Skip Header

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

Endoplasmin

Gene

HSP90B1

Organism
Mesocricetus auratus (Golden hamster)
Status
Reviewed-Annotation score: -Experimental evidence at protein 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 sitei45ATPBy similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionChaperone
LigandATP-binding, Calcium, Nucleotide-binding

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
OrganismiMesocricetus auratus (Golden hamster)
Taxonomic identifieri10036 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaCricetidaeCricetinaeMesocricetus
Proteomesi
  • UP000189706 Componenti: Genome assembly

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Endoplasmic reticulum

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_0000062926‹1 – 400EndoplasminAdd BLAST›400

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N6-succinyllysineBy similarity1
Glycosylationi42N-linked (GlcNAc...) asparagineSequence analysis1
Modified residuei44PhosphoserineBy similarity1
Modified residuei76N6-acetyllysineBy similarity1
Glycosylationi78N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi99N-linked (GlcNAc...) asparagineSequence analysis1
Modified residuei230N6-succinyllysineBy similarity1
Modified residuei379PhosphothreonineBy similarity1

Post-translational modificationi

Phosphorylated.By similarity

Keywords - PTMi

Acetylation, Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PRIDEiP08712

Expressioni

Tissue specificityi

Detected in the acrosome of the caput epididymal spermatazoa, not detected in the cauda epididymal spermatazoa (at protein level).1 Publication

Inductioni

The synthesis of this protein is stimulated when fibroblasts are deprived of glucose.

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

Structurei

3D structure databases

ProteinModelPortaliP08712
SMRiP08712
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi397 – 400Prevents secretion from ER4

Sequence similaritiesi

Belongs to the heat shock protein 90 family.Curated

Phylogenomic databases

HOVERGENiHBG007374

Family and domain databases

Gene3Di1.20.120.790, 1 hit
InterProiView protein in InterPro
IPR037196 HSP90_C
IPR001404 Hsp90_fam
IPR020568 Ribosomal_S5_D2-typ_fold
PANTHERiPTHR11528 PTHR11528, 1 hit
PfamiView protein in Pfam
PF00183 HSP90, 1 hit
SUPFAMiSSF110942 SSF110942, 1 hit
SSF54211 SSF54211, 1 hit
PROSITEiView protein in PROSITE
PS00014 ER_TARGET, 1 hit

Sequencei

Sequence statusi: Fragment.

P08712-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
KKSDYIKLYV RRVFITDDFH DMMPKYLNFV KGVVDSDDLP LNVSRETLQQ
60 70 80 90 100
HKLLKVIRKK LVRKTLDMIK KIADEKYNDT FWKEFGTNIK LGVIEDHSNR
110 120 130 140 150
TRLAKLLRFQ SSHHSTDITS LDQYVERMKE KQDKIYFMAG SSRKEAESSP
160 170 180 190 200
FVERLLKKGY EVIYLTEPVD EYCIQALPEF DGKRFQNVAK EGVKFDESEK
210 220 230 240 250
TKENREATEK EFEPLLNWMK DKALKDKIEK AVVSQRLTES PCALVASQYG
260 270 280 290 300
WSGNMERIMK AQAYQTGKDI STNYYASQKK TFEINPRHPL IRDMLRRVKE
310 320 330 340 350
DEDDKTVLDL AVVLFETATL RSGYLLPDTK AYADRIERML RLSLNIDPEA
360 370 380 390 400
QVEEEPEEEP EDTTEDTEQD EEEEVDAGTE EEEEEEQETA KESTAEKDEL
Length:400
Mass (Da):46,794
Last modified:January 1, 1988 - v1
Checksum:i3419AD98410EEB80
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Non-terminal residuei11

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X04850 mRNA Translation: CAA28541.1
PIRiA26258

Similar proteinsi

Entry informationi

Entry nameiENPL_MESAU
AccessioniPrimary (citable) accession number: P08712
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 1, 1988
Last modified: March 28, 2018
This is version 113 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health