Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P07901

- HS90A_MOUSE

UniProt

P07901 - HS90A_MOUSE

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

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

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. CTP binding Source: Ensembl
  4. dATP binding Source: Ensembl
  5. GTP binding Source: Ensembl
  6. mRNA binding Source: Ensembl
  7. nitric-oxide synthase regulator activity Source: UniProtKB
  8. protein homodimerization activity Source: MGI
  9. TPR domain binding Source: UniProtKB
  10. unfolded protein binding Source: UniProtKB
  11. UTP binding Source: Ensembl

GO - Biological processi

  1. cardiac muscle cell apoptotic process Source: Ensembl
  2. chaperone-mediated protein complex assembly Source: Ensembl
  3. neuron migration Source: Ensembl
  4. nitric oxide biosynthetic process Source: UniProtKB
  5. positive regulation of cardiac muscle contraction Source: Ensembl
  6. positive regulation of cell size Source: Ensembl
  7. positive regulation of cytotoxic T cell differentiation Source: UniProtKB
  8. positive regulation of lamellipodium assembly Source: Ensembl
  9. positive regulation of nitric oxide biosynthetic process Source: UniProtKB
  10. positive regulation of protein import into nucleus, translocation Source: Ensembl
  11. protein import into mitochondrial outer membrane Source: Ensembl
  12. protein refolding Source: UniProtKB
  13. regulation of catalytic activity Source: GOC
  14. response to estrogen Source: Ensembl
  15. response to heat Source: Ensembl
  16. response to salt stress Source: Ensembl
  17. response to unfolded protein Source: UniProtKB
  18. skeletal muscle contraction 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_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. apical plasma membrane Source: Ensembl
  2. basolateral plasma membrane Source: Ensembl
  3. brush border membrane Source: Ensembl
  4. cell surface Source: Ensembl
  5. cytoplasm Source: MGI
  6. cytosol Source: UniProtKB
  7. extracellular matrix Source: Ensembl
  8. extracellular vesicular exosome Source: Ensembl
  9. intracellular Source: MGI
  10. mitochondrion Source: Ensembl
  11. neuronal cell body Source: Ensembl
  12. neuron projection Source: Ensembl
  13. nucleus Source: Ensembl
  14. perinuclear region of cytoplasm Source: Ensembl
  15. protein complex Source: Ensembl
Complete GO annotation...

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.
ExpressionAtlasiP07901. baseline and differential.
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_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.

P07901-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MPEETQTQDQ PMEEEEVETF AFQAEIAQLM SLIINTFYSN KEIFLRELIS
60 70 80 90 100
NSSDALDKIR YESLTDPSKL DSGKELHINL IPSKQDRTLT IVDTGIGMTK
110 120 130 140 150
ADLINNLGTI AKSGTKAFME ALQAGADISM IGQFGVGFYS AYLVAEKVTV
160 170 180 190 200
ITKHNDDEQY AWESSAGGSF TVRTDTGEPM GRGTKVILHL KEDQTEYLEE
210 220 230 240 250
RRIKEIVKKH SQFIGYPITL FVEKERDKEV SDDEAEEKEE KEEEKEKEEK
260 270 280 290 300
ESDDKPEIED VGSDEEEEEK KDGDKKKKKK IKEKYIDQEE LNKTKPIWTR
310 320 330 340 350
NPDDITNEEY GEFYKSLTND WEEHLAVKHF SVEGQLEFRA LLFVPRRAPF
360 370 380 390 400
DLFENRKKKN NIKLYVRRVF IMDNCEELIP EYLNFIRGVV DSEDLPLNIS
410 420 430 440 450
REMLQQSKIL KVIRKNLVKK CLELFTELAE DKENYKKFYE QFSKNIKLGI
460 470 480 490 500
HEDSQNRKKL SELLRYYTSA SGDEMVSLKD YCTRMKENQK HIYFITGETK
510 520 530 540 550
DQVANSAFVE RLRKHGLEVI YMIEPIDEYC VQQLKEFEGK TLVSVTKEGL
560 570 580 590 600
ELPEDEEEKK KQEEKKTKFE NLCKIMKDIL EKKVEKVVVS NRLVTSPCCI
610 620 630 640 650
VTSTYGWTAN MERIMKAQAL RDNSTMGYMA AKKHLEINPD HSIIETLRQK
660 670 680 690 700
AEADKNDKSV KDLVILLYET ALLSSGFSLE DPQTHANRIY RMIKLGLGID
710 720 730
EDDPTVDDTS AAVTEEMPPL EGDDDTSRME EVD
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.
ExpressionAtlasi P07901. baseline and differential.
Genevestigatori P07901.

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. "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 29, 2014
This is version 162 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