Endoplasmin precursor - Homo sapiens (Human)

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Reviewed, UniProtKB/Swiss-Prot P14625 (ENPL_HUMAN)

Last modified February 9, 2010. Version 124. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Endoplasmin
Alternative name(s):
    Heat shock protein 90 kDa beta member 1
    94 kDa glucose-regulated protein
      Short name=GRP-94
    gp96 homolog
    Tumor rejection antigen 1

Gene names

Name:	HSP90B1
Synonyms:	GRP94, TRA1

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length	803 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	Molecular chaperone that functions in the processing and transport of secreted proteins. Functions in endoplasmic reticulum associated degradation (ERAD). Has ATPase activity. Ref.13
Subunit structure	Homodimer; disulfide-linked. Component of an EIF2 complex at least composed of CUGBP1, CALR, CALR3, EIF2S1, EIF2S2, HSP90B1 and HSPA5 By similarity. Part a large chaperone multiprotein complex comprising CABP1, DNAJB11, HSP90B1, HSPA5, HYOU, PDIA2, PDIA4, 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. Ref.13
Subcellular location	Endoplasmic reticulum lumen. Melanosome. Note: Identified by mass spectrometry in melanosome fractions from stage I to stage IV. Ref.7 Ref.9
Sequence similarities	Belongs to the heat shock protein 90 family.

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Ontologies

Keywords
Cellular component	Endoplasmic reticulum
Domain	Signal
Ligand	ATP-binding Calcium Nucleotide-binding
Molecular function	Chaperone
PTM	Disulfide bond Glycoprotein Phosphoprotein
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	ER-associated protein catabolic process Ref.13 Inferred from mutant phenotype. Source: UniProtKB anti-apoptosis Inferred from mutant phenotype. Source: UniProtKB protein folding Inferred from electronic annotation. Source: InterPro protein transport Non-traceable author statement. Source: UniProtKB response to hypoxia Inferred from direct assay. Source: UniProtKB sequestering of calcium ion Non-traceable author statement. Source: UniProtKB
Cellular component	cytosol Inferred from direct assay. Source: UniProtKB endoplasmic reticulum lumen Inferred from direct assay. Source: UniProtKB endoplasmic reticulum membrane Inferred from direct assay. Source: UniProtKB melanosome Inferred from electronic annotation. Source: UniProtKB-SubCell microsome Inferred from direct assay. Source: UniProtKB perinuclear region of cytoplasm Inferred from direct assay. Source: UniProtKB
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW RNA binding Inferred from direct assay. Source: UniProtKB calcium ion binding Traceable author statement. Source: UniProtKB low-density lipoprotein receptor binding Inferred from direct assay. Source: MGI unfolded protein binding Inferred from electronic annotation. Source: InterPro virion binding Inferred from physical interaction. Source: UniProtKB
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct	Notes
EIF2AK3	Q9NZJ5	1	EBI-359129,EBI-766076

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 21

Ref.5

Chain

22 – 803

782

Endoplasmin

PRO_0000013598

Regions

Motif

800 – 803

Prevents secretion from ER

Sites

Binding site

107

ATP By similarity

Binding site

149

ATP By similarity

Binding site

162

ATP By similarity

Binding site

199

ATP; via amide nitrogen By similarity

Amino acid modifications

Modified residue

306

Phosphoserine By similarity

Modified residue

677

Phosphotyrosine Ref.11

Glycosylation

N-linked (GlcNAc...) Ref.14

Glycosylation

107

N-linked (GlcNAc...) Ref.14 Ref.10

Glycosylation

217

N-linked (GlcNAc...) Ref.14 Ref.8

Glycosylation

445

N-linked (GlcNAc...) Ref.14 Ref.8

Glycosylation

481

N-linked (GlcNAc...) Potential

Glycosylation

502

N-linked (GlcNAc...) Potential

Disulfide bond

138

Interchain By similarity

Experimental info

Sequence conflict

188

T → S in AAK74072. Ref.4

Sequence conflict

419

T → P in AAK74072. Ref.4

Sequence conflict

803

L → F in AAK74072. Ref.4

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Sequences

Sequence

Length

Mass (Da)

Tools

P14625-1 [UniParc].

Last modified April 1, 1990. Version 1.
Checksum: 9BF6705A7A2ED0D0
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FASTA

803

92,469

        10         20         30         40         50         60 
MRALWVLGLC CVLLTFGSVR ADDEVDVDGT VEEDLGKSRE GSRTDDEVVQ REEEAIQLDG 

        70         80         90        100        110        120 
LNASQIRELR EKSEKFAFQA EVNRMMKLII NSLYKNKEIF LRELISNASD ALDKIRLISL 

       130        140        150        160        170        180 
TDENALSGNE ELTVKIKCDK EKNLLHVTDT GVGMTREELV KNLGTIAKSG TSEFLNKMTE 

       190        200        210        220        230        240 
AQEDGQSTSE LIGQFGVGFY SAFLVADKVI VTSKHNNDTQ HIWESDSNEF SVIADPRGNT 

       250        260        270        280        290        300 
LGRGTTITLV LKEEASDYLE LDTIKNLVKK YSQFINFPIY VWSSKTETVE EPMEEEEAAK 

       310        320        330        340        350        360 
EEKEESDDEA AVEEEEEEKK PKTKKVEKTV WDWELMNDIK PIWQRPSKEV EEDEYKAFYK 

       370        380        390        400        410        420 
SFSKESDDPM AYIHFTAEGE VTFKSILFVP TSAPRGLFDE YGSKKSDYIK LYVRRVFITD 

       430        440        450        460        470        480 
DFHDMMPKYL NFVKGVVDSD DLPLNVSRET LQQHKLLKVI RKKLVRKTLD MIKKIADDKY 

       490        500        510        520        530        540 
NDTFWKEFGT NIKLGVIEDH SNRTRLAKLL RFQSSHHPTD ITSLDQYVER MKEKQDKIYF 

       550        560        570        580        590        600 
MAGSSRKEAE SSPFVERLLK KGYEVIYLTE PVDEYCIQAL PEFDGKRFQN VAKEGVKFDE 

       610        620        630        640        650        660 
SEKTKESREA VEKEFEPLLN WMKDKALKDK IEKAVVSQRL TESPCALVAS QYGWSGNMER 

       670        680        690        700        710        720 
IMKAQAYQTG KDISTNYYAS QKKTFEINPR HPLIRDMLRR IKEDEDDKTV LDLAVVLFET 

       730        740        750        760        770        780 
ATLRSGYLLP DTKAYGDRIE RMLRLSLNID PDAKVEEEPE EEPEETAEDT TEDTEQDEDE 

       790        800 
EMDVGTDEEE ETAKESTAEK DEL

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Human homologue of murine tumor rejection antigen gp96: 5'-regulatory and coding regions and relationship to stress-induced proteins." Maki R.G., Old L.J., Srivastava P.K. Proc. Natl. Acad. Sci. U.S.A. 87:5658-5662(1990) [PubMed: 2377606] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-16. Tissue: Blood.
[2]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Skin.
[3]	"Glucose-regulated protein (GRP94 and GRP78) genes share common regulatory domains and are coordinately regulated by common trans-acting factors." Chang S.C., Erwin A.E., Lee A.S. Mol. Cell. Biol. 9:2153-2162(1989) [PubMed: 2546060] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-16. Tissue: Liver.
[4]	"The association of heat shock protein gp96 with HBV-derived peptides in vitro." Meng S., Tien P. Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 22-803. Tissue: Liver.
[5]	"Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides." Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J. Nat. Biotechnol. 21:566-569(2003) [PubMed: 12665801] [Abstract] Cited for: PROTEIN SEQUENCE OF 22-39. Tissue: Platelet.
[6]	"A subset of chaperones and folding enzymes form multiprotein complexes in endoplasmic reticulum to bind nascent proteins." Meunier L., Usherwood Y.-K., Chung K.T., Hendershot L.M. Mol. Biol. Cell 13:4456-4469(2002) [PubMed: 12475965] [Abstract] Cited for: COMPONENT OF A CHAPERONE COMPLEX.
[7]	"Proteomic analysis of early melanosomes: identification of novel melanosomal proteins." Basrur V., Yang F., Kushimoto T., Higashimoto Y., Yasumoto K., Valencia J., Muller J., Vieira W.D., Watabe H., Shabanowitz J., Hearing V.J., Hunt D.F., Appella E. J. Proteome Res. 2:69-79(2003) [PubMed: 12643545] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[8]	"Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry." Zhang H., Li X.-J., Martin D.B., Aebersold R. Nat. Biotechnol. 21:660-666(2003) [PubMed: 12754519] [Abstract] Cited for: GLYCOSYLATION AT ASN-217 AND ASN-445.
[9]	"Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes." Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H., Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R., Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E., Hunt D.F. J. Proteome Res. 5:3135-3144(2006) [PubMed: 17081065] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[10]	"Elucidation of N-glycosylation sites on human platelet proteins: a glycoproteomic approach." Lewandrowski U., Moebius J., Walter U., Sickmann A. Mol. Cell. Proteomics 5:226-233(2006) [PubMed: 16263699] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-107, MASS SPECTROMETRY. Tissue: Platelet.
[11]	"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer." Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M. Comb M.J. Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-677, MASS SPECTROMETRY.
[12]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[13]	"OS-9 and GRP94 deliver mutant alpha1-antitrypsin to the Hrd1-SEL1L ubiquitin ligase complex for ERAD." Christianson J.C., Shaler T.A., Tyler R.E., Kopito R.R. Nat. Cell Biol. 10:272-282(2008) [PubMed: 18264092] [Abstract] Cited for: FUNCTION, INTERACTION WITH OS9.
[14]	"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry." Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H. J. Proteome Res. 8:651-661(2009) [PubMed: 19159218] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-62; ASN-107; ASN-217 AND ASN-445, MASS SPECTROMETRY. Tissue: Liver.

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Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
IPI	IPI00027230.
PIR	A35954.
RefSeq	NP_003290.1.
UniGene	Hs.192374
3D structure databases
SMR	P14625. Positions 69-337, 73-594, 85-749, 340-755.
ModBase	Search...
Protein-protein interaction databases
IntAct	P14625. 5 interactions.
STRING	P14625.
PTM databases
PhosphoSite	P14625.
2-D gel databases
Aarhus/Ghent-2DPAGE	8602. IEF.
DOSAC-COBS-2DPAGE	P14625.
OGP	P14625.
REPRODUCTION-2DPAGE	IPI00027230.
Siena-2DPAGE	P14625.
Proteomic databases
PeptideAtlas	P14625.
PRIDE	P14625.
Genome annotation databases
Ensembl	ENST00000299767; ENSP00000299767; ENSG00000166598; Homo sapiens. [Genome view]
GeneID	7184.
KEGG	hsa:7184.
UCSC	uc001tkb.1. human.
Organism-specific databases
CTD	7184.
GeneCards	GC12P102848.
H-InvDB	HIX0010934. HIX0056796.
HGNC	HGNC:12028. HSP90B1.
HPA	CAB005224. HPA003901. HPA008424.
MIM	191175. gene.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG13016.
HOGENOM	HBG631012.
HOVERGEN	P14625.
InParanoid	P14625.
OMA	TKENREA.
PhylomeDB	P14625.
Enzyme and pathway databases
Pathway_Interaction_DB	il6_7pathway. IL6-mediated signaling events.
Gene expression databases
ArrayExpress	P14625.
Bgee	P14625.
CleanEx	HS_HSP90B1.
Genevestigator	P14625.
GermOnline	ENSG00000166598. Homo sapiens.
Family and domain databases
InterPro	IPR003594. ATPase-like_ATP-bd. IPR001404. Chaperone_htpG. IPR015566. Endoplasmin. IPR019805. Heat_shock_protein_90_CS. IPR020576. Hsp90_C. IPR020575. Hsp90_N. IPR020568. Ribosomal_S5_D2-typ_fold. [Graphical view]
Gene3D	G3DSA:3.30.565.10. ATP_bd_ATPase. 1 hit.
PANTHER	PTHR11528:SF21. Endoplasmin. 1 hit. PTHR11528. Hsp90. 1 hit.
Pfam	PF02518. HATPase_c. 1 hit. PF00183. HSP90. 1 hit. [Graphical view]
PIRSF	PIRSF002583. Hsp90. 1 hit.
PRINTS	PR00775. HEATSHOCK90.
SMART	SM00387. HATPase_c. 1 hit. [Graphical view]
PROSITE	PS00014. ER_TARGET. 1 hit. PS00298. HSP90. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
DrugBank	DB00615. Rifabutin.
NextBio	28164.
PMAP-CutDB	P14625.
SOURCE	Search...

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Entry information

Entry name

ENPL_HUMAN

Accession

Primary (citable) accession number: P14625
Secondary accession number(s): Q96A97

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1990
Last sequence update:	April 1, 1990
Last modified:	February 9, 2010
This is version 124 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any 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.

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Relevant documents

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Human chromosome 12: entries, gene names and cross-references to MIM

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

2-D gel databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents