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Protein

Heat shock protein HSP 90-beta

Gene

HSP90AB1

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 3 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)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

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
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 724723Heat shock protein HSP 90-betaPRO_0000247933Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei219 – 2191N6-succinyllysineBy similarity
Modified residuei226 – 2261PhosphoserineBy similarity
Modified residuei255 – 2551PhosphoserineBy similarity
Modified residuei261 – 2611PhosphoserineBy similarity
Modified residuei297 – 2971PhosphothreonineBy similarity
Modified residuei305 – 3051PhosphotyrosineBy similarity
Modified residuei307 – 3071PhosphoserineBy similarity
Modified residuei399 – 3991N6-malonyllysineBy similarity
Glycosylationi434 – 4341O-linked (GlcNAc)By similarity
Modified residuei435 – 4351N6-acetyllysineBy similarity
Modified residuei445 – 4451PhosphoserineBy similarity
Modified residuei452 – 4521Phosphoserine; alternateBy similarity
Glycosylationi452 – 4521O-linked (GlcNAc); alternateBy similarity
Modified residuei479 – 4791PhosphothreonineBy similarity
Modified residuei481 – 4811N6-acetyllysineBy similarity
Modified residuei484 – 4841PhosphotyrosineBy similarity
Modified residuei531 – 5311N6-succinyllysineBy similarity
Modified residuei532 – 5321PhosphoserineBy similarity
Modified residuei577 – 5771N6-succinyllysineBy similarity
Modified residuei624 – 6241N6-acetyllysineBy similarity
Modified residuei669 – 6691PhosphoserineBy similarity
Modified residuei718 – 7181Phosphoserine; by PLK2 and PLK3By similarity

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

PeptideAtlasiQ76LV1.
PRIDEiQ76LV1.

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

Protein-protein interaction databases

BioGridi613028. 4 interactions.

Structurei

3D structure databases

ProteinModelPortaliQ76LV1.
SMRiQ76LV1. Positions 11-219, 285-688.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi720 – 7245TPR repeat-binding

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

HOGENOMiHOG000031988.
HOVERGENiHBG007374.
InParanoidiQ76LV1.
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.

Q76LV1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPEEVHHGEE EVETFAFQAE IAQLMSLIIN TFYSNKEIFL RELISNASDA
60 70 80 90 100
LDKIRYESLT DPSKLDSGKE LKIDIIPNPQ ERTLTLVDTG IGMTKADLVN
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 DEDEVTAEEP
710 720
SAAVPDEIPP LEGDEDASRM EEVD
Length:724
Mass (Da):83,253
Last modified:January 23, 2007 - v3
Checksum:iF5C0C65A143CCBD8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB072369 mRNA. Translation: BAC82488.1.
BT025368 mRNA. Translation: ABF57324.1.
RefSeqiNP_001073105.1. NM_001079637.1.
UniGeneiBt.64721.

Genome annotation databases

GeneIDi767874.
KEGGibta:767874.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB072369 mRNA. Translation: BAC82488.1.
BT025368 mRNA. Translation: ABF57324.1.
RefSeqiNP_001073105.1. NM_001079637.1.
UniGeneiBt.64721.

3D structure databases

ProteinModelPortaliQ76LV1.
SMRiQ76LV1. Positions 11-219, 285-688.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi613028. 4 interactions.

Proteomic databases

PeptideAtlasiQ76LV1.
PRIDEiQ76LV1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi767874.
KEGGibta:767874.

Organism-specific databases

CTDi3326.

Phylogenomic databases

HOGENOMiHOG000031988.
HOVERGENiHBG007374.
InParanoidiQ76LV1.
KOiK04079.

Miscellaneous databases

PROiQ76LV1.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "cDNA sequences of two isoforms of bovine heat-shock protein 90."
    Watanabe A., Uchida I., Fujimoto Y., Nakata K., Oikawa S.
    Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Mammary gland.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].

Entry informationi

Entry nameiHS90B_BOVIN
AccessioniPrimary (citable) accession number: Q76LV1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 25, 2006
Last sequence update: January 23, 2007
Last modified: July 6, 2016
This is version 99 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.