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Q16611

- BAK_HUMAN

UniProt

Q16611 - BAK_HUMAN

Protein

Bcl-2 homologous antagonist/killer

Gene

BAK1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 166 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    Functioni

    In the presence of an appropriate stimulus, accelerates programmed cell death by binding to, and antagonizing the anti-apoptotic action of BCL2 or its adenovirus homolog E1B 19k protein. Low micromolar levels of zinc ions inhibit the promotion of apoptosis.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi160 – 1601Zinc; shared with dimeric partner
    Metal bindingi164 – 1641Zinc; shared with dimeric partner

    GO - Molecular functioni

    1. identical protein binding Source: IntAct
    2. metal ion binding Source: UniProtKB-KW
    3. protein binding Source: UniProtKB
    4. protein heterodimerization activity Source: UniProtKB
    5. protein homodimerization activity Source: RefGenome

    GO - Biological processi

    1. activation of cysteine-type endopeptidase activity Source: BHF-UCL
    2. activation of cysteine-type endopeptidase activity involved in apoptotic process by cytochrome c Source: Ensembl
    3. aging Source: Ensembl
    4. apoptotic process Source: Reactome
    5. apoptotic process involved in patterning of blood vessels Source: Ensembl
    6. apoptotic signaling pathway Source: UniProtKB
    7. B cell apoptotic process Source: Ensembl
    8. B cell homeostasis Source: Ensembl
    9. B cell negative selection Source: Ensembl
    10. blood vessel remodeling Source: Ensembl
    11. brain development Source: Ensembl
    12. cell proliferation Source: Ensembl
    13. cellular response to mechanical stimulus Source: UniProtKB
    14. cellular response to UV Source: UniProtKB
    15. endocrine pancreas development Source: Ensembl
    16. endoplasmic reticulum calcium ion homeostasis Source: UniProtKB
    17. establishment or maintenance of transmembrane electrochemical gradient Source: HGNC
    18. extrinsic apoptotic signaling pathway in absence of ligand Source: RefGenome
    19. fibroblast apoptotic process Source: Ensembl
    20. intrinsic apoptotic signaling pathway Source: Reactome
    21. intrinsic apoptotic signaling pathway in response to DNA damage Source: RefGenome
    22. intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress Source: Ensembl
    23. limb morphogenesis Source: Ensembl
    24. mitochondrial fusion Source: Ensembl
    25. myeloid cell homeostasis Source: Ensembl
    26. negative regulation of cell proliferation Source: Ensembl
    27. negative regulation of endoplasmic reticulum calcium ion concentration Source: Ensembl
    28. negative regulation of gene expression Source: Ensembl
    29. negative regulation of peptidyl-serine phosphorylation Source: Ensembl
    30. organ regeneration Source: Ensembl
    31. positive regulation of apoptotic process Source: UniProtKB
    32. positive regulation of calcium ion transport into cytosol Source: Ensembl
    33. positive regulation of endoplasmic reticulum unfolded protein response Source: UniProtKB
    34. positive regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway Source: Reactome
    35. positive regulation of proteolysis Source: BHF-UCL
    36. positive regulation of release of cytochrome c from mitochondria Source: Ensembl
    37. post-embryonic camera-type eye morphogenesis Source: Ensembl
    38. regulation of cell cycle Source: Ensembl
    39. regulation of mitochondrial membrane permeability Source: BHF-UCL
    40. regulation of mitochondrial membrane potential Source: HGNC
    41. regulation of protein heterodimerization activity Source: HGNC
    42. regulation of protein homodimerization activity Source: HGNC
    43. release of cytochrome c from mitochondria Source: BHF-UCL
    44. response to drug Source: Ensembl
    45. response to ethanol Source: Ensembl
    46. response to fungus Source: Ensembl
    47. response to gamma radiation Source: Ensembl
    48. response to hydrogen peroxide Source: Ensembl
    49. response to mycotoxin Source: Ensembl
    50. response to organic cyclic compound Source: Ensembl
    51. response to UV-C Source: Ensembl
    52. thymocyte apoptotic process Source: Ensembl
    53. vagina development Source: Ensembl

    Keywords - Biological processi

    Apoptosis

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_707. Activation and oligomerization of BAK protein.

    Protein family/group databases

    TCDBi1.A.21.1.3. the bcl-2 (bcl-2) family.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Bcl-2 homologous antagonist/killer
    Alternative name(s):
    Apoptosis regulator BAK
    Bcl-2-like protein 7
    Short name:
    Bcl2-L-7
    Gene namesi
    Name:BAK1
    Synonyms:BAK, BCL2L7, CDN1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:949. BAK1.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Ensembl
    2. endoplasmic reticulum Source: Ensembl
    3. integral component of mitochondrial outer membrane Source: BHF-UCL
    4. mitochondrial outer membrane Source: RefGenome
    5. mitochondrion Source: HGNC
    6. pore complex Source: HGNC

    Keywords - Cellular componenti

    Membrane, Mitochondrion

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi164 – 1641H → A: Strongly reduced zinc binding and homodimerization. 2 Publications

    Organism-specific databases

    PharmGKBiPA25253.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 211210Bcl-2 homologous antagonist/killerPRO_0000143059Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ16611.
    PaxDbiQ16611.
    PRIDEiQ16611.

    PTM databases

    PhosphoSiteiQ16611.

    Expressioni

    Tissue specificityi

    Expressed in a wide variety of tissues, with highest levels in the heart and skeletal muscle.

    Gene expression databases

    ArrayExpressiQ16611.
    BgeeiQ16611.
    CleanExiHS_BAK1.
    GenevestigatoriQ16611.

    Organism-specific databases

    HPAiCAB005029.

    Interactioni

    Subunit structurei

    Interacts with BCL2A1 By similarity. Homodimer. Formation of the homodimer is zinc-dependent. Forms heterodimers with BCL2, E1B 19k protein, and BCL2L1 isoform Bcl-X(L). Interacts with myxoma virus protein M11L. Interacts with BOP/C22orf29.By similarity4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself5EBI-519866,EBI-519866
    BAXQ078125EBI-519866,EBI-516580
    BCL2L1Q078173EBI-519866,EBI-78035
    BCL2L1Q07817-110EBI-519866,EBI-287195
    BIDP559572EBI-519866,EBI-519672
    MCL1Q0782010EBI-519866,EBI-1003422
    Mcl1P972873EBI-519866,EBI-707292From a different organism.
    VACWR040P243566EBI-519866,EBI-8041400From a different organism.

    Protein-protein interaction databases

    BioGridi107054. 26 interactions.
    DIPiDIP-935N.
    IntActiQ16611. 16 interactions.
    MINTiMINT-96576.
    STRINGi9606.ENSP00000363591.

    Structurei

    Secondary structure

    1
    211
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi24 – 5027
    Helixi51 – 533
    Helixi59 – 624
    Helixi70 – 8516
    Helixi87 – 9711
    Turni98 – 1003
    Helixi104 – 11815
    Turni119 – 1213
    Helixi125 – 14420
    Helixi151 – 16414
    Helixi167 – 1737
    Helixi177 – 1804

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1BXLNMR-B72-87[»]
    2IMSX-ray1.48A16-186[»]
    2IMTX-ray1.49A16-186[»]
    2JBYX-ray2.41B67-92[»]
    2JCNX-ray1.80A21-190[»]
    2M5BNMR-A18-186[»]
    2XPXX-ray2.05B67-92[»]
    2YV6X-ray2.50A23-185[»]
    3I1HX-ray2.20B72-87[»]
    3QBRX-ray2.60B/Y63-96[»]
    4D2LX-ray2.90B67-91[»]
    ProteinModelPortaliQ16611.
    SMRiQ16611. Positions 19-181.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ16611.

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei188 – 20518HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi74 – 8815BH3Add
    BLAST
    Motifi117 – 13620BH1Add
    BLAST
    Motifi169 – 18416BH2Add
    BLAST

    Domaini

    Intact BH3 motif is required by BIK, BID, BAK, BAD and BAX for their pro-apoptotic activity and for their interaction with anti-apoptotic members of the Bcl-2 family.

    Sequence similaritiesi

    Belongs to the Bcl-2 family.Curated

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG145601.
    HOGENOMiHOG000006521.
    HOVERGENiHBG002674.
    InParanoidiQ16611.
    KOiK14021.
    OMAiGDDINQR.
    OrthoDBiEOG70GMGD.
    PhylomeDBiQ16611.
    TreeFamiTF315834.

    Family and domain databases

    InterProiIPR026308. BAK.
    IPR002475. Bcl2-like.
    IPR020717. Bcl2_BH1_motif_CS.
    IPR020726. Bcl2_BH2_motif_CS.
    IPR020728. Bcl2_BH3_motif_CS.
    IPR026298. Blc2_fam.
    [Graphical view]
    PANTHERiPTHR11256. PTHR11256. 1 hit.
    PTHR11256:SF41. PTHR11256:SF41. 1 hit.
    PfamiPF00452. Bcl-2. 1 hit.
    [Graphical view]
    PRINTSiPR01862. BCL2FAMILY.
    PROSITEiPS50062. BCL2_FAMILY. 1 hit.
    PS01080. BH1. 1 hit.
    PS01258. BH2. 1 hit.
    PS01259. BH3. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q16611-1) [UniParc]FASTAAdd to Basket

    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

    MASGQGPGPP RQECGEPALP SASEEQVAQD TEEVFRSYVF YRHQQEQEAE    50
    GVAAPADPEM VTLPLQPSST MGQVGRQLAI IGDDINRRYD SEFQTMLQHL 100
    QPTAENAYEY FTKIATSLFE SGINWGRVVA LLGFGYRLAL HVYQHGLTGF 150
    LGQVTRFVVD FMLHHCIARW IAQRGGWVAA LNLGNGPILN VLVVLGVVLL 200
    GQFVVRRFFK S 211
    Length:211
    Mass (Da):23,409
    Last modified:November 1, 1996 - v1
    Checksum:iA2200FE72A46D04E
    GO
    Isoform 2 (identifier: Q16611-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         117-153: SLFESGINWGRVVALLGFGYRLALHVYQHGLTGFLGQ → RPAATPTACLRVASIGAVWWLFWASATVWPYTSTSMA
         154-211: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:153
    Mass (Da):16,872
    Checksum:iE047A2DEE63C2E95
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti28 – 281A → V.1 Publication
    Corresponds to variant rs4987115 [ dbSNP | Ensembl ].
    VAR_018829
    Natural varianti42 – 421R → H.
    Corresponds to variant rs1051911 [ dbSNP | Ensembl ].
    VAR_048417
    Natural varianti69 – 691S → R.1 Publication
    Corresponds to variant rs5745592 [ dbSNP | Ensembl ].
    VAR_018830

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei117 – 15337SLFES…GFLGQ → RPAATPTACLRVASIGAVWW LFWASATVWPYTSTSMA in isoform 2. 1 PublicationVSP_056551Add
    BLAST
    Alternative sequencei154 – 21158Missing in isoform 2. 1 PublicationVSP_056552Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X84213 mRNA. Translation: CAA58997.1.
    U23765 mRNA. Translation: AAA93066.1.
    U16811 mRNA. Translation: AAA74466.1.
    AY260471 Genomic DNA. Translation: AAO74828.1.
    CR457419 mRNA. Translation: CAG33700.1.
    Z93017 Genomic DNA. Translation: CAB65626.1.
    CH471081 Genomic DNA. Translation: EAX03740.1.
    CH471081 Genomic DNA. Translation: EAX03742.1.
    BC004431 mRNA. Translation: AAH04431.1.
    BC110337 mRNA. Translation: AAI10338.1.
    D88397 Genomic DNA. Translation: BAA13606.1.
    CCDSiCCDS4781.1.
    PIRiS58873.
    RefSeqiNP_001179.1. NM_001188.3.
    UniGeneiHs.485139.

    Genome annotation databases

    EnsembliENST00000360661; ENSP00000353878; ENSG00000030110.
    ENST00000374467; ENSP00000363591; ENSG00000030110.
    ENST00000442998; ENSP00000391258; ENSG00000030110.
    GeneIDi578.
    KEGGihsa:578.
    UCSCiuc003oer.3. human.

    Polymorphism databases

    DMDMi2493274.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs
    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X84213 mRNA. Translation: CAA58997.1 .
    U23765 mRNA. Translation: AAA93066.1 .
    U16811 mRNA. Translation: AAA74466.1 .
    AY260471 Genomic DNA. Translation: AAO74828.1 .
    CR457419 mRNA. Translation: CAG33700.1 .
    Z93017 Genomic DNA. Translation: CAB65626.1 .
    CH471081 Genomic DNA. Translation: EAX03740.1 .
    CH471081 Genomic DNA. Translation: EAX03742.1 .
    BC004431 mRNA. Translation: AAH04431.1 .
    BC110337 mRNA. Translation: AAI10338.1 .
    D88397 Genomic DNA. Translation: BAA13606.1 .
    CCDSi CCDS4781.1.
    PIRi S58873.
    RefSeqi NP_001179.1. NM_001188.3.
    UniGenei Hs.485139.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1BXL NMR - B 72-87 [» ]
    2IMS X-ray 1.48 A 16-186 [» ]
    2IMT X-ray 1.49 A 16-186 [» ]
    2JBY X-ray 2.41 B 67-92 [» ]
    2JCN X-ray 1.80 A 21-190 [» ]
    2M5B NMR - A 18-186 [» ]
    2XPX X-ray 2.05 B 67-92 [» ]
    2YV6 X-ray 2.50 A 23-185 [» ]
    3I1H X-ray 2.20 B 72-87 [» ]
    3QBR X-ray 2.60 B/Y 63-96 [» ]
    4D2L X-ray 2.90 B 67-91 [» ]
    ProteinModelPortali Q16611.
    SMRi Q16611. Positions 19-181.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107054. 26 interactions.
    DIPi DIP-935N.
    IntActi Q16611. 16 interactions.
    MINTi MINT-96576.
    STRINGi 9606.ENSP00000363591.

    Chemistry

    BindingDBi Q16611.
    ChEMBLi CHEMBL5609.

    Protein family/group databases

    TCDBi 1.A.21.1.3. the bcl-2 (bcl-2) family.

    PTM databases

    PhosphoSitei Q16611.

    Polymorphism databases

    DMDMi 2493274.

    Proteomic databases

    MaxQBi Q16611.
    PaxDbi Q16611.
    PRIDEi Q16611.

    Protocols and materials databases

    DNASUi 578.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000360661 ; ENSP00000353878 ; ENSG00000030110 .
    ENST00000374467 ; ENSP00000363591 ; ENSG00000030110 .
    ENST00000442998 ; ENSP00000391258 ; ENSG00000030110 .
    GeneIDi 578.
    KEGGi hsa:578.
    UCSCi uc003oer.3. human.

    Organism-specific databases

    CTDi 578.
    GeneCardsi GC06M033541.
    HGNCi HGNC:949. BAK1.
    HPAi CAB005029.
    MIMi 600516. gene.
    neXtProti NX_Q16611.
    PharmGKBi PA25253.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG145601.
    HOGENOMi HOG000006521.
    HOVERGENi HBG002674.
    InParanoidi Q16611.
    KOi K14021.
    OMAi GDDINQR.
    OrthoDBi EOG70GMGD.
    PhylomeDBi Q16611.
    TreeFami TF315834.

    Enzyme and pathway databases

    Reactomei REACT_707. Activation and oligomerization of BAK protein.

    Miscellaneous databases

    EvolutionaryTracei Q16611.
    GeneWikii Bcl-2_homologous_antagonist_killer.
    GenomeRNAii 578.
    NextBioi 2359.
    PROi Q16611.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q16611.
    Bgeei Q16611.
    CleanExi HS_BAK1.
    Genevestigatori Q16611.

    Family and domain databases

    InterProi IPR026308. BAK.
    IPR002475. Bcl2-like.
    IPR020717. Bcl2_BH1_motif_CS.
    IPR020726. Bcl2_BH2_motif_CS.
    IPR020728. Bcl2_BH3_motif_CS.
    IPR026298. Blc2_fam.
    [Graphical view ]
    PANTHERi PTHR11256. PTHR11256. 1 hit.
    PTHR11256:SF41. PTHR11256:SF41. 1 hit.
    Pfami PF00452. Bcl-2. 1 hit.
    [Graphical view ]
    PRINTSi PR01862. BCL2FAMILY.
    PROSITEi PS50062. BCL2_FAMILY. 1 hit.
    PS01080. BH1. 1 hit.
    PS01258. BH2. 1 hit.
    PS01259. BH3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning of a bcl-2 homologue by interaction with adenovirus E1B 19K."
      Farrow S.N., White J.H.M., Martinou I., Raven T., Pun K.-T., Grinham C.J., Martinou J.-C., Brown R.
      Nature 374:731-733(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: B-cell.
    2. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    3. "Modulation of apoptosis by the widely distributed Bcl-2 homologue Bak."
      Kiefer M.C., Brauer M.J., Powers V.C., Wu J.J., Umansky S.R., Tomei L.D., Barr P.J.
      Nature 374:736-739(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    4. NIEHS SNPs program
      Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS VAL-28 AND ARG-69.
    5. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    6. "The DNA sequence and analysis of human chromosome 6."
      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.
      Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "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] (ISOFORMS 1 AND 2).
      Tissue: Brain and Lung.
    9. "Estrogen alters expression of apoptosis-regulators, Bcl-2, Bcl-xL and Bak, as well as susceptibility to therapeutic agents of human breast cancer cells."
      Eguchi H., Hayashi S.
      Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 96-206.
    10. "A conserved domain in Bak, distinct from BH1 and BH2, mediates cell death and protein binding functions."
      Chittenden T., Flemington C., Houghton A.B., Ebb R.G., Gallo G.J., Elangovan B., Chinnadurai G., Lutz R.J.
      EMBO J. 14:5589-5596(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS, FUNCTION OF BH3 MOTIF.
    11. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "Human Bop is a novel BH3-only member of the Bcl-2 protein family."
      Zhang X., Weng C., Li Y., Wang X., Jiang C., Li X., Xu Y., Chen Q., Pan L., Tang H.
      Protein Cell 3:790-801(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH BOP/C22ORF29.
    14. "Structure of Bcl-xL-Bak peptide complex: recognition between regulators of apoptosis."
      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.
      Science 275:983-986(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 72-87 IN COMPLEX WITH BCL2L1 ISOFORM BCL-X(L).
    15. "The X-ray structure of a BAK homodimer reveals an inhibitory zinc binding site."
      Moldoveanu T., Liu Q., Tocilj A., Watson M., Shore G., Gehring K.
      Mol. Cell 24:677-688(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.48 ANGSTROMS) OF 16-186, FUNCTION, SUBUNIT, MUTAGENESIS OF HIS-164, ZINC-BINDING.
    16. "A structural viral mimic of prosurvival Bcl-2: a pivotal role for sequestering proapoptotic Bax and Bak."
      Kvansakul M., van Delft M.F., Lee E.F., Gulbis J.M., Fairlie W.D., Huang D.C.S., Colman P.M.
      Mol. Cell 25:933-942(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.41 ANGSTROMS) OF 67-92 IN COMPLEX WITH MYXOMA VIRUS PROTEIN M11L.
    17. "Crystal structure of MS0836."
      RIKEN structural genomics initiative (RSGI)
      Submitted (APR-2008) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).

    Entry informationi

    Entry nameiBAK_HUMAN
    AccessioniPrimary (citable) accession number: Q16611
    Secondary accession number(s): C0H5Y7, Q6I9T6, Q92533
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 166 of the entry and version 1 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

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 6
      Human chromosome 6: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3