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P11499

- HS90B_MOUSE

UniProt

P11499 - HS90B_MOUSE

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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

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. poly(A) RNA binding Source: Ensembl
  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
Complete GO annotation...

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.
REACT_254306. Sema3A PAK dependent Axon repulsion.

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. extracellular vesicular exosome Source: Ensembl
  9. inclusion body Source: Ensembl
  10. intracellular Source: MGI
  11. mitochondrion Source: MGI
Complete GO annotation...

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

BgeeiP11499.
ExpressionAtlasiP11499. baseline and differential.
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_C.
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

        10         20         30         40         50
MPEEVHHGEE EVETFAFQAE IAQLMSLIIN TFYSNKEIFL RELISNASDA
60 70 80 90 100
LDKIRYESLT DPSKLDSGKE LKIDIIPNPQ ERTLTLVDTG IGMTKADLIN
110 120 130 140 150
NLGTIAKSGT KAFMEALQAG ADISMIGQFG VGFYSAYLVA EKVVVITKHN
160 170 180 190 200
DDEQYAWESS AGGSFTVRAD HGEPIGRGTK VILHLKEDQT EYLEERRVKE
210 220 230 240 250
VVKKHSQFIG YPITLYLEKE REKEISDDEA EEEKGEKEEE DKEDEEKPKI
260 270 280 290 300
EDVGSDEEDD SGKDKKKKTK KIKEKYIDQE ELNKTKPIWT RNPDDITQEE
310 320 330 340 350
YGEFYKSLTN DWEDHLAVKH FSVEGQLEFR ALLFIPRRAP FDLFENKKKK
360 370 380 390 400
NNIKLYVRRV FIMDSCDELI PEYLNFIRGV VDSEDLPLNI SREMLQQSKI
410 420 430 440 450
LKVIRKNIVK KCLELFSELA EDKENYKKFY EAFSKNLKLG IHEDSTNRRR
460 470 480 490 500
LSELLRYHTS QSGDEMTSLS EYVSRMKETQ KSIYYITGES KEQVANSAFV
510 520 530 540 550
ERVRKRGFEV VYMTEPIDEY CVQQLKEFDG KSLVSVTKEG LELPEDEEEK
560 570 580 590 600
KKMEESKAKF ENLCKLMKEI LDKKVEKVTI SNRLVSSPCC IVTSTYGWTA
610 620 630 640 650
NMERIMKAQA LRDNSTMGYM MAKKHLEINP DHPIVETLRQ KAEADKNDKA
660 670 680 690 700
VKDLVVLLFE TALLSSGFSL EDPQTHSNRI YRMIKLGLGI DEDEVTAEEP
710 720
SAAVPDEIPP LEGDEDASRM EEVD
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.
REACT_254306. Sema3A PAK dependent Axon repulsion.

Miscellaneous databases

ChiTaRSi Hsp90ab1. mouse.
NextBioi 288432.
PROi P11499.
SOURCEi Search...

Gene expression databases

Bgeei P11499.
ExpressionAtlasi P11499. baseline and differential.
Genevestigatori P11499.

Family and domain databases

Gene3Di 3.30.565.10. 2 hits.
HAMAPi MF_00505. HSP90.
InterProi IPR003594. HATPase_C.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 163 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