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Q9UL15

- BAG5_HUMAN

UniProt

Q9UL15 - BAG5_HUMAN

Protein

BAG family molecular chaperone regulator 5

Gene

BAG5

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 120 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    Functioni

    Inhibits both auto-ubiquitination of PARK2 and ubiquitination of target proteins by PARK2 By similarity. May function as a nucleotide exchange factor for HSP/HSP70, promoting ADP release, and activating Hsp70-mediated refolding.By similarity1 Publication

    GO - Molecular functioni

    1. chaperone binding Source: BHF-UCL
    2. ubiquitin protein ligase 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. protein folding Source: ProtInc
    6. regulation of inclusion body assembly Source: BHF-UCL

    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
    Synonyms:KIAA0873
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 14

    Organism-specific databases

    HGNCiHGNC:941. BAG5.

    Subcellular locationi

    GO - Cellular componenti

    1. inclusion body Source: BHF-UCL
    2. membrane Source: UniProtKB
    3. nucleus Source: UniProt
    4. perinuclear region of cytoplasm Source: BHF-UCL

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA25241.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 447447BAG family molecular chaperone regulator 5PRO_0000088872Add
    BLAST

    Proteomic databases

    MaxQBiQ9UL15.
    PaxDbiQ9UL15.
    PRIDEiQ9UL15.

    PTM databases

    PhosphoSiteiQ9UL15.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9UL15.
    BgeeiQ9UL15.
    CleanExiHS_BAG5.
    GenevestigatoriQ9UL15.

    Organism-specific databases

    HPAiHPA016429.

    Interactioni

    Subunit structurei

    Binds to the ATPase domain of HSP/HSC70 chaperones. Binds PARK2.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Q53FC72EBI-356517,EBI-9356749
    HSPA1BP081076EBI-356517,EBI-629985
    LRRK1Q38SD23EBI-356517,EBI-1050422
    LRRK2Q5S00712EBI-356517,EBI-5323863

    Protein-protein interaction databases

    BioGridi114905. 15 interactions.
    DIPiDIP-53428N.
    IntActiQ9UL15. 20 interactions.
    MINTiMINT-1147557.
    STRINGi9606.ENSP00000338814.

    Structurei

    Secondary structure

    1
    447
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi277 – 29519
    Turni299 – 3013
    Helixi302 – 31716
    Helixi318 – 3203
    Helixi326 – 35025
    Turni356 – 3583
    Helixi364 – 38421
    Helixi393 – 41018
    Helixi418 – 44225

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2D9DNMR-A275-350[»]
    3A8YX-ray2.30C/D341-447[»]
    ProteinModelPortaliQ9UL15.
    SMRiQ9UL15. Positions 1-89, 276-447.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9UL15.

    Family & Domainsi

    Domains and Repeats

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

    Domaini

    The fifth BAG domain is responsible for the interaction with HSP70 nucleotide-binding domain.1 Publication

    Sequence similaritiesi

    Contains 5 BAG domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG262724.
    HOGENOMiHOG000070447.
    HOVERGENiHBG004810.
    InParanoidiQ9UL15.
    KOiK09559.
    OMAiDMGNQHP.
    OrthoDBiEOG7WX08F.
    PhylomeDBiQ9UL15.
    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]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9UL15-1) [UniParc]FASTAAdd to Basket

    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

    MDMGNQHPSI SRLQEIQKEV KSVEQQVIGF SGLSDDKNYK KLERILTKQL    50
    FEIDSVDTEG KGDIQQARKR AAQETERLLK ELEQNANHPH RIEIQNIFEE 100
    AQSLVREKIV PFYNGGNCVT DEFEEGIQDI ILRLTHVKTG GKISLRKARY 150
    HTLTKICAVQ EIIEDCMKKQ PSLPLSEDAH PSVAKINFVM CEVNKARGVL 200
    IALLMGVNNN ETCRHLSCVL SGLIADLDAL DVCGRTEIRN YRREVVEDIN 250
    KLLKYLDLEE EADTTKAFDL RQNHSILKIE KVLKRMREIK NELLQAQNPS 300
    ELYLSSKTEL QGLIGQLDEV SLEKNPCIRE ARRRAVIEVQ TLITYIDLKE 350
    ALEKRKLFAC EEHPSHKAVW NVLGNLSEIQ GEVLSFDGNR TDKNYIRLEE 400
    LLTKQLLALD AVDPQGEEKC KAARKQAVRL AQNILSYLDL KSDEWEY 447
    Length:447
    Mass (Da):51,200
    Last modified:May 1, 2000 - v1
    Checksum:i0D3F7EA6B612C1F5
    GO
    Isoform 2 (identifier: Q9UL15-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1: M → MRFHWLPTLSEPFDRNQELETCIRPLWTPSGSACETEHNKSM

    Note: No experimental confirmation available.

    Show »
    Length:488
    Mass (Da):56,027
    Checksum:i7A901A14F9B07AC2
    GO

    Sequence cautioni

    The sequence BAA74896.1 differs from that shown. Reason: Erroneous initiation.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti157 – 1571C → W.1 Publication
    Corresponds to variant rs17854644 [ dbSNP | Ensembl ].
    VAR_058712

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 11M → MRFHWLPTLSEPFDRNQELE TCIRPLWTPSGSACETEHNK SM in isoform 2. 1 PublicationVSP_037996

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF095195 mRNA. Translation: AAD16124.2.
    AB020680 mRNA. Translation: BAA74896.1. Different initiation.
    AL139300 Genomic DNA. No translation available.
    BC044216 mRNA. Translation: AAH44216.2.
    BC050551 mRNA. Translation: AAH50551.1.
    CCDSiCCDS41995.1. [Q9UL15-2]
    CCDS9982.1. [Q9UL15-1]
    RefSeqiNP_001015048.1. NM_001015048.2. [Q9UL15-1]
    NP_001015049.1. NM_001015049.2. [Q9UL15-2]
    NP_004864.1. NM_004873.3. [Q9UL15-1]
    UniGeneiHs.5443.

    Genome annotation databases

    EnsembliENST00000299204; ENSP00000299204; ENSG00000166170. [Q9UL15-1]
    ENST00000337322; ENSP00000338814; ENSG00000166170. [Q9UL15-2]
    ENST00000445922; ENSP00000391713; ENSG00000166170. [Q9UL15-1]
    GeneIDi9529.
    KEGGihsa:9529.
    UCSCiuc001ynh.2. human. [Q9UL15-2]
    uc001yni.2. human. [Q9UL15-1]

    Polymorphism databases

    DMDMi12643895.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF095195 mRNA. Translation: AAD16124.2 .
    AB020680 mRNA. Translation: BAA74896.1 . Different initiation.
    AL139300 Genomic DNA. No translation available.
    BC044216 mRNA. Translation: AAH44216.2 .
    BC050551 mRNA. Translation: AAH50551.1 .
    CCDSi CCDS41995.1. [Q9UL15-2 ]
    CCDS9982.1. [Q9UL15-1 ]
    RefSeqi NP_001015048.1. NM_001015048.2. [Q9UL15-1 ]
    NP_001015049.1. NM_001015049.2. [Q9UL15-2 ]
    NP_004864.1. NM_004873.3. [Q9UL15-1 ]
    UniGenei Hs.5443.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2D9D NMR - A 275-350 [» ]
    3A8Y X-ray 2.30 C/D 341-447 [» ]
    ProteinModelPortali Q9UL15.
    SMRi Q9UL15. Positions 1-89, 276-447.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114905. 15 interactions.
    DIPi DIP-53428N.
    IntActi Q9UL15. 20 interactions.
    MINTi MINT-1147557.
    STRINGi 9606.ENSP00000338814.

    PTM databases

    PhosphoSitei Q9UL15.

    Polymorphism databases

    DMDMi 12643895.

    Proteomic databases

    MaxQBi Q9UL15.
    PaxDbi Q9UL15.
    PRIDEi Q9UL15.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000299204 ; ENSP00000299204 ; ENSG00000166170 . [Q9UL15-1 ]
    ENST00000337322 ; ENSP00000338814 ; ENSG00000166170 . [Q9UL15-2 ]
    ENST00000445922 ; ENSP00000391713 ; ENSG00000166170 . [Q9UL15-1 ]
    GeneIDi 9529.
    KEGGi hsa:9529.
    UCSCi uc001ynh.2. human. [Q9UL15-2 ]
    uc001yni.2. human. [Q9UL15-1 ]

    Organism-specific databases

    CTDi 9529.
    GeneCardsi GC14M104022.
    HGNCi HGNC:941. BAG5.
    HPAi HPA016429.
    MIMi 603885. gene.
    neXtProti NX_Q9UL15.
    PharmGKBi PA25241.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG262724.
    HOGENOMi HOG000070447.
    HOVERGENi HBG004810.
    InParanoidi Q9UL15.
    KOi K09559.
    OMAi DMGNQHP.
    OrthoDBi EOG7WX08F.
    PhylomeDBi Q9UL15.
    TreeFami TF102014.

    Miscellaneous databases

    EvolutionaryTracei Q9UL15.
    GeneWikii BAG5.
    GenomeRNAii 9529.
    NextBioi 35720.
    PROi Q9UL15.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9UL15.
    Bgeei Q9UL15.
    CleanExi HS_BAG5.
    Genevestigatori Q9UL15.

    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

    1. "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: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "Prediction of the coding sequences of unidentified human genes. XII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
      Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
      DNA Res. 5:355-364(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Brain.
    3. "The DNA sequence and analysis of human chromosome 14."
      Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H.
      , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
      Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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] (ISOFORMS 1 AND 2), VARIANT TRP-157.
      Tissue: Brain.
    5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    6. "High-content genome-wide RNAi screens identify regulators of parkin upstream of mitophagy."
      Hasson S.A., Kane L.A., Yamano K., Huang C.H., Sliter D.A., Buehler E., Wang C., Heman-Ackah S.M., Hessa T., Guha R., Martin S.E., Youle R.J.
      Nature 504:291-295(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PARK2.
    7. "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 275-350, X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 341-447 IN COMPLEX WITH HSPA1, DOMAIN BAG, FUNCTION, SUBUNIT.

    Entry informationi

    Entry nameiBAG5_HUMAN
    AccessioniPrimary (citable) accession number: Q9UL15
    Secondary accession number(s): O94950, Q86W59
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 11, 2001
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 120 of the entry and version 1 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 14
      Human chromosome 14: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3