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Protein

Bcl-2 homologous antagonist/killer

Gene

BAK1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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

  • identical protein binding Source: IntAct
  • metal ion binding Source: UniProtKB-KW
  • protein heterodimerization activity Source: UniProtKB
  • protein homodimerization activity Source: GO_Central

GO - Biological processi

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 Componenti: Chromosome 6

Organism-specific databases

HGNCiHGNC:949. BAK1.

Subcellular locationi

Topology

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

GO - Cellular componenti

  • cytosol Source: Ensembl
  • endoplasmic reticulum Source: Ensembl
  • integral component of mitochondrial outer membrane Source: BHF-UCL
  • mitochondrial outer membrane Source: GO_Central
  • mitochondrion Source: HGNC
  • 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.

Polymorphism and mutation databases

BioMutaiBAK1.
DMDMi2493274.

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.
GenevisibleiQ16611. HS.

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
BCL2A1Q165483EBI-519866,EBI-1003550
BCL2L1Q078173EBI-519866,EBI-78035
BCL2L1Q07817-110EBI-519866,EBI-287195
BCL2L2Q928435EBI-519866,EBI-707714
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. 29 interactions.
DIPiDIP-935N.
IntActiQ16611. 18 interactions.
MINTiMINT-96576.
STRINGi9606.ENSP00000353878.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BXLNMR-B72-87[»]
2IMSX-ray1.48A16-186[»]
2IMTX-ray1.49A16-186[»]
2JBYX-ray2.41B67-92[»]
2JCNX-ray1.80A21-190[»]
2LP8NMR-B72-87[»]
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[»]
5AJKX-ray2.55B/D/F/H/J/L67-92[»]
ProteinModelPortaliQ16611.
SMRiQ16611. Positions 19-181.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ16611.

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.
OMAiFQAMLQH.
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. AlignAdd to basket

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:
EMBLi
GenBanki
DDBJi
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. [Q16611-1]
XP_011513081.1. XM_011514779.1. [Q16611-1]
UniGeneiHs.485139.

Genome annotation databases

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

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:
EMBLi
GenBanki
DDBJi
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. [Q16611-1]
XP_011513081.1. XM_011514779.1. [Q16611-1]
UniGeneiHs.485139.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BXLNMR-B72-87[»]
2IMSX-ray1.48A16-186[»]
2IMTX-ray1.49A16-186[»]
2JBYX-ray2.41B67-92[»]
2JCNX-ray1.80A21-190[»]
2LP8NMR-B72-87[»]
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[»]
5AJKX-ray2.55B/D/F/H/J/L67-92[»]
ProteinModelPortaliQ16611.
SMRiQ16611. Positions 19-181.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107054. 29 interactions.
DIPiDIP-935N.
IntActiQ16611. 18 interactions.
MINTiMINT-96576.
STRINGi9606.ENSP00000353878.

Chemistry

ChEMBLiCHEMBL5609.

Protein family/group databases

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

PTM databases

PhosphoSiteiQ16611.

Polymorphism and mutation databases

BioMutaiBAK1.
DMDMi2493274.

Proteomic databases

MaxQBiQ16611.
PaxDbiQ16611.
PRIDEiQ16611.

Protocols and materials databases

DNASUi578.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi578.
GeneCardsiGC06M033541.
HGNCiHGNC:949. BAK1.
HPAiCAB005029.
MIMi600516. gene.
neXtProtiNX_Q16611.
PharmGKBiPA25253.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG145601.
GeneTreeiENSGT00530000062935.
HOGENOMiHOG000006521.
HOVERGENiHBG002674.
InParanoidiQ16611.
KOiK14021.
OMAiFQAMLQH.
OrthoDBiEOG70GMGD.
PhylomeDBiQ16611.
TreeFamiTF315834.

Enzyme and pathway databases

ReactomeiREACT_707. Activation and oligomerization of BAK protein.

Miscellaneous databases

EvolutionaryTraceiQ16611.
GeneWikiiBcl-2_homologous_antagonist_killer.
GenomeRNAii578.
NextBioi2359.
PROiQ16611.
SOURCEiSearch...

Gene expression databases

BgeeiQ16611.
CleanExiHS_BAK1.
ExpressionAtlasiQ16611. baseline and differential.
GenevisibleiQ16611. HS.

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]
ProtoNetiSearch...

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: July 22, 2015
This is version 176 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

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 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.