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Protein

Heat shock protein HSP 90-beta

Gene

HSP90AB1

Organism
Equus caballus (Horse)
Status
Reviewed-Annotation score: Annotation score: 5 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).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei46ATPBy similarity1
Binding sitei88ATPBy similarity1
Binding sitei107ATPBy similarity1
Binding sitei133ATP; via amide nitrogenBy similarity1
Binding sitei392ATPBy similarity1

GO - Molecular functioni

GO - Biological processi

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-beta
Gene namesi
Name:HSP90AB1
Synonyms:HSPCB
OrganismiEquus caballus (Horse)
Taxonomic identifieri9796 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaPerissodactylaEquidaeEquus
Proteomesi
  • UP000002281 Componenti: Chromosome 20

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00000629162 – 724Heat shock protein HSP 90-betaAdd BLAST723

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei219N6-succinyllysineBy similarity1
Modified residuei226PhosphoserineBy similarity1
Modified residuei255PhosphoserineBy similarity1
Modified residuei261PhosphoserineBy similarity1
Modified residuei297PhosphothreonineBy similarity1
Modified residuei305PhosphotyrosineBy similarity1
Modified residuei307PhosphoserineBy similarity1
Modified residuei399N6-malonyllysineBy similarity1
Glycosylationi434O-linked (GlcNAc)By similarity1
Modified residuei435N6-acetyllysineBy similarity1
Modified residuei445PhosphoserineBy similarity1
Modified residuei452Phosphoserine; alternateBy similarity1
Glycosylationi452O-linked (GlcNAc); alternateBy similarity1
Modified residuei479PhosphothreonineBy similarity1
Modified residuei481N6-acetyllysineBy similarity1
Modified residuei484PhosphotyrosineBy similarity1
Modified residuei531N6-succinyllysineBy similarity1
Modified residuei532PhosphoserineBy similarity1
Modified residuei577N6-succinyllysineBy similarity1
Modified residuei624N6-acetyllysineBy similarity1
Modified residuei669PhosphoserineBy similarity1
Modified residuei718Phosphoserine; by PLK2 and PLK3By similarity1

Post-translational modificationi

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

Keywords - PTMi

Acetylation, Glycoprotein, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiQ9GKX8.
PeptideAtlasiQ9GKX8.
PRIDEiQ9GKX8.

Interactioni

Subunit structurei

Homodimer. Interacts with p53/TP53. Forms a complex with CDK6 and Hsp90/HSP90AB1. Interacts with UNC45A. Binding to UNC45A involves 2 UNC45A monomers per HSP90AB1 dimer. Interacts with CHORDC1 and DNAJC7. Interacts with FKBP4 (By similarity). May interact with NWD1 (By similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

IntActiQ9GKX8. 1 interactor.
MINTiMINT-6732879.
STRINGi9796.ENSECAP00000006887.

Structurei

3D structure databases

ProteinModelPortaliQ9GKX8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi720 – 724TPR repeat-binding5

Domaini

The TPR repeat-binding motif mediates interaction with TPR repeat-containing proteins.By similarity

Sequence similaritiesi

Belongs to the heat shock protein 90 family.Curated

Phylogenomic databases

eggNOGiKOG0019. Eukaryota.
KOG0020. Eukaryota.
COG0326. LUCA.
GeneTreeiENSGT00840000129758.
HOGENOMiHOG000031988.
HOVERGENiHBG007374.
InParanoidiQ9GKX8.
KOiK04079.
OMAiAFANDIC.
OrthoDBiEOG091G0270.
TreeFamiTF300686.

Family and domain databases

Gene3Di3.30.565.10. 2 hits.
HAMAPiMF_00505. HSP90. 1 hit.
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.

Q9GKX8-1 [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 DKDDEEKPKI
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 DEDEVAAEEP
710 720
SAAVPDEIPP LEGDEDASRM EEVD
Length:724
Mass (Da):83,237
Last modified:January 23, 2007 - v3
Checksum:i08FC18C214D03805
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti715E → D in BAB20776 (PubMed:11258446).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY383484 mRNA. Translation: AAQ88393.1.
AB043676 mRNA. Translation: BAB20776.1.
RefSeqiNP_001075407.1. NM_001081938.1.
UniGeneiEca.1802.

Genome annotation databases

EnsembliENSECAT00000009101; ENSECAP00000006887; ENSECAG00000008511.
GeneIDi100034150.
KEGGiecb:100034150.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY383484 mRNA. Translation: AAQ88393.1.
AB043676 mRNA. Translation: BAB20776.1.
RefSeqiNP_001075407.1. NM_001081938.1.
UniGeneiEca.1802.

3D structure databases

ProteinModelPortaliQ9GKX8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9GKX8. 1 interactor.
MINTiMINT-6732879.
STRINGi9796.ENSECAP00000006887.

Proteomic databases

PaxDbiQ9GKX8.
PeptideAtlasiQ9GKX8.
PRIDEiQ9GKX8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSECAT00000009101; ENSECAP00000006887; ENSECAG00000008511.
GeneIDi100034150.
KEGGiecb:100034150.

Organism-specific databases

CTDi3326.

Phylogenomic databases

eggNOGiKOG0019. Eukaryota.
KOG0020. Eukaryota.
COG0326. LUCA.
GeneTreeiENSGT00840000129758.
HOGENOMiHOG000031988.
HOVERGENiHBG007374.
InParanoidiQ9GKX8.
KOiK04079.
OMAiAFANDIC.
OrthoDBiEOG091G0270.
TreeFamiTF300686.

Family and domain databases

Gene3Di3.30.565.10. 2 hits.
HAMAPiMF_00505. HSP90. 1 hit.
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]
ProtoNetiSearch...

Entry informationi

Entry nameiHS90B_HORSE
AccessioniPrimary (citable) accession number: Q9GKX8
Secondary accession number(s): Q6TXV3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 16, 2002
Last sequence update: January 23, 2007
Last modified: November 30, 2016
This is version 115 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, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.