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P46633

- HS90A_CRIGR

UniProt

P46633 - HS90A_CRIGR

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Protein

Heat shock protein HSP 90-alpha

Gene

HSP90AA1

Organism
Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript 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. ATP binding Source: UniProtKB-KW
  2. nitric-oxide synthase regulator activity Source: UniProtKB
  3. TPR domain binding Source: UniProtKB

GO - Biological processi

  1. positive regulation of nitric oxide biosynthetic process Source: UniProtKB
  2. protein folding Source: InterPro
  3. regulation of catalytic activity Source: GOC
  4. response to stress Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Biological processi

Stress response

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Heat shock protein HSP 90-alpha
Gene namesi
Name:HSP90AA1
Synonyms:HSP90A, HSPCA
OrganismiCricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
Taxonomic identifieri10029 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaCricetidaeCricetinaeCricetulus

Subcellular locationi

Cytoplasm By similarity. Melanosome By similarity. Cell membrane By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
  2. plasma membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 733732Heat shock protein HSP 90-alphaPRO_0000062909Add
BLAST

Amino acid modifications

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

Post-translational modificationi

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

Keywords - PTMi

Acetylation, Phosphoprotein, S-nitrosylation, Ubl conjugation

Proteomic databases

PRIDEiP46633.

Interactioni

Subunit structurei

Homodimer. 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 (By similarity). Following LPS binding, may form a complex with CXCR4, GDF5 and HSPA8 (By similarity).By similarity

Structurei

3D structure databases

ProteinModelPortaliP46633.
SMRiP46633. Positions 9-223, 294-697.
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

HOVERGENiHBG007374.
KOiK04079.

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.

P46633-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MPEETQTQDQ PMEEEEVETF AFQAEIAQLM SLIINTFYSN KEIFLRELIS
60 70 80 90 100
NSSDALDKIR YESLTDPSKL DSGKELHINI IPNKQDRTLT IVDTGIGMTK
110 120 130 140 150
ADLINNLGTI AKSGTKAFME ALQAGADISM IGQFGVGFYT AYLVAEKVTV
160 170 180 190 200
ITKHNDDEQY AWESSAGGSF TVRTDTGEPM GRGTKVILHL KEDQTEYMEE
210 220 230 240 250
RRIKEIVKKH SQFIGYPITL FVEKERDKEV SDDEAEEKED KEEEKEKEEK
260 270 280 290 300
GIDDKPEIED VGSDEEEEEK KDGDKKKKKK IKEKYIDQEE LNKTKPIWTR
310 320 330 340 350
NPDDITNEEY GEFYKSLTND WEEHLAVKHF SVEGQLEFRA LLFVPRRAPF
360 370 380 390 400
DLFENRKKKN NIKLYVRRVF IMDNCEELFP EYLNFIRGVV DSEDLPLNIS
410 420 430 440 450
REILQQSKIL KVIRKNLVRK CLELFHELAE 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 MERIIKAQAL RDNSTMGYMA AKKHLEINPD HSIIETLRQK
660 670 680 690 700
AEADKNDKSV KDLVILLYET ALLSSGFSLE DPQTHANRIY RMIKLGLGID
710 720 730
EDDPTVDDTS AAVTEEMPPL EGDDDTSRME EVD
Length:733
Mass (Da):84,849
Last modified:January 23, 2007 - v2
Checksum:i95EECAFD0E410057
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L33676 mRNA. Translation: AAA36992.1.
RefSeqiNP_001233750.1. NM_001246821.1.

Genome annotation databases

GeneIDi100689397.
KEGGicge:100689397.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L33676 mRNA. Translation: AAA36992.1 .
RefSeqi NP_001233750.1. NM_001246821.1.

3D structure databases

ProteinModelPortali P46633.
SMRi P46633. Positions 9-223, 294-697.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PRIDEi P46633.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 100689397.
KEGGi cge:100689397.

Organism-specific databases

CTDi 3320.

Phylogenomic databases

HOVERGENi HBG007374.
KOi K04079.

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

  1. "Characterization of a cDNA clone encoding HSP90A from Chinese hamster cells."
    Chen M.-S.M.C., Laszlo A.
    Submitted (JUL-1995) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Entry informationi

Entry nameiHS90A_CRIGR
AccessioniPrimary (citable) accession number: P46633
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: January 23, 2007
Last modified: October 29, 2014
This is version 97 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3