Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P70444 (BID_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 124. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length195 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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.

p15 BID is ubiquitinated by ITCH; ubiquitination results in proteasome-dependent degradation.

Ontologies

Keywords
   Biological processApoptosis
   Cellular componentCytoplasm
Membrane
Mitochondrion
   PTMAcetylation
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processactivation of cysteine-type endopeptidase activity involved in apoptotic process

Inferred from mutant phenotype PubMed 12011074. Source: MGI

apoptotic mitochondrial changes

Inferred from direct assay PubMed 9727492. Source: MGI

brain development

Inferred from electronic annotation. Source: Ensembl

establishment of protein localization to membrane

Inferred from electronic annotation. Source: Ensembl

extrinsic apoptotic signaling pathway

Inferred from mutant phenotype PubMed 10476969. Source: MGI

glial cell apoptotic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of apoptotic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of extrinsic apoptotic signaling pathway

Inferred from electronic annotation. Source: Ensembl

positive regulation of protein homooligomerization

Inferred from direct assay PubMed 21041309. Source: BHF-UCL

positive regulation of release of cytochrome c from mitochondria

Inferred from genetic interaction PubMed 10950869PubMed 21041309. Source: BHF-UCL

protein homooligomerization

Inferred from direct assay PubMed 10950869. Source: BHF-UCL

protein targeting to mitochondrion

Inferred from mutant phenotype PubMed 11369777. Source: MGI

regulation of G1/S transition of mitotic cell cycle

Inferred from mutant phenotype PubMed 15855651. Source: MGI

regulation of cell proliferation

Inferred from mutant phenotype PubMed 15855651. Source: MGI

regulation of mitochondrial membrane permeability involved in apoptotic process

Inferred from genetic interaction PubMed 14963330PubMed 23744079. Source: MGI

regulation of protein oligomerization

Inferred from direct assay PubMed 20850011. Source: UniProtKB

release of cytochrome c from mitochondria

Inferred from direct assay Ref.4. Source: MGI

response to estradiol

Inferred from electronic annotation. Source: Ensembl

signal transduction in response to DNA damage

Traceable author statement PubMed 18309324. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from direct assay Ref.4. Source: MGI

cytosol

Inferred from direct assay PubMed 11369777PubMed 11980919. Source: MGI

integral component of mitochondrial membrane

Inferred from direct assay PubMed 10950869. Source: BHF-UCL

mitochondrion

Inferred from direct assay PubMed 11369777PubMed 18614015. Source: MGI

   Molecular_functionprotein binding

Inferred from physical interaction PubMed 19062087. Source: IntAct

ubiquitin protein ligase binding

Inferred from physical interaction Ref.5. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

BAXQ078122EBI-2128640,EBI-516580From a different organism.
ITCHQ96J022EBI-783400,EBI-1564678From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 195195BH3-interacting domain death agonist
PRO_0000143102
Chain61 – 195135BH3-interacting domain death agonist p15
PRO_0000223236
Chain76 – 195120BH3-interacting domain death agonist p13
PRO_0000223235
Chain99 – 19597BH3-interacting domain death agonist p11
PRO_0000223234

Regions

Motif87 – 10014BH3

Sites

Site60 – 612Cleavage
Site75 – 762Cleavage
Site98 – 992Cleavage

Amino acid modifications

Modified residue11N-acetylmethionine By similarity
Modified residue781Phosphoserine By similarity

Experimental info

Mutagenesis981D → A: Loss of proteolytical cleavage leading to the production of p11 BID. Ref.1 Ref.4
Sequence conflict141E → K in AAC71064. Ref.1

Secondary structure

..................... 195
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P70444 [UniParc].

Last modified February 21, 2006. Version 2.
Checksum: 52F412714FB867F3

FASTA19521,952
        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 

« Hide

References

« Hide '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] [Europe PMC] [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. expand/collapse author list , 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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.
CCDSCCDS20486.1.
RefSeqNP_031570.2. NM_007544.3.
XP_006505471.1. XM_006505408.1.
XP_006505472.1. XM_006505409.1.
XP_006505473.1. XM_006505410.1.
XP_006505474.1. XM_006505411.1.
XP_006507182.1. XM_006507119.1.
XP_006507183.1. XM_006507120.1.
XP_006507184.1. XM_006507121.1.
UniGeneMm.235081.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1DDBNMR-A1-195[»]
2VOIX-ray2.10B76-109[»]
ProteinModelPortalP70444.
SMRP70444. Positions 1-195.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid198349. 6 interactions.
DIPDIP-29808N.
IntActP70444. 5 interactions.
MINTMINT-143107.
STRING10090.ENSMUSP00000004560.

PTM databases

PhosphoSiteP70444.

Proteomic databases

PaxDbP70444.
PRIDEP70444.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000004560; ENSMUSP00000004560; ENSMUSG00000004446.
ENSMUST00000160684; ENSMUSP00000125731; ENSMUSG00000004446.
GeneID12122.
KEGGmmu:12122.
UCSCuc009dnv.1. mouse.

Organism-specific databases

CTD637.
MGIMGI:108093. Bid.

Phylogenomic databases

eggNOGNOG78659.
GeneTreeENSGT00390000002868.
HOGENOMHOG000010016.
HOVERGENHBG001703.
InParanoidP70444.
KOK04726.
OMAKVADHTP.
OrthoDBEOG73V6MW.
PhylomeDBP70444.
TreeFamTF102047.

Gene expression databases

ArrayExpressP70444.
BgeeP70444.
CleanExMM_BID.
GenevestigatorP70444.

Family and domain databases

InterProIPR020728. Bcl2_BH3_motif_CS.
IPR010479. BID.
[Graphical view]
PfamPF06393. BID. 1 hit.
[Graphical view]
PIRSFPIRSF038018. BID. 1 hit.
PROSITEPS01259. BH3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP70444.
NextBio280439.
PMAP-CutDBP70444.
PROP70444.
SOURCESearch...

Entry information

Entry nameBID_MOUSE
AccessionPrimary (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: July 9, 2014
This is version 124 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot