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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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei107 – 1071ATPBy similarity
Binding sitei149 – 1491ATPBy similarity
Binding sitei162 – 1621ATPBy similarity
Binding sitei168 – 1681ATPBy similarity
Binding sitei199 – 1991ATP; via amide nitrogenBy similarity
Binding sitei448 – 4481ATPBy similarity

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

ReactomeiR-HSA-1679131. Trafficking and processing of endosomal TLR.
R-HSA-3000480. Scavenging by Class A Receptors.
R-HSA-381183. 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

PharmGKBiPA36705.

Chemistry

ChEMBLiCHEMBL1075323.
DrugBankiDB00615. Rifabutin.

Polymorphism and mutation databases

DMDMi119360.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121Combined sources1 PublicationAdd
BLAST
Chaini22 – 803782EndoplasminPRO_0000013598Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi62 – 621N-linked (GlcNAc...)1 Publication
Modified residuei64 – 641PhosphoserineCombined sources
Glycosylationi107 – 1071N-linked (GlcNAc...)2 Publications
Disulfide bondi138 – 138InterchainBy similarity
Modified residuei172 – 1721PhosphoserineBy similarity
Glycosylationi217 – 2171N-linked (GlcNAc...)2 Publications
Modified residuei306 – 3061Phosphoserine; by FAM20CCombined sources1 Publication
Modified residuei403 – 4031PhosphoserineBy similarity
Modified residuei404 – 4041N6-succinyllysineBy similarity
Glycosylationi445 – 4451N-linked (GlcNAc...)2 Publications
Modified residuei447 – 4471PhosphoserineCombined sources
Modified residuei479 – 4791N6-acetyllysineBy similarity
Glycosylationi481 – 4811N-linked (GlcNAc...)Sequence analysis
Glycosylationi502 – 5021N-linked (GlcNAc...)Sequence analysis
Modified residuei633 – 6331N6-succinyllysineBy similarity
Modified residuei786 – 7861PhosphothreonineCombined sources

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.
PhosphoSiteiP14625.
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. 149 interactions.
DIPiDIP-36060N.
IntActiP14625. 76 interactions.
MINTiMINT-210408.
STRINGi9606.ENSP00000299767.

Chemistry

BindingDBiP14625.

Structurei

Secondary structure

1
803
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi80 – 9213Combined sources
Helixi99 – 11820Combined sources
Turni119 – 1213Combined sources
Turni123 – 1286Combined sources
Beta strandi134 – 1396Combined sources
Turni140 – 1434Combined sources
Beta strandi144 – 1496Combined sources
Helixi156 – 1605Combined sources
Helixi175 – 18410Combined sources
Helixi189 – 1946Combined sources
Helixi198 – 2047Combined sources
Beta strandi206 – 2149Combined sources
Beta strandi221 – 2255Combined sources
Beta strandi230 – 2345Combined sources
Beta strandi241 – 25111Combined sources
Helixi256 – 2594Combined sources
Helixi261 – 27111Combined sources
Beta strandi279 – 2846Combined sources
Beta strandi331 – 3355Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4NH9X-ray2.77A69-337[»]
ProteinModelPortaliP14625.
SMRiP14625. Positions 72-755.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi800 – 8034Prevents secretion from ER

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti188 – 1881T → S in AAK74072 (Ref. 4) Curated
Sequence conflicti419 – 4191T → P in AAK74072 (Ref. 4) Curated
Sequence conflicti803 – 8031L → F in AAK74072 (Ref. 4) Curated

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
EntryMethodResolution (Å)ChainPositionsPDBsum
4NH9X-ray2.77A69-337[»]
ProteinModelPortaliP14625.
SMRiP14625. Positions 72-755.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi113036. 149 interactions.
DIPiDIP-36060N.
IntActiP14625. 76 interactions.
MINTiMINT-210408.
STRINGi9606.ENSP00000299767.

Chemistry

BindingDBiP14625.
ChEMBLiCHEMBL1075323.
DrugBankiDB00615. Rifabutin.

PTM databases

iPTMnetiP14625.
PhosphoSiteiP14625.
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.
GeneCardsiHSP90B1.
H-InvDBHIX0056796.
HGNCiHGNC:12028. HSP90B1.
HPAiCAB005224.
HPA003901.
HPA008424.
MIMi191175. gene.
neXtProtiNX_P14625.
PharmGKBiPA36705.
GenAtlasiSearch...

Phylogenomic databases

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

Enzyme and pathway databases

ReactomeiR-HSA-1679131. Trafficking and processing of endosomal TLR.
R-HSA-3000480. Scavenging by Class A Receptors.
R-HSA-381183. 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: September 7, 2016
This is version 197 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.