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Q8CI32 (BAG5_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 102. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
BAG family molecular chaperone regulator 5

Short name=BAG-5
Alternative name(s):
Bcl-2-associated athanogene 5
Gene names
Name:Bag5
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length447 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May function as a nucleotide exchange factor for HSP/HSP70, promoting ADP release, and activating Hsp70-mediated refolding. Inhibits both auto-ubiquitination of PARK2 and ubiquitination of target proteins by PARK2 By similarity.

Subunit structure

Binds to the ATPase domain of HSP/HSC70 chaperones. Binds PARK2 By similarity.

Domain

The fifth BAG domain is responsible for the interaction with HSP70 nucleotide-binding domain By similarity.

Sequence similarities

Contains 5 BAG domains.

Sequence caution

The sequence AAH27827.1 differs from that shown. Reason: Erroneous initiation.

The sequence BAB24105.1 differs from that shown. Reason: Frameshift at positions 5, 8, 16, 34, 40, 42, 44, 54, 56 and 64.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 447447BAG family molecular chaperone regulator 5
PRO_0000088873

Regions

Domain9 – 8678BAG 1
Domain95 – 16773BAG 2
Domain182 – 26079BAG 3
Domain275 – 35076BAG 4
Domain365 – 44278BAG 5

Experimental info

Sequence conflict61Q → H in BAB24105. Ref.1
Sequence conflict231I → K in BAB24105. Ref.1
Sequence conflict361D → E in BAB24105. Ref.1
Sequence conflict521E → G in BAB24105. Ref.1
Sequence conflict1421K → E in BAB24105. Ref.1
Sequence conflict1481A → S in BAB24105. Ref.1
Sequence conflict3411I → T in AAH27827. Ref.2

Secondary structure

......... 447
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q8CI32 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 72E2C5472DA95416

FASTA44750,943
        10         20         30         40         50         60 
MDMGNQHPSI SRLQEIQREV KAIEPQVVGF SGLSDDKNYK RLERILTKQL FEIDSVDTEG 

        70         80         90        100        110        120 
KGDIQQARKR AAQETERLLK ELEQNANHPH RIEIQNIFKE AQALVKDKIV PFYSGGNCVT 

       130        140        150        160        170        180 
DEFEEGIQDI ILRLTHVKTG GKVSLRKARY RTLTKICAVQ EVIEDCMKKQ PSLPLSEDVH 

       190        200        210        220        230        240 
PSVAKINSVM CEVNKARGTL IALLMGVDSS ETCRHLSCVL SGLIADLDAL DVCGRTEIRN 

       250        260        270        280        290        300 
YRREVVEDIN KLLKYLDLEE EADSTHAFDL GQNHSIIKIE NVLKRMREIK NELLQAQSPP 

       310        320        330        340        350        360 
ELYLRAKTEL QGLIGQLDEV SLEKNPCIRE ARRRAVIEVQ ILITYLDLKE ALEKRKLFPC 

       370        380        390        400        410        420 
EEHPPHKAVW EILGNLSEIL GEVLSFGGNR TDKNYIRLEE LLTKQLLALD AVDPQGEEKC 

       430        440 
KAARKQAVKL AQNILSYLDM KSDEWEY 

« Hide

References

« Hide 'large scale' references
[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Placenta and Testis.
[2]"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].
Strain: Czech II and FVB/N.
Tissue: Mammary tumor.
[3]"The C-terminal BAG domain of BAG5 induces conformational changes of the Hsp70 nucleotide-binding domain for ADP-ATP exchange."
Arakawa A., Handa N., Ohsawa N., Shida M., Kigawa T., Hayashi F., Shirouzu M., Yokoyama S.
Structure 18:309-319(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 1-86.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK005534 mRNA. Translation: BAB24105.1. Frameshift.
AK160246 mRNA. Translation: BAE35711.1.
BC027827 mRNA. Translation: AAH27827.1. Different initiation.
BC037642 mRNA. Translation: AAH37642.1.
RefSeqNP_081680.1. NM_027404.2.
XP_006516279.1. XM_006516216.1.
XP_006516280.1. XM_006516217.1.
XP_006516281.1. XM_006516218.1.
UniGeneMm.44239.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1UGONMR-A1-86[»]
ProteinModelPortalQ8CI32.
SMRQ8CI32. Positions 1-89, 178-264, 276-447.
ModBaseSearch...
MobiDBSearch...

PTM databases

PhosphoSiteQ8CI32.

Proteomic databases

PaxDbQ8CI32.
PRIDEQ8CI32.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000054636; ENSMUSP00000051049; ENSMUSG00000049792.
ENSMUST00000160576; ENSMUSP00000125183; ENSMUSG00000049792.
GeneID70369.
KEGGmmu:70369.
UCSCuc007pdr.3. mouse.

Organism-specific databases

CTD9529.
MGIMGI:1917619. Bag5.

Phylogenomic databases

eggNOGNOG262724.
GeneTreeENSGT00530000063256.
HOGENOMHOG000070447.
HOVERGENHBG004810.
InParanoidQ8CI32.
KOK09559.
OMADMGNQHP.
OrthoDBEOG7WX08F.
PhylomeDBQ8CI32.
TreeFamTF102014.

Gene expression databases

ArrayExpressQ8CI32.
BgeeQ8CI32.
CleanExMM_BAG5.
GenevestigatorQ8CI32.

Family and domain databases

Gene3D1.20.58.120. 4 hits.
InterProIPR003103. BAG_domain.
[Graphical view]
PfamPF02179. BAG. 4 hits.
[Graphical view]
SMARTSM00264. BAG. 4 hits.
[Graphical view]
PROSITEPS51035. BAG. 4 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ8CI32.
NextBio331467.
PROQ8CI32.
SOURCESearch...

Entry information

Entry nameBAG5_MOUSE
AccessionPrimary (citable) accession number: Q8CI32
Secondary accession number(s): Q3TVA8, Q8K175, Q9DAU0
Entry history
Integrated into UniProtKB/Swiss-Prot: June 21, 2005
Last sequence update: March 1, 2003
Last modified: April 16, 2014
This is version 102 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot