Q92934 (BAD_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	168 AA.
Sequence status	Complete.
Protein existence	Evidence 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 process	Apoptosis
Cellular component	Cytoplasm Membrane Mitochondrion Mitochondrion outer membrane
Coding sequence diversity	Polymorphism
PTM	Methylation Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	ADP metabolic process Inferred from sequence or structural similarity. Source: UniProtKB ATP metabolic process Inferred from sequence or structural similarity. Source: UniProtKB cellular process regulating host cell cycle in response to virus Inferred from electronic annotation. Source: Compara cellular response to chromate Inferred from electronic annotation. Source: Compara cellular response to hypoxia Inferred from expression pattern PubMed 20810912. Source: UniProtKB cellular response to lipid Inferred from electronic annotation. Source: Compara 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: Compara epidermal growth factor receptor signaling pathway Traceable author statement. Source: Reactome extrinsic apoptotic signaling pathway Inferred from mutant phenotype PubMed 18852119. Source: UniProtKB fibroblast growth factor receptor signaling pathway Traceable author statement. Source: Reactome glucose catabolic process Inferred from electronic annotation. Source: Compara glucose homeostasis Inferred from sequence or structural similarity. Source: UniProtKB induction of apoptosis Inferred from direct assay PubMed 19667065. Source: UniProtKB intrinsic apoptotic signaling pathway Inferred from mutant phenotype PubMed 18676776. Source: UniProtKB nerve growth factor 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: Compara positive regulation of T cell differentiation Inferred from electronic annotation. Source: Compara positive regulation of autophagy Traceable author statement PubMed 18309324. 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: Compara positive regulation of mitochondrial membrane potential Inferred from sequence or structural similarity. Source: UniProtKB 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 response to amino acid stimulus Inferred from electronic annotation. Source: Compara response to calcium ion Inferred from electronic annotation. Source: Compara response to drug Inferred from electronic annotation. Source: Compara response to estradiol stimulus Inferred from electronic annotation. Source: Compara response to ethanol Inferred from electronic annotation. Source: Compara response to glucocorticoid stimulus Inferred from electronic annotation. Source: Compara response to glucose stimulus Inferred from electronic annotation. Source: Compara response to hydrogen peroxide Inferred from electronic annotation. Source: Compara response to oleic acid Inferred from electronic annotation. Source: Compara response to progesterone stimulus Inferred from electronic annotation. Source: Compara response to testosterone stimulus Inferred from electronic annotation. Source: Compara type B pancreatic cell proliferation Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	cytosol Inferred from direct assay PubMed 20700721. Source: UniProtKB mitochondrial outer membrane Inferred from direct assay PubMed 20700721. Source: UniProtKB
Molecular_function	cysteine-type endopeptidase activator activity involved in apoptotic process Inferred from direct assay PubMed 18402937. Source: UniProtKB phospholipid binding Inferred from mutant phenotype PubMed 21081150. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
BCL2	P10415	5	EBI-700771,EBI-77694
BCL2L1	Q07817-1	6	EBI-700771,EBI-287195
BNIP3L	O60238	2	EBI-700771,EBI-849893

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 168

168

Bcl2 antagonist of cell death

PRO_0000143103

Regions

Motif

110 – 124

15

BH3

Amino acid modifications

Modified residue

75

1

Phosphoserine; by PKA, PKB, PIM2, PIM3, PAK1, PAK2, PAK4, PAK7/PAK5, RPS6KA1 and RAF1 By similarity

Modified residue

91

1

Phosphoserine Ref.17

Modified residue

94

1

Asymmetric dimethylarginine; by PRMT1 Ref.18

Modified residue

96

1

Asymmetric dimethylarginine; by PRMT1 Ref.18

Modified residue

99

1

Phosphoserine; by PKA, PKB, PAK1, RPS6KA1, RPS6KB1 and PKC/PRKCQ; alternate By similarity

Modified residue

99

1

Phosphoserine; by PKB/AKT1; alternate Ref.11

Modified residue

118

1

Phosphoserine Ref.16 Ref.17

Modified residue

134

1

Phosphoserine By similarity

Natural variations

Natural variant

107

1

A → S.
Corresponds to variant rs3729933 [ dbSNP | Ensembl ].

VAR_015380

Experimental info

Mutagenesis

94

1

R → K: Decreased methylation; when associated with K-96. Ref.18

Mutagenesis

96

1

R → K: Decreased methylation; when associated with K-94. Ref.18

Secondary structure

1

.

.

.

.

.

168

Helix Strand Turn

Details...

Helix

106 – 121

16

Beta strand

123 – 125

3

Sequences

	Sequence		Length	Mass (Da)
	Q92934 [UniParc]. Last modified September 26, 2001. Version 3. Checksum: 69FD8D27DDEE3241	FASTA	168	18,392
	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

References

	« Hide 'large scale' referencesShow '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. , 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]	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. , 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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]	"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

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Wikipedia

Bcl 2-associated death promoter entry

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.

IPI

IPI00024291.

RefSeq

NP_004313.1. NM_004322.3.
NP_116784.1. NM_032989.2.

UniGene

Hs.370254.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1G5J	NMR	-	B	103-127	[»]

ProteinModelPortal

Q92934.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29184N.

IntAct

Q92934. 19 interactions.

MINT

MINT-216253.

STRING

9606.ENSP00000309103.

PTM databases

PhosphoSite

Q92934.

Polymorphism databases

DMDM

17371773.

Proteomic databases

PaxDb

Q92934.

PeptideAtlas

Q92934.

PRIDE

Q92934.

Protocols and materials databases

DNASU

572.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000309032; ENSP00000309103; ENSG00000002330.
ENST00000394532; ENSP00000378040; ENSG00000002330.

GeneID

572.

KEGG

hsa:572.

UCSC

uc001nzc.3. human.

Organism-specific databases

CTD

572.

GeneCards

GC11M064037.

HGNC

HGNC:936. BAD.

HPA

CAB004205.
HPA028185.

MIM

603167. gene.

neXtProt

NX_Q92934.

PharmGKB

PA25236.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG43412.

HOGENOM

HOG000095169.

HOVERGEN

HBG001653.

InParanoid

Q92934.

KO

K02158.

OMA

SMFQIPE.

OrthoDB

EOG42RD8W.

PhylomeDB

Q92934.

Enzyme and pathway databases

Pathway_Interaction_DB

alphasynuclein_pathway. Alpha-synuclein signaling.
ceramidepathway. Ceramide signaling pathway.
pi3kciaktpathway. Class I PI3K signaling events mediated by Akt.
igf1_pathway. IGF1 pathway.
p75ntrpathway. p75(NTR)-mediated signaling.
nfat_3pathway. Role of Calcineurin-dependent NFAT signaling in lymphocytes.
met_pathway. Signaling events activated by Hepatocyte Growth Factor Receptor (c-Met).
kitpathway. Signaling events mediated by Stem cell factor receptor (c-Kit).
pi3kplctrkpathway. Trk receptor signaling mediated by PI3K and PLC-gamma.

Reactome

REACT_111102. Signal Transduction.
REACT_116125. Disease.
REACT_578. Apoptosis.
REACT_6900. Immune System.

Gene expression databases

ArrayExpress

Q92934.

Bgee

Q92934.

CleanEx

HS_BAD.

Genevestigator

Q92934.

GermOnline

ENSG00000002330. Homo sapiens.

Family and domain databases

InterPro

IPR018868. Bcl-2_BAD.
[Graphical view]

Pfam

PF10514. Bcl-2_BAD. 1 hit.
[Graphical view]

PROSITE

PS01259. BH3. False negative.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

Q92934.

ChEMBL

CHEMBL3817.

ChiTaRS

BAD. human.

EvolutionaryTrace

Q92934.

GenomeRNAi

572.

NextBio

2331.

PMAP-CutDB

Q92934.

SOURCE

Search...

Entry information

Entry name

BAD_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 138 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.