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Reviewed, UniProtKB/Swiss-Prot P70444 (BID_MOUSE)

Last modified June 16, 2009. Version 78. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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- Recommended name:
            BH3-interacting domain death agonist p15
        Alternative name(s):
            p15 BID
    2- Recommended name:
            BH3-interacting domain death agonist p13
        Alternative name(s):
            p13 BID
    3- Recommended name:
            BH3-interacting domain death agonist p11
        Alternative name(s):
            p11 BID
Gene names
Name: Bid
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMus

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.

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.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

BCL2L2Q928431EBI-783400,EBI-707714From 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 residue781Phosphoserine By similarity

Experimental info

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

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
P70444-1 [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: 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. 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: 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]"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

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.
IPIIPI00308086.
RefSeqNP_031570.2.
UniGeneMm.235081

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1DDBNMR-A1-195[»]
2VOIX-ray2.10B76-109[»]
ModBaseSearch...

Protein-protein interaction databases

IntActP70444. 4 interactions.

PTM databases

PhosphoSiteP70444.

Proteomic databases

PRIDEP70444.

Genome annotation databases

EnsemblENSMUSG00000004446. Mus musculus. [Contig view]
GeneID12122.
KEGGmmu:12122.

Organism-specific databases

MGIMGI:108093. Bid.

Phylogenomic databases

HOGENOMP70444.
HOVERGENP70444.
OMAP70444. YDDELQT.

Gene expression databases

ArrayExpressP70444.
BgeeP70444.
CleanExMM_BID.
GermOnlineENSMUSG00000004446. Mus musculus.

Family and domain databases

InterProIPR000712. Bcl2_BH.
IPR010479. BID.
[Graphical view]
PfamPF06393. BID. 1 hit.
[Graphical view]
PIRSFPIRSF038018. BID. 1 hit.
PROSITEPS01259. BH3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio280439.
PMAP-CutDBP70444.
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: June 16, 2009
This is version 78 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

MGD cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents