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UniProtKB/Swiss-Prot entry P55957


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name BID_HUMAN
Primary accession number P55957
Secondary accession numbers Q549M7 Q71T04 Q7Z4M9 Q8IY86
Integrated into Swiss-Prot on November 1, 1997
Sequence was last modified on November 1, 1997 (Sequence version 1)
Annotations were last modified on    June 16, 2009 (Entry version 91)
Name and origin of the protein
Protein name BH3-interacting domain death agonist
Synonyms p22 BID
BID
Contains BH3-interacting domain death agonist p15
     (p15 BID)
BH3-interacting domain death agonist p13
     (p13 BID)
BH3-interacting domain death agonist p11
     (p11 BID)
Gene name
Name: BID
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE (ISOFORM 1).
PubMed=8918887 [NCBI, ExPASy, EBI, Israel, Japan]
Wang K., Yin X.-M., Chao D.T., Milliman C.L., Korsmeyer S.J.;
"BID: a novel BH3 domain-only death agonist.";
Genes Dev. 10:2859-2869(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
DOI=10.1006/geno.1998.5392; PubMed=9721221 [NCBI, ExPASy, EBI, Israel, Japan]
Footz T.K., Birren B., Minoshima S., Asakawa S., Shimizu N., Riazi M.A., McDermid H.E.;
"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.";
Genomics 51:472-475(1998).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4), SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND FUNCTION.
DOI=10.1074/jbc.M309769200; PubMed=14583606 [NCBI, ExPASy, EBI, Israel, Japan]
Renshaw S.A., Dempsey C.E., Barnes F.A., Bagstaff S.M., Dower S.K., Bingle C.D., Whyte M.K.;
"Three novel Bid proteins generated by alternative splicing of the human Bid gene.";
J. Biol. Chem. 279:2846-2855(2004).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Dai F.Y., Yu L., Huang H.B., Jiang C.L., Cui Y.Y., Zhao S.Y.;
"Cloning and expression of a new human cDNA homology to murine apoptic death agonist (BID) mRNA.";
Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
DOI=10.1186/gb-2004-5-10-r84; PubMed=15461802 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"A genome annotation-driven approach to cloning the human ORFeome.";
Genome Biol. 5:RESEARCH84.1-RESEARCH84.11(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201).";
Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT GLY-10.
NIEHS SNPs program;
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT GLN-162.
TISSUE=Brain, and Skin;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-54, AND MASS SPECTROMETRY.
DOI=10.1038/nbt1046; PubMed=15592455 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
Nat. Biotechnol. 23:94-101(2005).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-78, AND MASS SPECTROMETRY.
DOI=10.1126/science.1140321; PubMed=17525332 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage.";
Science 316:1160-1166(2007).
[11]
IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
Colinge J., Superti-Furga G., Bennett K.L.;
Submitted (OCT-2008) to UniProtKB.
[12]
STRUCTURE BY NMR.
DOI=10.1016/S0092-8674(00)80572-3; PubMed=10089877 [NCBI, ExPASy, EBI, Israel, Japan]
Chou J.J., Li H., Salvesen G.S., Yuan J., Wagner G.;
"Solution structure of BID, an intracellular amplifier of apoptotic signaling.";
Cell 96:615-624(1999).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AF042083; AAC34365.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF250233; AAO32633.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY005151; AAF89091.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF087891; AAP97190.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CR456389; CAG30275.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CR407603; CAG28531.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY309922; AAP50259.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC009197; AAH09197.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC022072; AAH22072.2; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC033634; AAH33634.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC036364; AAH36364.2; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00385121; -.
IPI00413587; -.
IPI00420084; -.
IPI00472003; -.
RefSeq NP_001187.1; -.
NP_932070.1; -.
NP_932071.1; -.
UniGene Hs.591054
3D structure databases
PDB
1ZY3; NMR; -; B=82-101.[ExPASy / RCSB / EBI]
2BID; NMR; -; A=1-195.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1ZY3; -.
2BID; -.
ModBase P55957.
Protein-protein interaction databases
IntAct P55957; 8.
PTM databases
PhosphoSite P55957; -.
Enzyme and pathway databases
Pathway_Interaction_DB caspase_pathway; Caspase cascade in apoptosis.
ceramidepathway; Ceramide signaling pathway.
faspathway; FAS signaling pathway (CD95).
hivnefpathway; HIV-1 Nef: Negative effector of Fas and TNF-alpha.
Reactome REACT_578; Apoptosis.
2D gel databases
OGP P55957; -.
Organism-specific databases
GeneCards GC22M016592; -.
H-InvDB HIX0016217; -.
HGNC HGNC:1050; BID.
GenAtlas BID.
HPA CAB003771; -.
HPA000722; -.
MIM 601997; gene. [NCBI / EBI]
PharmGKB PA25353; -.
Gene expression databases
ArrayExpress P55957; -.
Bgee P55957; -.
CleanEx HS_BID; -.
GermOnline ENSG00000015475; Homo sapiens.
Ontologies
GO
GO:0005829; Cellular component: cytosol (inferred from experiment from Reactome).
GO:0005624; Cellular component: membrane fraction (traceable author statement from ProtInc).
GO:0005741; Cellular component: mitochondrial outer membrane (inferred from experiment from Reactome).
GO:0005123; Molecular function: death receptor binding (traceable author statement from ProtInc).
GO:0008633; Biological process: activation of pro-apoptotic gene products (inferred from experiment from Reactome).
GO:0008625; Biological process: induction of apoptosis via death domain receptors (traceable author statement from ProtInc).
GO:0051402; Biological process: neuron apoptosis (traceable author statement from HGNC).
GO:0001836; Biological process: release of cytochrome c from mitochondria (inferred from direct assay from HGNC).
QuickGo view.
Family and domain databases
InterPro IPR000712; Bcl2_BH.
IPR010479; BID.
Graphical view of domain structure.
Pfam PF06393; BID; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF038018; BID; 1.
PROSITE PS01259; BH3; 1.
Proteomic databases
PRIDE P55957; -.
Genome annotation databases
Ensembl ENSG00000015475; Homo sapiens. [Contig view]
GeneID 637; -.
KEGG hsa:637; -.
Phylogenomic databases
HOGENOM P55957; -.
HOVERGEN P55957; -.
OMA P55957; YDDELQT.
Other
NextBio 2578; -.
PMAP-CutDB P55957; -.
SOURCE BID; Homo sapiens.
ProtoNet P55957.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Alternative splicing; Apoptosis; Cytoplasm; Membrane; Mitochondrion; Phosphoprotein; Polymorphism.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   195  195     BH3-interacting domain death agonist. PRO_0000143101
CHAIN   62   195  134     BH3-interacting domain death agonist p15 (By similarity). PRO_0000223233
CHAIN   77   195  119     BH3-interacting domain death agonist p13 (By similarity). PRO_0000223232
CHAIN   100   195  96     BH3-interacting domain death agonist p11 (By similarity). PRO_0000223231
MOTIF   86   100  15     BH3. 
SITE   61    62  2     Cleavage (By similarity). 
SITE   76    77  2     Cleavage (By similarity). 
SITE   99   100  2     Cleavage (By similarity). 
MOD_RES   54    54        Phosphotyrosine. 
MOD_RES   78    78        Phosphoserine. 
VAR_SEQ   1    96        Missing (in isoform 4). VSP_017266
VAR_SEQ   1     1        M -> MCSGAGVMMARWAARGRAGWRSTVRILSPLGHCEPGVSRS CRAAQAM (in isoform 2). VSP_017267
VAR_SEQ   75   137        DSESQEDIIRNIARHLAQVGDSMDRSIPPGLVNGLALQLR NTSRSEEDRNRDLATALEQLLQA -> GASDNNTASAEEETEAAGSVAVERGLHGAATVILKVKKTS SGILPGTSPRSGTAWTVASLRAW (in isoform 3). VSP_017268
VAR_SEQ   138   195        Missing (in isoform 3). VSP_017269
VARIANT   10    10  1     S -> G (in dbSNP:rs8190315 [NCBI]). VAR_018845 
VARIANT   162   162  1     H -> Q (in dbSNP:rs17853595 [NCBI]). VAR_025332 
HELIX   15    27  13      
STRAND   31    33  3      
HELIX   34    40  7      
HELIX   41    43  3      
HELIX   84    98  15      
HELIX   106   114  9      
HELIX   116   118  3      
HELIX   119   135  17      
HELIX   145   162  18      
HELIX   167   179  13      
TURN   180   182  3      
HELIX   183   191  9      
Sequence information
Length: 195 AA [This is the length of the unprocessed precursor] Molecular weight: 21995 Da [This is the MW of the unprocessed precursor] CRC64: B17A07334C1AFBEF [This is a checksum on the sequence]
        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 

P55957 in FASTA format

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