Tag Content
SG ID
SG00000419 
UniProt Accession
Theoretical PI
5.01  
Molecular Weight
72333 Da  
Genbank Nucleotide ID
Genbank Protein ID
Gene Name
HSPA5 
Gene Synonyms/Alias
GRP78 
Protein Name
78 kDa glucose-regulated protein 
Protein Synonyms/Alias
GRP-78 Endoplasmic reticulum lumenal Ca(2+)-binding protein grp78; Heat shock 70 kDa protein 5; Immunoglobulin heavy chain-binding protein;BiPFlags: Precursor 
Organism
Homo sapiens (Human) 
NCBI Taxonomy ID
9606 
Chromosome Location
chr:9;127997132-128003622;-1
View in Ensembl genome browser  
Function in Stage
Function in Cell Type
Description
These results indicate that in addition to being expressed in human testis spermatogenic cells, both Hsp60 and Grp78 proteins persist in ejaculated spermatozoa. These findings are in agreement with the involvement of Hsp60 and Grp78 during spermatogenesis and in sperm functions such as fertilization. 
The information of related literatures
1. C. Lachance, M. Fortier, V. Thimon, R. Sullivan, J. L. Bailey and P. Leclerc (2010) Localization of Hsp60 and Grp78 in the human testis, epididymis and mature spermatozoa. Int J Androl 33(1): 33-44. 

Abstract
Molecular chaperones of the heat shock proteins (HSP) family are important in numerous cellular processes. In this study, the expression of Hsp60 and Grp78 proteins was investigated in the male reproductive tract. The cellular distribution of Hsp60 and Grp78 proteins was analysed in the human testis and epididymis by immunohistochemical approaches. DNA microarray technology was used to analyse HSP60 and GRP78 gene expression along human epididymis. The cellular localization of these chaperone proteins in ejaculated spermatozoa was investigated by indirect immunofluorescence and by Western blot following sperm sub-cellular fractionation. In the human testis, Hsp60 was detected in spermatogonia, whereas a strong Grp78 staining was observed in spermatocytes and round spermatids. Grp78 protein was also observed in the epididymal epithelium, whereas no Hsp60 staining was observed in this organ by immunohistochemistry. The presence of both Hsp60 and Grp78 RNA in human epididymis was confirmed by microarrays. In ejaculated spermatozoa, Hsp60 was localized in the mid-piece, whereas Grp78 was detected in the neck region. These results indicate that in addition to being expressed in human testis spermatogenic cells, both Hsp60 and Grp78 proteins persist in ejaculated spermatozoa. These findings are in agreement with the involvement of Hsp60 and Grp78 during spermatogenesis and in sperm functions such as fertilization. PMID: [19207617] 

Back to Top
Figures for illustrating the function of this protein/gene
Ref: C. Lachance, M. Fortier, V. Thimon, R. Sullivan, J. L. Bailey and P. Leclerc (2010) Localization of Hsp60 and Grp78 in the human testis, epididymis and mature spermatozoa. Int J Androl 33(1): 33-44. PMID: [19207617]
Ref: C. Lachance, M. Fortier, V. Thimon, R. Sullivan, J. L. Bailey and P. Leclerc (2010) Localization of Hsp60 and Grp78 in the human testis, epididymis and mature spermatozoa. Int J Androl 33(1): 33-44. PMID: [19207617]
Ref: C. Lachance, M. Fortier, V. Thimon, R. Sullivan, J. L. Bailey and P. Leclerc (2010) Localization of Hsp60 and Grp78 in the human testis, epididymis and mature spermatozoa. Int J Androl 33(1): 33-44. PMID: [19207617]
Function
Probably plays a role in facilitating the assembly ofmultimeric protein complexes inside the ER. 
Back to Top
Subcellular Location
Endoplasmic reticulum lumen. Melanosome.Note=Identified by mass spectrometry in melanosome fractions fromstage I to stage IV. 
Tissue Specificity
 
Gene Ontology
GO IDGO termEvidence
GO:0009986 C:cell surface IDA:UniProtKB.
GO:0034663 C:endoplasmic reticulum chaperone complex IDA:UniProtKB.
GO:0005788 C:endoplasmic reticulum lumen TAS:UniProtKB.
GO:0005793 C:endoplasmic reticulum-Golgi intermediate compartment IDA:UniProtKB.
GO:0030176 C:integral to endoplasmic reticulum membrane IDA:UniProtKB.
GO:0042470 C:melanosome IEA:UniProtKB-SubCell.
GO:0030496 C:midbody IDA:UniProtKB.
GO:0005634 C:nucleus IDA:UniProtKB.
GO:0048471 C:perinuclear region of cytoplasm IDA:UniProtKB.
GO:0005524 F:ATP binding NAS:UniProtKB.
GO:0016887 F:ATPase activity ISS:UniProtKB.
GO:0005509 F:calcium ion binding TAS:UniProtKB.
GO:0043027 F:cysteine-type endopeptidase inhibitor activity involved in apoptotic process IDA:UniProtKB.
GO:0043022 F:ribosome binding IEA:Compara.
GO:0006987 P:activation of signaling protein activity involved in unfolded protein response TAS:Reactome.
GO:0006916 P:anti-apoptosis IMP:UniProtKB.
GO:0042149 P:cellular response to glucose starvation IDA:UniProtKB.
GO:0021680 P:cerebellar Purkinje cell layer development IEA:Compara.
GO:0021589 P:cerebellum structural organization IEA:Compara.
GO:0006983 P:ER overload response IEA:Compara.
GO:0030433 P:ER-associated protein catabolic process TAS:BHF-UCL.
GO:0030512 P:negative regulation of transforming growth factor beta receptor signaling pathway IEA:Compara.
GO:0030168 P:platelet activation TAS:Reactome.
GO:0002576 P:platelet degranulation TAS:Reactome.
GO:0031398 P:positive regulation of protein ubiquitination IEA:Compara.
GO:0060904 P:regulation of protein folding in endoplasmic reticulum TAS:BHF-UCL.
Back to Top
Interpro
IPR018181;    Heat_shock_70_CS.
IPR013126;    Hsp_70_fam.
Back to Top
Pfam
PF00012;    HSP70;    1.
Back to Top
SMART
PROSITE
PS00014;    ER_TARGET;    1.
PS00297;    HSP70_1;    1.
PS00329;    HSP70_2;    1.
PS01036;    HSP70_3;    1.
Back to Top
PRINTS
PR00301;    HEATSHOCK70.;   
Back to Top
Created Date
18-Oct-2012 
Record Type
Experiment identified 
Protein sequence Annotation
SIGNAL        1     18
CHAIN        19    654       78 kDa glucose-regulated protein.
                             /FTId=PRO_0000013566.
MOTIF       651    654       Prevents secretion from ER.
MOD_RES     166    166       Phosphothreonine (By similarity).
MOD_RES     268    268       N6-acetyllysine.
MOD_RES     466    466       Phosphotyrosine.
MOD_RES     571    571       Phosphoserine (By similarity).
VARIANT     543    543       N -> H (in dbSNP:rs35356639).
                             /FTId=VAR_025815.
CONFLICT    297    297       Missing (in Ref. 1 and 2).
CONFLICT    418    418       D -> H (in Ref. 1 and 2).
CONFLICT    439    439       R -> S (in Ref. 1 and 2).
CONFLICT    447    447       K -> N (in Ref. 1 and 2).
STRAND       31     34
STRAND       37     46
STRAND       49     52
STRAND       60     63
STRAND       66     68
STRAND       74     76
HELIX        78     82
HELIX        84     86
HELIX        88     90
STRAND       91     93
HELIX        95     97
TURN         98    100
HELIX       106    114
STRAND      116    122
STRAND      125    131
STRAND      137    140
HELIX       142    161
STRAND      167    172
HELIX       178    190
STRAND      194    200
HELIX       201    208
HELIX       211    213
STRAND      215    225
STRAND      230    238
STRAND      241    250
HELIX       255    273
HELIX       278    280
HELIX       282    298
TURN        299    301
STRAND      302    313
STRAND      316    323
HELIX       324    336
HELIX       339    348
HELIX       353    355
STRAND      358    363
HELIX       364    367
HELIX       369    378
TURN        379    381
TURN        390    392
HELIX       393    406
Back to Top
Nucleotide Sequence
Length: 5470 bp   Go to nucleotide: FASTA
Protein Sequence
Length: 654 bp   Go to amino acid: FASTA
The verified Protein-Protein interaction information
UniProt
Gene Symbol Ref Databases
YWHABHPRD 
YWHAZMINT 
HLA-CBioGRID 
HLA-CBioGRID 
HLA-CHPRD 
HLA-CBioGRID 
PPP2R2BIntAct 
HTR3AHPRD 
HLA-CBioGRID 
HLA-CBioGRID 
PRKAA1IntAct 
EIF2C4IntAct 
AIREBioGRID 
APCBioGRID 
ARRB1IntAct 
ARRB2IntAct 
GRB2BioGRID 
HLA-CBioGRID 
HLA-CBioGRID 
_BioGRID 
AIREBioGRID 
_BioGRID 
_HPRD 
_BioGRID 
_BioGRID 
_HPRD 
_BioGRID 
_BioGRID 
_HPRD 
_BioGRID 
_BioGRID 
_HPRD 
BCAR1BioGRID 
BRAFIntAct 
CASP7HPRD 
CASP8IntAct 
CAV1IntAct 
CDK9BioGRID 
CFTRIntAct 
HSPD1IntAct 
COPS5IntAct 
BCDIN3BioGRID 
DDX24BioGRID 
DNAJC10HPRD 
DNAJC1HPRD 
Dnajc3MINT 
DPH1HPRD 
DPYSL5MINT 
EIF2AK3HPRD 
HLA-CBioGRID 
BCAR1BioGRID 
BCAR1BioGRID 
EBNA-LPMINT 
EGFRIntAct 
EPM2ABioGRID 
ERN1HPRD 
ERP29HPRD 
ESR1IntAct 
F8HPRD 
FCHSD2IntAct 
GABARAPIntAct 
GABARAPL1IntAct 
GRB2BioGRID 
GRIA1HPRD 
TSHRBioGRID 
A2MHPRD 
APOBHPRD 
_HPRD 
_BioGRID 
_BioGRID 
_HPRD 
_BioGRID 
_BioGRID 
_BioGRID 
BCAR1HPRD 
CASP7BioGRID 
NFKB2IntAct 
DDX24HPRD 
DNAJB11MINT 
DNAJC10BioGRID 
DPH1BioGRID 
DPYSL5HPRD 
EIF2AK3IntAct 
ERN1BioGRID 
GRB2IntAct 
IGHMHPRD 
NFKBIAIntAct 
NFKBIBIntAct 
NFKBIEIntAct 
IKBKBIntAct 
KRT8BioGRID 
LDLRBioGRID 
MAP3K1IntAct 
MAP3K3IntAct 
MAP3K8IntAct 
PDE4DIPString 
NDRG1IntAct 
IKBKGIntAct 
NFKB2IntAct 
MAP3K7IntAct 
PAWRIntAct 
POLDIP3String 
PSME3HPRD 
PTENIntAct 
RELAIntAct 
_BioGRID 
_HPRD 
_IntAct 
APOBHPRD 
TSHRBioGRID 
RAF1IntAct 
RELBIntAct 
RELIntAct 
RIPK1IntAct 
RIPK3IntAct 
SH3BP4IntAct 
SIL1BioGRID 
TAB1IntAct 
TAB2IntAct 
TANKIntAct 
TBK1IntAct 
TGBioGRID 
TMEM62HPRD 
TNFRSF1AIntAct 
TNFRSF1BIntAct 
TRAF2IntAct 
TRAF6IntAct 
TSHRBioGRID 
H2AFXBioGRID 
HFEMINT 
HSPBP1HPRD 
IKBKBMINT 
KRT18HPRD 
KRT8HPRD 
LDLRHPRD 
LCTHPRD 
MAP3K14IntAct 
MAP3K1MINT 
MAP3K3MINT 
MEPCEBioGRID 
MAPK13IntAct 
MAP1LC3AIntAct 
MAP1LC3BIntAct 
MTNR1AHPRD 
MTNR1BHPRD 
PDE4DIPString 
NDRG1HPRD 
IKBKGMINT 
NFKB1MINT 
NFKB2MINT 
NHLRC1BioGRID 
MAP3K7MINT 
TP53MINT 
PAWRHPRD 
PawrIntAct 
PCSK7HPRD 
POLDIP3String 
Pias1BioGRID 
PRNPHPRD 
PSME3BioGRID 
_MINT 
RELAMINT 
F8BHPRD 
Pias1BioGRID 
APCBioGRID 
PRNPHPRD 
SVILHPRD 
_HPRD 
HLA-CBioGRID 
HLA-CBioGRID 
GABARAPL2IntAct 
TRA@HPRD 
EPM2ABioGRID 
BCAR1BioGRID 
HLA-CwHPRD 
_BioGRID 
_MINT 
DKFZp434N1610BioGRID 
TSHRHPRD 
HLA-CHPRD 
_IntAct 
RAF1IntAct 
RELBMINT 
RIPK1MINT 
RIPK3MINT 
POLR3HBioGRID 
RUVBL2BioGRID 
SIL1HPRD 
SIRT1IntAct 
SIRT3IntAct 
SPG20IntAct 
SREBF2BioGRID 
SUMO4HPRD 
SVILMINT 
SVILHPRD 
TMEM132AHPRD 
TAB1MINT 
TAB2MINT 
TANKMINT 
TBK1MINT 
TCERG1HPRD 
TGHPRD 
TMEM62IntAct 
TNFRSF1AMINT 
TNFRSF1BMINT 
TRAF2MINT 
TRAF6MINT 
TSHRHPRD 
UBQLN4BioGRID 
VWFHPRD 
Other Protein-Protein interaction resources
String database  
View Microarray data
Temporarily unavailable 
Comments