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UniProtKB/Swiss-Prot entry O95429


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

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Entry information
Entry name BAG4_HUMAN
Primary accession number O95429
Secondary accession number O95818
Integrated into Swiss-Prot on January 11, 2001
Sequence was last modified on May 1, 1999 (Sequence version 1)
Annotations were last modified on    June 16, 2009 (Entry version 82)
Name and origin of the protein
Protein name BAG family molecular chaperone regulator 4
Synonyms BAG-4
Bcl-2-associated athanogene 4
Silencer of death domains
Gene name
Name: BAG4
Synonyms: SODD
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 [MRNA].
TISSUE=Leukemic T-cell;
DOI=10.1074/jbc.274.2.781; PubMed=9873016 [NCBI, ExPASy, EBI, Israel, Japan]
Takayama S., Xie Z., Reed J.C.;
"An evolutionarily conserved family of Hsp70/Hsc70 molecular chaperone regulators.";
J. Biol. Chem. 274:781-786(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH TNFRSF1A AND TNFRSF12.
TISSUE=Leukemic T-cell;
DOI=10.1126/science.283.5401.543; PubMed=9915703 [NCBI, ExPASy, EBI, Israel, Japan]
Jiang Y., Woronicz J.D., Liu W., Goeddel D.V.;
"Prevention of constitutive TNF receptor 1 signaling by silencer of death domains.";
Science 283:543-546(1999).
[3]
ERRATUM.
Jiang Y., Woronicz J.D., Liu W., Goeddel D.V.;
Science 283:1852-1852(1999).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
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).
[5]
STRUCTURE BY NMR OF 376-457, INTERACTION WITH HSP70, AND MUTAGENESIS OF GLU-414; ASP-424; 438-ARG-LYS-439 AND GLN-446.
DOI=10.1074/jbc.M202792200; PubMed=12058034 [NCBI, ExPASy, EBI, Israel, Japan]
Briknarova K., Takayama S., Homma S., Baker K., Cabezas E., Hoyt D.W., Li Z., Satterthwait A.C., Ely K.R.;
"BAG4/SODD protein contains a short BAG domain.";
J. Biol. Chem. 277:31172-31178(2002).
Comments
  • FUNCTION: Inhibits the chaperone activity of HSP70/HSC70 by promoting substrate release (By similarity). Prevents constitutive TNFRSF1A signaling.
  • SUBUNIT: Binds to the ATPase domain of HSP70/HSC chaperones. Binds to the death domain of TNFRSF1A in the absence of TNF and thereby prevents binding of adapter molecules such as TRADD or TRAF2. Binds to the death domain of TNFRSF12.
  • SUBCELLULAR LOCATION: Cytoplasm.
  • TISSUE SPECIFICITY: Ubiquitous.
  • SIMILARITY: Contains 1 BAG domain.
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
AF095194; AAD16123.2; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF111116; AAD05226.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC038505; AAH38505.2; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00030695; -.
RefSeq NP_004865.1; -.
UniGene Hs.194726
3D structure databases
PDB
1M62; NMR; -; A=376-457.[ExPASy / RCSB / EBI]
1M7K; NMR; -; A=358-456.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1M62; -.
1M7K; -.
SMR O95429; 372-457.
ModBase O95429.
PTM databases
PhosphoSite O95429; -.
Enzyme and pathway databases
Pathway_Interaction_DB ceramidepathway; Ceramide signaling pathway.
hivnefpathway; HIV-1 Nef: Negative effector of Fas and TNF-alpha.
tnfpathway; TNF receptor signaling pathway.
Organism-specific databases
GeneCards GC08P038153; -.
H-InvDB HIX0020972; -.
HGNC HGNC:940; BAG4.
GenAtlas BAG4.
HPA CAB013716; -.
MIM 603884; gene. [NCBI / EBI]
PharmGKB PA25240; -.
Gene expression databases
ArrayExpress O95429; -.
Bgee O95429; -.
CleanEx HS_BAG4; -.
GermOnline ENSG00000156735; Homo sapiens.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-SubCell).
GO:0005057; Molecular function: receptor signaling protein activity (traceable author statement from ProtInc).
GO:0006916; Biological process: anti-apoptosis (traceable author statement from ProtInc).
GO:0006915; Biological process: apoptosis (inferred from electronic annotation from InterPro).
GO:0006457; Biological process: protein folding (traceable author statement from ProtInc).
QuickGo view.
Family and domain databases
InterPro IPR003103; Apoptosis_reg_Bcl-2_prot_BAG.
Graphical view of domain structure.
Pfam PF02179; BAG; 1.
Pfam graphical view of domain structure.
SMART SM00264; BAG; 1.
SMART graphical view of domain structure.
PROSITE PS51035; BAG; 1.
PROSITE graphical view of domain structure (profiles).
Proteomic databases
PRIDE O95429; -.
Genome annotation databases
Ensembl ENSG00000156735; Homo sapiens. [Contig view]
GeneID 9530; -.
KEGG hsa:9530; -.
Phylogenomic databases
HOGENOM O95429; -.
HOVERGEN O95429; -.
OMA O95429; YGNATNE.
Other
NextBio 35728; -.
SOURCE BAG4; Homo sapiens.
ProtoNet O95429.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Chaperone; Cytoplasm.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   457  457     BAG family molecular chaperone regulator 4. PRO_0000088870
DOMAIN   379   456  78     BAG. 
MUTAGEN   414   414        E->A: Reduces interaction with HSP70. 
MUTAGEN   424   424        D->A: Abolishes interaction with HSP70. 
MUTAGEN   438   439        RK->AA: Reduces interaction with HSP70. 
MUTAGEN   446   446        Q->A: Abolishes interaction with HSP70. 
HELIX   380   399  20      
HELIX   407   423  17      
HELIX   432   456  25      
Sequence information
Length: 457 AA [This is the length of the unprocessed precursor] Molecular weight: 49594 Da [This is the MW of the unprocessed precursor] CRC64: B89D59E8118684A3 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSALRRSGYG PSDGPSYGRY YGPGGGDVPV HPPPPLYPLR PEPPQPPISW RVRGGGPAET 

        70         80         90        100        110        120 
TWLGEGGGGD GYYPSGGAWP EPGRAGGSHQ EQPPYPSYNS NYWNSTARSR APYPSTYPVR 

       130        140        150        160        170        180 
PELQGQSLNS YTNGAYGPTY PPGPGANTAS YSGAYYAPGY TQTSYSTEVP STYRSSGNSP 

       190        200        210        220        230        240 
TPVSRWIYPQ QDCQTEAPPL RGQVPGYPPS QNPGMTLPHY PYGDGNRSVP QSGPTVRPQE 

       250        260        270        280        290        300 
DAWASPGAYG MGGRYPWPSS APSAPPGNLY MTESTSPWPS SGSPQSPPSP PVQQPKDSSY 

       310        320        330        340        350        360 
PYSQSDQSMN RHNFPCSVHQ YESSGTVNND DSDLLDSQVQ YSAEPQLYGN ATSDHPNNQD 

       370        380        390        400        410        420 
QSSSLPEECV PSDESTPPSI KKIIHVLEKV QYLEQEVEEF VGKKTDKAYW LLEEMLTKEL 

       430        440        450 
LELDSVETGG QDSVRQARKE AVCKIQAILE KLEKKGL 

O95429 in FASTA format

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