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Protein

Endoplasmin

Gene

HSP90B1

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

Molecular chaperone that functions in the processing and transport of secreted proteins. When associated with CNPY3, required for proper folding of Toll-like receptors. Functions in endoplasmic reticulum associated degradation (ERAD). Has ATPase activity (By similarity).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei107ATPBy similarity1
Binding sitei149ATPBy similarity1
Binding sitei168ATPBy similarity1
Binding sitei199ATP; via amide nitrogenBy similarity1
Binding sitei448ATPBy similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Ligandi

ATP-binding, Calcium, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-BTA-1679131. Trafficking and processing of endosomal TLR.
R-BTA-3000480. Scavenging by Class A Receptors.

Names & Taxonomyi

Protein namesi
Recommended name:
Endoplasmin
Alternative name(s):
94 kDa glucose-regulated protein
Short name:
GRP-94
Heat shock protein 90 kDa beta member 1
Gene namesi
Name:HSP90B1
Synonyms:GRP94, TRA1
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 5

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 21Sequence analysisAdd BLAST21
ChainiPRO_000001359622 – 804EndoplasminAdd BLAST783

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi62N-linked (GlcNAc...)Sequence analysis1
Modified residuei64PhosphoserineBy similarity1
Glycosylationi107N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi138InterchainBy similarity
Modified residuei172PhosphoserineBy similarity1
Glycosylationi217N-linked (GlcNAc...)Sequence analysis1
Modified residuei306PhosphoserineBy similarity1
Modified residuei403PhosphoserineBy similarity1
Modified residuei404N6-succinyllysineBy similarity1
Glycosylationi445N-linked (GlcNAc...)Sequence analysis1
Modified residuei447PhosphoserineBy similarity1
Modified residuei479N6-acetyllysineBy similarity1
Glycosylationi481N-linked (GlcNAc...)Sequence analysis1
Glycosylationi502N-linked (GlcNAc...)Sequence analysis1
Modified residuei633N6-succinyllysineBy similarity1
Modified residuei786PhosphothreonineBy similarity1

Post-translational modificationi

Phosphorylated.By similarity

Keywords - PTMi

Acetylation, Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiQ95M18.
PeptideAtlasiQ95M18.
PRIDEiQ95M18.

Expressioni

Gene expression databases

BgeeiENSBTAG00000003362.

Interactioni

Subunit structurei

Homodimer; disulfide-linked. Component of an EIF2 complex at least composed of CELF1/CUGBP1, CALR, CALR3, EIF2S1, EIF2S2, HSP90B1 and HSPA5 (By similarity). Part of a large chaperone multiprotein complex comprising DNAJB11, HSP90B1, HSPA5, HYOU, PDIA2, PDIA4, PDIA6, PPIB, SDF2L1, UGT1A1 and very small amounts of ERP29, but not, or at very low levels, CALR nor CANX. Interacts with AIMP1; regulates its retention in the endoplasmic reticulum. Interacts with OS9 (By similarity). Interacts with CNPY3; this interaction is disrupted in the presence of ATP. Interacts with several TLRs, including TLR4 and TLR9, but not with TLR3 (By similarity). Interacts with MZB1 in a calcium-dependent manner (By similarity). Interacts with METTL23 (By similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

IntActiQ95M18. 1 interactor.
STRINGi9913.ENSBTAP00000004364.

Structurei

3D structure databases

ProteinModelPortaliQ95M18.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi801 – 804Prevents secretion from ERSequence analysis4

Sequence similaritiesi

Belongs to the heat shock protein 90 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG0020. Eukaryota.
COG0326. LUCA.
GeneTreeiENSGT00840000129758.
HOGENOMiHOG000031988.
HOVERGENiHBG007374.
InParanoidiQ95M18.
KOiK09487.
OMAiRKPADVT.
OrthoDBiEOG091G0270.
TreeFamiTF105969.

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]
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. 2 hits.
PROSITEiPS00014. ER_TARGET. 1 hit.
PS00298. HSP90. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q95M18-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRALWVLGLC CVLLTFGSVR ADDEVDVDGT VEEDLGKSRE GSRTDDEVVQ
60 70 80 90 100
REEEAIQLDG LNASQIRELR EKSEKFAFQA EVNRMMKLII NSLYKNKEIF
110 120 130 140 150
LRELISNASD ALDKIRLISL TDENALAGNE ELTVKIKCDK EKNLLHVTDT
160 170 180 190 200
GVGMTREELV KNLGTIAKSG TSEFLNKMTE AQEDGQSTSE LIGQFGVGFY
210 220 230 240 250
SAFLVADKVI VTSKHNNDTQ HIWESDSNEF SVIADPRGNT LGRGTTITLV
260 270 280 290 300
LKEEASDYLE LDTIKNLVKK YSQFINFPIY VWSSKTETVE EPAEEEEAAK
310 320 330 340 350
EDKEESDDEA AVEEEEDEKK PKTKKVEKTV WDWELMNDIK PIWQRPSKEV
360 370 380 390 400
EEDEYKAFYK SFSKESDDPM AYIHFTAEGE VTFKSILFVP TSAPRGLFDE
410 420 430 440 450
YGSKKSDYIK LYVRRVFITD DFHDMMPKYL NFVKGVVDSD DLPLNVSRET
460 470 480 490 500
LQQHKLLKVI RKKLVRKTLD MIKKIADEKY NDTFWKEFGT NIKLGVIEDH
510 520 530 540 550
SNRTRLAKLL RFQSSHHPSD MTSLDQYVER MKEKQDKIYF MAGASRKEAE
560 570 580 590 600
SSPFVERLLK KGYEVIYLTE PVDEYCIQAL PEFDGKRFQN VAKEGVKFDE
610 620 630 640 650
SEKSKESREA VEKEFEPLLN WMKDKALKDK IEKAVVSQRL TESPCALVAS
660 670 680 690 700
QYGWSGNMER IMKAQAYQTG KDISTNYYAS QKKTFEINPR HPLIRDMLRR
710 720 730 740 750
VKEDEDDKTV SDLAVVLFET ATLRSGYLLP DTKAYGDRIE RMLRLSLNID
760 770 780 790 800
PDAKVEEEPE EEPEETTEDT AEDTEQDEEE EMDAGTDEEE QETAEKSTAE

KDEL
Length:804
Mass (Da):92,427
Last modified:December 1, 2001 - v1
Checksum:i0A204A77E61F1FDE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB025193 mRNA. Translation: BAB69766.1.
BC104549 mRNA. Translation: AAI04550.1.
RefSeqiNP_777125.1. NM_174700.2.
UniGeneiBt.8686.

Genome annotation databases

EnsembliENSBTAT00000004364; ENSBTAP00000004364; ENSBTAG00000003362.
GeneIDi282646.
KEGGibta:282646.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB025193 mRNA. Translation: BAB69766.1.
BC104549 mRNA. Translation: AAI04550.1.
RefSeqiNP_777125.1. NM_174700.2.
UniGeneiBt.8686.

3D structure databases

ProteinModelPortaliQ95M18.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ95M18. 1 interactor.
STRINGi9913.ENSBTAP00000004364.

Proteomic databases

PaxDbiQ95M18.
PeptideAtlasiQ95M18.
PRIDEiQ95M18.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000004364; ENSBTAP00000004364; ENSBTAG00000003362.
GeneIDi282646.
KEGGibta:282646.

Organism-specific databases

CTDi7184.

Phylogenomic databases

eggNOGiKOG0020. Eukaryota.
COG0326. LUCA.
GeneTreeiENSGT00840000129758.
HOGENOMiHOG000031988.
HOVERGENiHBG007374.
InParanoidiQ95M18.
KOiK09487.
OMAiRKPADVT.
OrthoDBiEOG091G0270.
TreeFamiTF105969.

Enzyme and pathway databases

ReactomeiR-BTA-1679131. Trafficking and processing of endosomal TLR.
R-BTA-3000480. Scavenging by Class A Receptors.

Gene expression databases

BgeeiENSBTAG00000003362.

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]
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. 2 hits.
PROSITEiPS00014. ER_TARGET. 1 hit.
PS00298. HSP90. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiENPL_BOVIN
AccessioniPrimary (citable) accession number: Q95M18
Secondary accession number(s): Q3MHX8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 25, 2003
Last sequence update: December 1, 2001
Last modified: October 5, 2016
This is version 124 of the entry and version 1 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.