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Q9JLV1

- BAG3_MOUSE

UniProt

Q9JLV1 - BAG3_MOUSE

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Protein

BAG family molecular chaperone regulator 3

Gene

Bag3

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Inhibits the chaperone activity of HSP70/HSC70 by promoting substrate release. Has anti-apoptotic activity.

GO - Molecular functioni

  1. protein complex binding Source: MGI

GO - Biological processi

  1. brain development Source: Ensembl
  2. cellular response to mechanical stimulus Source: MGI
  3. extrinsic apoptotic signaling pathway in absence of ligand Source: MGI
  4. extrinsic apoptotic signaling pathway via death domain receptors Source: MGI
  5. negative regulation of striated muscle cell apoptotic process Source: MGI
  6. protein stabilization Source: MGI
  7. spinal cord development Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Biological processi

Apoptosis

Names & Taxonomyi

Protein namesi
Recommended name:
BAG family molecular chaperone regulator 3
Short name:
BAG-3
Alternative name(s):
Bcl-2-associated athanogene 3
Bcl-2-binding protein Bis
Gene namesi
Name:Bag3
Synonyms:Bis
ORF Names:MNCb-2243
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 7

Organism-specific databases

MGIiMGI:1352493. Bag3.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: MGI
  2. neuron projection Source: Ensembl
  3. plasma membrane Source: Ensembl
  4. Z disc Source: MGI
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 577576BAG family molecular chaperone regulator 3PRO_0000088869Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity
Modified residuei204 – 2041PhosphoserineBy similarity
Modified residuei280 – 2801PhosphoserineBy similarity
Modified residuei281 – 2811PhosphoserineBy similarity
Modified residuei285 – 2851PhosphoserineBy similarity
Modified residuei291 – 2911PhosphothreonineBy similarity
Modified residuei297 – 2971Phosphoserine1 Publication
Modified residuei382 – 3821PhosphoserineBy similarity
Modified residuei390 – 3901Phosphoserine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9JLV1.
PaxDbiQ9JLV1.
PRIDEiQ9JLV1.

PTM databases

PhosphoSiteiQ9JLV1.

Expressioni

Gene expression databases

BgeeiQ9JLV1.
CleanExiMM_BAG3.
GenevestigatoriQ9JLV1.

Interactioni

Subunit structurei

Binds to the ATPase domain of HSP/HSC70 chaperones. Binds to Bcl-2 and PLC-gamma (By similarity). Interacts with DNAJB6 (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
EBNA-LPQ8AZK72EBI-309231,EBI-1185167From a different organism.

Protein-protein interaction databases

BioGridi205891. 6 interactions.
IntActiQ9JLV1. 4 interactions.
MINTiMINT-4124913.

Structurei

Secondary structure

1
577
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi417 – 4204
Helixi425 – 44521
Beta strandi451 – 4533
Helixi454 – 47118
Helixi479 – 50325

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1UK5NMR-A406-503[»]
ProteinModelPortaliQ9JLV1.
SMRiQ9JLV1. Positions 18-57, 401-503.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9JLV1.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini22 – 5635WW 1PROSITE-ProRule annotationAdd
BLAST
Domaini126 – 15732WW 2PROSITE-ProRule annotationAdd
BLAST
Domaini426 – 50378BAGPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi186 – 1938Poly-Ser

Sequence similaritiesi

Contains 1 BAG domain.PROSITE-ProRule annotation
Contains 2 WW domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG238690.
GeneTreeiENSGT00530000063256.
HOGENOMiHOG000050234.
HOVERGENiHBG003419.
InParanoidiQ9JLV1.
KOiK09557.
OMAiVYPQLRP.
OrthoDBiEOG75B85S.
TreeFamiTF102013.

Family and domain databases

Gene3Di1.20.58.120. 1 hit.
InterProiIPR003103. BAG_domain.
IPR001202. WW_dom.
[Graphical view]
PfamiPF02179. BAG. 1 hit.
PF00397. WW. 1 hit.
[Graphical view]
SMARTiSM00264. BAG. 1 hit.
SM00456. WW. 1 hit.
[Graphical view]
SUPFAMiSSF51045. SSF51045. 1 hit.
PROSITEiPS51035. BAG. 1 hit.
PS01159. WW_DOMAIN_1. 1 hit.
PS50020. WW_DOMAIN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9JLV1-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSAATQSPMM QMASGNGASD RDPLPPGWEI KIDPQTGWPF FVDHNSRTTT
60 70 80 90 100
WNDPRVPPEG PKDTASSANG PSRDGSRLLP IREGHPIYPQ LRPGYIPIPV
110 120 130 140 150
LHEGSENRQP HLFHAYSQPG VQRFRTEAAA ATPQRSQSPL RGGMTEAAQT
160 170 180 190 200
DKQCGQMPAT ATTAAAQPPT AHGPERSQSP AASDCSSSSS SASLPSSGRS
210 220 230 240 250
SLGSHQLPRG YIPIPVIHEQ NITRPAAQPS FHQAQKTHYP AQQGEYQPQQ
260 270 280 290 300
PVYHKIQGDD WEPRPLRAAS PFRSPVRGAS SREGSPARSG TPVHCPSPIR
310 320 330 340 350
VHTVVDRPQP MTHREPPPVT QPENKPESKP GPAGPDLPPG HIPIQVIRRE
360 370 380 390 400
ADSKPVSQKS PPPAEKVEVK VSSAPIPCPS PSPAPSAVPS PPKNVAAEQK
410 420 430 440 450
AAPSPAPAEP AAPKSGEAET PPKHPGVLKV EAILEKVQGL EQAVDSFEGK
460 470 480 490 500
KTDKKYLMIE EYLTKELLAL DSVDPEGRAD VRQARRDGVR KVQTILEKLE
510 520 530 540 550
QKAIDVPGQV QVYELQPSNL EAEQPLQEIM GAVVADKDKK GPENKDPQTE
560 570
SQQLEAKAAT PPNPSNPADS AGNLVAP
Length:577
Mass (Da):61,860
Last modified:July 27, 2011 - v2
Checksum:i7BBF296A4A2EF7E3
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti74 – 741D → N in AAF26840. (PubMed:10597216)Curated
Sequence conflicti527 – 5271Q → P in AAF26840. (PubMed:10597216)Curated
Sequence conflicti539 – 5391K → E in BAA95066. 1 PublicationCurated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF130471 mRNA. Translation: AAF26840.1.
AB041583 mRNA. Translation: BAA95066.1.
AK007414 mRNA. Translation: BAB25024.1.
AK016510 mRNA. Translation: BAB30278.1.
AK036675 mRNA. Translation: BAC29531.1.
CH466531 Genomic DNA. Translation: EDL17651.1.
CCDSiCCDS21898.1.
RefSeqiNP_038891.4. NM_013863.5.
UniGeneiMm.84073.

Genome annotation databases

EnsembliENSMUST00000033136; ENSMUSP00000033136; ENSMUSG00000030847.
GeneIDi29810.
KEGGimmu:29810.
UCSCiuc009jzb.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF130471 mRNA. Translation: AAF26840.1 .
AB041583 mRNA. Translation: BAA95066.1 .
AK007414 mRNA. Translation: BAB25024.1 .
AK016510 mRNA. Translation: BAB30278.1 .
AK036675 mRNA. Translation: BAC29531.1 .
CH466531 Genomic DNA. Translation: EDL17651.1 .
CCDSi CCDS21898.1.
RefSeqi NP_038891.4. NM_013863.5.
UniGenei Mm.84073.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1UK5 NMR - A 406-503 [» ]
ProteinModelPortali Q9JLV1.
SMRi Q9JLV1. Positions 18-57, 401-503.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 205891. 6 interactions.
IntActi Q9JLV1. 4 interactions.
MINTi MINT-4124913.

PTM databases

PhosphoSitei Q9JLV1.

Proteomic databases

MaxQBi Q9JLV1.
PaxDbi Q9JLV1.
PRIDEi Q9JLV1.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000033136 ; ENSMUSP00000033136 ; ENSMUSG00000030847 .
GeneIDi 29810.
KEGGi mmu:29810.
UCSCi uc009jzb.2. mouse.

Organism-specific databases

CTDi 9531.
MGIi MGI:1352493. Bag3.

Phylogenomic databases

eggNOGi NOG238690.
GeneTreei ENSGT00530000063256.
HOGENOMi HOG000050234.
HOVERGENi HBG003419.
InParanoidi Q9JLV1.
KOi K09557.
OMAi VYPQLRP.
OrthoDBi EOG75B85S.
TreeFami TF102013.

Miscellaneous databases

EvolutionaryTracei Q9JLV1.
NextBioi 306958.
PROi Q9JLV1.
SOURCEi Search...

Gene expression databases

Bgeei Q9JLV1.
CleanExi MM_BAG3.
Genevestigatori Q9JLV1.

Family and domain databases

Gene3Di 1.20.58.120. 1 hit.
InterProi IPR003103. BAG_domain.
IPR001202. WW_dom.
[Graphical view ]
Pfami PF02179. BAG. 1 hit.
PF00397. WW. 1 hit.
[Graphical view ]
SMARTi SM00264. BAG. 1 hit.
SM00456. WW. 1 hit.
[Graphical view ]
SUPFAMi SSF51045. SSF51045. 1 hit.
PROSITEi PS51035. BAG. 1 hit.
PS01159. WW_DOMAIN_1. 1 hit.
PS50020. WW_DOMAIN_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Bis, a Bcl-2-binding protein that synergizes with Bcl-2 in preventing cell death."
    Lee J.H., Takahashi T., Yasuhara N., Inazawa J., Kamada S., Tsujimoto Y.
    Oncogene 18:6183-6190(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Isolation of full-length cDNA clones from mouse brain cDNA library made by oligo-capping method."
    Osada N., Kusuda J., Tanuma R., Ito A., Hirata M., Sugano S., Hashimoto K.
    Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6.
    Tissue: Brain.
  3. "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: Bone, Pancreas and Testis.
  4. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-297 AND SER-390, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  6. "Solution structure of the murine BAG domain of Bcl2-associated athanogene 3."
    RIKEN structural genomics initiative (RSGI)
    Submitted (FEB-2004) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 404-503.

Entry informationi

Entry nameiBAG3_MOUSE
AccessioniPrimary (citable) accession number: Q9JLV1
Secondary accession number(s): Q9CQL3, Q9JJC7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: July 27, 2011
Last modified: October 29, 2014
This is version 122 of the entry and version 2 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