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P08712

- ENPL_MESAU

UniProt

P08712 - ENPL_MESAU

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Protein

Endoplasmin

Gene
HSP90B1, GRP94
Organism
Mesocricetus auratus (Golden hamster)
Status
Reviewed - Annotation score: 4 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. Functions in endoplasmic reticulum associated degradation (ERAD). Has ATPase activity By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei45 – 451ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW

GO - Biological processi

  1. ER-associated ubiquitin-dependent protein catabolic process Source: UniProtKB
  2. protein folding Source: InterPro
  3. response to stress Source: InterPro
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
OrganismiMesocricetus auratus (Golden hamster)
Taxonomic identifieri10036 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaCricetidaeCricetinaeMesocricetus

Subcellular locationi

GO - Cellular componenti

  1. endoplasmic reticulum lumen Source: UniProtKB-SubCell
  2. melanosome Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini‹1 – 400›400EndoplasminPRO_0000062926Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N6-succinyllysine By similarity
Glycosylationi42 – 421N-linked (GlcNAc...) Reviewed prediction
Modified residuei76 – 761N6-acetyllysine By similarity
Glycosylationi78 – 781N-linked (GlcNAc...) Reviewed prediction
Glycosylationi99 – 991N-linked (GlcNAc...) Reviewed prediction
Modified residuei230 – 2301N6-succinyllysine By similarity

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.

Structurei

3D structure databases

ProteinModelPortaliP08712.
SMRiP08712. Positions 5-346.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi397 – 4004Prevents secretion from ER

Sequence similaritiesi

Phylogenomic databases

HOVERGENiHBG007374.

Family and domain databases

InterProiIPR001404. Hsp90_fam.
IPR020568. Ribosomal_S5_D2-typ_fold.
[Graphical view]
PANTHERiPTHR11528. PTHR11528. 1 hit.
PfamiPF00183. HSP90. 1 hit.
[Graphical view]
SUPFAMiSSF54211. SSF54211. 1 hit.
PROSITEiPS00014. ER_TARGET. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Fragment.

P08712-1 [UniParc]FASTAAdd to Basket

« Hide

KKSDYIKLYV RRVFITDDFH DMMPKYLNFV KGVVDSDDLP LNVSRETLQQ    50
HKLLKVIRKK LVRKTLDMIK KIADEKYNDT FWKEFGTNIK LGVIEDHSNR 100
TRLAKLLRFQ SSHHSTDITS LDQYVERMKE KQDKIYFMAG SSRKEAESSP 150
FVERLLKKGY EVIYLTEPVD EYCIQALPEF DGKRFQNVAK EGVKFDESEK 200
TKENREATEK EFEPLLNWMK DKALKDKIEK AVVSQRLTES PCALVASQYG 250
WSGNMERIMK AQAYQTGKDI STNYYASQKK TFEINPRHPL IRDMLRRVKE 300
DEDDKTVLDL AVVLFETATL RSGYLLPDTK AYADRIERML RLSLNIDPEA 350
QVEEEPEEEP EDTTEDTEQD EEEEVDAGTE EEEEEEQETA KESTAEKDEL 400
Length:400
Mass (Da):46,794
Last modified:January 1, 1988 - v1
Checksum:i3419AD98410EEB80
GO

Non-terminal residue

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 11

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X04850 mRNA. Translation: CAA28541.1.
PIRiA26258.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X04850 mRNA. Translation: CAA28541.1 .
PIRi A26258.

3D structure databases

ProteinModelPortali P08712.
SMRi P08712. Positions 5-346.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PRIDEi P08712.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

HOVERGENi HBG007374.

Family and domain databases

InterProi IPR001404. Hsp90_fam.
IPR020568. Ribosomal_S5_D2-typ_fold.
[Graphical view ]
PANTHERi PTHR11528. PTHR11528. 1 hit.
Pfami PF00183. HSP90. 1 hit.
[Graphical view ]
SUPFAMi SSF54211. SSF54211. 1 hit.
PROSITEi PS00014. ER_TARGET. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "The glucose-regulated protein grp94 is related to heat shock protein hsp90."
    Sorger P.K., Pelham H.R.B.
    J. Mol. Biol. 194:341-344(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Glucose-regulated protein precursor (GRP78) and tumor rejection antigen (GP96) are unique to hamster caput epididymal spermatozoa."
    Kameshwari D.B., Bhande S., Sundaram C.S., Kota V., Siva A.B., Shivaji S.
    Asian J. Androl. 12:344-355(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, TISSUE SPECIFICITY.

Entry informationi

Entry nameiENPL_MESAU
AccessioniPrimary (citable) accession number: P08712
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 1, 1988
Last modified: June 11, 2014
This is version 100 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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