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Protein

Endoplasmin

Gene

HSP90B1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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 (By similarity). Functions in endoplasmic reticulum associated degradation (ERAD). Has ATPase activity.By similarity1 Publication

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

  • ATP binding Source: UniProtKB-KW
  • calcium ion binding Source: UniProtKB
  • low-density lipoprotein particle receptor binding Source: MGI
  • protein phosphatase binding Source: MGI
  • RNA binding Source: UniProtKB
  • virion binding Source: UniProtKB

GO - Biological processi

  • actin rod assembly Source: MGI
  • ATF6-mediated unfolded protein response Source: Reactome
  • cellular response to ATP Source: MGI
  • ER-associated ubiquitin-dependent protein catabolic process Source: UniProtKB
  • negative regulation of apoptotic process Source: UniProtKB
  • protein folding in endoplasmic reticulum Source: ParkinsonsUK-UCL
  • protein transport Source: UniProtKB
  • receptor-mediated endocytosis Source: Reactome
  • regulation of phosphoprotein phosphatase activity Source: MGI
  • response to endoplasmic reticulum stress Source: ParkinsonsUK-UCL
  • response to hypoxia Source: UniProtKB
  • retrograde protein transport, ER to cytosol Source: ParkinsonsUK-UCL
  • sequestering of calcium ion Source: UniProtKB
  • toll-like receptor signaling pathway Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Ligandi

ATP-binding, Calcium, Nucleotide-binding

Enzyme and pathway databases

BioCyciZFISH:ENSG00000166598-MONOMER.
ReactomeiR-HSA-1679131. Trafficking and processing of endosomal TLR.
R-HSA-3000480. Scavenging by Class A Receptors.
R-HSA-381183. ATF6 (ATF6-alpha) activates chaperone genes.

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
Tumor rejection antigen 1
gp96 homolog
Gene namesi
Name:HSP90B1
Synonyms:GRP94, TRA1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:12028. HSP90B1.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: UniProtKB
  • endocytic vesicle lumen Source: Reactome
  • endoplasmic reticulum Source: UniProtKB
  • endoplasmic reticulum chaperone complex Source: Ensembl
  • endoplasmic reticulum lumen Source: UniProtKB
  • endoplasmic reticulum membrane Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • extracellular matrix Source: UniProtKB
  • extracellular region Source: Reactome
  • focal adhesion Source: UniProtKB
  • melanosome Source: UniProtKB-SubCell
  • membrane Source: UniProtKB
  • midbody Source: UniProtKB
  • nucleus Source: UniProtKB
  • perinuclear region of cytoplasm Source: UniProtKB
  • plasma membrane Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

Pathology & Biotechi

Organism-specific databases

DisGeNETi7184.
OpenTargetsiENSG00000166598.
PharmGKBiPA36705.

Chemistry databases

ChEMBLiCHEMBL1075323.
DrugBankiDB00615. Rifabutin.
GuidetoPHARMACOLOGYi2904.

Polymorphism and mutation databases

DMDMi119360.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 21Combined sources1 PublicationAdd BLAST21
ChainiPRO_000001359822 – 803EndoplasminAdd BLAST782

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi62N-linked (GlcNAc...)1 Publication1
Modified residuei64PhosphoserineCombined sources1
Glycosylationi107N-linked (GlcNAc...)2 Publications1
Disulfide bondi138InterchainBy similarity
Modified residuei172PhosphoserineBy similarity1
Glycosylationi217N-linked (GlcNAc...)2 Publications1
Modified residuei306Phosphoserine; by FAM20CCombined sources1 Publication1
Modified residuei403PhosphoserineBy similarity1
Modified residuei404N6-succinyllysineBy similarity1
Glycosylationi445N-linked (GlcNAc...)2 Publications1
Modified residuei447PhosphoserineCombined sources1
Modified residuei479N6-acetyllysineBy similarity1
Glycosylationi481N-linked (GlcNAc...)Sequence analysis1
Glycosylationi502N-linked (GlcNAc...)Sequence analysis1
Modified residuei633N6-succinyllysineBy similarity1
Modified residuei786PhosphothreonineCombined sources1

Keywords - PTMi

Acetylation, Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

EPDiP14625.
PaxDbiP14625.
PeptideAtlasiP14625.
PRIDEiP14625.
TopDownProteomicsiP14625.

2D gel databases

DOSAC-COBS-2DPAGEP14625.
OGPiP14625.
REPRODUCTION-2DPAGEIPI00027230.

PTM databases

iPTMnetiP14625.
PhosphoSitePlusiP14625.
SwissPalmiP14625.

Miscellaneous databases

PMAP-CutDBP14625.

Expressioni

Gene expression databases

BgeeiENSG00000166598.
CleanExiHS_HSP90B1.
ExpressionAtlasiP14625. baseline and differential.
GenevisibleiP14625. HS.

Organism-specific databases

HPAiCAB005224.
HPA003901.
HPA008424.

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. Interacts with CNPY3. This interaction is disrupted in the presence of ATP (By similarity). Interacts with TLR4 and TLR9, but not with TLR3. Interacts with MZB1 in a calcium-dependent manner (By similarity). Interacts with METTL23.By similarity3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
FANCCQ005974EBI-359129,EBI-81625

GO - Molecular functioni

  • low-density lipoprotein particle receptor binding Source: MGI
  • protein phosphatase binding Source: MGI

Protein-protein interaction databases

BioGridi113036. 150 interactors.
DIPiDIP-36060N.
IntActiP14625. 76 interactors.
MINTiMINT-210408.
STRINGi9606.ENSP00000299767.

Chemistry databases

BindingDBiP14625.

Structurei

Secondary structure

1803
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi80 – 92Combined sources13
Helixi99 – 118Combined sources20
Turni119 – 121Combined sources3
Turni123 – 128Combined sources6
Beta strandi134 – 139Combined sources6
Turni140 – 143Combined sources4
Beta strandi144 – 149Combined sources6
Helixi156 – 160Combined sources5
Helixi175 – 184Combined sources10
Helixi189 – 194Combined sources6
Helixi198 – 204Combined sources7
Beta strandi206 – 214Combined sources9
Beta strandi221 – 225Combined sources5
Beta strandi230 – 234Combined sources5
Beta strandi241 – 251Combined sources11
Helixi256 – 259Combined sources4
Helixi261 – 271Combined sources11
Beta strandi279 – 284Combined sources6
Beta strandi331 – 335Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4NH9X-ray2.77A69-337[»]
ProteinModelPortaliP14625.
SMRiP14625.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi800 – 803Prevents secretion from ER4

Sequence similaritiesi

Belongs to the heat shock protein 90 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG0020. Eukaryota.
COG0326. LUCA.
GeneTreeiENSGT00840000129758.
HOGENOMiHOG000031988.
HOVERGENiHBG007374.
InParanoidiP14625.
KOiK09487.
OMAiRKPADVT.
OrthoDBiEOG091G0270.
PhylomeDBiP14625.
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]
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: Complete.

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

P14625-1 [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 TDENALSGNE 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 EPMEEEEAAK
310 320 330 340 350
EEKEESDDEA AVEEEEEEKK 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 MIKKIADDKY NDTFWKEFGT NIKLGVIEDH
510 520 530 540 550
SNRTRLAKLL RFQSSHHPTD ITSLDQYVER MKEKQDKIYF MAGSSRKEAE
560 570 580 590 600
SSPFVERLLK KGYEVIYLTE PVDEYCIQAL PEFDGKRFQN VAKEGVKFDE
610 620 630 640 650
SEKTKESREA VEKEFEPLLN WMKDKALKDK IEKAVVSQRL TESPCALVAS
660 670 680 690 700
QYGWSGNMER IMKAQAYQTG KDISTNYYAS QKKTFEINPR HPLIRDMLRR
710 720 730 740 750
IKEDEDDKTV LDLAVVLFET ATLRSGYLLP DTKAYGDRIE RMLRLSLNID
760 770 780 790 800
PDAKVEEEPE EEPEETAEDT TEDTEQDEDE EMDVGTDEEE ETAKESTAEK

DEL
Length:803
Mass (Da):92,469
Last modified:April 1, 1990 - v1
Checksum:i9BF6705A7A2ED0D0
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti188T → S in AAK74072 (Ref. 4) Curated1
Sequence conflicti419T → P in AAK74072 (Ref. 4) Curated1
Sequence conflicti803L → F in AAK74072 (Ref. 4) Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X15187 mRNA. Translation: CAA33261.1.
M33716 Genomic DNA. Translation: AAA68201.1.
BC066656 mRNA. Translation: AAH66656.1.
M26596 Genomic DNA. Translation: AAA58621.1.
AY040226 mRNA. Translation: AAK74072.1.
CCDSiCCDS9094.1.
PIRiA35954.
RefSeqiNP_003290.1. NM_003299.2.
UniGeneiHs.192374.

Genome annotation databases

EnsembliENST00000299767; ENSP00000299767; ENSG00000166598.
GeneIDi7184.
KEGGihsa:7184.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X15187 mRNA. Translation: CAA33261.1.
M33716 Genomic DNA. Translation: AAA68201.1.
BC066656 mRNA. Translation: AAH66656.1.
M26596 Genomic DNA. Translation: AAA58621.1.
AY040226 mRNA. Translation: AAK74072.1.
CCDSiCCDS9094.1.
PIRiA35954.
RefSeqiNP_003290.1. NM_003299.2.
UniGeneiHs.192374.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4NH9X-ray2.77A69-337[»]
ProteinModelPortaliP14625.
SMRiP14625.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi113036. 150 interactors.
DIPiDIP-36060N.
IntActiP14625. 76 interactors.
MINTiMINT-210408.
STRINGi9606.ENSP00000299767.

Chemistry databases

BindingDBiP14625.
ChEMBLiCHEMBL1075323.
DrugBankiDB00615. Rifabutin.
GuidetoPHARMACOLOGYi2904.

PTM databases

iPTMnetiP14625.
PhosphoSitePlusiP14625.
SwissPalmiP14625.

Polymorphism and mutation databases

DMDMi119360.

2D gel databases

DOSAC-COBS-2DPAGEP14625.
OGPiP14625.
REPRODUCTION-2DPAGEIPI00027230.

Proteomic databases

EPDiP14625.
PaxDbiP14625.
PeptideAtlasiP14625.
PRIDEiP14625.
TopDownProteomicsiP14625.

Protocols and materials databases

DNASUi7184.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000299767; ENSP00000299767; ENSG00000166598.
GeneIDi7184.
KEGGihsa:7184.

Organism-specific databases

CTDi7184.
DisGeNETi7184.
GeneCardsiHSP90B1.
H-InvDBHIX0056796.
HGNCiHGNC:12028. HSP90B1.
HPAiCAB005224.
HPA003901.
HPA008424.
MIMi191175. gene.
neXtProtiNX_P14625.
OpenTargetsiENSG00000166598.
PharmGKBiPA36705.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0020. Eukaryota.
COG0326. LUCA.
GeneTreeiENSGT00840000129758.
HOGENOMiHOG000031988.
HOVERGENiHBG007374.
InParanoidiP14625.
KOiK09487.
OMAiRKPADVT.
OrthoDBiEOG091G0270.
PhylomeDBiP14625.
TreeFamiTF105969.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000166598-MONOMER.
ReactomeiR-HSA-1679131. Trafficking and processing of endosomal TLR.
R-HSA-3000480. Scavenging by Class A Receptors.
R-HSA-381183. ATF6 (ATF6-alpha) activates chaperone genes.

Miscellaneous databases

ChiTaRSiHSP90B1. human.
GeneWikiiHSP90B1.
GenomeRNAii7184.
PMAP-CutDBP14625.
PROiP14625.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000166598.
CleanExiHS_HSP90B1.
ExpressionAtlasiP14625. baseline and differential.
GenevisibleiP14625. HS.

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_HUMAN
AccessioniPrimary (citable) accession number: P14625
Secondary accession number(s): Q96A97
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: November 30, 2016
This is version 200 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.