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Q8CI32

- BAG5_MOUSE

UniProt

Q8CI32 - BAG5_MOUSE

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Protein
BAG family molecular chaperone regulator 5
Gene
Bag5
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at protein leveli

Functioni

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.

GO - Molecular functioni

  1. chaperone binding Source: BHF-UCL

GO - Biological processi

  1. negative regulation of protein refolding Source: BHF-UCL
  2. negative regulation of protein ubiquitination Source: BHF-UCL
  3. negative regulation of ubiquitin-protein transferase activity Source: BHF-UCL
  4. neuron death Source: BHF-UCL
  5. regulation of inclusion body assembly Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Names & Taxonomyi

Protein namesi
Recommended name:
BAG family molecular chaperone regulator 5
Short name:
BAG-5
Alternative name(s):
Bcl-2-associated athanogene 5
Gene namesi
Name:Bag5
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 12

Organism-specific databases

MGIiMGI:1917619. Bag5.

Subcellular locationi

GO - Cellular componenti

  1. inclusion body Source: BHF-UCL
  2. perinuclear region of cytoplasm Source: BHF-UCL
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 447447BAG family molecular chaperone regulator 5
PRO_0000088873Add
BLAST

Proteomic databases

MaxQBiQ8CI32.
PaxDbiQ8CI32.
PRIDEiQ8CI32.

PTM databases

PhosphoSiteiQ8CI32.

Expressioni

Gene expression databases

ArrayExpressiQ8CI32.
BgeeiQ8CI32.
CleanExiMM_BAG5.
GenevestigatoriQ8CI32.

Interactioni

Subunit structurei

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

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi10 – 2213
Helixi24 – 285
Helixi38 – 5518
Helixi62 – 8625

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1UGONMR-A1-86[»]
ProteinModelPortaliQ8CI32.
SMRiQ8CI32. Positions 1-89, 276-447.

Miscellaneous databases

EvolutionaryTraceiQ8CI32.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini9 – 8678BAG 1
Add
BLAST
Domaini95 – 16773BAG 2
Add
BLAST
Domaini182 – 26079BAG 3
Add
BLAST
Domaini275 – 35076BAG 4
Add
BLAST
Domaini365 – 44278BAG 5
Add
BLAST

Domaini

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

Sequence similaritiesi

Contains 5 BAG domains.

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG262724.
GeneTreeiENSGT00530000063256.
HOGENOMiHOG000070447.
HOVERGENiHBG004810.
InParanoidiQ8CI32.
KOiK09559.
OMAiDMGNQHP.
OrthoDBiEOG7WX08F.
PhylomeDBiQ8CI32.
TreeFamiTF102014.

Family and domain databases

Gene3Di1.20.58.120. 4 hits.
InterProiIPR003103. BAG_domain.
[Graphical view]
PfamiPF02179. BAG. 4 hits.
[Graphical view]
SMARTiSM00264. BAG. 4 hits.
[Graphical view]
PROSITEiPS51035. BAG. 4 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8CI32-1 [UniParc]FASTAAdd to Basket

« Hide

MDMGNQHPSI SRLQEIQREV KAIEPQVVGF SGLSDDKNYK RLERILTKQL    50
FEIDSVDTEG KGDIQQARKR AAQETERLLK ELEQNANHPH RIEIQNIFKE 100
AQALVKDKIV PFYSGGNCVT DEFEEGIQDI ILRLTHVKTG GKVSLRKARY 150
RTLTKICAVQ EVIEDCMKKQ PSLPLSEDVH PSVAKINSVM CEVNKARGTL 200
IALLMGVDSS ETCRHLSCVL SGLIADLDAL DVCGRTEIRN YRREVVEDIN 250
KLLKYLDLEE EADSTHAFDL GQNHSIIKIE NVLKRMREIK NELLQAQSPP 300
ELYLRAKTEL QGLIGQLDEV SLEKNPCIRE ARRRAVIEVQ ILITYLDLKE 350
ALEKRKLFPC EEHPPHKAVW EILGNLSEIL GEVLSFGGNR TDKNYIRLEE 400
LLTKQLLALD AVDPQGEEKC KAARKQAVKL AQNILSYLDM KSDEWEY 447
Length:447
Mass (Da):50,943
Last modified:March 1, 2003 - v1
Checksum:i72E2C5472DA95416
GO

Sequence cautioni

The sequence BAB24105.1 differs from that shown. Reason: Frameshift at positions 5, 8, 16, 34, 40, 42, 44, 54, 56 and 64.
The sequence AAH27827.1 differs from that shown. Reason: Erroneous initiation.

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti6 – 61Q → H in BAB24105. 1 Publication
Sequence conflicti23 – 231I → K in BAB24105. 1 Publication
Sequence conflicti36 – 361D → E in BAB24105. 1 Publication
Sequence conflicti52 – 521E → G in BAB24105. 1 Publication
Sequence conflicti142 – 1421K → E in BAB24105. 1 Publication
Sequence conflicti148 – 1481A → S in BAB24105. 1 Publication
Sequence conflicti341 – 3411I → T in AAH27827. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK005534 mRNA. Translation: BAB24105.1. Frameshift.
AK160246 mRNA. Translation: BAE35711.1.
BC027827 mRNA. Translation: AAH27827.1. Different initiation.
BC037642 mRNA. Translation: AAH37642.1.
CCDSiCCDS26185.1.
RefSeqiNP_081680.1. NM_027404.2.
XP_006516279.1. XM_006516216.1.
XP_006516280.1. XM_006516217.1.
XP_006516281.1. XM_006516218.1.
UniGeneiMm.44239.

Genome annotation databases

EnsembliENSMUST00000054636; ENSMUSP00000051049; ENSMUSG00000049792.
ENSMUST00000160576; ENSMUSP00000125183; ENSMUSG00000049792.
GeneIDi70369.
KEGGimmu:70369.
UCSCiuc007pdr.3. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK005534 mRNA. Translation: BAB24105.1 . Frameshift.
AK160246 mRNA. Translation: BAE35711.1 .
BC027827 mRNA. Translation: AAH27827.1 . Different initiation.
BC037642 mRNA. Translation: AAH37642.1 .
CCDSi CCDS26185.1.
RefSeqi NP_081680.1. NM_027404.2.
XP_006516279.1. XM_006516216.1.
XP_006516280.1. XM_006516217.1.
XP_006516281.1. XM_006516218.1.
UniGenei Mm.44239.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1UGO NMR - A 1-86 [» ]
ProteinModelPortali Q8CI32.
SMRi Q8CI32. Positions 1-89, 276-447.
ModBasei Search...
MobiDBi Search...

PTM databases

PhosphoSitei Q8CI32.

Proteomic databases

MaxQBi Q8CI32.
PaxDbi Q8CI32.
PRIDEi Q8CI32.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000054636 ; ENSMUSP00000051049 ; ENSMUSG00000049792 .
ENSMUST00000160576 ; ENSMUSP00000125183 ; ENSMUSG00000049792 .
GeneIDi 70369.
KEGGi mmu:70369.
UCSCi uc007pdr.3. mouse.

Organism-specific databases

CTDi 9529.
MGIi MGI:1917619. Bag5.

Phylogenomic databases

eggNOGi NOG262724.
GeneTreei ENSGT00530000063256.
HOGENOMi HOG000070447.
HOVERGENi HBG004810.
InParanoidi Q8CI32.
KOi K09559.
OMAi DMGNQHP.
OrthoDBi EOG7WX08F.
PhylomeDBi Q8CI32.
TreeFami TF102014.

Miscellaneous databases

EvolutionaryTracei Q8CI32.
NextBioi 331467.
PROi Q8CI32.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q8CI32.
Bgeei Q8CI32.
CleanExi MM_BAG5.
Genevestigatori Q8CI32.

Family and domain databases

Gene3Di 1.20.58.120. 4 hits.
InterProi IPR003103. BAG_domain.
[Graphical view ]
Pfami PF02179. BAG. 4 hits.
[Graphical view ]
SMARTi SM00264. BAG. 4 hits.
[Graphical view ]
PROSITEi PS51035. BAG. 4 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiBAG5_MOUSE
AccessioniPrimary (citable) accession number: Q8CI32
Secondary accession number(s): Q3TVA8, Q8K175, Q9DAU0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 21, 2005
Last sequence update: March 1, 2003
Last modified: September 3, 2014
This is version 106 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi