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Reviewed, UniProtKB/Swiss-Prot O95816 (BAG2_HUMAN)

Last modified June 16, 2009. Version 70. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    BAG family molecular chaperone regulator 2
      Short name=BAG-2
Alternative name(s):
    Bcl-2-associated athanogene 2
Gene names
Name: BAG2
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length211 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

Inhibits the chaperone activity of HSP70/HSC70 by promoting substrate release.

Subunit structure

Binds to the ATPase domain of HSP70/HSC chaperones.

Sequence similarities

Contains 1 BAG domain.

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Ontologies

Keywords
   DomainCoiled coil
   Molecular functionChaperone
   PTMPhosphoprotein
Gene Ontology (GO)
   Biological processapoptosis

Inferred from electronic annotation. Source: InterPro

protein folding Ref.1

Traceable author statement. Source: ProtInc

   Molecular functionprotein binding

Inferred from physical interaction. Source: IntAct

Complete GO annotation...

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Binary interactions

With

Entry

#Exp.

IntAct

Notes

MLF2Q157731EBI-355275,EBI-1051875
PSMC4P436861EBI-355275,EBI-743997

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 211211BAG family molecular chaperone regulator 2
PRO_0000088866

Regions

Domain109 – 18981BAG
Coiled coil20 – 6142 Potential

Amino acid modifications

Modified residue731Phosphoserine Ref.6

Experimental info

Sequence conflict1801N → D in CAG38527. Ref.3

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Sequences

Sequence LengthMass (Da)Tools
O95816-1 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: CAF631F4578FCCA3

FASTA21123,772
        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

« Hide

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References

« Hide 'large scale' references
[1]"An evolutionarily conserved family of Hsp70/Hsc70 molecular chaperone regulators."
Takayama S., Xie Z., Reed J.C.
J. Biol. Chem. 274:781-786(1999) [PubMed: 9873016] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs."
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. expand/collapse author list , Tampe J., Heubner D., Wambutt R., Korn B., Klein M., Poustka A.
Genome Res. 11:422-435(2001) [PubMed: 11230166] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Uterus.
[3]"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 (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]"The DNA sequence and analysis of human chromosome 6."
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. expand/collapse author list , 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.
Nature 425:805-811(2003) [PubMed: 14574404] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[6]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed: 18691976] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-73, MASS SPECTROMETRY.
[7]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
+Additional computationally mapped references.

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Cross-references

Sequence databases

AF095192 mRNA. Translation: AAD16121.1.
AL050287 mRNA. Translation: CAB43388.1.
CR533496 mRNA. Translation: CAG38527.1.
AL031321, AL136311 Genomic DNA. Translation: CAI21565.1.
AL136311, AL031321 Genomic DNA. Translation: CAI20515.1.
BC125039 mRNA. Translation: AAI25040.1.
IPIIPI00000643.
PIRT08764.
RefSeqNP_004273.1.
UniGeneHs.55220

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

IntActO95816. 22 interactions.

PTM databases

PhosphoSiteO95816.

Proteomic databases

PeptideAtlasO95816.
PRIDEO95816.

Genome annotation databases

EnsemblENSG00000112208. Homo sapiens. [Contig view]
GeneID9532.
KEGGhsa:9532.

Organism-specific databases

GeneCardsGC06P057145.
H-InvDBHIX0022299.
HGNCHGNC:938. BAG2.
MIM603882. gene.
PharmGKBPA25238.
GenAtlasSearch...

Phylogenomic databases

HOGENOMO95816.
HOVERGENO95816.
OMAO95816. VVSKFLD.

Gene expression databases

ArrayExpressO95816.
BgeeO95816.
CleanExHS_BAG2.
GermOnlineENSG00000112208. Homo sapiens.

Family and domain databases

InterProIPR003103. Apoptosis_reg_Bcl-2_prot_BAG.
[Graphical view]
PfamPF02179. BAG. 1 hit.
[Graphical view]
SMARTSM00264. BAG. 1 hit.
[Graphical view]
PROSITEPS51035. BAG. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio35736.
SOURCESearch...

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Entry information

Entry nameBAG2_HUMAN
AccessionPrimary (citable) accession number: O95816
Secondary accession number(s): Q08AS9, Q6FID0
Entry history
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: May 1, 1999
Last modified: June 16, 2009
This is version 70 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents