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

P55957 (BID_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 146. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

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

The major proteolytic product p15 BID allows the release of cytochrome c By similarity. Isoform 1, isoform 2 and isoform 4 induce ICE-like proteases and apoptosis. Isoform 3 does not induce apoptosis. Counters the protective effect of Bcl-2. Ref.3

Subunit structure

Forms heterodimers either with the pro-apoptotic protein BAX or the anti-apoptotic protein Bcl-2 By similarity. p15 BID interacts with ITCH. Ref.11

Subcellular location

Cytoplasm By similarity. Mitochondrion membrane By similarity. Note: When uncleaved, it is predominantly cytoplasmic. Ref.3

BH3-interacting domain death agonist p15: Mitochondrion membrane By similarity. Note: Translocates to mitochondria as an integral membrane protein By similarity. Ref.3

BH3-interacting domain death agonist p13: Mitochondrion membrane By similarity. Note: Associated with the mitochondrial membrane By similarity. Ref.3

Isoform 1: Cytoplasm Ref.3.

Isoform 3: Cytoplasm Ref.3.

Isoform 2: Mitochondrion membrane. Note: A significant proportion of isoform 2 localizes to mitochondria, it may be cleaved constitutively. Ref.3

Tissue specificity

Isoform 2 and isoform 3 are expressed in spleen, bone marrow, cerebral and cerebellar cortex. Isoform 2 is expressed in spleen, pancreas and placenta (at protein level). Isoform 3 is expressed in lung, pancreas and spleen (at protein level). Isoform 4 is expressed in lung and pancreas (at protein level). Ref.3

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.

Post-translational modification

TNF-alpha induces a caspase-mediated cleavage of p22 BID into a major p15 and minor p13 and p11 products By similarity.

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

Sequence caution

The sequence AAH22072.2 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processApoptosis
   Cellular componentCytoplasm
Membrane
Mitochondrion
   Coding sequence diversityAlternative splicing
Polymorphism
   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 electronic annotation. Source: Ensembl

apoptotic mitochondrial changes

Traceable author statement PubMed 9727492. Source: ProtInc

apoptotic process

Traceable author statement. Source: Reactome

brain development

Inferred from electronic annotation. Source: Ensembl

establishment of protein localization to membrane

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

extrinsic apoptotic signaling pathway via death domain receptors

Traceable author statement PubMed 9727491. Source: ProtInc

glial cell apoptotic process

Inferred from electronic annotation. Source: Ensembl

intrinsic apoptotic signaling pathway

Traceable author statement. Source: Reactome

neuron apoptotic process

Traceable author statement PubMed 16167175. Source: HGNC

positive regulation of apoptotic process

Inferred from mutant phenotype PubMed 17289999PubMed 21525171. Source: UniProtKB

positive regulation of extrinsic apoptotic signaling pathway

Inferred from mutant phenotype PubMed 21459798. Source: UniProtKB

positive regulation of intrinsic apoptotic signaling pathway

Traceable author statement. Source: Reactome

positive regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway

Traceable author statement. Source: Reactome

positive regulation of protein homooligomerization

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

positive regulation of protein insertion into mitochondrial membrane involved in apoptotic signaling pathway

Traceable author statement. Source: Reactome

positive regulation of protein oligomerization

Inferred from direct assay PubMed 19074440. Source: UniProtKB

positive regulation of release of cytochrome c from mitochondria

Inferred from mutant phenotype PubMed 17289999. Source: UniProtKB

protein homooligomerization

Inferred from electronic annotation. Source: Ensembl

protein targeting to mitochondrion

Inferred from electronic annotation. Source: Ensembl

regulation of G1/S transition of mitotic cell cycle

Inferred from electronic annotation. Source: Ensembl

regulation of cell proliferation

Inferred from electronic annotation. Source: Ensembl

regulation of mitochondrial membrane permeability involved in apoptotic process

Inferred from electronic annotation. Source: Ensembl

release of cytochrome c from mitochondria

Inferred from direct assay PubMed 17052454. Source: HGNC

response to estradiol

Inferred from electronic annotation. Source: Ensembl

signal transduction in response to DNA damage

Traceable author statement PubMed 18309324. Source: UniProtKB

   Cellular_componentcytosol

Traceable author statement. Source: Reactome

integral component of mitochondrial membrane

Inferred from electronic annotation. Source: Ensembl

membrane

Traceable author statement Ref.1. Source: ProtInc

mitochondrial outer membrane

Traceable author statement. Source: Reactome

mitochondrion

Traceable author statement PubMed 9727491. Source: ProtInc

   Molecular_functiondeath receptor binding

Traceable author statement Ref.1. Source: ProtInc

protein binding

Inferred from physical interaction PubMed 12624108PubMed 14963330PubMed 15694340PubMed 16697956PubMed 17123957PubMed 17289999PubMed 17485524PubMed 19074440PubMed 21382479PubMed 23374347PubMed 23782464PubMed 9463381. Source: IntAct

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P55957-1)

Also known as: BID(L);

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P55957-2)

Also known as: BID(EL);

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MCSGAGVMMARWAARGRAGWRSTVRILSPLGHCEPGVSRSCRAAQAM
Isoform 3 (identifier: P55957-3)

Also known as: BID(S);

The sequence of this isoform differs from the canonical sequence as follows:
     75-137: DSESQEDIIR...ATALEQLLQA → GASDNNTASA...AWTVASLRAW
     138-195: Missing.
Isoform 4 (identifier: P55957-4)

Also known as: BID(ES);

The sequence of this isoform differs from the canonical sequence as follows:
     1-96: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 195195BH3-interacting domain death agonist
PRO_0000143101
Chain62 – 195134BH3-interacting domain death agonist p15 By similarity
PRO_0000223233
Chain77 – 195119BH3-interacting domain death agonist p13 By similarity
PRO_0000223232
Chain100 – 19596BH3-interacting domain death agonist p11 By similarity
PRO_0000223231

Regions

Motif86 – 10015BH3

Sites

Site61 – 622Cleavage By similarity
Site76 – 772Cleavage By similarity
Site99 – 1002Cleavage By similarity

Amino acid modifications

Modified residue11N-acetylmethionine Ref.13
Modified residue541Phosphotyrosine Ref.9
Modified residue781Phosphoserine Ref.10

Natural variations

Alternative sequence1 – 9696Missing in isoform 4.
VSP_017266
Alternative sequence11M → MCSGAGVMMARWAARGRAGW RSTVRILSPLGHCEPGVSRS CRAAQAM in isoform 2.
VSP_017267
Alternative sequence75 – 13763DSESQ…QLLQA → GASDNNTASAEEETEAAGSV AVERGLHGAATVILKVKKTS SGILPGTSPRSGTAWTVASL RAW in isoform 3.
VSP_017268
Alternative sequence138 – 19558Missing in isoform 3.
VSP_017269
Natural variant101S → G. Ref.7
Corresponds to variant rs8190315 [ dbSNP | Ensembl ].
VAR_018845
Natural variant1621H → Q. Ref.8
Corresponds to variant rs17853595 [ dbSNP | Ensembl ].
VAR_025332
Natural variant1941M → T.
Corresponds to variant rs59225839 [ dbSNP | Ensembl ].
VAR_061041

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (BID(L)) [UniParc].

Last modified November 1, 1997. Version 1.
Checksum: B17A07334C1AFBEF

FASTA19521,995
        10         20         30         40         50         60 
MDCEVNNGSS LRDECITNLL VFGFLQSCSD NSFRRELDAL GHELPVLAPQ WEGYDELQTD 

        70         80         90        100        110        120 
GNRSSHSRLG RIEADSESQE DIIRNIARHL AQVGDSMDRS IPPGLVNGLA LQLRNTSRSE 

       130        140        150        160        170        180 
EDRNRDLATA LEQLLQAYPR DMEKEKTMLV LALLLAKKVA SHTPSLLRDV FHTTVNFINQ 

       190 
NLRTYVRSLA RNGMD 

« Hide

Isoform 2 (BID(EL)) [UniParc].

Checksum: 437706F65542B380
Show »

FASTA24126,836
Isoform 3 (BID(S)) [UniParc].

Checksum: 00B4D060E01FA1B8
Show »

FASTA13714,620
Isoform 4 (BID(ES)) [UniParc].

Checksum: 482F50C9C7DF86B0
Show »

FASTA9911,263

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 (ISOFORM 1).
[2]"The gene for death agonist BID maps to the region of human 22q11.2 duplicated in cat eye syndrome chromosomes and to mouse chromosome 6."
Footz T.K., Birren B., Minoshima S., Asakawa S., Shimizu N., Riazi M.A., McDermid H.E.
Genomics 51:472-475(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]"Three novel Bid proteins generated by alternative splicing of the human Bid gene."
Renshaw S.A., Dempsey C.E., Barnes F.A., Bagstaff S.M., Dower S.K., Bingle C.D., Whyte M.K.
J. Biol. Chem. 279:2846-2855(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4), SUBCELLULAR LOCATION, TISSUE SPECIFICITY, FUNCTION.
[4]"Cloning and expression of a new human cDNA homology to murine apoptic death agonist (BID) mRNA."
Dai F.Y., Yu L., Huang H.B., Jiang C.L., Cui Y.Y., Zhao S.Y.
Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[5]"A genome annotation-driven approach to cloning the human ORFeome."
Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., Beare D.M., Dunham I.
Genome Biol. 5:R84.1-R84.11(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[6]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[7]NIEHS SNPs program
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT GLY-10.
[8]"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] (ISOFORMS 1 AND 2), VARIANT GLN-162.
Tissue: Brain and Skin.
[9]"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-54, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-78, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
[11]"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.
[12]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"Solution structure of BID, an intracellular amplifier of apoptotic signaling."
Chou J.J., Li H., Salvesen G.S., Yuan J., Wagner G.
Cell 96:615-624(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF042083 mRNA. Translation: AAC34365.1.
AF250233 mRNA. Translation: AAO32633.1.
AY005151 mRNA. Translation: AAF89091.1.
AF087891 mRNA. Translation: AAP97190.1.
CR456389 mRNA. Translation: CAG30275.1.
CR407603 mRNA. Translation: CAG28531.1.
AY309922 Genomic DNA. Translation: AAP50259.1.
BC009197 mRNA. Translation: AAH09197.1.
BC022072 mRNA. Translation: AAH22072.2. Different initiation.
BC033634 mRNA. Translation: AAH33634.1.
BC036364 mRNA. Translation: AAH36364.2.
CCDSCCDS13747.1. [P55957-2]
CCDS13748.1. [P55957-1]
CCDS13749.1. [P55957-4]
RefSeqNP_001187.1. NM_001196.3. [P55957-1]
NP_001231496.1. NM_001244567.1. [P55957-1]
NP_001231498.1. NM_001244569.1. [P55957-4]
NP_001231499.1. NM_001244570.1. [P55957-4]
NP_001231501.1. NM_001244572.1. [P55957-4]
NP_932070.1. NM_197966.2. [P55957-2]
NP_932071.1. NM_197967.2. [P55957-4]
UniGeneHs.591054.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1ZY3NMR-B82-101[»]
2BIDNMR-A1-195[»]
2KBWNMR-B76-106[»]
2M5BNMR-B80-101[»]
2M5INMR-A61-195[»]
4BD2X-ray2.21C76-109[»]
ProteinModelPortalP55957.
SMRP55957. Positions 1-195.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107106. 43 interactions.
DIPDIP-34937N.
IntActP55957. 27 interactions.
MINTMINT-270277.
STRING9606.ENSP00000318822.

Chemistry

BindingDBP55957.

PTM databases

PhosphoSiteP55957.

Polymorphism databases

DMDM2493285.

2D gel databases

OGPP55957.

Proteomic databases

MaxQBP55957.
PaxDbP55957.
PRIDEP55957.

Protocols and materials databases

DNASU637.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000317361; ENSP00000318822; ENSG00000015475. [P55957-2]
ENST00000342111; ENSP00000344594; ENSG00000015475. [P55957-3]
ENST00000399765; ENSP00000382667; ENSG00000015475. [P55957-4]
ENST00000399767; ENSP00000382669; ENSG00000015475. [P55957-4]
ENST00000399774; ENSP00000382674; ENSG00000015475. [P55957-1]
ENST00000551952; ENSP00000449236; ENSG00000015475. [P55957-1]
GeneID637.
KEGGhsa:637.
UCSCuc002znc.2. human. [P55957-2]
uc002znd.2. human. [P55957-1]

Organism-specific databases

CTD637.
GeneCardsGC22M018216.
HGNCHGNC:1050. BID.
HPACAB003771.
HPA000722.
MIM601997. gene.
neXtProtNX_P55957.
PharmGKBPA25353.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG78659.
HOGENOMHOG000010016.
HOVERGENHBG001703.
InParanoidP55957.
KOK04726.
OMAKVADHTP.
OrthoDBEOG73V6MW.
PhylomeDBP55957.
TreeFamTF102047.

Enzyme and pathway databases

ReactomeREACT_578. Apoptosis.

Gene expression databases

ArrayExpressP55957.
BgeeP55957.
CleanExHS_BID.
GenevestigatorP55957.

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

ChiTaRSBID. human.
EvolutionaryTraceP55957.
GeneWikiBH3_interacting-domain_death_agonist.
BH3_interacting_domain_death_agonist.
GenomeRNAi637.
NextBio2578.
PMAP-CutDBP55957.
PROP55957.
SOURCESearch...

Entry information

Entry nameBID_HUMAN
AccessionPrimary (citable) accession number: P55957
Secondary accession number(s): Q549M7 expand/collapse secondary AC list , Q71T04, Q7Z4M9, Q8IY86
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: July 9, 2014
This is version 146 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 22

Human chromosome 22: entries, gene names and cross-references to MIM