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O95816 (BAG2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 120. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length211 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Subunit structure

Binds to the ATPase domain of HSP/HSC70 chaperones.

Sequence similarities

Contains 1 BAG domain.

Ontologies

Keywords
   DomainCoiled coil
   Molecular functionChaperone
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processprotein folding

Traceable author statement Ref.1. Source: ProtInc

protein metabolic process

Inferred from direct assay PubMed 9873015. Source: MGI

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

EBNA-LPQ8AZK72EBI-355275,EBI-1185167From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.9
Chain2 – 211210BAG family molecular chaperone regulator 2
PRO_0000088866

Regions

Domain109 – 18981BAG
Coiled coil20 – 6142 Potential

Amino acid modifications

Modified residue21N-acetylalanine Ref.9
Modified residue201Phosphoserine Ref.7
Modified residue731Phosphoserine Ref.6

Experimental info

Sequence conflict1801N → D in CAG38527. Ref.3

Sequences

Sequence LengthMass (Da)Tools
O95816 [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

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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-73, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[7]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[8]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRT08764.
RefSeqNP_004273.1. NM_004282.3.
UniGeneHs.745046.

3D structure databases

ProteinModelPortalO95816.
SMRO95816. Positions 108-188.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114908. 61 interactions.
IntActO95816. 28 interactions.
MINTMINT-5002329.
STRING9606.ENSP00000359727.

PTM databases

PhosphoSiteO95816.

Proteomic databases

PaxDbO95816.
PeptideAtlasO95816.
PRIDEO95816.

Protocols and materials databases

DNASU9532.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000370693; ENSP00000359727; ENSG00000112208.
GeneID9532.
KEGGhsa:9532.
UCSCuc003pdr.3. human.

Organism-specific databases

CTD9532.
GeneCardsGC06P057084.
HGNCHGNC:938. BAG2.
HPAHPA018862.
HPA019918.
MIM603882. gene.
neXtProtNX_O95816.
PharmGKBPA25238.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG251652.
HOGENOMHOG000073529.
HOVERGENHBG004808.
InParanoidO95816.
KOK09556.
OMAIQAKMNE.
PhylomeDBO95816.
TreeFamTF102012.

Gene expression databases

ArrayExpressO95816.
BgeeO95816.
CleanExHS_BAG2.
GenevestigatorO95816.

Family and domain databases

InterProIPR003103. BAG_domain.
[Graphical view]
PfamPF02179. BAG. 1 hit.
[Graphical view]
SMARTSM00264. BAG. 1 hit.
[Graphical view]
PROSITEPS51035. BAG. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiBAG2.
GenomeRNAi9532.
NextBio35736.
PROO95816.
SOURCESearch...

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: April 16, 2014
This is version 120 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

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

Human chromosome 6

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