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Q16611

- BAK_HUMAN

UniProt

Q16611 - BAK_HUMAN

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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

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 heterodimerization activity Source: UniProtKB
  4. 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
Complete GO annotation...

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
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi164 – 1641H → A: Strongly reduced zinc binding and homodimerization. 1 Publication

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

BgeeiQ16611.
CleanExiHS_BAK1.
ExpressionAtlasiQ16611. baseline and differential.
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[»]
4U2UX-ray2.90A/B23-186[»]
4U2VX-ray2.30A/B/C/D68-148[»]
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.
GeneTreeiENSGT00530000062935.
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

        10         20         30         40         50
MASGQGPGPP RQECGEPALP SASEEQVAQD TEEVFRSYVF YRHQQEQEAE
60 70 80 90 100
GVAAPADPEM VTLPLQPSST MGQVGRQLAI IGDDINRRYD SEFQTMLQHL
110 120 130 140 150
QPTAENAYEY FTKIATSLFE SGINWGRVVA LLGFGYRLAL HVYQHGLTGF
160 170 180 190 200
LGQVTRFVVD FMLHHCIARW IAQRGGWVAA LNLGNGPILN VLVVLGVVLL
210
GQFVVRRFFK S
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. [Q16611-1]
PIRiS58873.
RefSeqiNP_001179.1. NM_001188.3.
UniGeneiHs.485139.

Genome annotation databases

EnsembliENST00000374467; ENSP00000363591; ENSG00000030110. [Q16611-1]
ENST00000442998; ENSP00000391258; ENSG00000030110. [Q16611-2]
GeneIDi578.
KEGGihsa:578.
UCSCiuc003oer.3. human. [Q16611-1]

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. [Q16611-1 ]
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 [» ]
4U2U X-ray 2.90 A/B 23-186 [» ]
4U2V X-ray 2.30 A/B/C/D 68-148 [» ]
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 ENST00000374467 ; ENSP00000363591 ; ENSG00000030110 . [Q16611-1 ]
ENST00000442998 ; ENSP00000391258 ; ENSG00000030110 . [Q16611-2 ]
GeneIDi 578.
KEGGi hsa:578.
UCSCi uc003oer.3. human. [Q16611-1 ]

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.
GeneTreei ENSGT00530000062935.
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

Bgeei Q16611.
CleanExi HS_BAK1.
ExpressionAtlasi Q16611. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 167 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