEN Q16611; -.
OMA Q16611; NAYELFT.
Other
NextBio 2359; -.
SOURCE BAK1; Homo sapiens.
ProtoNet Q16611.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Apoptosis; Membrane; Metal-binding; Polymorphism; Transmembrane; Zinc.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   211  211     Bcl-2 homologous antagonist/killer. PRO_0000143059
TRANSMEM   188   205  18     Potential. 
MOTIF   74    88  15     BH3. 
MOTIF   117   136  20     BH1. 
MOTIF   169   184  16     BH2. 
METAL   160   160        Zinc; shared with dimeric partner. 
METAL   164   164        Zinc; shared with dimeric partner. 
VARIANT   28    28  1     A -> V (in dbSNP:rs4987115 [NCBI]). VAR_018829 [3D]
VARIANT   42    42  1     R -> H (in dbSNP:rs1051911 [NCBI]). VAR_048417 [3D]
VARIANT   69    69  1     S -> R (in dbSNP:rs5745592 [NCBI]). VAR_018830 [3D]
MUTAGEN   164   164        H->A: Strongly reduced zinc binding and homodimerization. 
HELIX   24    50  27      
HELIX   51    53  3      
HELIX   59    62  4      
HELIX   70    85  16      
HELIX   87    97  11      
HELIX   104   118  15      
TURN   119   121  3      
HELIX   125   144  20      
HELIX   151   164  14      
HELIX   167   173  7      
HELIX   177   180  4      
Sequence information
Length: 211 AA [This is the length of the unprocessed precursor] Molecular weight: 23409 Da [This is the MW of the unprocessed precursor] CRC64: A2200FE72A46D04E [This is a checksum on the sequence]
        10         20         30         40         50         60 
MASGQGPGPP RQECGEPALP SASEEQVAQD TEEVFRSYVF YRHQQEQEAE GVAAPADPEM 

        70         80         90        100        110        120 
VTLPLQPSST MGQVGRQLAI IGDDINRRYD SEFQTMLQHL QPTAENAYEY FTKIATSLFE 

       130        140        150        160        170        180 
SGINWGRVVA LLGFGYRLAL HVYQHGLTGF LGQVTRFVVD FMLHHCIARW IAQRGGWVAA 

       190        200        210 
LNLGNGPILN VLVVLGVVLL GQFVVRRFFK S 

Q16611 in FASTA format

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