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Q60739

- BAG1_MOUSE

UniProt

Q60739 - BAG1_MOUSE

Protein

BAG family molecular chaperone regulator 1

Gene

Bag1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 132 (01 Oct 2014)
      Sequence version 3 (15 Jul 1999)
      Previous versions | rss
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    Functioni

    Inhibits the chaperone activity of HSP70/HSC70 by promoting substrate release. Inhibits the pro-apoptotic function of PPP1R15A, and has anti-apoptotic activity. Markedly increases the anti-cell death function of BCL2 induced by various stimuli.1 Publication

    GO - Molecular functioni

    1. phosphoprotein binding Source: MGI
    2. protein binding Source: MGI

    GO - Biological processi

    1. apoptotic process Source: UniProtKB-KW
    2. negative regulation of apoptotic process Source: MGI
    3. negative regulation of motor neuron apoptotic process Source: MGI
    4. negative regulation of protein phosphorylation Source: MGI
    5. neuron differentiation Source: MGI
    6. positive regulation of neuron apoptotic process Source: MGI
    7. positive regulation of transcription from RNA polymerase II promoter Source: MGI
    8. protein localization to mitochondrion Source: MGI

    Keywords - Molecular functioni

    Chaperone

    Keywords - Biological processi

    Apoptosis

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    BAG family molecular chaperone regulator 1
    Short name:
    BAG-1
    Alternative name(s):
    Bcl-2-associated athanogene 1
    Gene namesi
    Name:Bag1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 4

    Organism-specific databases

    MGIiMGI:108047. Bag1.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: MGI
    2. cytosol Source: MGI
    3. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 355355BAG family molecular chaperone regulator 1PRO_0000002782Add
    BLAST

    Post-translational modificationi

    Ubiquitinated; mediated by SIAH1 or SIAH2 and leading to its subsequent proteasomal degradation.1 Publication

    Keywords - PTMi

    Ubl conjugation

    Proteomic databases

    MaxQBiQ60739.
    PaxDbiQ60739.
    PRIDEiQ60739.

    PTM databases

    PhosphoSiteiQ60739.

    Expressioni

    Tissue specificityi

    Isoform 2 is expressed in the heart, lung, kidney and spinal cord. Isoform 1 and isoform 2 are expressed in hematopoietic cell lines. The levels of isoform 2 are relatively constant in all the cell lines examined while the levels of isoform 1 are more variable (at protein level). Isoform 1 is expressed in the lung and kidney. Isoform 2 is expressed in various tissues, with highest levels in testis and stomach.2 Publications

    Gene expression databases

    ArrayExpressiQ60739.
    BgeeiQ60739.
    CleanExiMM_BAG1.
    GenevestigatoriQ60739.

    Interactioni

    Subunit structurei

    Homodimer. Forms a heteromeric complex with HSP70/HSC70. Binds to the ATPase domain of HSP/HSC70 chaperones. Interacts with NR3C1. Interacts with the N-terminal region of STK19. Interacts with PPP1R15A. Interacts with BCL2 in an ATP-dependent manner By similarity.By similarity

    Protein-protein interaction databases

    BioGridi198298. 6 interactions.
    DIPiDIP-272N.

    Structurei

    Secondary structure

    1
    355
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi149 – 1535
    Beta strandi155 – 1606
    Beta strandi163 – 1686
    Beta strandi171 – 1733
    Beta strandi175 – 1773
    Helixi180 – 19112
    Helixi195 – 1973
    Beta strandi200 – 2023
    Beta strandi205 – 2106
    Turni215 – 2184
    Beta strandi220 – 2223
    Beta strandi226 – 2283
    Helixi234 – 26835
    Beta strandi270 – 2723
    Helixi274 – 30330
    Helixi312 – 34635

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1I6ZNMR-A226-355[»]
    2LWPNMR-A137-233[»]
    2M8SNMR-A137-233[»]
    ProteinModelPortaliQ60739.
    SMRiQ60739. Positions 137-355.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ60739.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati103 – 10861
    Repeati111 – 11662
    Repeati117 – 12263
    Repeati123 – 12864
    Repeati129 – 13465
    Repeati141 – 14666
    Repeati147 – 15267
    Domaini154 – 23481Ubiquitin-likePROSITE-ProRule annotationAdd
    BLAST
    Domaini256 – 33681BAGPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni111 – 209997 X 6 AA tandem repeat of E-E-X(4)Add
    BLAST
    Regioni182 – 22948Interaction with HSPA8By similarityAdd
    BLAST
    Regioni226 – 355130Interaction with PPP1R15ABy similarityAdd
    BLAST

    Sequence similaritiesi

    Contains 1 BAG domain.PROSITE-ProRule annotation
    Contains 1 ubiquitin-like domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG72809.
    GeneTreeiENSGT00450000040296.
    HOGENOMiHOG000286009.
    HOVERGENiHBG000236.
    InParanoidiQ9D7K6.
    KOiK09555.
    OrthoDBiEOG7J4482.
    PhylomeDBiQ60739.

    Family and domain databases

    Gene3Di1.20.58.120. 1 hit.
    InterProiIPR003103. BAG_domain.
    IPR017093. Molecular_chp_reg_BAG_1.
    IPR000626. Ubiquitin-like.
    IPR029071. Ubiquitin-rel_dom.
    [Graphical view]
    PfamiPF02179. BAG. 1 hit.
    PF00240. ubiquitin. 1 hit.
    [Graphical view]
    PIRSFiPIRSF037029. BAG_1. 1 hit.
    SMARTiSM00264. BAG. 1 hit.
    SM00213. UBQ. 1 hit.
    [Graphical view]
    SUPFAMiSSF54236. SSF54236. 1 hit.
    PROSITEiPS51035. BAG. 1 hit.
    PS50053. UBIQUITIN_2. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative initiation. Align

    Isoform 1 (identifier: Q60739-1) [UniParc]FASTAAdd to Basket

    Also known as: BAG-1L, p50

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MAGRSAARRP RGDREPLGPR LRAPRPAREP RQSESRAERG LPPSQRSSVR    50
    SAASGHDRST RGAPAGACKP RVKKKVRPRS SQSEKVGSSS RELTRSKKVT 100
    RSKNVTGTQV EEVTKIEEAT QTEEVTVAEE VTQTDNMAKT EEMVQTEEME 150
    TPRLSVIVTH SNERYDLLVT PQQGNSEPVV QDLAQLVEEA TGVPLPFQKL 200
    IFKGKSLKEM ETPLSALGMQ NGCRVMLIGE KSNPEEEVEL KKLKDLEVSA 250
    EKIANHLQEL NKELSGIQQG FLAKELQAEA LCKLDRKVKA TIEQFMKILE 300
    EIDTMVLPEQ FKDSRLKRKN LVKKVQVFLA ECDTVEQYIC QETERLQSTN 350
    LALAE 355
    Length:355
    Mass (Da):39,740
    Last modified:July 15, 1999 - v3
    Checksum:i077A765CA869D3A7
    GO
    Isoform 2 (identifier: Q60739-2) [UniParc]FASTAAdd to Basket

    Also known as: BAG-1S, p32

    The sequence of this isoform differs from the canonical sequence as follows:
         1-136: Missing.

    Show »
    Length:219
    Mass (Da):24,875
    Checksum:i569C8AFFFBB6FBD1
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti64 – 641P → A in AAH93509. (PubMed:15489334)Curated
    Sequence conflicti64 – 641P → A in AAH69918. (PubMed:15489334)Curated
    Sequence conflicti64 – 641P → A in AAH03722. (PubMed:15489334)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 136136Missing in isoform 2. 1 PublicationVSP_018667Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF022223 mRNA. Translation: AAC34259.1.
    AK009149 mRNA. Translation: BAB26106.1.
    AL837521 Genomic DNA. Translation: CAM19843.1.
    CH466538 Genomic DNA. Translation: EDL05422.1.
    BC003722 mRNA. Translation: AAH03722.2.
    BC069918 mRNA. Translation: AAH69918.2.
    BC093509 mRNA. Translation: AAH93509.2.
    CCDSiCCDS38713.1. [Q60739-1]
    CCDS51139.1. [Q60739-2]
    RefSeqiNP_001165210.1. NM_001171739.1. [Q60739-2]
    NP_033866.4. NM_009736.3.
    UniGeneiMm.688.

    Genome annotation databases

    EnsembliENSMUST00000108089; ENSMUSP00000103724; ENSMUSG00000028416. [Q60739-2]
    GeneIDi12017.
    KEGGimmu:12017.

    Keywords - Coding sequence diversityi

    Alternative initiation

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF022223 mRNA. Translation: AAC34259.1 .
    AK009149 mRNA. Translation: BAB26106.1 .
    AL837521 Genomic DNA. Translation: CAM19843.1 .
    CH466538 Genomic DNA. Translation: EDL05422.1 .
    BC003722 mRNA. Translation: AAH03722.2 .
    BC069918 mRNA. Translation: AAH69918.2 .
    BC093509 mRNA. Translation: AAH93509.2 .
    CCDSi CCDS38713.1. [Q60739-1 ]
    CCDS51139.1. [Q60739-2 ]
    RefSeqi NP_001165210.1. NM_001171739.1. [Q60739-2 ]
    NP_033866.4. NM_009736.3.
    UniGenei Mm.688.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1I6Z NMR - A 226-355 [» ]
    2LWP NMR - A 137-233 [» ]
    2M8S NMR - A 137-233 [» ]
    ProteinModelPortali Q60739.
    SMRi Q60739. Positions 137-355.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 198298. 6 interactions.
    DIPi DIP-272N.

    PTM databases

    PhosphoSitei Q60739.

    Proteomic databases

    MaxQBi Q60739.
    PaxDbi Q60739.
    PRIDEi Q60739.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000108089 ; ENSMUSP00000103724 ; ENSMUSG00000028416 . [Q60739-2 ]
    GeneIDi 12017.
    KEGGi mmu:12017.

    Organism-specific databases

    CTDi 573.
    MGIi MGI:108047. Bag1.

    Phylogenomic databases

    eggNOGi NOG72809.
    GeneTreei ENSGT00450000040296.
    HOGENOMi HOG000286009.
    HOVERGENi HBG000236.
    InParanoidi Q9D7K6.
    KOi K09555.
    OrthoDBi EOG7J4482.
    PhylomeDBi Q60739.

    Miscellaneous databases

    EvolutionaryTracei Q60739.
    NextBioi 280235.
    PROi Q60739.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q60739.
    Bgeei Q60739.
    CleanExi MM_BAG1.
    Genevestigatori Q60739.

    Family and domain databases

    Gene3Di 1.20.58.120. 1 hit.
    InterProi IPR003103. BAG_domain.
    IPR017093. Molecular_chp_reg_BAG_1.
    IPR000626. Ubiquitin-like.
    IPR029071. Ubiquitin-rel_dom.
    [Graphical view ]
    Pfami PF02179. BAG. 1 hit.
    PF00240. ubiquitin. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF037029. BAG_1. 1 hit.
    SMARTi SM00264. BAG. 1 hit.
    SM00213. UBQ. 1 hit.
    [Graphical view ]
    SUPFAMi SSF54236. SSF54236. 1 hit.
    PROSITEi PS51035. BAG. 1 hit.
    PS50053. UBIQUITIN_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and functional analysis of BAG-1: a novel Bcl-2-binding protein with anti-cell death activity."
      Takayama S., Sato T., Krajewski S., Kochel K., Irie S., Millan J.A., Reed J.C.
      Cell 80:279-284(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Embryo.
    2. "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] (ISOFORM 2).
      Strain: C57BL/6J.
      Tissue: Tongue.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    4. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
      Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
      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] (ISOFORM 1).
      Strain: Czech II and NMRI.
      Tissue: Mammary tumor.
    6. "Mammalian cells express two differently localized Bag-1 isoforms generated by alternative translation initiation."
      Packham G., Brimmell M., Cleveland J.L.
      Biochem. J. 328:807-813(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION OF ISOFORMS 1 AND 2, ALTERNATIVE INITIATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    7. "Expression and location of Hsp70/Hsc-binding anti-apoptotic protein BAG-1 and its variants in normal tissues and tumor cell lines."
      Takayama S., Krajewski S., Krajewska M., Kitada S., Zapata J.M., Kochel K., Knee D., Scudiero D., Tudor G., Miller G.J., Miyashita T., Yamada M., Reed J.C.
      Cancer Res. 58:3116-3131(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION OF ISOFORMS 1 AND 2, ALTERNATIVE INITIATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    8. "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: FUNCTION.
    9. "Alteration of the stability of Bag-1 protein in the control of olfactory neuronal apoptosis."
      Sourisseau T., Desbois C., Debure L., Bowtell D.D.L., Cato A.C.B., Schneikert J., Moyse E., Michel D.
      J. Cell Sci. 114:1409-1416(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SIAH2, UBIQUITINATION.

    Entry informationi

    Entry nameiBAG1_MOUSE
    AccessioniPrimary (citable) accession number: Q60739
    Secondary accession number(s): Q561N1, Q6IS45, Q9D7K6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: July 15, 1999
    Last modified: October 1, 2014
    This is version 132 of the entry and version 3 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