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Protein

BH3-interacting domain death agonist

Gene

BID

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.By similarity1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei61 – 622CleavageBy similarity
Sitei76 – 772CleavageBy similarity
Sitei99 – 1002CleavageBy similarity

GO - Molecular functioni

  1. death receptor binding Source: ProtInc

GO - Biological processi

  1. activation of cysteine-type endopeptidase activity involved in apoptotic process Source: Ensembl
  2. apoptotic mitochondrial changes Source: ProtInc
  3. apoptotic process Source: Reactome
  4. brain development Source: Ensembl
  5. establishment of protein localization to membrane Source: BHF-UCL
  6. extrinsic apoptotic signaling pathway via death domain receptors Source: ProtInc
  7. glial cell apoptotic process Source: Ensembl
  8. hepatocyte apoptotic process Source: Ensembl
  9. intrinsic apoptotic signaling pathway Source: Reactome
  10. mitochondrial outer membrane permeabilization Source: Ensembl
  11. neuron apoptotic process Source: HGNC
  12. positive regulation of apoptotic process Source: UniProtKB
  13. positive regulation of extrinsic apoptotic signaling pathway Source: UniProtKB
  14. positive regulation of intrinsic apoptotic signaling pathway Source: Reactome
  15. positive regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway Source: Reactome
  16. positive regulation of protein homooligomerization Source: BHF-UCL
  17. positive regulation of protein insertion into mitochondrial membrane involved in apoptotic signaling pathway Source: Reactome
  18. positive regulation of protein oligomerization Source: UniProtKB
  19. positive regulation of release of cytochrome c from mitochondria Source: UniProtKB
  20. protein homooligomerization Source: Ensembl
  21. protein targeting to mitochondrion Source: Ensembl
  22. regulation of cell proliferation Source: Ensembl
  23. regulation of G1/S transition of mitotic cell cycle Source: Ensembl
  24. release of cytochrome c from mitochondria Source: HGNC
  25. response to estradiol Source: Ensembl
  26. signal transduction in response to DNA damage Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Apoptosis

Enzyme and pathway databases

ReactomeiREACT_330. BH3-only proteins associate with and inactivate anti-apoptotic BCL-2 members.
REACT_549. Activation of BAD and translocation to mitochondria.
REACT_584. Activation, translocation and oligomerization of BAX.
REACT_701. Activation, myristolyation of BID and translocation to mitochondria.
REACT_707. Activation and oligomerization of BAK protein.

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
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 22

Organism-specific databases

HGNCiHGNC:1050. BID.

Subcellular locationi

  1. Cytoplasm By similarity
  2. Mitochondrion membrane By similarity

  3. Note: When uncleaved, it is predominantly cytoplasmic.1 Publication
Chain BH3-interacting domain death agonist p15 :
  1. Mitochondrion membrane By similarity

  2. Note: Translocates to mitochondria as an integral membrane protein.By similarity
Chain BH3-interacting domain death agonist p13 :
  1. Mitochondrion membrane By similarity

  2. Note: Associated with the mitochondrial membrane.By similarity
Isoform 2 :
  1. Mitochondrion membrane

  2. Note: A significant proportion of isoform 2 localizes to mitochondria, it may be cleaved constitutively.

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. extracellular vesicular exosome Source: UniProtKB
  3. integral component of mitochondrial membrane Source: Ensembl
  4. membrane Source: ProtInc
  5. mitochondrial outer membrane Source: Reactome
  6. mitochondrion Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane, Mitochondrion

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA25353.

Polymorphism and mutation databases

BioMutaiBID.
DMDMi2493285.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 195195BH3-interacting domain death agonistPRO_0000143101Add
BLAST
Chaini62 – 195134BH3-interacting domain death agonist p15By similarityPRO_0000223233Add
BLAST
Chaini77 – 195119BH3-interacting domain death agonist p13By similarityPRO_0000223232Add
BLAST
Chaini100 – 19596BH3-interacting domain death agonist p11By similarityPRO_0000223231Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication
Modified residuei54 – 541Phosphotyrosine1 Publication
Modified residuei78 – 781Phosphoserine1 Publication

Post-translational modificationi

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.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP55957.
PaxDbiP55957.
PRIDEiP55957.

2D gel databases

OGPiP55957.

PTM databases

PhosphoSiteiP55957.

Miscellaneous databases

PMAP-CutDBP55957.

Expressioni

Tissue specificityi

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).1 Publication

Gene expression databases

BgeeiP55957.
CleanExiHS_BID.
ExpressionAtlasiP55957. baseline and differential.
GenevestigatoriP55957.

Organism-specific databases

HPAiCAB003771.
HPA000722.

Interactioni

Subunit structurei

Forms heterodimers either with the pro-apoptotic protein BAX or the anti-apoptotic protein Bcl-2 (By similarity). p15 BID interacts with ITCH.By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
AHCYL1O438653EBI-10215147,EBI-2371423
BAK1Q166112EBI-519672,EBI-519866
BAXQ0781216EBI-519672,EBI-516580
BCL2P104158EBI-519672,EBI-77694
Bcl2a1Q074403EBI-519672,EBI-707754From a different organism.
BCL2L1Q078172EBI-519672,EBI-78035
BCL2L1Q07817-16EBI-519672,EBI-287195
BCL2L2Q928435EBI-519672,EBI-707714
CAV1Q031353EBI-519672,EBI-603614
RELQ048643EBI-519672,EBI-307352
VACWR028P173612EBI-519672,EBI-7115640From a different organism.

Protein-protein interaction databases

BioGridi107106. 48 interactions.
DIPiDIP-34937N.
IntActiP55957. 34 interactions.
MINTiMINT-270277.
STRINGi9606.ENSP00000318822.

Structurei

Secondary structure

1
195
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi15 – 2713Combined sources
Beta strandi31 – 333Combined sources
Helixi34 – 407Combined sources
Helixi41 – 433Combined sources
Helixi77 – 9620Combined sources
Helixi97 – 993Combined sources
Beta strandi100 – 1023Combined sources
Helixi106 – 1149Combined sources
Helixi116 – 1183Combined sources
Helixi119 – 13517Combined sources
Helixi145 – 16218Combined sources
Helixi167 – 17913Combined sources
Turni180 – 1823Combined sources
Helixi183 – 1919Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ZY3NMR-B82-101[»]
2BIDNMR-A1-195[»]
2KBWNMR-B76-106[»]
2M5BNMR-B80-101[»]
2M5INMR-A61-195[»]
4BD2X-ray2.21C76-109[»]
ProteinModelPortaliP55957.
SMRiP55957. Positions 1-195.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP55957.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi86 – 10015BH3Add
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.

Phylogenomic databases

eggNOGiNOG78659.
GeneTreeiENSGT00390000002868.
HOGENOMiHOG000010016.
HOVERGENiHBG001703.
InParanoidiP55957.
KOiK04726.
OMAiRDVFRTT.
OrthoDBiEOG73V6MW.
PhylomeDBiP55957.
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]

Sequences (4)i

Sequence statusi: Complete.

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

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P55957-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MDCEVNNGSS LRDECITNLL VFGFLQSCSD NSFRRELDAL GHELPVLAPQ
60 70 80 90 100
WEGYDELQTD GNRSSHSRLG RIEADSESQE DIIRNIARHL AQVGDSMDRS
110 120 130 140 150
IPPGLVNGLA LQLRNTSRSE EDRNRDLATA LEQLLQAYPR DMEKEKTMLV
160 170 180 190
LALLLAKKVA SHTPSLLRDV FHTTVNFINQ NLRTYVRSLA RNGMD
Length:195
Mass (Da):21,995
Last modified:November 1, 1997 - v1
Checksum:iB17A07334C1AFBEF
GO
Isoform 2 (identifier: P55957-2) [UniParc]FASTAAdd to basket

Also known as: BID(EL)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MCSGAGVMMARWAARGRAGWRSTVRILSPLGHCEPGVSRSCRAAQAM

Show »
Length:241
Mass (Da):26,836
Checksum:i437706F65542B380
GO
Isoform 3 (identifier: P55957-3) [UniParc]FASTAAdd to basket

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.

Show »
Length:137
Mass (Da):14,620
Checksum:i00B4D060E01FA1B8
GO
Isoform 4 (identifier: P55957-4) [UniParc]FASTAAdd to basket

Also known as: BID(ES)

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

Show »
Length:99
Mass (Da):11,263
Checksum:i482F50C9C7DF86B0
GO

Sequence cautioni

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

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti10 – 101S → G.1 Publication
Corresponds to variant rs8190315 [ dbSNP | Ensembl ].
VAR_018845
Natural varianti162 – 1621H → Q.1 Publication
Corresponds to variant rs17853595 [ dbSNP | Ensembl ].
VAR_025332
Natural varianti194 – 1941M → T.
Corresponds to variant rs59225839 [ dbSNP | Ensembl ].
VAR_061041

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 9696Missing in isoform 4. 1 PublicationVSP_017266Add
BLAST
Alternative sequencei1 – 11M → MCSGAGVMMARWAARGRAGW RSTVRILSPLGHCEPGVSRS CRAAQAM in isoform 2. 2 PublicationsVSP_017267
Alternative sequencei75 – 13763DSESQ…QLLQA → GASDNNTASAEEETEAAGSV AVERGLHGAATVILKVKKTS SGILPGTSPRSGTAWTVASL RAW in isoform 3. 1 PublicationVSP_017268Add
BLAST
Alternative sequencei138 – 19558Missing in isoform 3. 1 PublicationVSP_017269Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS13747.1. [P55957-2]
CCDS13748.1. [P55957-1]
CCDS13749.1. [P55957-4]
RefSeqiNP_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]
UniGeneiHs.591054.

Genome annotation databases

EnsembliENST00000317361; 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]
ENST00000611040; ENSP00000483709; ENSG00000015475. [P55957-4]
ENST00000614949; ENSP00000477773; ENSG00000015475. [P55957-4]
ENST00000615414; ENSP00000483534; ENSG00000015475. [P55957-4]
ENST00000622694; ENSP00000480414; ENSG00000015475. [P55957-1]
GeneIDi637.
KEGGihsa:637.
UCSCiuc002znc.2. human. [P55957-2]
uc002znd.2. human. [P55957-1]

Polymorphism and mutation databases

BioMutaiBID.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS13747.1. [P55957-2]
CCDS13748.1. [P55957-1]
CCDS13749.1. [P55957-4]
RefSeqiNP_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]
UniGeneiHs.591054.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ZY3NMR-B82-101[»]
2BIDNMR-A1-195[»]
2KBWNMR-B76-106[»]
2M5BNMR-B80-101[»]
2M5INMR-A61-195[»]
4BD2X-ray2.21C76-109[»]
ProteinModelPortaliP55957.
SMRiP55957. Positions 1-195.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107106. 48 interactions.
DIPiDIP-34937N.
IntActiP55957. 34 interactions.
MINTiMINT-270277.
STRINGi9606.ENSP00000318822.

Chemistry

BindingDBiP55957.

PTM databases

PhosphoSiteiP55957.

Polymorphism and mutation databases

BioMutaiBID.
DMDMi2493285.

2D gel databases

OGPiP55957.

Proteomic databases

MaxQBiP55957.
PaxDbiP55957.
PRIDEiP55957.

Protocols and materials databases

DNASUi637.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000317361; 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]
ENST00000611040; ENSP00000483709; ENSG00000015475. [P55957-4]
ENST00000614949; ENSP00000477773; ENSG00000015475. [P55957-4]
ENST00000615414; ENSP00000483534; ENSG00000015475. [P55957-4]
ENST00000622694; ENSP00000480414; ENSG00000015475. [P55957-1]
GeneIDi637.
KEGGihsa:637.
UCSCiuc002znc.2. human. [P55957-2]
uc002znd.2. human. [P55957-1]

Organism-specific databases

CTDi637.
GeneCardsiGC22M018216.
HGNCiHGNC:1050. BID.
HPAiCAB003771.
HPA000722.
MIMi601997. gene.
neXtProtiNX_P55957.
PharmGKBiPA25353.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG78659.
GeneTreeiENSGT00390000002868.
HOGENOMiHOG000010016.
HOVERGENiHBG001703.
InParanoidiP55957.
KOiK04726.
OMAiRDVFRTT.
OrthoDBiEOG73V6MW.
PhylomeDBiP55957.
TreeFamiTF102047.

Enzyme and pathway databases

ReactomeiREACT_330. BH3-only proteins associate with and inactivate anti-apoptotic BCL-2 members.
REACT_549. Activation of BAD and translocation to mitochondria.
REACT_584. Activation, translocation and oligomerization of BAX.
REACT_701. Activation, myristolyation of BID and translocation to mitochondria.
REACT_707. Activation and oligomerization of BAK protein.

Miscellaneous databases

ChiTaRSiBID. human.
EvolutionaryTraceiP55957.
GeneWikiiBH3_interacting-domain_death_agonist.
BH3_interacting_domain_death_agonist.
GenomeRNAii637.
NextBioi2578.
PMAP-CutDBP55957.
PROiP55957.
SOURCEiSearch...

Gene expression databases

BgeeiP55957.
CleanExiHS_BID.
ExpressionAtlasiP55957. baseline and differential.
GenevestigatoriP55957.

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 (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. 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. 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  15. "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.

Entry informationi

Entry nameiBID_HUMAN
AccessioniPrimary (citable) accession number: P55957
Secondary accession number(s): Q549M7
, Q71T04, Q7Z4M9, Q8IY86
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: April 29, 2015
This is version 154 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 22
    Human chromosome 22: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. 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.