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P11499 (HS90B_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 159. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:Hsp90ab1
Synonyms:Hsp84, Hsp84-1, Hspcb
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length724 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. HAMAP-Rule MF_00505

Subunit structure

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. Ref.8 Ref.13

Subcellular location

Cytoplasm. Melanosome By similarity HAMAP-Rule MF_00505.

Post-translational modification

Ubiquitinated in the presence of STUB1-UBE2D1 complex (in vitro) By similarity. HAMAP-Rule MF_00505

ISGylated. Ref.14

S-nitrosylated; negatively regulates the ATPase activity By similarity. HAMAP-Rule MF_00505

Sequence similarities

Belongs to the heat shock protein 90 family.

Ontologies

Keywords
   Biological processStress response
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionChaperone
   PTMAcetylation
Glycoprotein
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcellular response to interleukin-4

Inferred from direct assay Ref.10. Source: MGI

cellular response to organic cyclic compound

Inferred from electronic annotation. Source: Ensembl

negative regulation of neuron apoptotic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of proteasomal ubiquitin-dependent protein catabolic process

Inferred from electronic annotation. Source: Ensembl

placenta development

Inferred from mutant phenotype PubMed 10654595. Source: MGI

positive regulation of cell size

Inferred from electronic annotation. Source: Ensembl

positive regulation of nitric oxide biosynthetic process

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of protein binding

Inferred from electronic annotation. Source: Ensembl

positive regulation of protein import into nucleus, translocation

Inferred from electronic annotation. Source: Ensembl

positive regulation of protein serine/threonine kinase activity

Inferred from electronic annotation. Source: Ensembl

protein folding

Inferred from electronic annotation. Source: InterPro

regulation of interferon-gamma-mediated signaling pathway

Inferred from electronic annotation. Source: Ensembl

regulation of type I interferon-mediated signaling pathway

Inferred from electronic annotation. Source: Ensembl

response to salt stress

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentCOP9 signalosome

Inferred from electronic annotation. Source: Ensembl

apical plasma membrane

Inferred from electronic annotation. Source: Ensembl

basolateral plasma membrane

Inferred from electronic annotation. Source: Ensembl

brush border membrane

Inferred from electronic annotation. Source: Ensembl

cell surface

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Inferred from direct assay PubMed 17908927. Source: MGI

cytosol

Inferred from electronic annotation. Source: Ensembl

inclusion body

Inferred from electronic annotation. Source: Ensembl

intracellular

Inferred from direct assay PubMed 9122205. Source: MGI

melanosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

mitochondrion

Inferred from direct assay PubMed 14651853. Source: MGI

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

CTP binding

Inferred from electronic annotation. Source: Ensembl

GTP binding

Inferred from electronic annotation. Source: Ensembl

TPR domain binding

Inferred from sequence or structural similarity. Source: UniProtKB

UTP binding

Inferred from electronic annotation. Source: Ensembl

dATP binding

Inferred from electronic annotation. Source: Ensembl

double-stranded RNA binding

Inferred from sequence orthology PubMed 21266579. Source: MGI

nitric-oxide synthase regulator activity

Inferred from sequence or structural similarity. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 11751894PubMed 22579285. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

NelfeP194262EBI-492813,EBI-6142845
Nr3c1P065372EBI-492813,EBI-492753

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.2 Ref.7 Ref.8
Chain2 – 724723Heat shock protein HSP 90-beta HAMAP-Rule MF_00505
PRO_0000062918

Regions

Motif720 – 7245TPR repeat-binding HAMAP-Rule MF_00505

Sites

Binding site461ATP By similarity
Binding site881ATP By similarity
Binding site1071ATP By similarity
Binding site1331ATP; via amide nitrogen By similarity
Binding site3921ATP By similarity

Amino acid modifications

Modified residue2191N6-succinyllysine Ref.23
Modified residue2261Phosphoserine Ref.17
Modified residue2551Phosphoserine Ref.12 Ref.16 Ref.17 Ref.19 Ref.20 Ref.21
Modified residue2611Phosphoserine Ref.16 Ref.17
Modified residue2971Phosphothreonine By similarity
Modified residue3051Phosphotyrosine Ref.18
Modified residue3071Phosphoserine By similarity
Modified residue3991N6-malonyllysine By similarity
Modified residue4351N6-acetyllysine By similarity
Modified residue4521Phosphoserine; alternate By similarity
Modified residue4811N6-acetyllysine By similarity
Modified residue4841Phosphotyrosine Ref.15
Modified residue5311N6-succinyllysine Ref.23
Modified residue5321Phosphoserine By similarity
Modified residue5771N6-succinyllysine Ref.23
Modified residue6241N6-acetyllysine Ref.23
Modified residue7181Phosphoserine; by PLK2 and PLK3 By similarity
Glycosylation4341O-linked (GlcNAc) Ref.22
Glycosylation4521O-linked (GlcNAc); alternate Ref.22

Experimental info

Sequence conflict761I → L in AAA37865. Ref.2
Sequence conflict2791Q → R in AAC36532. Ref.10
Sequence conflict3061K → R in AAC36532. Ref.10
Sequence conflict3181V → I in BAE27449. Ref.5
Sequence conflict3321L → F in AAA37865. Ref.2
Sequence conflict3561Y → H in AAC36532. Ref.10
Sequence conflict4951A → P in AAA37865. Ref.2
Sequence conflict4971S → P in AAA37866. Ref.1
Sequence conflict531 – 5355KSLVS → GGPGT in AAB23704. Ref.11
Sequence conflict5381K → N in AAB23704. Ref.11
Sequence conflict5751V → F in AAB23704. Ref.11
Sequence conflict6671G → V in AAA37865. Ref.2
Sequence conflict6991E → G in BAE27449. Ref.5
Sequence conflict7191R → P in AAA37866. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P11499 [UniParc].

Last modified July 27, 2011. Version 3.
Checksum: CE323E81CE173ECB

FASTA72483,281
        10         20         30         40         50         60 
MPEEVHHGEE EVETFAFQAE IAQLMSLIIN TFYSNKEIFL RELISNASDA LDKIRYESLT 

        70         80         90        100        110        120 
DPSKLDSGKE LKIDIIPNPQ ERTLTLVDTG IGMTKADLIN NLGTIAKSGT KAFMEALQAG 

       130        140        150        160        170        180 
ADISMIGQFG VGFYSAYLVA EKVVVITKHN DDEQYAWESS AGGSFTVRAD HGEPIGRGTK 

       190        200        210        220        230        240 
VILHLKEDQT EYLEERRVKE VVKKHSQFIG YPITLYLEKE REKEISDDEA EEEKGEKEEE 

       250        260        270        280        290        300 
DKEDEEKPKI EDVGSDEEDD SGKDKKKKTK KIKEKYIDQE ELNKTKPIWT RNPDDITQEE 

       310        320        330        340        350        360 
YGEFYKSLTN DWEDHLAVKH FSVEGQLEFR ALLFIPRRAP FDLFENKKKK NNIKLYVRRV 

       370        380        390        400        410        420 
FIMDSCDELI PEYLNFIRGV VDSEDLPLNI SREMLQQSKI LKVIRKNIVK KCLELFSELA 

       430        440        450        460        470        480 
EDKENYKKFY EAFSKNLKLG IHEDSTNRRR LSELLRYHTS QSGDEMTSLS EYVSRMKETQ 

       490        500        510        520        530        540 
KSIYYITGES KEQVANSAFV ERVRKRGFEV VYMTEPIDEY CVQQLKEFDG KSLVSVTKEG 

       550        560        570        580        590        600 
LELPEDEEEK KKMEESKAKF ENLCKLMKEI LDKKVEKVTI SNRLVSSPCC IVTSTYGWTA 

       610        620        630        640        650        660 
NMERIMKAQA LRDNSTMGYM MAKKHLEINP DHPIVETLRQ KAEADKNDKA VKDLVVLLFE 

       670        680        690        700        710        720 
TALLSSGFSL EDPQTHSNRI YRMIKLGLGI DEDEVTAEEP SAAVPDEIPP LEGDEDASRM 


EEVD 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
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
Cited for: PROTEIN SEQUENCE OF 42-53; 56-64; 73-95; 149-168; 181-196; 205-219; 250-266; 276-330; 339-347; 360-392; 429-435; 439-448; 457-475; 482-491; 539-552; 558-565; 575-583 AND 624-639.
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]"Phosphoproteomic analysis of the developing mouse brain."
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.
Mol. Cell. Proteomics 3:1093-1101(2004) [PubMed] [Europe PMC] [Abstract]
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]"Proteomic identification of proteins conjugated to ISG15 in mouse and human cells."
Giannakopoulos N.V., Luo J.K., Papov V., Zou W., Lenschow D.J., Jacobs B.S., Borden E.C., Li J., Virgin H.W., Zhang D.E.
Biochem. Biophys. Res. Commun. 336:496-506(2005) [PubMed] [Europe PMC] [Abstract]
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]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS28812.1.
PIRHHMS84. A35569.
I57523.
RefSeqNP_032328.2. NM_008302.3.
UniGeneMm.2180.

3D structure databases

ProteinModelPortalP11499.
SMRP11499. Positions 8-691.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid200454. 39 interactions.
DIPDIP-461N.
IntActP11499. 24 interactions.
MINTMINT-152750.

PTM databases

PhosphoSiteP11499.

2D gel databases

SWISS-2DPAGEP11499.

Proteomic databases

MaxQBP11499.
PaxDbP11499.
PRIDEP11499.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000024739; ENSMUSP00000024739; ENSMUSG00000023944.
GeneID15516.
KEGGmmu:15516.
UCSCuc008cqz.1. mouse.

Organism-specific databases

CTD3326.
MGIMGI:96247. Hsp90ab1.

Phylogenomic databases

eggNOGCOG0326.
HOGENOMHOG000031988.
HOVERGENHBG007374.
InParanoidP11499.
KOK04079.
OMAMKETQKC.
OrthoDBEOG780RM0.
TreeFamTF300686.

Gene expression databases

ArrayExpressP11499.
BgeeP11499.
GenevestigatorP11499.

Family and domain databases

Gene3D3.30.565.10. 2 hits.
HAMAPMF_00505. HSP90.
InterProIPR003594. HATPase_ATP-bd.
IPR019805. Heat_shock_protein_90_CS.
IPR001404. Hsp90_fam.
IPR020575. Hsp90_N.
IPR020568. Ribosomal_S5_D2-typ_fold.
[Graphical view]
PANTHERPTHR11528. PTHR11528. 1 hit.
PfamPF02518. HATPase_c. 1 hit.
PF00183. HSP90. 1 hit.
[Graphical view]
PIRSFPIRSF002583. Hsp90. 1 hit.
PRINTSPR00775. HEATSHOCK90.
SMARTSM00387. HATPase_c. 1 hit.
[Graphical view]
SUPFAMSSF54211. SSF54211. 1 hit.
SSF55874. SSF55874. 1 hit.
PROSITEPS00298. HSP90. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSHSP90AB1. mouse.
NextBio288432.
PROP11499.
SOURCESearch...

Entry information

Entry nameHS90B_MOUSE
AccessionPrimary (citable) accession number: P11499
Secondary accession number(s): O89078, Q3UIQ7
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: July 27, 2011
Last modified: July 9, 2014
This is version 159 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot