P70444 (BID_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
BH3-interacting domain death agonist

Alternative name(s):
p22 BID
Short name=BID

Cleaved into the following 3 chains:

1. BH3-interacting domain death agonist p15
   Alternative name(s):
   p15 BID
2. BH3-interacting domain death agonist p13
   Alternative name(s):
   p13 BID
3. BH3-interacting domain death agonist p11
   Alternative name(s):
   p11 BID

Gene names

Name:

Bid

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	195 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Induces caspases and apoptosis. Counters the protective effect of Bcl-2. The major proteolytic product p15 BID allows the release of cytochrome c. Ref.4
Subunit structure	Forms heterodimers either with the pro-apoptotic protein BAX or the anti-apoptotic protein Bcl-2. p15 BID interacts with ITCH. Ref.5
Subcellular location	Cytoplasm. Mitochondrion membrane. Note: When uncleaved, it is predominantly cytoplasmic. p15 BID translocates to mitochondria as an integral membrane protein. p13 and p22 BID are associated with the mitochondrial membrane. Ref.4
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. Apoptotic members of the Bcl-2 family.
Post-translational modification	TNF-alpha induces a caspase-mediated cleavage of p22 BID into a major p15 and minor p13 and p11 products. Phosphorylated upon DNA damage, probably by ATM or ATR By similarity. p15 BID is ubiquitinated by ITCH; ubiquitination results in proteasome-dependent degradation.

Ontologies

Keywords
Biological process	Apoptosis
Cellular component	Cytoplasm Membrane Mitochondrion
PTM	Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	positive regulation of apoptotic process Inferred from electronic annotation. Source: InterPro positive regulation of protein homooligomerization Inferred from direct assay. Source: BHF-UCL positive regulation of release of cytochrome c from mitochondria Inferred from genetic interaction. Source: BHF-UCL protein homooligomerization Inferred from direct assay. Source: BHF-UCL protein targeting to mitochondrion Inferred from mutant phenotype. Source: MGI regulation of G1/S transition of mitotic cell cycle Inferred from mutant phenotype. Source: MGI regulation of cell proliferation Inferred from mutant phenotype. Source: MGI regulation of mitochondrial membrane permeability Inferred from genetic interaction. Source: MGI release of cytochrome c from mitochondria Inferred from direct assay Ref.4. Source: MGI
Cellular component	cytosol Inferred from direct assay. Source: MGI integral to mitochondrial membrane Inferred from direct assay. Source: BHF-UCL mitochondrion Inferred from direct assay. Source: MGI
Molecular function	ubiquitin protein ligase binding Inferred from physical interaction Ref.5. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
BAX	Q07812	2	EBI-2128640,EBI-516580	From a different organism.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 195

195

BH3-interacting domain death agonist

PRO_0000143102

Chain

61 – 195

135

BH3-interacting domain death agonist p15

PRO_0000223236

Chain

76 – 195

120

BH3-interacting domain death agonist p13

PRO_0000223235

Chain

99 – 195

97

BH3-interacting domain death agonist p11

PRO_0000223234

Regions

Motif

87 – 100

14

BH3

Sites

Site

60 – 61

2

Cleavage

Site

75 – 76

2

Cleavage

Site

98 – 99

2

Cleavage

Amino acid modifications

Modified residue

78

1

Phosphoserine By similarity

Experimental info

Mutagenesis

98

1

D → A: Loss of proteolytical cleavage leading to the production of p11 BID. Ref.1 Ref.4

Sequence conflict

14

1

E → K in AAC71064. Ref.1

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

195

Helix Strand Turn

Details...

Helix

15 – 27

13

Beta strand

28 – 30

3

Helix

32 – 39

8

Helix

79 – 99

21

Beta strand

103 – 105

3

Helix

106 – 113

8

Beta strand

116 – 122

7

Helix

125 – 137

13

Helix

142 – 162

21

Helix

167 – 180

14

Helix

185 – 192

8

Sequences

	Sequence		Length	Mass (Da)
	P70444 [UniParc]. Last modified February 21, 2006. Version 2. Checksum: 52F412714FB867F3	FASTA	195	21,952
	10 20 30 40 50 60 MDSEVSNGSG LGAEHITDLL VFGFLQSSGC TRQELEVLGR ELPVQAYWEA DLEDELQTDG 70 80 90 100 110 120 SQASRSFNQG RIEPDSESQE EIIHNIARHL AQIGDEMDHN IQPTLVRQLA AQFMNGSLSE 130 140 150 160 170 180 EDKRNCLAKA LDEVKTAFPR DMENDKAMLI MTMLLAKKVA SHAPSLLRDV FHTTVNFINQ 190 NLFSYVRNLV RNEMD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"BID: a novel BH3 domain-only death agonist." Wang K., Yin X.-M., Chao D.T., Milliman C.L., Korsmeyer S.J. Genes Dev. 10:2859-2869(1996) [PubMed: 8918887] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], MUTAGENESIS OF BH3 MOTIF. Tissue: T-cell.
[2]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J.
[3]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Mammary gland.
[4]	"Caspase cleaved BID targets mitochondria and is required for cytochrome c release, while BCL-XL prevents this release but not tumor necrosis factor-R1/Fas death." Gross A., Yin X.-M., Wang K., Wei M.C., Jockel J., Milliman C., Erdjument-Bromage H., Tempst P., Korsmeyer S.J. J. Biol. Chem. 274:1156-1163(1999) [PubMed: 9873064] [Abstract] Cited for: CLEAVAGE SITES, SUBCELLULAR LOCATION, MUTAGENESIS OF ASP-98, FUNCTION.
[5]	"The ubiquitin ligase Itch mediates the antiapoptotic activity of epidermal growth factor by promoting the ubiquitylation and degradation of the truncated C-terminal portion of Bid." Azakir B.A., Desrochers G., Angers A. FEBS J. 277:1319-1330(2010) [PubMed: 20392206] [Abstract] Cited for: INTERACTION WITH ITCH, UBIQUITINATION BY ITCH.
[6]	"Solution structure of the proapoptotic molecule BID: a structural basis for apoptotic agonists and antagonists." McDonnell J.M., Fushman D., Milliman C.L., Korsmeyer S.J., Cowburn D. Cell 96:625-634(1999) [PubMed: 10089878] [Abstract] Cited for: STRUCTURE BY NMR.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U75506 mRNA. Translation: AAC71064.1.
AK045731 mRNA. Translation: BAC32475.1.
AK051076 mRNA. Translation: BAC34518.1.
AK052356 mRNA. Translation: BAC34955.1.
AK077657 mRNA. Translation: BAC36932.1.
AK161235 mRNA. Translation: BAE36258.1.
BC002031 mRNA. Translation: AAH02031.1.

IPI

IPI00308086.

RefSeq

NP_031570.2. NM_007544.3.

UniGene

Mm.235081.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1DDB	NMR	-	A	1-195	[»]
2VOI	X-ray	2.10	B	76-109	[»]

ProteinModelPortal

P70444.

SMR

P70444. Positions 1-195.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29808N.

IntAct

P70444. 3 interactions.

MINT

MINT-143107.

STRING

P70444.

PTM databases

PhosphoSite

P70444.

Proteomic databases

PRIDE

P70444.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000004560; ENSMUSP00000004560; ENSMUSG00000004446.
ENSMUST00000160684; ENSMUSP00000125731; ENSMUSG00000004446.

GeneID

12122.

KEGG

mmu:12122.

UCSC

uc009dnv.1. mouse.

Organism-specific databases

CTD

637.

MGI

MGI:108093. Bid.

Phylogenomic databases

eggNOG

maNOG20103.

GeneTree

ENSGT00390000002868.

HOGENOM

HBG278752.

HOVERGEN

HBG001703.

InParanoid

P70444.

OMA

DSEVSNG.

OrthoDB

EOG4J9N1J.

PhylomeDB

P70444.

Gene expression databases

ArrayExpress

P70444.

Bgee

P70444.

CleanEx

MM_BID.

Genevestigator

P70444.

GermOnline

ENSMUSG00000004446. Mus musculus.

Family and domain databases

InterPro

IPR020728. Bcl2_BH3_motif_CS.
IPR010479. BID.
[Graphical view]

KO

K04726.

Pfam

PF06393. BID. 1 hit.
[Graphical view]

PIRSF

PIRSF038018. BID. 1 hit.

PROSITE

PS01259. BH3. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

280439.

PMAP-CutDB

P70444.

SOURCE

Search...

Entry information

Entry name

BID_MOUSE

Accession

Primary (citable) accession number: P70444
Secondary accession number(s): Q99M39

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	February 21, 2006
Last modified:	November 16, 2011
This is version 101 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program