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Protein

BH3-interacting domain death agonist

Gene

Bid

Organism
Rattus norvegicus (Rat)
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 (By similarity).By similarity

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Apoptosis

Enzyme and pathway databases

ReactomeiR-RNO-111447. Activation of BAD and translocation to mitochondria.
R-RNO-111452. Activation and oligomerization of BAK protein.
R-RNO-111453. BH3-only proteins associate with and inactivate anti-apoptotic BCL-2 members.
R-RNO-114294. Activation, translocation and oligomerization of BAX.
R-RNO-75108. Activation, myristolyation of BID and translocation to mitochondria.

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
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 4

Organism-specific databases

RGDi620160. Bid.

Subcellular locationi

  • 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 (By similarity).By similarity

GO - Cellular componenti

  • cytosol Source: RGD
  • extracellular exosome Source: Ensembl
  • integral component of mitochondrial membrane Source: Ensembl
  • mitochondrion Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane, Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002233691 – 196BH3-interacting domain death agonistAdd BLAST196
ChainiPRO_000022337061 – 196BH3-interacting domain death agonist p15By similarityAdd BLAST136
ChainiPRO_000022337177 – 196BH3-interacting domain death agonist p13By similarityAdd BLAST120
ChainiPRO_0000223372100 – 196BH3-interacting domain death agonist p11By similarityAdd BLAST97

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineBy similarity1
Modified residuei79PhosphoserineCombined sources1

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.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei60 – 61CleavageBy similarity2
Sitei76 – 77CleavageBy similarity2
Sitei99 – 100CleavageBy similarity2

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiQ9JLT6.
PRIDEiQ9JLT6.

PTM databases

iPTMnetiQ9JLT6.
PhosphoSitePlusiQ9JLT6.

Expressioni

Gene expression databases

BgeeiENSRNOG00000012439.
ExpressionAtlasiQ9JLT6. baseline and differential.
GenevisibleiQ9JLT6. RN.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

IntActiQ9JLT6. 1 interactor.
MINTiMINT-270234.
STRINGi10116.ENSRNOP00000016776.

Structurei

3D structure databases

ProteinModelPortaliQ9JLT6.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi87 – 101BH3By similarityAdd BLAST15

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

eggNOGiENOG410IVZ7. Eukaryota.
ENOG410ZF8F. LUCA.
GeneTreeiENSGT00390000002868.
HOGENOMiHOG000010016.
HOVERGENiHBG001703.
InParanoidiQ9JLT6.
KOiK04726.
OMAiRDVFRTT.
OrthoDBiEOG091G0LRX.
PhylomeDBiQ9JLT6.
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.

Q9JLT6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDSEVSNGSG LGAEHITNLL VFGFLRNNDR DFHQELEVLG QELPVQVYLE
60 70 80 90 100
GDREDELQTD GSRASRSFYH GRIEPDSESQ DEVIHNIARH LAQAGDELDH
110 120 130 140 150
SIQPTLVRQL AAQFMNGSLS EEDKRNCLAK ALDEVKTSFP RDMENDKAML
160 170 180 190
IMTMLLAKKV ASHAPSLLRD VFRTTVNFIN QNLFSYVRDL VRNEMD
Length:196
Mass (Da):22,249
Last modified:February 21, 2006 - v2
Checksum:iC5F6AD2F5D9B52E3
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti176V → A in AAF61422 (Ref. 2) Curated1
Sequence conflicti185S → F in AAF61422 (Ref. 2) Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF259503 mRNA. Translation: AAF71759.1.
AF136282 mRNA. Translation: AAF61422.1.
RefSeqiNP_073175.1. NM_022684.1.
XP_017448369.1. XM_017592880.1.
UniGeneiRn.31142.

Genome annotation databases

EnsembliENSRNOT00000016776; ENSRNOP00000016776; ENSRNOG00000012439.
GeneIDi64625.
KEGGirno:64625.
UCSCiRGD:620160. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF259503 mRNA. Translation: AAF71759.1.
AF136282 mRNA. Translation: AAF61422.1.
RefSeqiNP_073175.1. NM_022684.1.
XP_017448369.1. XM_017592880.1.
UniGeneiRn.31142.

3D structure databases

ProteinModelPortaliQ9JLT6.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9JLT6. 1 interactor.
MINTiMINT-270234.
STRINGi10116.ENSRNOP00000016776.

PTM databases

iPTMnetiQ9JLT6.
PhosphoSitePlusiQ9JLT6.

Proteomic databases

PaxDbiQ9JLT6.
PRIDEiQ9JLT6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000016776; ENSRNOP00000016776; ENSRNOG00000012439.
GeneIDi64625.
KEGGirno:64625.
UCSCiRGD:620160. rat.

Organism-specific databases

CTDi637.
RGDi620160. Bid.

Phylogenomic databases

eggNOGiENOG410IVZ7. Eukaryota.
ENOG410ZF8F. LUCA.
GeneTreeiENSGT00390000002868.
HOGENOMiHOG000010016.
HOVERGENiHBG001703.
InParanoidiQ9JLT6.
KOiK04726.
OMAiRDVFRTT.
OrthoDBiEOG091G0LRX.
PhylomeDBiQ9JLT6.
TreeFamiTF102047.

Enzyme and pathway databases

ReactomeiR-RNO-111447. Activation of BAD and translocation to mitochondria.
R-RNO-111452. Activation and oligomerization of BAK protein.
R-RNO-111453. BH3-only proteins associate with and inactivate anti-apoptotic BCL-2 members.
R-RNO-114294. Activation, translocation and oligomerization of BAX.
R-RNO-75108. Activation, myristolyation of BID and translocation to mitochondria.

Miscellaneous databases

PROiQ9JLT6.

Gene expression databases

BgeeiENSRNOG00000012439.
ExpressionAtlasiQ9JLT6. baseline and differential.
GenevisibleiQ9JLT6. RN.

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...

Entry informationi

Entry nameiBID_RAT
AccessioniPrimary (citable) accession number: Q9JLT6
Secondary accession number(s): Q9JK60
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 21, 2006
Last sequence update: February 21, 2006
Last modified: November 30, 2016
This is version 103 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

Complete proteome, Reference proteome

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 one 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.