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P07901

- HS90A_MOUSE

UniProt

P07901 - HS90A_MOUSE

Protein

Heat shock protein HSP 90-alpha

Gene

Hsp90aa1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 161 (01 Oct 2014)
      Sequence version 4 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function By similarity. Binds bacterial lipopolysaccharide (LPS) et mediates LPS-induced inflammatory response, including TNF secretion By similarity.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei51 – 511ATPBy similarity
    Binding sitei93 – 931ATPBy similarity
    Binding sitei112 – 1121ATPBy similarity
    Binding sitei138 – 1381ATP; via amide nitrogenBy similarity
    Binding sitei401 – 4011ATPBy similarity

    GO - Molecular functioni

    1. ATPase activity Source: Ensembl
    2. ATP binding Source: UniProtKB-KW
    3. nitric-oxide synthase regulator activity Source: UniProtKB
    4. protein binding Source: UniProtKB
    5. protein homodimerization activity Source: MGI
    6. TPR domain binding Source: UniProtKB
    7. unfolded protein binding Source: UniProtKB

    GO - Biological processi

    1. chaperone-mediated protein complex assembly Source: Ensembl
    2. nitric oxide biosynthetic process Source: UniProtKB
    3. positive regulation of cytotoxic T cell differentiation Source: UniProtKB
    4. positive regulation of nitric oxide biosynthetic process Source: UniProtKB
    5. protein import into mitochondrial outer membrane Source: Ensembl
    6. protein refolding Source: UniProtKB
    7. regulation of catalytic activity Source: GOC
    8. response to unfolded protein Source: UniProtKB

    Keywords - Molecular functioni

    Chaperone

    Keywords - Biological processi

    Stress response

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_188191. Signaling by ERBB2.
    REACT_196603. Scavenging by Class F Receptors.
    REACT_196635. Regulation of PLK1 Activity at G2/M Transition.
    REACT_198374. Regulation of actin dynamics for phagocytic cup formation.
    REACT_199047. Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation.
    REACT_199123. Signaling by constitutively active EGFR.
    REACT_213550. HSF1-dependent transactivation.
    REACT_221264. eNOS activation.
    REACT_223784. Attenuation phase.
    REACT_225256. HSF1 activation.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Heat shock protein HSP 90-alpha
    Alternative name(s):
    Heat shock 86 kDa
    Short name:
    HSP 86
    Short name:
    HSP86
    Tumor-specific transplantation 86 kDa antigen
    Short name:
    TSTA
    Gene namesi
    Name:Hsp90aa1
    Synonyms:Hsp86, Hsp86-1, Hspca
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 12

    Organism-specific databases

    MGIiMGI:96250. Hsp90aa1.

    Subcellular locationi

    Cytoplasm 1 Publication. Melanosome By similarity. Cell membrane By similarity

    GO - Cellular componenti

    1. cytoplasm Source: MGI
    2. cytosol Source: UniProtKB
    3. intracellular Source: MGI
    4. melanosome Source: UniProtKB-SubCell
    5. mitochondrion Source: GOC
    6. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 733732Heat shock protein HSP 90-alphaPRO_0000062912Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei5 – 51Phosphothreonine; by PRKDC1 Publication
    Modified residuei7 – 71Phosphothreonine; by PRKDC1 Publication
    Modified residuei58 – 581N6-acetyllysine1 Publication
    Modified residuei84 – 841N6-acetyllysine1 Publication
    Modified residuei231 – 2311PhosphoserineBy similarity
    Modified residuei252 – 2521PhosphoserineBy similarity
    Modified residuei263 – 2631Phosphoserine3 Publications
    Modified residuei314 – 3141Phosphotyrosine1 Publication
    Modified residuei400 – 4001PhosphoserineBy similarity
    Modified residuei444 – 4441N6-acetyllysineBy similarity
    Modified residuei459 – 4591N6-acetyllysineBy similarity
    Modified residuei490 – 4901N6-acetyllysineBy similarity
    Modified residuei493 – 4931Phosphotyrosine1 Publication
    Modified residuei586 – 5861N6-acetyllysineBy similarity
    Modified residuei599 – 5991S-nitrosocysteineBy similarity

    Post-translational modificationi

    ISGylated.1 Publication
    S-nitrosylated; negatively regulates the ATPase activity and the activation of eNOS by HSP90AA1.By similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein, S-nitrosylation, Ubl conjugation

    Proteomic databases

    MaxQBiP07901.
    PaxDbiP07901.
    PRIDEiP07901.

    2D gel databases

    REPRODUCTION-2DPAGEP07901.

    PTM databases

    PhosphoSiteiP07901.

    Expressioni

    Gene expression databases

    BgeeiP07901.
    GenevestigatoriP07901.

    Interactioni

    Subunit structurei

    Homodimer. Identified in NR3C1/GCR steroid receptor-chaperone complexes formed at least by NR3C1, HSP90AA1 and a variety of proteins containing TPR repeats such as FKBP4, FKBP5, PPID, PPP5C or STIP1. Interacts with AHSA1, FNIP1, HSF1, SMYD3 and TOM34. Interacts with TERT; the interaction, together with PTGES3, is required for correct assembly and stabilization of the TERT holoenzyme complex. Interacts with CHORDC1 and DNAJC7. Interacts with STUB1 and UBE2N; may couple the chaperone and ubiquitination systems. Interacts (via TPR repeat-binding motif) with PPP5C (via TPR repeats); the interaction is direct and activates PPP5C phosphatase activity. Following LPS binding, may form a complex with CXCR4, GDF5 and HSPA8 By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Akt1P317506EBI-78930,EBI-298707
    Itgb1bp2Q9R0005EBI-78930,EBI-7922331

    Protein-protein interaction databases

    BioGridi200455. 18 interactions.
    DIPiDIP-30975N.
    IntActiP07901. 25 interactions.
    MINTiMINT-152660.

    Structurei

    3D structure databases

    ProteinModelPortaliP07901.
    SMRiP07901. Positions 11-700.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni683 – 73351Required for homodimerizationBy similarityAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi729 – 7335TPR repeat-binding

    Domaini

    The TPR repeat-binding motif mediates interaction with TPR repeat-containing proteins like the co-chaperone STUB1.By similarity

    Sequence similaritiesi

    Belongs to the heat shock protein 90 family.Curated

    Phylogenomic databases

    eggNOGiCOG0326.
    HOGENOMiHOG000031988.
    HOVERGENiHBG007374.
    InParanoidiP07901.
    KOiK04079.
    OMAiKEDQTEF.
    OrthoDBiEOG780RM0.
    PhylomeDBiP07901.
    TreeFamiTF300686.

    Family and domain databases

    Gene3Di3.30.565.10. 2 hits.
    HAMAPiMF_00505. HSP90.
    InterProiIPR003594. HATPase_ATP-bd.
    IPR019805. Heat_shock_protein_90_CS.
    IPR001404. Hsp90_fam.
    IPR020575. Hsp90_N.
    IPR020568. Ribosomal_S5_D2-typ_fold.
    [Graphical view]
    PANTHERiPTHR11528. PTHR11528. 1 hit.
    PfamiPF02518. HATPase_c. 1 hit.
    PF00183. HSP90. 1 hit.
    [Graphical view]
    PIRSFiPIRSF002583. Hsp90. 1 hit.
    PRINTSiPR00775. HEATSHOCK90.
    SMARTiSM00387. HATPase_c. 1 hit.
    [Graphical view]
    SUPFAMiSSF54211. SSF54211. 1 hit.
    SSF55874. SSF55874. 1 hit.
    PROSITEiPS00298. HSP90. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P07901-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPEETQTQDQ PMEEEEVETF AFQAEIAQLM SLIINTFYSN KEIFLRELIS    50
    NSSDALDKIR YESLTDPSKL DSGKELHINL IPSKQDRTLT IVDTGIGMTK 100
    ADLINNLGTI AKSGTKAFME ALQAGADISM IGQFGVGFYS AYLVAEKVTV 150
    ITKHNDDEQY AWESSAGGSF TVRTDTGEPM GRGTKVILHL KEDQTEYLEE 200
    RRIKEIVKKH SQFIGYPITL FVEKERDKEV SDDEAEEKEE KEEEKEKEEK 250
    ESDDKPEIED VGSDEEEEEK KDGDKKKKKK IKEKYIDQEE LNKTKPIWTR 300
    NPDDITNEEY GEFYKSLTND WEEHLAVKHF SVEGQLEFRA LLFVPRRAPF 350
    DLFENRKKKN NIKLYVRRVF IMDNCEELIP EYLNFIRGVV DSEDLPLNIS 400
    REMLQQSKIL KVIRKNLVKK CLELFTELAE DKENYKKFYE QFSKNIKLGI 450
    HEDSQNRKKL SELLRYYTSA SGDEMVSLKD YCTRMKENQK HIYFITGETK 500
    DQVANSAFVE RLRKHGLEVI YMIEPIDEYC VQQLKEFEGK TLVSVTKEGL 550
    ELPEDEEEKK KQEEKKTKFE NLCKIMKDIL EKKVEKVVVS NRLVTSPCCI 600
    VTSTYGWTAN MERIMKAQAL RDNSTMGYMA AKKHLEINPD HSIIETLRQK 650
    AEADKNDKSV KDLVILLYET ALLSSGFSLE DPQTHANRIY RMIKLGLGID 700
    EDDPTVDDTS AAVTEEMPPL EGDDDTSRME EVD 733
    Length:733
    Mass (Da):84,788
    Last modified:January 23, 2007 - v4
    Checksum:iD92B8FD38A463B4E
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti7 – 71T → A in AAA37868. (PubMed:2469626)Curated
    Sequence conflicti242 – 2454Missing in AAA37868. (PubMed:2469626)Curated
    Sequence conflicti356 – 3561R → K in AAA37868. (PubMed:2469626)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J04633 mRNA. Translation: AAA53068.1.
    M57673 Genomic DNA. Translation: AAA37867.1.
    BC046614 mRNA. Translation: AAH46614.1.
    M36830 mRNA. Translation: AAA37868.1.
    X16857 mRNA. Translation: CAA34748.1.
    CCDSiCCDS26172.1.
    PIRiB32848. HHMS86.
    RefSeqiNP_034610.1. NM_010480.5.
    UniGeneiMm.1843.
    Mm.315997.
    Mm.341186.
    Mm.440626.
    Mm.486334.

    Genome annotation databases

    EnsembliENSMUST00000021698; ENSMUSP00000021698; ENSMUSG00000021270.
    ENSMUST00000094361; ENSMUSP00000091921; ENSMUSG00000021270.
    GeneIDi15519.
    KEGGimmu:15519.
    UCSCiuc007pbq.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J04633 mRNA. Translation: AAA53068.1 .
    M57673 Genomic DNA. Translation: AAA37867.1 .
    BC046614 mRNA. Translation: AAH46614.1 .
    M36830 mRNA. Translation: AAA37868.1 .
    X16857 mRNA. Translation: CAA34748.1 .
    CCDSi CCDS26172.1.
    PIRi B32848. HHMS86.
    RefSeqi NP_034610.1. NM_010480.5.
    UniGenei Mm.1843.
    Mm.315997.
    Mm.341186.
    Mm.440626.
    Mm.486334.

    3D structure databases

    ProteinModelPortali P07901.
    SMRi P07901. Positions 11-700.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 200455. 18 interactions.
    DIPi DIP-30975N.
    IntActi P07901. 25 interactions.
    MINTi MINT-152660.

    Chemistry

    BindingDBi P07901.
    ChEMBLi CHEMBL4197.

    PTM databases

    PhosphoSitei P07901.

    2D gel databases

    REPRODUCTION-2DPAGE P07901.

    Proteomic databases

    MaxQBi P07901.
    PaxDbi P07901.
    PRIDEi P07901.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000021698 ; ENSMUSP00000021698 ; ENSMUSG00000021270 .
    ENSMUST00000094361 ; ENSMUSP00000091921 ; ENSMUSG00000021270 .
    GeneIDi 15519.
    KEGGi mmu:15519.
    UCSCi uc007pbq.1. mouse.

    Organism-specific databases

    CTDi 3320.
    MGIi MGI:96250. Hsp90aa1.

    Phylogenomic databases

    eggNOGi COG0326.
    HOGENOMi HOG000031988.
    HOVERGENi HBG007374.
    InParanoidi P07901.
    KOi K04079.
    OMAi KEDQTEF.
    OrthoDBi EOG780RM0.
    PhylomeDBi P07901.
    TreeFami TF300686.

    Enzyme and pathway databases

    Reactomei REACT_188191. Signaling by ERBB2.
    REACT_196603. Scavenging by Class F Receptors.
    REACT_196635. Regulation of PLK1 Activity at G2/M Transition.
    REACT_198374. Regulation of actin dynamics for phagocytic cup formation.
    REACT_199047. Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation.
    REACT_199123. Signaling by constitutively active EGFR.
    REACT_213550. HSF1-dependent transactivation.
    REACT_221264. eNOS activation.
    REACT_223784. Attenuation phase.
    REACT_225256. HSF1 activation.

    Miscellaneous databases

    NextBioi 288436.
    PROi P07901.
    SOURCEi Search...

    Gene expression databases

    Bgeei P07901.
    Genevestigatori P07901.

    Family and domain databases

    Gene3Di 3.30.565.10. 2 hits.
    HAMAPi MF_00505. HSP90.
    InterProi IPR003594. HATPase_ATP-bd.
    IPR019805. Heat_shock_protein_90_CS.
    IPR001404. Hsp90_fam.
    IPR020575. Hsp90_N.
    IPR020568. Ribosomal_S5_D2-typ_fold.
    [Graphical view ]
    PANTHERi PTHR11528. PTHR11528. 1 hit.
    Pfami PF02518. HATPase_c. 1 hit.
    PF00183. HSP90. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF002583. Hsp90. 1 hit.
    PRINTSi PR00775. HEATSHOCK90.
    SMARTi SM00387. HATPase_c. 1 hit.
    [Graphical view ]
    SUPFAMi SSF54211. SSF54211. 1 hit.
    SSF55874. SSF55874. 1 hit.
    PROSITEi PS00298. HSP90. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Murine 86- and 84-kDa heat shock proteins, cDNA sequences, chromosome assignments, and evolutionary origins."
      Moore S.K., Kozak C., Robinson E.A., Ullrich S.J., Appella E.
      J. Biol. Chem. 264:5343-5351(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: BALB/c.
    2. "Mapping of the mouse 86-kDa heat-shock protein expressed gene (Hsp86-1) on chromosome 12 and related genes on chromosomes 3, 4, 9, and 11."
      Moore S.K., Appella E., Villar C.J., Kozak C.A.
      Genomics 10:1019-1029(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: BALB/c.
    3. "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].
      Tissue: Retina.
    4. "A mouse tumor-specific transplantation antigen is a heat shock-related protein."
      Ullrich S.J., Robinson E.A., Law L.W., Willingham M., Appella E.
      Proc. Natl. Acad. Sci. U.S.A. 83:3121-3125(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-31.
    5. "The carboxy-terminal region of mammalian HSP90 is required for its dimerization and function in vivo."
      Minami Y., Kimura Y., Kawasaki H., Suzuki K., Yahara I.
      Mol. Cell. Biol. 14:1459-1464(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-12, HOMODIMERIZATION.
    6. "Heat-shock proteins, Hsp84 and Hsp86, of mice and men: two related genes encode formerly identified tumour-specific transplantation antigens."
      Hoffmann T., Hovemann B.
      Gene 74:491-501(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 6-356.
    7. Lubec G., Kang S.U., Klug S., Sunyer B., Chen W.-Q.
      Submitted (JAN-2009) to UniProtKB
      Strain: C57BL/6 and OF1.
      Tissue: Brain and Hippocampus.
    8. "High constitutive transcription of HSP86 gene in murine embryonal carcinoma cells."
      Legagneux V., Mezger V., Quelard C., Barnier J.V., Bensaude O., Morange M.
      Differentiation 41:42-48(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 460-733.
    9. "Protein phosphatase 5 is a major component of glucocorticoid receptor.hsp90 complexes with properties of an FK506-binding immunophilin."
      Silverstein A.M., Galigniana M.D., Chen M.S., Owens-Grillo J.K., Chinkers M., Pratt W.B.
      J. Biol. Chem. 272:16224-16230(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A COMPLEX WITH NR3C1 AND FKBP4; PPID; PPP5C OR STIP1.
    10. "Evidence that the peptidylprolyl isomerase domain of the hsp90-binding immunophilin FKBP52 is involved in both dynein interaction and glucocorticoid receptor movement to the nucleus."
      Galigniana M.D., Radanyi C., Renoir J.-M., Housley P.R., Pratt W.B.
      J. Biol. Chem. 276:14884-14889(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A COMPLEX WITH NR3C1 AND FKBP4.
    11. "A new first step in activation of steroid receptors: hormone-induced switching of FKBP51 and FKBP52 immunophilins."
      Davies T.H., Ning Y.M., Sanchez E.R.
      J. Biol. Chem. 277:4597-4600(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A HETEROMULTIMERIC COMPLEX WITH NR3C1 AND FKBP4 OR FKBP5, SUBCELLULAR LOCATION.
    12. "The human double-stranded DNA-activated protein kinase phosphorylates the 90-kDa heat-shock protein, hsp90 alpha at two NH2-terminal threonine residues."
      Lees-Miller S.P., Anderson C.W.
      J. Biol. Chem. 264:17275-17280(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT THR-5 AND THR-7 BY PRKDC.
    13. Cited for: ISGYLATION.
    14. "Quantitative time-resolved phosphoproteomic analysis of mast cell signaling."
      Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y., Kawakami T., Salomon A.R.
      J. Immunol. 179:5864-5876(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-493, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Mast cell.
    15. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    16. "Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain."
      Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.
      J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-314, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Brain.
    17. "Specific phosphopeptide enrichment with immobilized titanium ion affinity chromatography adsorbent for phosphoproteome analysis."
      Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.
      J. Proteome Res. 7:3957-3967(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    18. "The phagosomal proteome in interferon-gamma-activated macrophages."
      Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
      Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
      Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
      Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-58 AND LYS-84, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.

    Entry informationi

    Entry nameiHS90A_MOUSE
    AccessioniPrimary (citable) accession number: P07901
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1988
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 161 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

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

    External Data

    Dasty 3