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UniProtKB/Swiss-Prot entry O95816


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

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Entry information
Entry name BAG2_HUMAN
Primary accession number O95816
Secondary accession numbers Q08AS9 Q6FID0
Integrated into Swiss-Prot on January 11, 2001
Sequence was last modified on May 1, 1999 (Sequence version 1)
Annotations were last modified on    December 16, 2008 (Entry version 64)
Name and origin of the protein
Protein name BAG family molecular chaperone regulator 2
Synonyms BAG-2
Bcl-2-associated athanogene 2
Gene name
Name: BAG2
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].
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 [LARGE SCALE MRNA].
TISSUE=Uterus;
DOI=10.1101/gr.GR1547R; PubMed=11230166 [NCBI, ExPASy, EBI, Israel, Japan]
Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B., Klein M., Poustka A.;
"Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs.";
Genome Res. 11:422-435(2001).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature02055; PubMed=14574404 [NCBI, ExPASy, EBI, Israel, Japan]
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-73, AND MASS SPECTROMETRY.
DOI=10.1016/j.molcel.2008.07.007; PubMed=18691976 [NCBI, ExPASy, EBI, Israel, Japan]
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
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
AF095192; AAD16121.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL050287; CAB43388.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CR533496; CAG38527.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL031321; CAI21565.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL136311; CAI21565.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL136311; CAI20515.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL031321; CAI20515.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC125039; AAI25040.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR T08764; T08764.
RefSeq NP_004273.1; -.
UniGene Hs.55220
3D structure databases
ModBase O95816.
Protein-protein interaction databases
IntAct O95816; 20.
PTM databases
PhosphoSite O95816; -.
Organism-specific databases
GeneCards GC06P057145; -.
H-InvDB HIX0022299; -.
HGNC HGNC:938; BAG2.
GenAtlas BAG2.
MIM 603882; gene. [NCBI / EBI]
PharmGKB PA25238; -.
GeneCards O95816.
Gene expression databases
ArrayExpress O95816; -.
CleanEx HS_BAG2; -.
GermOnline ENSG00000112208; Homo sapiens.
Ontologies
GO
GO:0030188; Molecular function: chaperone regulator activity (inferred from direct assay from MGI).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
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; 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
PeptideAtlas O95816; -.
Proteomics databases
PRIDE O95816; -.
Genome annotation databases
Ensembl ENSG00000112208; Homo sapiens. [Contig view]
GeneID 9532; -.
KEGG hsa:9532; -.
Phylogenomic databases
HOGENOM O95816; -.
HOVERGEN O95816; -.
Other
NextBio 35736; -.
SOURCE BAG2; Homo sapiens.
ProtoNet O95816.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Chaperone; Coiled coil; Phosphoprotein.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   211  211     BAG family molecular chaperone regulator 2. PRO_0000088866
DOMAIN   109   189  81     BAG. 
COILED   20    61  42     Potential. 
MOD_RES   73    73        Phosphoserine. 
CONFLICT   180   180        N -> D (in Ref. 3; CAG38527). 
Sequence information
Length: 211 AA [This is the length of the unprocessed precursor] Molecular weight: 23772 Da [This is the MW of the unprocessed precursor] CRC64: CAF631F4578FCCA3 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MAQAKINAKA NEGRFCRSSS MADRSSRLLE SLDQLELRVE ALREAATAVE QEKEILLEMI 

        70         80         90        100        110        120 
HSIQNSQDMR QISDGEREEL NLTANRLMGR TLTVEVSVET IRNPQQQESL KHATRIIDEV 

       130        140        150        160        170        180 
VNKFLDDLGN AKSHLMSLYS ACSSEVPHGP VDQKFQSIVI GCALEDQKKI KRRLETLLRN 

       190        200        210 
IENSDKAIKL LEHSKGAGSK TLQQNAESRF N 

O95816 in FASTA format

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BLAST logo BLAST submission on ExPASy/SIB
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Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
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