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Q99933

- BAG1_HUMAN

UniProt

Q99933 - BAG1_HUMAN

Protein

BAG family molecular chaperone regulator 1

Gene

BAG1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 151 (01 Oct 2014)
      Sequence version 4 (18 May 2010)
      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.3 Publications

    GO - Molecular functioni

    1. protein binding Source: UniProtKB
    2. receptor signaling protein activity Source: ProtInc

    GO - Biological processi

    1. apoptotic process Source: UniProtKB-KW
    2. cell surface receptor signaling pathway Source: ProtInc
    3. chaperone cofactor-dependent protein refolding Source: UniProtKB
    4. intracellular signal transduction Source: GOC
    5. negative regulation of apoptotic process Source: ProtInc

    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
    Synonyms:HAP
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 9

    Organism-specific databases

    HGNCiHGNC:937. BAG1.

    Subcellular locationi

    Isoform 1 : Nucleus. Cytoplasm
    Note: Isoform 1 localizes predominantly to the nucleus.
    Isoform 2 : Cytoplasm. Nucleus
    Note: Isoform 2 localizes to the cytoplasm and shuttles into the nucleus in response to heat shock.
    Isoform 4 : Cytoplasm. Nucleus
    Note: Isoform 4 localizes predominantly to the cytoplasm. The cellular background in which it is expressed can influence whether it resides primarily in the cytoplasm or is also found in the nucleus. In the presence of BCL2, localizes to intracellular membranes (what appears to be the nuclear envelope and perinuclear membranes) as well as punctate cytosolic structures suggestive of mitochondria.

    GO - Cellular componenti

    1. cytoplasm Source: ProtInc
    2. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA25237.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 345345BAG family molecular chaperone regulator 1PRO_0000088865Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei223 – 2231Phosphoserine1 Publication

    Post-translational modificationi

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

    Keywords - PTMi

    Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ99933.
    PaxDbiQ99933.
    PRIDEiQ99933.

    PTM databases

    PhosphoSiteiQ99933.

    Expressioni

    Tissue specificityi

    Isoform 4 is the most abundantly expressed isoform. It is ubiquitously expressed throughout most tissues, except the liver, colon, breast and uterine myometrium. Isoform 1 is expressed in the ovary and testis. Isoform 4 is expressed in several types of tumor cell lines, and at consistently high levels in leukemia and lymphoma cell lines. Isoform 1 is expressed in the prostate, breast and leukemia cell lines. Isoform 3 is the least abundant isoform in tumor cell lines (at protein level).1 Publication

    Inductioni

    Up-regulated during differentiation of bladder epithelial cells and down-regulated during differentiation of prostate epithelium.1 Publication

    Gene expression databases

    ArrayExpressiQ99933.
    BgeeiQ99933.
    CleanExiHS_BAG1.
    GenevestigatoriQ99933.

    Organism-specific databases

    HPAiCAB002486.
    HPA018121.

    Interactioni

    Subunit structurei

    Homodimer. Forms a heteromeric complex with HSP70/HSC70. Binds to the ATPase domain of HSP/HSC70 chaperones. Isoform 1, isoform 3 and isoform 4 but not isoform 2 interact with HSPA8/HSC70. Interacts with NR3C1. Interacts with the N-terminal region of STK19. Interacts with PPP1R15A. Interacts with BCL2 in an ATP-dependent manner. Isoform 2 does not interact with BCL2.7 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Q53FC72EBI-1030678,EBI-9356749
    Q96BE02EBI-1030678,EBI-9356686
    HSPA8P1114210EBI-1030678,EBI-351896
    PSMD2Q132002EBI-1030678,EBI-357648
    STUB1Q9UNE72EBI-1030678,EBI-357085

    Protein-protein interaction databases

    BioGridi107049. 49 interactions.
    DIPiDIP-3341N.
    IntActiQ99933. 31 interactions.
    MINTiMINT-189058.

    Structurei

    Secondary structure

    1
    345
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi144 – 1496
    Beta strandi151 – 1599
    Beta strandi163 – 1675
    Helixi170 – 18011
    Turni185 – 1873
    Beta strandi189 – 1924
    Beta strandi195 – 1973
    Beta strandi200 – 2034
    Helixi204 – 2074
    Beta strandi211 – 2199
    Helixi224 – 25936
    Helixi264 – 2729
    Helixi275 – 29218
    Helixi302 – 32625

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1HX1X-ray1.90B222-334[»]
    1WXVNMR-A144-222[»]
    3FZFX-ray2.20B222-334[»]
    3FZHX-ray2.00B222-334[»]
    3FZKX-ray2.10B222-334[»]
    3FZLX-ray2.20B222-334[»]
    3FZMX-ray2.30B222-334[»]
    3LDQX-ray1.90B222-334[»]
    3M3ZX-ray2.10B222-334[»]
    ProteinModelPortaliQ99933.
    SMRiQ99933. Positions 140-331.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ99933.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati96 – 10161
    Repeati102 – 10762
    Repeati108 – 11363
    Repeati114 – 11964
    Repeati120 – 12565
    Repeati126 – 13166
    Repeati132 – 13767
    Domaini144 – 22481Ubiquitin-likePROSITE-ProRule annotationAdd
    BLAST
    Domaini246 – 32681BAGPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni96 – 137427 X 6 AA tandem repeat of E-E-X(4)Add
    BLAST
    Regioni172 – 21948Interaction with HSPA8Add
    BLAST
    Regioni216 – 345130Interaction with PPP1R15AAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi4 – 8279Arg-richAdd
    BLAST

    Sequence similaritiesi

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

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG72809.
    HOVERGENiHBG000236.
    InParanoidiQ99933.
    KOiK09555.
    PhylomeDBiQ99933.

    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 (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing and alternative initiation. Align

    Isoform 1 (identifier: Q99933-1) [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

    MAQRGGARRP RGDRERLGSR LRALRPGREP RQSEPPAQRG PPPSGRPPAR    50
    STASGHDRPT RGAAAGARRP RMKKKTRRRS TRSEELTRSE ELTLSEEATW 100
    SEEATQSEEA TQGEEMNRSQ EVTRDEESTR SEEVTREEMA AAGLTVTVTH 150
    SNEKHDLHVT SQQGSSEPVV QDLAQVVEEV IGVPQSFQKL IFKGKSLKEM 200
    ETPLSALGIQ DGCRVMLIGK KNSPQEEVEL KKLKHLEKSV EKIADQLEEL 250
    NKELTGIQQG FLPKDLQAEA LCKLDRRVKA TIEQFMKILE EIDTLILPEN 300
    FKDSRLKRKG LVKKVQAFLA ECDTVEQNIC QETERLQSTN FALAE 345
    Length:345
    Mass (Da):38,779
    Last modified:May 18, 2010 - v4
    Checksum:i8B40EF078C66335F
    GO
    Isoform 2 (identifier: Q99933-2) [UniParc]FASTAAdd to Basket

    Also known as: BAG1V, HAPV

    The sequence of this isoform differs from the canonical sequence as follows:
         302-345: KDSRLKRKGLVKKVQAFLAECDTVEQNICQETERLQSTNFALAE → PTLTLVLNEK

    Note: Produced by alternative splicing.

    Show »
    Length:311
    Mass (Da):34,866
    Checksum:i1F94BA55E21694D3
    GO
    Isoform 3 (identifier: Q99933-3) [UniParc]FASTAAdd to Basket

    Also known as: BAG-1M, RAP46

    The sequence of this isoform differs from the canonical sequence as follows:
         1-71: Missing.

    Note: Produced by alternative initiation at Met-72 of isoform 1.

    Show »
    Length:274
    Mass (Da):31,117
    Checksum:iC13E200ED63A2CF0
    GO
    Isoform 4 (identifier: Q99933-4) [UniParc]FASTAAdd to Basket

    Also known as: BAG-1, p32

    The sequence of this isoform differs from the canonical sequence as follows:
         1-115: Missing.

    Note: Produced by alternative initiation at Met-116 of isoform 1.

    Show »
    Length:230
    Mass (Da):25,989
    Checksum:iD4B34A8F54DE684D
    GO

    Sequence cautioni

    The sequence BAD96469.1 differs from that shown. Reason: Unusual initiator. The initiator methionine is coded by a non-canonical CTG leucine codon.
    The sequence AAD11467.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence AAD25045.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence CAA84624.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence CAH72516.1 differs from that shown. Reason: Erroneous gene model prediction.
    The sequence CAH72518.1 differs from that shown. Reason: Erroneous gene model prediction.
    The sequence CAH72741.1 differs from that shown. Reason: Erroneous gene model prediction.
    The sequence CAH72742.1 differs from that shown. Reason: Erroneous gene model prediction.
    The sequence EAW58515.1 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti45 – 451G → R in AAC34258. (PubMed:8812483)Curated
    Sequence conflicti45 – 451G → R in BAD96469. 1 PublicationCurated
    Sequence conflicti45 – 451G → R in AAH01936. (PubMed:15489334)Curated
    Sequence conflicti45 – 451G → R in AAH14774. (PubMed:15489334)Curated
    Sequence conflicti79 – 791R → F in AAD11467. (PubMed:8812483)Curated
    Sequence conflicti84 – 841E → K in AAD11467. (PubMed:8812483)Curated
    Sequence conflicti90 – 901E → K in AAD11467. (PubMed:8812483)Curated
    Sequence conflicti245 – 2451D → N in AAD11467. (PubMed:8812483)Curated
    Sequence conflicti293 – 2931D → H in AAD11467. (PubMed:8812483)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 115115Missing in isoform 4. CuratedVSP_038394Add
    BLAST
    Alternative sequencei1 – 7171Missing in isoform 3. CuratedVSP_038395Add
    BLAST
    Alternative sequencei302 – 34544KDSRL…FALAE → PTLTLVLNEK in isoform 2. 1 PublicationVSP_000453Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z35491 mRNA. Translation: CAA84624.1. Different initiation.
    U46917 mRNA. Translation: AAD11467.1. Different initiation.
    AF022224 mRNA. Translation: AAC34258.1.
    AF116273 mRNA. Translation: AAD25045.1. Different initiation.
    AK222749 mRNA. Translation: BAD96469.1. Different initiation.
    AL161445, AL356472 Genomic DNA. Translation: CAH72516.1. Sequence problems.
    AL161445, AL356472 Genomic DNA. Translation: CAH72517.1.
    AL161445, AL356472 Genomic DNA. Translation: CAH72518.1. Sequence problems.
    AL356472, AL161445 Genomic DNA. Translation: CAH72741.1. Sequence problems.
    AL356472, AL161445 Genomic DNA. Translation: CAH72742.1. Sequence problems.
    AL356472, AL161445 Genomic DNA. Translation: CAH72743.1.
    CH471071 Genomic DNA. Translation: EAW58514.1.
    CH471071 Genomic DNA. Translation: EAW58515.1. Sequence problems.
    BC001936 mRNA. Translation: AAH01936.2.
    BC014774 mRNA. Translation: AAH14774.2.
    CCDSiCCDS35004.1. [Q99933-1]
    CCDS55301.1. [Q99933-4]
    RefSeqiNP_001165886.1. NM_001172415.1. [Q99933-4]
    NP_004314.5. NM_004323.5.
    UniGeneiHs.377484.

    Genome annotation databases

    EnsembliENST00000379704; ENSP00000369026; ENSG00000107262. [Q99933-4]
    GeneIDi573.
    KEGGihsa:573.
    UCSCiuc003zsi.3. human. [Q99933-1]

    Polymorphism databases

    DMDMi296439462.

    Keywords - Coding sequence diversityi

    Alternative initiation, Alternative splicing

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z35491 mRNA. Translation: CAA84624.1 . Different initiation.
    U46917 mRNA. Translation: AAD11467.1 . Different initiation.
    AF022224 mRNA. Translation: AAC34258.1 .
    AF116273 mRNA. Translation: AAD25045.1 . Different initiation.
    AK222749 mRNA. Translation: BAD96469.1 . Different initiation.
    AL161445 , AL356472 Genomic DNA. Translation: CAH72516.1 . Sequence problems.
    AL161445 , AL356472 Genomic DNA. Translation: CAH72517.1 .
    AL161445 , AL356472 Genomic DNA. Translation: CAH72518.1 . Sequence problems.
    AL356472 , AL161445 Genomic DNA. Translation: CAH72741.1 . Sequence problems.
    AL356472 , AL161445 Genomic DNA. Translation: CAH72742.1 . Sequence problems.
    AL356472 , AL161445 Genomic DNA. Translation: CAH72743.1 .
    CH471071 Genomic DNA. Translation: EAW58514.1 .
    CH471071 Genomic DNA. Translation: EAW58515.1 . Sequence problems.
    BC001936 mRNA. Translation: AAH01936.2 .
    BC014774 mRNA. Translation: AAH14774.2 .
    CCDSi CCDS35004.1. [Q99933-1 ]
    CCDS55301.1. [Q99933-4 ]
    RefSeqi NP_001165886.1. NM_001172415.1. [Q99933-4 ]
    NP_004314.5. NM_004323.5.
    UniGenei Hs.377484.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1HX1 X-ray 1.90 B 222-334 [» ]
    1WXV NMR - A 144-222 [» ]
    3FZF X-ray 2.20 B 222-334 [» ]
    3FZH X-ray 2.00 B 222-334 [» ]
    3FZK X-ray 2.10 B 222-334 [» ]
    3FZL X-ray 2.20 B 222-334 [» ]
    3FZM X-ray 2.30 B 222-334 [» ]
    3LDQ X-ray 1.90 B 222-334 [» ]
    3M3Z X-ray 2.10 B 222-334 [» ]
    ProteinModelPortali Q99933.
    SMRi Q99933. Positions 140-331.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107049. 49 interactions.
    DIPi DIP-3341N.
    IntActi Q99933. 31 interactions.
    MINTi MINT-189058.

    PTM databases

    PhosphoSitei Q99933.

    Polymorphism databases

    DMDMi 296439462.

    Proteomic databases

    MaxQBi Q99933.
    PaxDbi Q99933.
    PRIDEi Q99933.

    Protocols and materials databases

    DNASUi 573.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000379704 ; ENSP00000369026 ; ENSG00000107262 . [Q99933-4 ]
    GeneIDi 573.
    KEGGi hsa:573.
    UCSCi uc003zsi.3. human. [Q99933-1 ]

    Organism-specific databases

    CTDi 573.
    GeneCardsi GC09M033245.
    HGNCi HGNC:937. BAG1.
    HPAi CAB002486.
    HPA018121.
    MIMi 601497. gene.
    neXtProti NX_Q99933.
    PharmGKBi PA25237.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG72809.
    HOVERGENi HBG000236.
    InParanoidi Q99933.
    KOi K09555.
    PhylomeDBi Q99933.

    Miscellaneous databases

    ChiTaRSi BAG1. human.
    EvolutionaryTracei Q99933.
    GeneWikii BAG1.
    GenomeRNAii 573.
    NextBioi 2337.
    PROi Q99933.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q99933.
    Bgeei Q99933.
    CleanExi HS_BAG1.
    Genevestigatori Q99933.

    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. "A protein that interacts with members of the nuclear hormone receptor family: identification and cDNA cloning."
      Zeiner M., Gehring U.
      Proc. Natl. Acad. Sci. U.S.A. 92:11465-11469(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Liver.
    2. "Cloning of cDNAs encoding the human BAG1 protein and localization of the human BAG1 gene to chromosome 9p12."
      Takayama S., Kochel K., Irie S., Inazawa J., Abe T., Sato T., Druck T., Huebner K., Reed J.C.
      Genomics 35:494-498(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Mammary gland.
    3. Takayama S.
      Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION TO N-TERMINUS; 79; 84; 90; 245 AND 293.
    4. "Characterization of Hap/BAG-1 variants as RP1 binding proteins with antiapoptotic activity."
      Wadle A., Mischo A., Henrich P.P., Stenner-Lieven F., Scherer C., Imig J., Petersen G., Pfreundschuh M., Renner C.
      Int. J. Cancer 117:896-904(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), ANTI-APOPTOTIC ACTIVITY, SUBCELLULAR LOCATION, INTERACTION WITH STK19.
      Tissue: T-cell.
    5. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
      Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Dermoid cancer.
    6. "DNA sequence and analysis of human chromosome 9."
      Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
      , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
      Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "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).
      Tissue: Cervix and Lung.
    9. "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 4, ALTERNATIVE INITIATION.
    10. Cited for: FUNCTION, SUBUNIT, INTERACTION WITH BCL2; HSP70 AND HSPA8.
    11. "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; 3 AND 4, ALTERNATIVE INITIATION, SUBCELLULAR LOCATION, INTERACTION WITH HSPA8, INDUCTION, TISSUE SPECIFICITY.
    12. "p53-inducible human homologue of Drosophila seven in absentia (Siah) inhibits cell growth: suppression by BAG-1."
      Matsuzawa S., Takayama S., Froesch B.A., Zapata J.M., Reed J.C.
      EMBO J. 17:2736-2747(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SIAH1.
    13. "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.
    14. "A nuclear action of the eukaryotic cochaperone RAP46 in downregulation of glucocorticoid receptor activity."
      Schneikert J., Huebner S., Martin E., Cato A.B.C.
      J. Cell Biol. 146:929-940(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NR3C1.
    15. "Human BAG-1 proteins bind to the cellular stress response protein GADD34 and interfere with GADD34 functions."
      Hung W.J., Roberson R.S., Taft J., Wu D.Y.
      Mol. Cell. Biol. 23:3477-3486(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PPP1R15A, FUNCTION.
    16. "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-223, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. "Structure of a Bag/Hsc70 complex: convergent functional evolution of Hsp70 nucleotide exchange factors."
      Sondermann H., Scheufler C., Schneider C., Hohfeld J., Hartl F.U., Moarefi I.
      Science 291:1553-1557(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 222-334 IN COMPLEX WITH HSC70.
    19. "Solution structure of the ubiquitin domain of Bcl-2 binding athanogene-1."
      RIKEN structural genomics initiative (RSGI)
      Submitted (AUG-2005) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 143-223.

    Entry informationi

    Entry nameiBAG1_HUMAN
    AccessioniPrimary (citable) accession number: Q99933
    Secondary accession number(s): O75315
    , Q14414, Q53H32, Q5VZE8, Q5VZE9, Q5VZF0, Q96TG2, Q9Y2V4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: May 18, 2010
    Last modified: October 1, 2014
    This is version 151 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 9
      Human chromosome 9: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3