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Protein

Endoplasmin

Gene

HSP90B1

Organism
Sus scrofa (Pig)
Status
Reviewed-Annotation score: Annotation score: 4 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 sitei162ATPBy similarity1
Binding sitei168ATPBy similarity1
Binding sitei199ATP; via amide nitrogenBy similarity1
Binding sitei448ATPBy 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
98 kDa protein kinase
Short name:
PPK 98
Short name:
ppk98
Heat shock protein 90 kDa beta member 1
gp96 homolog
Gene namesi
Name:HSP90B1
Synonyms:GRP94, TRA1
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
Proteomesi
  • UP000008227 Componenti: Unplaced

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

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL3425397.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 21Sequence analysisAdd BLAST21
ChainiPRO_000001360022 – 804EndoplasminAdd BLAST783

Amino acid modifications

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

Post-translational modificationi

Phosphorylated.By similarity

Keywords - PTMi

Acetylation, Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PeptideAtlasiQ29092.
PRIDEiQ29092.

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

ELMiQ29092.

Chemistry databases

BindingDBiQ29092.

Structurei

3D structure databases

ProteinModelPortaliQ29092.
SMRiQ29092.
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

HOGENOMiHOG000031988.
HOVERGENiHBG007374.
InParanoidiQ29092.
KOiK09487.

Family and domain databases

CDDicd00075. HATPase_c. 1 hit.
Gene3Di3.30.565.10. 1 hit.
HAMAPiMF_00505. HSP90. 1 hit.
InterProiView protein in InterPro
IPR003594. HATPase_C.
IPR036890. HATPase_C_sf.
IPR019805. Heat_shock_protein_90_CS.
IPR037196. HSP90_C.
IPR001404. Hsp90_fam.
IPR020575. Hsp90_N.
IPR020568. Ribosomal_S5_D2-typ_fold.
PANTHERiPTHR11528. PTHR11528. 1 hit.
PfamiView protein in Pfam
PF02518. HATPase_c. 1 hit.
PF00183. HSP90. 1 hit.
PIRSFiPIRSF002583. Hsp90. 1 hit.
PRINTSiPR00775. HEATSHOCK90.
SMARTiView protein in SMART
SM00387. HATPase_c. 1 hit.
SUPFAMiSSF110942. SSF110942. 1 hit.
SSF54211. SSF54211. 1 hit.
SSF55874. SSF55874. 1 hit.
PROSITEiView protein in PROSITE
PS00014. ER_TARGET. 1 hit.
PS00298. HSP90. 1 hit.

Sequencei

Sequence statusi: Complete.

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

Q29092-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRALWVLGLC CVLLTFGSVR AEDEVDVDGT 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 TSEFLNKMAE AQEDGQSTSE LIGQFGVGFY
210 220 230 240 250
SAFLVADKVI VTSKHNNDTQ HIWESDSNEF SVIADPRGNT LGRGTTITLV
260 270 280 290 300
LKEEASDYLE LDTIKNLVKK YSQFINFPIY VWSSKTETVE EPMEEEEAAK
310 320 330 340 350
EEKEESDDEA AVEEEEEEKK PKTKKVEKTV WDWELMNDIK PIWQRPSKEV
360 370 380 390 400
EDDEYKAFYK 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 ITSLDQYVER MKEKQDKIYF MAGSSRKEAE
560 570 580 590 600
SSPFVERLLK KGYEVIYLTE PVDEYCIQAL PEFDGKRFQN VAKEGVKFDE
610 620 630 640 650
SEKSKENREA 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 TEDTEQDDDE EMDAGADEEE QETSETSTAE

KDEL
Length:804
Mass (Da):92,471
Last modified:December 13, 2001 - v3
Checksum:iFF823A77406F0190
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti48V → I in CAA70347 (Ref. 2) Curated1
Sequence conflicti179A → T in CAA70347 (Ref. 2) Curated1
Sequence conflicti332 – 334DWE → ELG in CAA62352 (PubMed:9407008).Curated3
Sequence conflicti795E → EFVFQ in CAA62352 (PubMed:9407008).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X76301 mRNA. Translation: CAA53948.1.
Y09136 mRNA. Translation: CAA70347.1.
X90848 Genomic DNA. Translation: CAA62352.1.
PIRiPL0137.
S51358.
RefSeqiNP_999268.1. NM_214103.1.
UniGeneiSsc.94181.
Ssc.9889.

Genome annotation databases

GeneIDi397191.
KEGGissc:397191.

Similar proteinsi

Entry informationi

Entry nameiENPL_PIG
AccessioniPrimary (citable) accession number: Q29092
Secondary accession number(s): O19070, Q29091
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: December 13, 2001
Last modified: October 25, 2017
This is version 137 of the entry and version 3 of the sequence. See 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