Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P70444

- BID_MOUSE

UniProt

P70444 - BID_MOUSE

Protein

BH3-interacting domain death agonist

Gene

Bid

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 126 (01 Oct 2014)
      Sequence version 2 (21 Feb 2006)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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

    1. protein binding Source: IntAct
    2. ubiquitin protein ligase binding Source: UniProtKB

    GO - Biological processi

    1. activation of cysteine-type endopeptidase activity involved in apoptotic process Source: MGI
    2. apoptotic mitochondrial changes Source: MGI
    3. brain development Source: Ensembl
    4. establishment of protein localization to membrane Source: Ensembl
    5. extrinsic apoptotic signaling pathway Source: MGI
    6. glial cell apoptotic process Source: Ensembl
    7. hepatocyte apoptotic process Source: MGI
    8. mitochondrial outer membrane permeabilization Source: MGI
    9. positive regulation of apoptotic process Source: Ensembl
    10. positive regulation of extrinsic apoptotic signaling pathway Source: Ensembl
    11. positive regulation of protein homooligomerization Source: BHF-UCL
    12. positive regulation of release of cytochrome c from mitochondria Source: BHF-UCL
    13. protein homooligomerization Source: BHF-UCL
    14. protein targeting to mitochondrion Source: MGI
    15. regulation of cell proliferation Source: MGI
    16. regulation of G1/S transition of mitotic cell cycle Source: MGI
    17. regulation of mitochondrial membrane permeability involved in apoptotic process Source: MGI
    18. regulation of protein oligomerization Source: UniProtKB
    19. release of cytochrome c from mitochondria Source: MGI
    20. response to estradiol Source: Ensembl
    21. signal transduction in response to DNA damage Source: UniProtKB

    Keywords - Biological processi

    Apoptosis

    Enzyme and pathway databases

    ReactomeiREACT_202639. Activation, translocation and oligomerization of BAX.
    REACT_208000. Activation, myristolyation of BID and translocation to mitochondria.
    REACT_210929. Activation and oligomerization of BAK protein.
    REACT_223399. BH3-only proteins associate with and inactivate anti-apoptotic BCL-2 members.

    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: Chromosome 6

    Organism-specific databases

    MGIiMGI:108093. Bid.

    Subcellular locationi

    Cytoplasm 1 Publication. Mitochondrion membrane 1 Publication
    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.

    GO - Cellular componenti

    1. cytoplasm Source: MGI
    2. cytosol Source: MGI
    3. integral component of mitochondrial membrane Source: BHF-UCL
    4. membrane Source: MGI
    5. mitochondrion Source: MGI

    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. 2 Publications

    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

    PaxDbiP70444.
    PRIDEiP70444.

    PTM databases

    PhosphoSiteiP70444.

    Miscellaneous databases

    PMAP-CutDBP70444.

    Expressioni

    Gene expression databases

    ArrayExpressiP70444.
    BgeeiP70444.
    CleanExiMM_BID.
    GenevestigatoriP70444.

    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 – 2713
    Beta strandi28 – 303
    Helixi32 – 398
    Helixi79 – 9921
    Beta strandi103 – 1053
    Helixi106 – 1138
    Beta strandi116 – 1227
    Helixi125 – 13713
    Helixi142 – 16221
    Helixi167 – 18014
    Helixi185 – 1928

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    OMAiKVADHTP.
    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

    MDSEVSNGSG LGAEHITDLL VFGFLQSSGC TRQELEVLGR ELPVQAYWEA    50
    DLEDELQTDG SQASRSFNQG RIEPDSESQE EIIHNIARHL AQIGDEMDHN 100
    IQPTLVRQLA AQFMNGSLSE EDKRNCLAKA LDEVKTAFPR DMENDKAMLI 150
    MTMLLAKKVA SHAPSLLRDV FHTTVNFINQ NLFSYVRNLV RNEMD 195
    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:
    EMBL
    GenBank
    DDBJ
    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_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.
    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:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS20486.1.
    RefSeqi NP_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.
    UniGenei Mm.235081.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1DDB NMR - A 1-195 [» ]
    2VOI X-ray 2.10 B 76-109 [» ]
    ProteinModelPortali P70444.
    SMRi P70444. Positions 1-195.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 198349. 6 interactions.
    DIPi DIP-29808N.
    IntActi P70444. 5 interactions.
    MINTi MINT-143107.
    STRINGi 10090.ENSMUSP00000004560.

    PTM databases

    PhosphoSitei P70444.

    Proteomic databases

    PaxDbi P70444.
    PRIDEi P70444.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000004560 ; ENSMUSP00000004560 ; ENSMUSG00000004446 .
    ENSMUST00000160684 ; ENSMUSP00000125731 ; ENSMUSG00000004446 .
    GeneIDi 12122.
    KEGGi mmu:12122.
    UCSCi uc009dnv.1. mouse.

    Organism-specific databases

    CTDi 637.
    MGIi MGI:108093. Bid.

    Phylogenomic databases

    eggNOGi NOG78659.
    GeneTreei ENSGT00390000002868.
    HOGENOMi HOG000010016.
    HOVERGENi HBG001703.
    InParanoidi P70444.
    KOi K04726.
    OMAi KVADHTP.
    OrthoDBi EOG73V6MW.
    PhylomeDBi P70444.
    TreeFami TF102047.

    Enzyme and pathway databases

    Reactomei REACT_202639. Activation, translocation and oligomerization of BAX.
    REACT_208000. Activation, myristolyation of BID and translocation to mitochondria.
    REACT_210929. Activation and oligomerization of BAK protein.
    REACT_223399. BH3-only proteins associate with and inactivate anti-apoptotic BCL-2 members.

    Miscellaneous databases

    EvolutionaryTracei P70444.
    NextBioi 280439.
    PMAP-CutDB P70444.
    PROi P70444.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P70444.
    Bgeei P70444.
    CleanExi MM_BID.
    Genevestigatori P70444.

    Family and domain databases

    InterProi IPR020728. Bcl2_BH3_motif_CS.
    IPR010479. BID.
    [Graphical view ]
    Pfami PF06393. BID. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF038018. BID. 1 hit.
    PROSITEi PS01259. BH3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 126 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