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Q92934

- BAD_HUMAN

UniProt

Q92934 - BAD_HUMAN

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Protein

Bcl2-associated agonist of cell death

Gene
BAD, BBC6, BCL2L8
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Promotes cell death. Successfully competes for the binding to Bcl-X(L), Bcl-2 and Bcl-W, thereby affecting the level of heterodimerization of these proteins with BAX. Can reverse the death repressor activity of Bcl-X(L), but not that of Bcl-2 By similarity. Appears to act as a link between growth factor receptor signaling and the apoptotic pathways.

GO - Molecular functioni

  1. cysteine-type endopeptidase activator activity involved in apoptotic process Source: UniProtKB
  2. lipid binding Source: UniProtKB
  3. phospholipid binding Source: UniProtKB
  4. protein binding Source: UniProtKB
  5. protein kinase binding Source: UniProtKB

GO - Biological processi

  1. activation of cysteine-type endopeptidase activity Source: BHF-UCL
  2. activation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
  3. ADP metabolic process Source: UniProtKB
  4. apoptotic process Source: UniProtKB
  5. apoptotic signaling pathway Source: Reactome
  6. ATP metabolic process Source: UniProtKB
  7. cellular process regulating host cell cycle in response to virus Source: Ensembl
  8. cellular response to chromate Source: Ensembl
  9. cellular response to hypoxia Source: UniProtKB
  10. cellular response to lipid Source: Ensembl
  11. cellular response to mechanical stimulus Source: UniProtKB
  12. cellular response to nicotine Source: UniProtKB
  13. cytokine-mediated signaling pathway Source: Ensembl
  14. epidermal growth factor receptor signaling pathway Source: Reactome
  15. extrinsic apoptotic signaling pathway Source: UniProtKB
  16. extrinsic apoptotic signaling pathway in absence of ligand Source: Ensembl
  17. extrinsic apoptotic signaling pathway via death domain receptors Source: Ensembl
  18. Fc-epsilon receptor signaling pathway Source: Reactome
  19. fibroblast growth factor receptor signaling pathway Source: Reactome
  20. glucose catabolic process Source: Ensembl
  21. glucose homeostasis Source: UniProtKB
  22. innate immune response Source: Reactome
  23. intrinsic apoptotic signaling pathway Source: UniProtKB
  24. intrinsic apoptotic signaling pathway in response to DNA damage Source: Ensembl
  25. neurotrophin TRK receptor signaling pathway Source: Reactome
  26. phosphatidylinositol-mediated signaling Source: Reactome
  27. pore complex assembly Source: UniProtKB
  28. positive regulation of apoptotic process Source: UniProtKB
  29. positive regulation of apoptotic process by virus Source: Ensembl
  30. positive regulation of autophagy Source: UniProtKB
  31. positive regulation of B cell differentiation Source: Ensembl
  32. positive regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
  33. positive regulation of epithelial cell proliferation Source: UniProtKB
  34. positive regulation of glucokinase activity Source: UniProtKB
  35. positive regulation of insulin secretion Source: UniProtKB
  36. positive regulation of insulin secretion involved in cellular response to glucose stimulus Source: Ensembl
  37. positive regulation of intrinsic apoptotic signaling pathway Source: Reactome
  38. positive regulation of mitochondrial membrane potential Source: UniProtKB
  39. positive regulation of neuron death Source: Ensembl
  40. positive regulation of protein insertion into mitochondrial membrane involved in apoptotic signaling pathway Source: Reactome
  41. positive regulation of proteolysis Source: BHF-UCL
  42. positive regulation of release of cytochrome c from mitochondria Source: UniProtKB
  43. positive regulation of T cell differentiation Source: Ensembl
  44. positive regulation of type B pancreatic cell development Source: UniProtKB
  45. regulation of mitochondrial membrane permeability Source: UniProtKB
  46. release of cytochrome c from mitochondria Source: Ensembl
  47. response to amino acid Source: Ensembl
  48. response to calcium ion Source: Ensembl
  49. response to drug Source: Ensembl
  50. response to estradiol Source: Ensembl
  51. response to ethanol Source: Ensembl
  52. response to glucocorticoid Source: Ensembl
  53. response to glucose Source: Ensembl
  54. response to hydrogen peroxide Source: Ensembl
  55. response to oleic acid Source: Ensembl
  56. response to progesterone Source: Ensembl
  57. response to testosterone Source: Ensembl
  58. suppression by virus of host apoptotic process Source: Ensembl
  59. type B pancreatic cell proliferation Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Apoptosis

Enzyme and pathway databases

ReactomeiREACT_12564. AKT phosphorylates targets in the cytosol.
REACT_13638. NRAGE signals death through JNK.
REACT_147727. Constitutive PI3K/AKT Signaling in Cancer.
REACT_330. BH3-only proteins associate with and inactivate anti-apoptotic BCL-2 members.

Names & Taxonomyi

Protein namesi
Recommended name:
Bcl2-associated agonist of cell death
Short name:
BAD
Alternative name(s):
Bcl-2-binding component 6
Bcl-2-like protein 8
Short name:
Bcl2-L-8
Bcl-xL/Bcl-2-associated death promoter
Bcl2 antagonist of cell death
Gene namesi
Name:BAD
Synonyms:BBC6, BCL2L8
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 11

Organism-specific databases

HGNCiHGNC:936. BAD.

Subcellular locationi

Mitochondrion outer membrane. Cytoplasm
Note: Upon phosphorylation, locates to the cytoplasm.

GO - Cellular componenti

  1. cytosol Source: UniProtKB
  2. mitochondrial outer membrane Source: UniProtKB
  3. mitochondrion Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane, Mitochondrion, Mitochondrion outer membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi94 – 941R → K: Decreased methylation; when associated with K-96. 1 Publication
Mutagenesisi96 – 961R → K: Decreased methylation; when associated with K-94. 1 Publication

Organism-specific databases

PharmGKBiPA25236.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 168168Bcl2-associated agonist of cell deathPRO_0000143103Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication
Modified residuei75 – 751Phosphoserine; by PKA, PKB, PIM2, PIM3, PAK1, PAK2, PAK4, PAK7/PAK5, RPS6KA1 and RAF1 By similarity
Modified residuei91 – 911Phosphoserine1 Publication
Modified residuei94 – 941Asymmetric dimethylarginine; by PRMT11 Publication
Modified residuei96 – 961Asymmetric dimethylarginine; by PRMT11 Publication
Modified residuei99 – 991Phosphoserine; by PKA, PKB, PAK1, RPS6KA1, RPS6KB1 and PKC/PRKCQ; alternate By similarity
Modified residuei99 – 991Phosphoserine; by PKB/AKT1; alternate1 Publication
Modified residuei118 – 1181Phosphoserine2 Publications
Modified residuei134 – 1341Phosphoserine By similarity

Post-translational modificationi

Phosphorylated on one or more of Ser-75, Ser-99, Ser-118 and Ser-134 in response to survival stimuli, which blocks its pro-apoptotic activity. Phosphorylation on Ser-99 or Ser-75 promotes heterodimerization with 14-3-3 proteins. This interaction then facilitates the phosphorylation at Ser-118, a site within the BH3 motif, leading to the release of Bcl-X(L) and the promotion of cell survival. Ser-99 is the major site of AKT/PKB phosphorylation, Ser-118 the major site of protein kinase A (CAPK) phosphorylation. Phosphorylation at Ser-99 by PKB/AKT1 is almost completely blocked by the apoptotic C-terminus cleavage product of PKN2 generated by caspases-3 activity during apoptosis.5 Publications
Methylation at Arg-94 and Arg-96 by PRMT1 inhibits Akt-mediated phosphorylation at Ser-99.1 Publication

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein

Proteomic databases

MaxQBiQ92934.
PaxDbiQ92934.
PeptideAtlasiQ92934.
PRIDEiQ92934.

PTM databases

PhosphoSiteiQ92934.

Miscellaneous databases

PMAP-CutDBQ92934.

Expressioni

Tissue specificityi

Expressed in a wide variety of tissues.

Gene expression databases

ArrayExpressiQ92934.
BgeeiQ92934.
CleanExiHS_BAD.
GenevestigatoriQ92934.

Organism-specific databases

HPAiCAB004205.
HPA028185.

Interactioni

Subunit structurei

Forms heterodimers with the anti-apoptotic proteins, Bcl-X(L), Bcl-2 and Bcl-W. Also binds protein S100A10 By similarity. The Ser-75/Ser-99 phosphorylated form binds 14-3-3 proteins By similarity. Interacts with AKT1 and PIM3.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
BCL2P104155EBI-700771,EBI-77694
BCL2L1Q078172EBI-700771,EBI-78035
BCL2L1Q07817-16EBI-700771,EBI-287195
BCL2L11O435212EBI-700771,EBI-526406
BNIP3LO602382EBI-700771,EBI-849893
MAPK8P459832EBI-700771,EBI-286483
NSP034952EBI-700771,EBI-2548993From a different organism.
SFNP319474EBI-700771,EBI-476295
VACWR028P173612EBI-700771,EBI-7115640From a different organism.
YWHAZP631045EBI-700771,EBI-347088

Protein-protein interaction databases

BioGridi107048. 35 interactions.
DIPiDIP-29184N.
IntActiQ92934. 29 interactions.
MINTiMINT-216253.
STRINGi9606.ENSP00000309103.

Structurei

Secondary structure

1
168
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi106 – 12116

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1G5JNMR-B103-127[»]
ProteinModelPortaliQ92934.
SMRiQ92934. Positions 100-126.

Miscellaneous databases

EvolutionaryTraceiQ92934.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi110 – 12415BH3Add
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.

Phylogenomic databases

eggNOGiNOG43412.
HOGENOMiHOG000095169.
HOVERGENiHBG001653.
InParanoidiQ92934.
KOiK02158.
OMAiGEAGHQQ.
OrthoDBiEOG7MD4RF.
PhylomeDBiQ92934.
TreeFamiTF102001.

Family and domain databases

InterProiIPR018868. Bcl-2_BAD.
[Graphical view]
PfamiPF10514. Bcl-2_BAD. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q92934-1 [UniParc]FASTAAdd to Basket

« Hide

MFQIPEFEPS EQEDSSSAER GLGPSPAGDG PSGSGKHHRQ APGLLWDASH    50
QQEQPTSSSH HGGAGAVEIR SRHSSYPAGT EDDEGMGEEP SPFRGRSRSA 100
PPNLWAAQRY GRELRRMSDE FVDSFKKGLP RPKSAGTATQ MRQSSSWTRV 150
FQSWWDRNLG RGSSAPSQ 168
Length:168
Mass (Da):18,392
Last modified:September 26, 2001 - v3
Checksum:i69FD8D27DDEE3241
GO

Sequence cautioni

The sequence AAB36516.1 differs from that shown. Reason: Frameshift at positions 64 and 91.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti107 – 1071A → S.
Corresponds to variant rs3729933 [ dbSNP | Ensembl ].
VAR_015380

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U66879 mRNA. Translation: AAB36516.1. Frameshift.
AF021792 mRNA. Translation: AAB72092.1.
AF031523 mRNA. Translation: AAB88124.1.
AK291863 mRNA. Translation: BAF84552.1.
BT006678 mRNA. Translation: AAP35324.1.
CR541935 mRNA. Translation: CAG46733.1.
CR541959 mRNA. Translation: CAG46757.1.
AB451254 mRNA. Translation: BAG70068.1.
AB451378 mRNA. Translation: BAG70192.1.
CH471076 Genomic DNA. Translation: EAW74235.1.
BC001901 mRNA. Translation: AAH01901.1.
BC095431 mRNA. Translation: AAH95431.1.
CCDSiCCDS8065.1.
RefSeqiNP_004313.1. NM_004322.3.
NP_116784.1. NM_032989.2.
UniGeneiHs.370254.

Genome annotation databases

EnsembliENST00000309032; ENSP00000309103; ENSG00000002330.
ENST00000394532; ENSP00000378040; ENSG00000002330.
GeneIDi572.
KEGGihsa:572.
UCSCiuc001nzc.3. human.

Polymorphism databases

DMDMi17371773.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology
Wikipedia

Bcl 2-associated death promoter entry

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U66879 mRNA. Translation: AAB36516.1 . Frameshift.
AF021792 mRNA. Translation: AAB72092.1 .
AF031523 mRNA. Translation: AAB88124.1 .
AK291863 mRNA. Translation: BAF84552.1 .
BT006678 mRNA. Translation: AAP35324.1 .
CR541935 mRNA. Translation: CAG46733.1 .
CR541959 mRNA. Translation: CAG46757.1 .
AB451254 mRNA. Translation: BAG70068.1 .
AB451378 mRNA. Translation: BAG70192.1 .
CH471076 Genomic DNA. Translation: EAW74235.1 .
BC001901 mRNA. Translation: AAH01901.1 .
BC095431 mRNA. Translation: AAH95431.1 .
CCDSi CCDS8065.1.
RefSeqi NP_004313.1. NM_004322.3.
NP_116784.1. NM_032989.2.
UniGenei Hs.370254.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1G5J NMR - B 103-127 [» ]
ProteinModelPortali Q92934.
SMRi Q92934. Positions 100-126.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107048. 35 interactions.
DIPi DIP-29184N.
IntActi Q92934. 29 interactions.
MINTi MINT-216253.
STRINGi 9606.ENSP00000309103.

Chemistry

BindingDBi Q92934.
ChEMBLi CHEMBL3817.

PTM databases

PhosphoSitei Q92934.

Polymorphism databases

DMDMi 17371773.

Proteomic databases

MaxQBi Q92934.
PaxDbi Q92934.
PeptideAtlasi Q92934.
PRIDEi Q92934.

Protocols and materials databases

DNASUi 572.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000309032 ; ENSP00000309103 ; ENSG00000002330 .
ENST00000394532 ; ENSP00000378040 ; ENSG00000002330 .
GeneIDi 572.
KEGGi hsa:572.
UCSCi uc001nzc.3. human.

Organism-specific databases

CTDi 572.
GeneCardsi GC11M064037.
HGNCi HGNC:936. BAD.
HPAi CAB004205.
HPA028185.
MIMi 603167. gene.
neXtProti NX_Q92934.
PharmGKBi PA25236.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG43412.
HOGENOMi HOG000095169.
HOVERGENi HBG001653.
InParanoidi Q92934.
KOi K02158.
OMAi GEAGHQQ.
OrthoDBi EOG7MD4RF.
PhylomeDBi Q92934.
TreeFami TF102001.

Enzyme and pathway databases

Reactomei REACT_12564. AKT phosphorylates targets in the cytosol.
REACT_13638. NRAGE signals death through JNK.
REACT_147727. Constitutive PI3K/AKT Signaling in Cancer.
REACT_330. BH3-only proteins associate with and inactivate anti-apoptotic BCL-2 members.

Miscellaneous databases

ChiTaRSi BAD. human.
EvolutionaryTracei Q92934.
GeneWikii Bcl-2-associated_death_promoter.
GenomeRNAii 572.
NextBioi 2331.
PMAP-CutDB Q92934.
PROi Q92934.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q92934.
Bgeei Q92934.
CleanExi HS_BAD.
Genevestigatori Q92934.

Family and domain databases

InterProi IPR018868. Bcl-2_BAD.
[Graphical view ]
Pfami PF10514. Bcl-2_BAD. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "A human protein that interacts with Bcl-2 and have homology to mouse BAD."
    Yin D.X., Li Z., Huang B., Chen S., Zhou H.
    Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Bcl-2 targets the protein kinase Raf-1 to mitochondria."
    Wang H.-G., Rapp U.R., Reed J.C.
    Cell 87:629-638(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PHOSPHORYLATION BY RAF-1.
  3. Takayama S., Reed J.C.
    Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  4. "Dimerization properties of human BAD. Identification of a BH-3 domain and analysis of its binding to mutant BCL-2 and BCL-XL proteins."
    Ottilie S., Diaz J.-L., Horne W., Chang J., Wang Y., Wilson G., Chang S., Weeks S., Fritz L.C., Oltersdorf T.
    J. Biol. Chem. 272:30866-30872(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], DIMERIZATION.
    Tissue: Bone marrow.
  5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Skeletal muscle.
  6. "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].
  7. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  8. "Human protein factory for converting the transcriptome into an in vitro-expressed proteome."
    Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R., Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y., Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.
    , Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S., Nomura N.
    Nat. Methods 5:1011-1017(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  9. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  10. "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].
    Tissue: Lung.
  11. "Inhibition of Akt and its anti-apoptotic activities by tumor necrosis factor-induced protein kinase C-related kinase 2 (PRK2) cleavage."
    Koh H., Lee K.H., Kim D., Kim S., Kim J.W., Chung J.
    J. Biol. Chem. 275:34451-34458(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH AKT1, PHOSPHORYLATION AT SER-99.
  12. "The serine/threonine kinase PAK4 prevents caspase activation and protects cells from apoptosis."
    Gnesutta N., Qu J., Minden A.
    J. Biol. Chem. 276:14414-14419(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-75.
  13. "p21-Activated kinase 5 (Pak5) localizes to mitochondria and inhibits apoptosis by phosphorylating BAD."
    Cotteret S., Jaffer Z.M., Beeser A., Chernoff J.
    Mol. Cell. Biol. 23:5526-5539(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-75.
  14. "Pim-3, a proto-oncogene with serine/threonine kinase activity, is aberrantly expressed in human pancreatic cancer and phosphorylates bad to block bad-mediated apoptosis in human pancreatic cancer cell lines."
    Li Y.Y., Popivanova B.K., Nagai Y., Ishikura H., Fujii C., Mukaida N.
    Cancer Res. 66:6741-6747(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-75.
  15. "Proto-oncogene, Pim-3 with serine/threonine kinase activity, is aberrantly expressed in human colon cancer cells and can prevent Bad-mediated apoptosis."
    Popivanova B.K., Li Y.Y., Zheng H., Omura K., Fujii C., Tsuneyama K., Mukaida N.
    Cancer Sci. 98:321-328(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PIM3.
  16. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-118, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  17. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-91 AND SER-118, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  18. "Arginine methylation of BCL-2 antagonist of cell death (BAD) counteracts its phosphorylation and inactivation by Akt."
    Sakamaki J., Daitoku H., Ueno K., Hagiwara A., Yamagata K., Fukamizu A.
    Proc. Natl. Acad. Sci. U.S.A. 108:6085-6090(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: METHYLATION AT ARG-94 AND ARG-96 BY PRMT1, MUTAGENESIS OF ARG-94 AND ARG-96.
  19. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  20. "Rationale for Bcl-xL/Bad peptide complex formation from structure, mutagenesis, and biophysical studies."
    Petros A.M., Nettesheim D.G., Wang Y., Olejniczak E.T., Meadows R.P., Mack J., Swift K., Matayoshi E.D., Zhang H., Thompson C.B., Fesik S.W.
    Protein Sci. 9:2528-2534(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 103-127.

Entry informationi

Entry nameiBAD_HUMAN
AccessioniPrimary (citable) accession number: Q92934
Secondary accession number(s): O14803, Q6FH21
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: September 26, 2001
Last modified: September 3, 2014
This is version 152 of the entry and version 3 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

Caution

The protein name 'Bcl2 antagonist of cell death' may be misleading. The protein antagonises Bcl2-mediated repression of cell death, hence it promotes apoptosis.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: 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

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