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P11499

- HS90B_MOUSE

UniProt

P11499 - HS90B_MOUSE

Protein

Heat shock protein HSP 90-beta

Gene

Hsp90ab1

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 3 (27 Jul 2011)
      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.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei46 – 461ATPBy similarity
    Binding sitei88 – 881ATPBy similarity
    Binding sitei107 – 1071ATPBy similarity
    Binding sitei133 – 1331ATP; via amide nitrogenBy similarity
    Binding sitei392 – 3921ATPBy similarity

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. CTP binding Source: Ensembl
    3. dATP binding Source: Ensembl
    4. double-stranded RNA binding Source: MGI
    5. GTP binding Source: Ensembl
    6. nitric-oxide synthase regulator activity Source: UniProtKB
    7. protein binding Source: IntAct
    8. TPR domain binding Source: UniProtKB
    9. UTP binding Source: Ensembl

    GO - Biological processi

    1. cellular response to interleukin-4 Source: MGI
    2. cellular response to organic cyclic compound Source: Ensembl
    3. negative regulation of neuron apoptotic process Source: Ensembl
    4. negative regulation of proteasomal ubiquitin-dependent protein catabolic process Source: Ensembl
    5. placenta development Source: MGI
    6. positive regulation of cell size Source: Ensembl
    7. positive regulation of nitric oxide biosynthetic process Source: UniProtKB
    8. positive regulation of protein binding Source: Ensembl
    9. positive regulation of protein import into nucleus, translocation Source: Ensembl
    10. positive regulation of protein serine/threonine kinase activity Source: Ensembl
    11. protein folding Source: InterPro
    12. regulation of interferon-gamma-mediated signaling pathway Source: Ensembl
    13. regulation of type I interferon-mediated signaling pathway Source: Ensembl
    14. response to salt stress Source: Ensembl

    Keywords - Molecular functioni

    Chaperone

    Keywords - Biological processi

    Stress response

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_198374. Regulation of actin dynamics for phagocytic cup formation.
    REACT_198644. The NLRP3 inflammasome.
    REACT_213550. HSF1-dependent transactivation.
    REACT_223784. Attenuation phase.
    REACT_225256. HSF1 activation.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Heat shock protein HSP 90-beta
    Alternative name(s):
    Heat shock 84 kDa
    Short name:
    HSP 84
    Short name:
    HSP84
    Tumor-specific transplantation 84 kDa antigen
    Short name:
    TSTA
    Gene namesi
    Name:Hsp90ab1
    Synonyms:Hsp84, Hsp84-1, Hspcb
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 17

    Organism-specific databases

    MGIiMGI:96247. Hsp90ab1.

    Subcellular locationi

    Cytoplasm. Melanosome By similarity

    GO - Cellular componenti

    1. apical plasma membrane Source: Ensembl
    2. basolateral plasma membrane Source: Ensembl
    3. brush border membrane Source: Ensembl
    4. cell surface Source: Ensembl
    5. COP9 signalosome Source: Ensembl
    6. cytoplasm Source: MGI
    7. cytosol Source: Ensembl
    8. inclusion body Source: Ensembl
    9. intracellular Source: MGI
    10. melanosome Source: UniProtKB-SubCell
    11. mitochondrion Source: MGI

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed3 Publications
    Chaini2 – 724723Heat shock protein HSP 90-betaPRO_0000062918Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei219 – 2191N6-succinyllysine1 Publication
    Modified residuei226 – 2261Phosphoserine1 Publication
    Modified residuei255 – 2551Phosphoserine6 Publications
    Modified residuei261 – 2611Phosphoserine2 Publications
    Modified residuei297 – 2971PhosphothreonineBy similarity
    Modified residuei305 – 3051Phosphotyrosine1 Publication
    Modified residuei307 – 3071PhosphoserineBy similarity
    Modified residuei399 – 3991N6-malonyllysineBy similarity
    Glycosylationi434 – 4341O-linked (GlcNAc)1 Publication
    Modified residuei435 – 4351N6-acetyllysineBy similarity
    Modified residuei452 – 4521Phosphoserine; alternateBy similarity
    Glycosylationi452 – 4521O-linked (GlcNAc); alternate1 Publication
    Modified residuei481 – 4811N6-acetyllysineBy similarity
    Modified residuei484 – 4841Phosphotyrosine1 Publication
    Modified residuei531 – 5311N6-succinyllysine1 Publication
    Modified residuei532 – 5321PhosphoserineBy similarity
    Modified residuei577 – 5771N6-succinyllysine1 Publication
    Modified residuei624 – 6241N6-acetyllysine1 Publication
    Modified residuei718 – 7181Phosphoserine; by PLK2 and PLK3By similarity

    Post-translational modificationi

    Ubiquitinated in the presence of STUB1-UBE2D1 complex (in vitro).By similarity
    ISGylated.1 Publication
    S-nitrosylated; negatively regulates the ATPase activity.By similarity

    Keywords - PTMi

    Acetylation, Glycoprotein, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP11499.
    PaxDbiP11499.
    PRIDEiP11499.

    2D gel databases

    SWISS-2DPAGEP11499.

    PTM databases

    PhosphoSiteiP11499.

    Expressioni

    Gene expression databases

    ArrayExpressiP11499.
    BgeeiP11499.
    GenevestigatoriP11499.

    Interactioni

    Subunit structurei

    Homodimer. Interacts with p53/TP53. Forms a complex with CDK6 and Hsp90/HSP90AB1 By similarity. Interacts with UNC45A. Binding to UNC45A involves 2 UNC45A monomers per HSP90AB1 dimer. Interacts with CHORDC1. Interacts with DNAJC7 By similarity. Interacts with FKBP4 By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    NelfeP194262EBI-492813,EBI-6142845
    Nr3c1P065372EBI-492813,EBI-492753

    Protein-protein interaction databases

    BioGridi200454. 39 interactions.
    DIPiDIP-461N.
    IntActiP11499. 24 interactions.
    MINTiMINT-152750.

    Structurei

    3D structure databases

    ProteinModelPortaliP11499.
    SMRiP11499. Positions 8-691.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi720 – 7245TPR repeat-binding

    Sequence similaritiesi

    Belongs to the heat shock protein 90 family.Curated

    Phylogenomic databases

    eggNOGiCOG0326.
    HOGENOMiHOG000031988.
    HOVERGENiHBG007374.
    InParanoidiP11499.
    KOiK04079.
    OMAiMKETQKC.
    OrthoDBiEOG780RM0.
    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.

    P11499-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPEEVHHGEE EVETFAFQAE IAQLMSLIIN TFYSNKEIFL RELISNASDA    50
    LDKIRYESLT DPSKLDSGKE LKIDIIPNPQ ERTLTLVDTG IGMTKADLIN 100
    NLGTIAKSGT KAFMEALQAG ADISMIGQFG VGFYSAYLVA EKVVVITKHN 150
    DDEQYAWESS AGGSFTVRAD HGEPIGRGTK VILHLKEDQT EYLEERRVKE 200
    VVKKHSQFIG YPITLYLEKE REKEISDDEA EEEKGEKEEE DKEDEEKPKI 250
    EDVGSDEEDD SGKDKKKKTK KIKEKYIDQE ELNKTKPIWT RNPDDITQEE 300
    YGEFYKSLTN DWEDHLAVKH FSVEGQLEFR ALLFIPRRAP FDLFENKKKK 350
    NNIKLYVRRV FIMDSCDELI PEYLNFIRGV VDSEDLPLNI SREMLQQSKI 400
    LKVIRKNIVK KCLELFSELA EDKENYKKFY EAFSKNLKLG IHEDSTNRRR 450
    LSELLRYHTS QSGDEMTSLS EYVSRMKETQ KSIYYITGES KEQVANSAFV 500
    ERVRKRGFEV VYMTEPIDEY CVQQLKEFDG KSLVSVTKEG LELPEDEEEK 550
    KKMEESKAKF ENLCKLMKEI LDKKVEKVTI SNRLVSSPCC IVTSTYGWTA 600
    NMERIMKAQA LRDNSTMGYM MAKKHLEINP DHPIVETLRQ KAEADKNDKA 650
    VKDLVVLLFE TALLSSGFSL EDPQTHSNRI YRMIKLGLGI DEDEVTAEEP 700
    SAAVPDEIPP LEGDEDASRM EEVD 724
    Length:724
    Mass (Da):83,281
    Last modified:July 27, 2011 - v3
    Checksum:iCE323E81CE173ECB
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti76 – 761I → L in AAA37865. (PubMed:2445630)Curated
    Sequence conflicti279 – 2791Q → R in AAC36532. (PubMed:9798653)Curated
    Sequence conflicti306 – 3061K → R in AAC36532. (PubMed:9798653)Curated
    Sequence conflicti318 – 3181V → I in BAE27449. (PubMed:16141072)Curated
    Sequence conflicti332 – 3321L → F in AAA37865. (PubMed:2445630)Curated
    Sequence conflicti356 – 3561Y → H in AAC36532. (PubMed:9798653)Curated
    Sequence conflicti495 – 4951A → P in AAA37865. (PubMed:2445630)Curated
    Sequence conflicti497 – 4971S → P in AAA37866. (PubMed:2469626)Curated
    Sequence conflicti531 – 5355KSLVS → GGPGT in AAB23704. (PubMed:1406681)Curated
    Sequence conflicti538 – 5381K → N in AAB23704. (PubMed:1406681)Curated
    Sequence conflicti575 – 5751V → F in AAB23704. (PubMed:1406681)Curated
    Sequence conflicti667 – 6671G → V in AAA37865. (PubMed:2445630)Curated
    Sequence conflicti699 – 6991E → G in BAE27449. (PubMed:16141072)Curated
    Sequence conflicti719 – 7191R → P in AAA37866. (PubMed:2469626)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M36829 mRNA. Translation: AAA37866.1.
    M18186 mRNA. Translation: AAA37865.1.
    AK146809 mRNA. Translation: BAE27449.1.
    AC163677 Genomic DNA. No translation available.
    U89426 mRNA. Translation: AAC36532.1.
    S46109 mRNA. Translation: AAB23704.1.
    CCDSiCCDS28812.1.
    PIRiA35569. HHMS84.
    I57523.
    RefSeqiNP_032328.2. NM_008302.3.
    UniGeneiMm.2180.

    Genome annotation databases

    EnsembliENSMUST00000024739; ENSMUSP00000024739; ENSMUSG00000023944.
    GeneIDi15516.
    KEGGimmu:15516.
    UCSCiuc008cqz.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M36829 mRNA. Translation: AAA37866.1 .
    M18186 mRNA. Translation: AAA37865.1 .
    AK146809 mRNA. Translation: BAE27449.1 .
    AC163677 Genomic DNA. No translation available.
    U89426 mRNA. Translation: AAC36532.1 .
    S46109 mRNA. Translation: AAB23704.1 .
    CCDSi CCDS28812.1.
    PIRi A35569. HHMS84.
    I57523.
    RefSeqi NP_032328.2. NM_008302.3.
    UniGenei Mm.2180.

    3D structure databases

    ProteinModelPortali P11499.
    SMRi P11499. Positions 8-691.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 200454. 39 interactions.
    DIPi DIP-461N.
    IntActi P11499. 24 interactions.
    MINTi MINT-152750.

    PTM databases

    PhosphoSitei P11499.

    2D gel databases

    SWISS-2DPAGE P11499.

    Proteomic databases

    MaxQBi P11499.
    PaxDbi P11499.
    PRIDEi P11499.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000024739 ; ENSMUSP00000024739 ; ENSMUSG00000023944 .
    GeneIDi 15516.
    KEGGi mmu:15516.
    UCSCi uc008cqz.1. mouse.

    Organism-specific databases

    CTDi 3326.
    MGIi MGI:96247. Hsp90ab1.

    Phylogenomic databases

    eggNOGi COG0326.
    HOGENOMi HOG000031988.
    HOVERGENi HBG007374.
    InParanoidi P11499.
    KOi K04079.
    OMAi MKETQKC.
    OrthoDBi EOG780RM0.
    TreeFami TF300686.

    Enzyme and pathway databases

    Reactomei REACT_198374. Regulation of actin dynamics for phagocytic cup formation.
    REACT_198644. The NLRP3 inflammasome.
    REACT_213550. HSF1-dependent transactivation.
    REACT_223784. Attenuation phase.
    REACT_225256. HSF1 activation.

    Miscellaneous databases

    ChiTaRSi HSP90AB1. mouse.
    NextBioi 288432.
    PROi P11499.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P11499.
    Bgeei P11499.
    Genevestigatori P11499.

    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. "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].
    2. "Cloning and nucleotide sequence of the murine hsp84 cDNA and chromosome assignment of related sequences."
      Moore S.K., Kozak C., Robinson E.A., Ullrich S.J., Appella E.
      Gene 56:29-40(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 2-31; 94-156; 158-161; 467-513; 554-566; 622-640; 684-688 AND 690-720.
    3. "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].
    4. "Characterization of the mouse 84-kD heat shock protein gene family."
      Moore S.K., Rijli F., Appella E.
      DNA Cell Biol. 9:387-400(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    5. "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: Kidney.
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    7. "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 AND 114-125.
    8. "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 2-6, HOMODIMERIZATION.
    9. Lubec G., Kang S.U., Klug S., Yang J.W., Zigmond M., Sunyer B., Chen W.-Q.
      Submitted (JAN-2009) to UniProtKB
      Strain: C57BL/6 and OF1.
      Tissue: Brain and Hippocampus.
    10. "Expressed genes in interleukin-4 treated B cells identified by cDNA representational difference analysis."
      Chu C.C., Paul W.E.
      Mol. Immunol. 35:487-502(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 272-400.
      Strain: BALB/c.
      Tissue: Spleen.
    11. "Conformational activation of a basic helix-loop-helix protein (MyoD1) by the C-terminal region of murine HSP90 (HSP84)."
      Shaknovich R., Shue G., Kohtz D.S.
      Mol. Cell. Biol. 12:5059-5068(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 531-724.
      Tissue: Heart.
    12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-255, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic brain.
    13. "Mammalian CHORD-containing protein 1 is a novel heat shock protein 90-interacting protein."
      Wu J., Luo S., Jiang H., Li H.
      FEBS Lett. 579:421-426(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CHORDC1.
    14. Cited for: ISGYLATION.
    15. "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-484, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Mast cell.
    16. "A differential phosphoproteomic analysis of retinoic acid-treated P19 cells."
      Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.
      J. Proteome Res. 6:3174-3186(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-255 AND SER-261, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Teratocarcinoma.
    17. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226; SER-255 AND SER-261, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    18. "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-305, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Brain.
    19. "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-255, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    20. "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-255, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    21. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
      Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
      Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-255, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.
    22. "Mapping of O-GlcNAc sites of 20 S proteasome subunits and Hsp90 by a novel biotin-cystamine tag."
      Overath T., Kuckelkorn U., Henklein P., Strehl B., Bonar D., Kloss A., Siele D., Kloetzel P.M., Janek K.
      Mol. Cell. Proteomics 11:467-477(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION AT SER-434 AND SER-452.
      Tissue: Liver.
    23. "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-624, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-219; LYS-531 AND LYS-577, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.

    Entry informationi

    Entry nameiHS90B_MOUSE
    AccessioniPrimary (citable) accession number: P11499
    Secondary accession number(s): O89078, Q3UIQ7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1989
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 161 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

    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