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Protein

BH3-interacting domain death agonist

Gene

Bid

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Induces caspases and apoptosis. Counters the protective effect of Bcl-2. The major proteolytic product p15 BID allows the release of cytochrome c.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei60 – 612Cleavage
Sitei75 – 762Cleavage
Sitei98 – 992Cleavage

GO - Molecular functioni

  • ubiquitin protein ligase binding Source: UniProtKB

GO - Biological processi

  • activation of cysteine-type endopeptidase activity involved in apoptotic process Source: MGI
  • apoptotic mitochondrial changes Source: MGI
  • brain development Source: Ensembl
  • establishment of protein localization to membrane Source: MGI
  • extrinsic apoptotic signaling pathway Source: MGI
  • glial cell apoptotic process Source: Ensembl
  • hepatocyte apoptotic process Source: MGI
  • mitochondrial outer membrane permeabilization Source: MGI
  • positive regulation of apoptotic process Source: MGI
  • positive regulation of extrinsic apoptotic signaling pathway Source: MGI
  • positive regulation of protein homooligomerization Source: BHF-UCL
  • positive regulation of protein oligomerization Source: MGI
  • positive regulation of release of cytochrome c from mitochondria Source: BHF-UCL
  • protein homooligomerization Source: BHF-UCL
  • protein targeting to mitochondrion Source: MGI
  • regulation of cell proliferation Source: MGI
  • regulation of G1/S transition of mitotic cell cycle Source: MGI
  • regulation of mitochondrial membrane permeability involved in apoptotic process Source: MGI
  • regulation of protein oligomerization Source: UniProtKB
  • release of cytochrome c from mitochondria Source: CACAO
  • response to estradiol Source: Ensembl
  • signal transduction in response to DNA damage Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Apoptosis

Enzyme and pathway databases

ReactomeiREACT_287135. Activation and oligomerization of BAK protein.
REACT_307563. BH3-only proteins associate with and inactivate anti-apoptotic BCL-2 members.
REACT_318722. Activation of BAD and translocation to mitochondria.
REACT_335353. Activation, myristolyation of BID and translocation to mitochondria.
REACT_340204. Activation, translocation and oligomerization of BAX.

Names & Taxonomyi

Protein namesi
Recommended name:
BH3-interacting domain death agonist
Alternative name(s):
p22 BID
Short name:
BID
Cleaved into the following 3 chains:
Alternative name(s):
p15 BID
Alternative name(s):
p13 BID
Alternative name(s):
p11 BID
Gene namesi
Name:Bid
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 6

Organism-specific databases

MGIiMGI:108093. Bid.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: MGI
  • cytosol Source: MGI
  • extracellular exosome Source: MGI
  • integral component of mitochondrial membrane Source: BHF-UCL
  • membrane Source: MGI
  • mitochondrion Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane, Mitochondrion

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi98 – 981D → A: Loss of proteolytical cleavage leading to the production of p11 BID. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 195195BH3-interacting domain death agonistPRO_0000143102Add
BLAST
Chaini61 – 195135BH3-interacting domain death agonist p15PRO_0000223236Add
BLAST
Chaini76 – 195120BH3-interacting domain death agonist p13PRO_0000223235Add
BLAST
Chaini99 – 19597BH3-interacting domain death agonist p11PRO_0000223234Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei78 – 781PhosphoserineBy similarity

Post-translational modificationi

TNF-alpha induces a caspase-mediated cleavage of p22 BID into a major p15 and minor p13 and p11 products.1 Publication
p15 BID is ubiquitinated by ITCH; ubiquitination results in proteasome-dependent degradation.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP70444.
PaxDbiP70444.
PRIDEiP70444.

PTM databases

PhosphoSiteiP70444.

Miscellaneous databases

PMAP-CutDBP70444.

Expressioni

Gene expression databases

BgeeiP70444.
CleanExiMM_BID.
ExpressionAtlasiP70444. baseline and differential.
GenevisibleiP70444. MM.

Interactioni

Subunit structurei

Forms heterodimers either with the pro-apoptotic protein BAX or the anti-apoptotic protein Bcl-2. p15 BID interacts with ITCH.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
BAXQ078122EBI-2128640,EBI-516580From a different organism.
ITCHQ96J022EBI-783400,EBI-1564678From a different organism.

Protein-protein interaction databases

BioGridi198349. 6 interactions.
DIPiDIP-29808N.
IntActiP70444. 5 interactions.
MINTiMINT-143107.
STRINGi10090.ENSMUSP00000004560.

Structurei

Secondary structure

1
195
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi15 – 2713Combined sources
Beta strandi28 – 303Combined sources
Helixi32 – 398Combined sources
Helixi79 – 9921Combined sources
Beta strandi103 – 1053Combined sources
Helixi106 – 1138Combined sources
Beta strandi116 – 1227Combined sources
Helixi125 – 13713Combined sources
Helixi142 – 16221Combined sources
Helixi167 – 18014Combined sources
Helixi185 – 1928Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DDBNMR-A1-195[»]
2VOIX-ray2.10B76-109[»]
ProteinModelPortaliP70444.
SMRiP70444. Positions 1-195.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP70444.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi87 – 10014BH3Add
BLAST

Domaini

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.

Phylogenomic databases

eggNOGiNOG78659.
GeneTreeiENSGT00390000002868.
HOGENOMiHOG000010016.
HOVERGENiHBG001703.
InParanoidiP70444.
KOiK04726.
OMAiRDVFRTT.
OrthoDBiEOG73V6MW.
PhylomeDBiP70444.
TreeFamiTF102047.

Family and domain databases

InterProiIPR020728. Bcl2_BH3_motif_CS.
IPR010479. BID.
[Graphical view]
PfamiPF06393. BID. 1 hit.
[Graphical view]
PIRSFiPIRSF038018. BID. 1 hit.
PROSITEiPS01259. BH3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P70444-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDSEVSNGSG LGAEHITDLL VFGFLQSSGC TRQELEVLGR ELPVQAYWEA
60 70 80 90 100
DLEDELQTDG SQASRSFNQG RIEPDSESQE EIIHNIARHL AQIGDEMDHN
110 120 130 140 150
IQPTLVRQLA AQFMNGSLSE EDKRNCLAKA LDEVKTAFPR DMENDKAMLI
160 170 180 190
MTMLLAKKVA SHAPSLLRDV FHTTVNFINQ NLFSYVRNLV RNEMD
Length:195
Mass (Da):21,952
Last modified:February 21, 2006 - v2
Checksum:i52F412714FB867F3
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti14 – 141E → K in AAC71064 (PubMed:8918887).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS20486.1.
RefSeqiNP_031570.2. NM_007544.3.
XP_006505472.1. XM_006505409.2.
XP_006505473.1. XM_006505410.2.
XP_006505474.1. XM_006505411.2.
XP_006507183.1. XM_006507120.2.
XP_006507184.1. XM_006507121.2.
UniGeneiMm.235081.

Genome annotation databases

EnsembliENSMUST00000004560; ENSMUSP00000004560; ENSMUSG00000004446.
ENSMUST00000160684; ENSMUSP00000125731; ENSMUSG00000004446.
GeneIDi12122.
KEGGimmu:12122.
UCSCiuc009dnv.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS20486.1.
RefSeqiNP_031570.2. NM_007544.3.
XP_006505472.1. XM_006505409.2.
XP_006505473.1. XM_006505410.2.
XP_006505474.1. XM_006505411.2.
XP_006507183.1. XM_006507120.2.
XP_006507184.1. XM_006507121.2.
UniGeneiMm.235081.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DDBNMR-A1-195[»]
2VOIX-ray2.10B76-109[»]
ProteinModelPortaliP70444.
SMRiP70444. Positions 1-195.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198349. 6 interactions.
DIPiDIP-29808N.
IntActiP70444. 5 interactions.
MINTiMINT-143107.
STRINGi10090.ENSMUSP00000004560.

PTM databases

PhosphoSiteiP70444.

Proteomic databases

MaxQBiP70444.
PaxDbiP70444.
PRIDEiP70444.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000004560; ENSMUSP00000004560; ENSMUSG00000004446.
ENSMUST00000160684; ENSMUSP00000125731; ENSMUSG00000004446.
GeneIDi12122.
KEGGimmu:12122.
UCSCiuc009dnv.1. mouse.

Organism-specific databases

CTDi637.
MGIiMGI:108093. Bid.

Phylogenomic databases

eggNOGiNOG78659.
GeneTreeiENSGT00390000002868.
HOGENOMiHOG000010016.
HOVERGENiHBG001703.
InParanoidiP70444.
KOiK04726.
OMAiRDVFRTT.
OrthoDBiEOG73V6MW.
PhylomeDBiP70444.
TreeFamiTF102047.

Enzyme and pathway databases

ReactomeiREACT_287135. Activation and oligomerization of BAK protein.
REACT_307563. BH3-only proteins associate with and inactivate anti-apoptotic BCL-2 members.
REACT_318722. Activation of BAD and translocation to mitochondria.
REACT_335353. Activation, myristolyation of BID and translocation to mitochondria.
REACT_340204. Activation, translocation and oligomerization of BAX.

Miscellaneous databases

EvolutionaryTraceiP70444.
NextBioi280439.
PMAP-CutDBP70444.
PROiP70444.
SOURCEiSearch...

Gene expression databases

BgeeiP70444.
CleanExiMM_BID.
ExpressionAtlasiP70444. baseline and differential.
GenevisibleiP70444. MM.

Family and domain databases

InterProiIPR020728. Bcl2_BH3_motif_CS.
IPR010479. BID.
[Graphical view]
PfamiPF06393. BID. 1 hit.
[Graphical view]
PIRSFiPIRSF038018. BID. 1 hit.
PROSITEiPS01259. BH3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. 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] [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.

Entry informationi

Entry nameiBID_MOUSE
AccessioniPrimary (citable) accession number: P70444
Secondary accession number(s): Q99M39
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: February 21, 2006
Last modified: June 24, 2015
This is version 135 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.