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Q92934 (BAD_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 148. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Bcl2 antagonist 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
Gene names
Name:BAD
Synonyms:BBC6, BCL2L8
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length168 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subunit structure

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. Ref.4 Ref.11 Ref.15

Subcellular location

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

Tissue specificity

Expressed in a wide variety of tissues.

Domain

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.

Post-translational modification

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. Ref.2 Ref.11 Ref.12 Ref.13 Ref.14

Methylation at Arg-94 and Arg-96 by PRMT1 inhibits Akt-mediated phosphorylation at Ser-99. Ref.18

Sequence similarities

Belongs to the Bcl-2 family.

Sequence caution

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

Ontologies

Keywords
   Biological processApoptosis
   Cellular componentCytoplasm
Membrane
Mitochondrion
Mitochondrion outer membrane
   Coding sequence diversityPolymorphism
   PTMAcetylation
Methylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processADP metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

ATP metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

Fc-epsilon receptor signaling pathway

Traceable author statement. Source: Reactome

activation of cysteine-type endopeptidase activity

Inferred from direct assay PubMed 18387192. Source: BHF-UCL

activation of cysteine-type endopeptidase activity involved in apoptotic process

Inferred from sequence or structural similarity. Source: UniProtKB

apoptotic process

Inferred from direct assay PubMed 19667065. Source: UniProtKB

apoptotic signaling pathway

Traceable author statement. Source: Reactome

cellular process regulating host cell cycle in response to virus

Inferred from electronic annotation. Source: Ensembl

cellular response to chromate

Inferred from electronic annotation. Source: Ensembl

cellular response to hypoxia

Inferred from expression pattern PubMed 20810912. Source: UniProtKB

cellular response to lipid

Inferred from electronic annotation. Source: Ensembl

cellular response to mechanical stimulus

Inferred from expression pattern PubMed 19593445. Source: UniProtKB

cellular response to nicotine

Inferred from direct assay PubMed 18676776. Source: UniProtKB

cytokine-mediated signaling pathway

Inferred from electronic annotation. Source: Ensembl

epidermal growth factor receptor signaling pathway

Traceable author statement. Source: Reactome

extrinsic apoptotic signaling pathway

Inferred from mutant phenotype PubMed 18852119. Source: UniProtKB

extrinsic apoptotic signaling pathway in absence of ligand

Inferred from electronic annotation. Source: Ensembl

extrinsic apoptotic signaling pathway via death domain receptors

Inferred from electronic annotation. Source: Ensembl

fibroblast growth factor receptor signaling pathway

Traceable author statement. Source: Reactome

glucose catabolic process

Inferred from electronic annotation. Source: Ensembl

glucose homeostasis

Inferred from sequence or structural similarity. Source: UniProtKB

innate immune response

Traceable author statement. Source: Reactome

intrinsic apoptotic signaling pathway

Inferred from mutant phenotype PubMed 18676776. Source: UniProtKB

intrinsic apoptotic signaling pathway in response to DNA damage

Inferred from electronic annotation. Source: Ensembl

neurotrophin TRK receptor signaling pathway

Traceable author statement. Source: Reactome

phosphatidylinositol-mediated signaling

Traceable author statement. Source: Reactome

pore complex assembly

Inferred from direct assay PubMed 19667065PubMed 21081150. Source: UniProtKB

positive regulation of B cell differentiation

Inferred from electronic annotation. Source: Ensembl

positive regulation of T cell differentiation

Inferred from electronic annotation. Source: Ensembl

positive regulation of apoptotic process

Inferred from direct assay Ref.4. Source: UniProtKB

positive regulation of apoptotic process by virus

Inferred from electronic annotation. Source: Ensembl

positive regulation of autophagy

Traceable author statement PubMed 18309324. Source: UniProtKB

positive regulation of cysteine-type endopeptidase activity involved in apoptotic process

Inferred from direct assay PubMed 18402937. Source: UniProtKB

positive regulation of epithelial cell proliferation

Inferred from mutant phenotype PubMed 19593445. Source: UniProtKB

positive regulation of glucokinase activity

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of insulin secretion

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of insulin secretion involved in cellular response to glucose stimulus

Inferred from electronic annotation. Source: Ensembl

positive regulation of intrinsic apoptotic signaling pathway

Traceable author statement. Source: Reactome

positive regulation of mitochondrial membrane potential

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of neuron death

Inferred from electronic annotation. Source: Ensembl

positive regulation of protein insertion into mitochondrial membrane involved in apoptotic signaling pathway

Traceable author statement. Source: Reactome

positive regulation of proteolysis

Inferred from direct assay PubMed 18387192. Source: BHF-UCL

positive regulation of release of cytochrome c from mitochondria

Inferred from mutant phenotype PubMed 17289999. Source: UniProtKB

positive regulation of type B pancreatic cell development

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of mitochondrial membrane permeability

Inferred from mutant phenotype PubMed 20700721. Source: UniProtKB

release of cytochrome c from mitochondria

Inferred from electronic annotation. Source: Ensembl

response to amino acid

Inferred from electronic annotation. Source: Ensembl

response to calcium ion

Inferred from electronic annotation. Source: Ensembl

response to drug

Inferred from electronic annotation. Source: Ensembl

response to estradiol

Inferred from electronic annotation. Source: Ensembl

response to ethanol

Inferred from electronic annotation. Source: Ensembl

response to glucocorticoid

Inferred from electronic annotation. Source: Ensembl

response to glucose

Inferred from electronic annotation. Source: Ensembl

response to hydrogen peroxide

Inferred from electronic annotation. Source: Ensembl

response to oleic acid

Inferred from electronic annotation. Source: Ensembl

response to progesterone

Inferred from electronic annotation. Source: Ensembl

response to testosterone

Inferred from electronic annotation. Source: Ensembl

suppression by virus of host apoptotic process

Inferred from electronic annotation. Source: Ensembl

type B pancreatic cell proliferation

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentcytosol

Inferred from direct assay PubMed 20700721. Source: UniProtKB

mitochondrial outer membrane

Inferred from direct assay PubMed 20700721. Source: UniProtKB

mitochondrion

Inferred from direct assay. Source: HPA

   Molecular_functioncysteine-type endopeptidase activator activity involved in apoptotic process

Inferred from direct assay PubMed 18402937. Source: UniProtKB

lipid binding

Inferred from direct assay PubMed 19667065. Source: UniProtKB

phospholipid binding

Inferred from mutant phenotype PubMed 21081150. Source: UniProtKB

protein kinase binding

Inferred from physical interaction Ref.15. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 168168Bcl2 antagonist of cell death
PRO_0000143103

Regions

Motif110 – 12415BH3

Amino acid modifications

Modified residue11N-acetylmethionine Ref.19
Modified residue751Phosphoserine; by PKA, PKB, PIM2, PIM3, PAK1, PAK2, PAK4, PAK7/PAK5, RPS6KA1 and RAF1 By similarity
Modified residue911Phosphoserine Ref.17
Modified residue941Asymmetric dimethylarginine; by PRMT1 Ref.18
Modified residue961Asymmetric dimethylarginine; by PRMT1 Ref.18
Modified residue991Phosphoserine; by PKA, PKB, PAK1, RPS6KA1, RPS6KB1 and PKC/PRKCQ; alternate By similarity
Modified residue991Phosphoserine; by PKB/AKT1; alternate Ref.11
Modified residue1181Phosphoserine Ref.16 Ref.17
Modified residue1341Phosphoserine By similarity

Natural variations

Natural variant1071A → S.
Corresponds to variant rs3729933 [ dbSNP | Ensembl ].
VAR_015380

Experimental info

Mutagenesis941R → K: Decreased methylation; when associated with K-96. Ref.18
Mutagenesis961R → K: Decreased methylation; when associated with K-94. Ref.18

Secondary structure

... 168
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q92934 [UniParc].

Last modified September 26, 2001. Version 3.
Checksum: 69FD8D27DDEE3241

FASTA16818,392
        10         20         30         40         50         60 
MFQIPEFEPS EQEDSSSAER GLGPSPAGDG PSGSGKHHRQ APGLLWDASH QQEQPTSSSH 

        70         80         90        100        110        120 
HGGAGAVEIR SRHSSYPAGT EDDEGMGEEP SPFRGRSRSA PPNLWAAQRY GRELRRMSDE 

       130        140        150        160 
FVDSFKKGLP RPKSAGTATQ MRQSSSWTRV FQSWWDRNLG RGSSAPSQ 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_004313.1. NM_004322.3.
NP_116784.1. NM_032989.2.
UniGeneHs.370254.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1G5JNMR-B103-127[»]
ProteinModelPortalQ92934.
SMRQ92934. Positions 100-126.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107048. 35 interactions.
DIPDIP-29184N.
IntActQ92934. 29 interactions.
MINTMINT-216253.
STRING9606.ENSP00000309103.

Chemistry

BindingDBQ92934.
ChEMBLCHEMBL3817.

PTM databases

PhosphoSiteQ92934.

Polymorphism databases

DMDM17371773.

Proteomic databases

PaxDbQ92934.
PeptideAtlasQ92934.
PRIDEQ92934.

Protocols and materials databases

DNASU572.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000309032; ENSP00000309103; ENSG00000002330.
ENST00000394532; ENSP00000378040; ENSG00000002330.
GeneID572.
KEGGhsa:572.
UCSCuc001nzc.3. human.

Organism-specific databases

CTD572.
GeneCardsGC11M064037.
HGNCHGNC:936. BAD.
HPACAB004205.
HPA028185.
MIM603167. gene.
neXtProtNX_Q92934.
PharmGKBPA25236.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG43412.
HOGENOMHOG000095169.
HOVERGENHBG001653.
InParanoidQ92934.
KOK02158.
OMAGEAGHQQ.
OrthoDBEOG7MD4RF.
PhylomeDBQ92934.
TreeFamTF102001.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_116125. Disease.
REACT_578. Apoptosis.
REACT_6900. Immune System.

Gene expression databases

ArrayExpressQ92934.
BgeeQ92934.
CleanExHS_BAD.
GenevestigatorQ92934.

Family and domain databases

InterProIPR018868. Bcl-2_BAD.
[Graphical view]
PfamPF10514. Bcl-2_BAD. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSBAD. human.
EvolutionaryTraceQ92934.
GeneWikiBcl-2-associated_death_promoter.
GenomeRNAi572.
NextBio2331.
PMAP-CutDBQ92934.
PROQ92934.
SOURCESearch...

Entry information

Entry nameBAD_HUMAN
AccessionPrimary (citable) accession number: Q92934
Secondary accession number(s): O14803, Q6FH21
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: September 26, 2001
Last modified: April 16, 2014
This is version 148 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM