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Protein

Endoplasmin

Gene

HSP90B1

Organism
Oryctolagus cuniculus (Rabbit)
Status
Reviewed-Annotation score: Annotation score: 3 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 sitei28ATPBy similarity1
Binding sitei70ATPBy similarity1
Binding sitei83ATPBy similarity1
Binding sitei89ATPBy similarity1
Binding sitei120ATP; via amide nitrogenBy similarity1
Binding sitei368ATPBy similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Ligandi

ATP-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
OrganismiOryctolagus cuniculus (Rabbit)
Taxonomic identifieri9986 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
Proteomesi
  • UP000001811 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_0000062927‹1 – 716EndoplasminAdd BLAST›716

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi28N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi59InterchainBy similarity
Modified residuei93PhosphoserineBy similarity1
Glycosylationi138N-linked (GlcNAc...)Sequence analysis1
Modified residuei323PhosphoserineBy similarity1
Modified residuei324N6-succinyllysineBy similarity1
Glycosylationi365N-linked (GlcNAc...)Sequence analysis1
Modified residuei367PhosphoserineBy similarity1
Modified residuei399N6-acetyllysineBy similarity1
Glycosylationi421N-linked (GlcNAc...)Sequence analysis1
Modified residuei552N6-succinyllysineBy similarity1
Modified residuei696PhosphothreonineBy similarity1

Post-translational modificationi

Phosphorylated.By similarity

Keywords - PTMi

Acetylation, Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PRIDEiO18750.

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

Structurei

3D structure databases

ProteinModelPortaliO18750.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi713 – 716Prevents secretion from ERSequence analysis4

Sequence similaritiesi

Belongs to the heat shock protein 90 family.Curated

Phylogenomic databases

HOVERGENiHBG007374.
InParanoidiO18750.

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

Sequencei

Sequence statusi: Fragment.

O18750-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
AEVNRMMKLI INSLYKNKEI FLRELISNAS DALDKIRLIS LTDEQALSGN
60 70 80 90 100
EELTVKIKCD KEKNLLHVTD TGVGMTREEL VKNLGTIAKS GTSEFLNKMT
110 120 130 140 150
EAQEDGQSTS ELIGQFGVGF YSAFLVADKV IVTSKHNNDT QHIWESDSNE
160 170 180 190 200
FSVIADPRGN TLGRGTTITL VLKEEASDYL ELDTIKNLVK KYSQFINFPI
210 220 230 240 250
YVWSSKTETV EEPAGEEEAA KEEKEEAVDE AAVEEEEEEK KPKTKKVEKQ
260 270 280 290 300
VWDWELMNDI KPIWQRPSKE VEEDEYKAFY KSFSKESDDP MAYIHFTAEE
310 320 330 340 350
STFKSILFVP TSAPRGLFDE YGSKKSDYIK LYVRRVFITD DFHDMMPKYL
360 370 380 390 400
NFVKGVVDSD DLPLNVSRET LQQHKLLKVI RKKLVRKTLD MIKKIADEKY
410 420 430 440 450
NDDTFWKGTN IKLGVIEDHS NRTRLAKLLR FQSSHHPTDI TSLDQYVERM
460 470 480 490 500
KEKQDKIYFM AGASRKEAES SPFVERLLKK GYEVIYLTEP VDEYCIQALP
510 520 530 540 550
EFDGKRFQNV AKEGVKFDES EKTKESREAT EKEFEPLLNW MKDKALKDKI
560 570 580 590 600
EKAVVSQRLT ESPCALVASQ YGWSANMERI MKAQAYQTGK DSTKYYASQK
610 620 630 640 650
TFEINPRHPL IRDMLRIKED DKTVMDLAVV LFETAILRSG YLLPDTKAYG
660 670 680 690 700
DRIERIVRLS LNIDPDAKVE EEPEEEPEDT TEDTEQDEEE EMDAGTDEQE
710
QEQEPEKKST AEKDEL
Length:716
Mass (Da):82,608
Last modified:January 1, 1998 - v1
Checksum:i7098C6442F0EC84B
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Non-terminal residuei11

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF001631 mRNA. Translation: AAC48853.1.
UniGeneiOcu.4906.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF001631 mRNA. Translation: AAC48853.1.
UniGeneiOcu.4906.

3D structure databases

ProteinModelPortaliO18750.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiO18750.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG007374.
InParanoidiO18750.

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

Entry informationi

Entry nameiENPL_RABIT
AccessioniPrimary (citable) accession number: O18750
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: January 1, 1998
Last modified: October 5, 2016
This is version 117 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.