Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  78 kDa glucose-regulated protein  

UniProtKB / Swiss-Prot ID :  GRP78_HUMAN

Gene Name (Synonyms) : 
HSPA5, GRP78  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Endoplasmic reticulum lumen. Melanosome. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV. 

Protein Function :  Probably plays a role in facilitating the assembly of multimeric protein complexes inside the ER. 

Protein Sequence MKLSLVAAMLLLLSAARAEEEDKKEDVGTVVGIDLGTTYSCVGVFKNGRVEIIANDQGNRITPSYVAFTP...
Predicted Secondary Structure CCHHHHHHHHHHHHHCCCCCCCCCHHCCCEEEEEECCCCEEEEEEECCEEEEEECCCCCCCCCEEEEECC...
Protein Variant
LocationDescription
543N -> H (in dbSNP:rs35356639). VAR_025815
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
Protein Variant
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
37PhosphothreonineIDLGTTYSC
EEECCCCEE
29.83Phosphositeplus
Link
81Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)GDAAKNQLT
CHHHHHHHH
47.12Phosphositeplus
Link
96Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)VFDAKRLIG
HHHHHHHHC
49.97Phosphositeplus
Link
113Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)QQDIKFLPF
HHHHHHCCE
49.49Phosphositeplus
Link
118Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)FLPFKVVEK
HCCEEEEEC
43.35Phosphositeplus
Link
118N6-acetyllysineFLPFKVVEK
HCCEEEEEC
43.35Phosphositeplus
Link
122N6-acetyllysineKVVEKKTKP
EEEECCCCC
54.88Phosphositeplus
Link
123N6-acetyllysineVVEKKTKPY
EEECCCCCE
48.56Phosphositeplus
Link
125Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)EKKTKPYIQ
ECCCCCEEE
44.71Phosphositeplus
Link
125N6-acetyllysineEKKTKPYIQ
ECCCCCEEE
44.71Phosphositeplus
Link
138Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)GGQTKTFAP
CCCCCEECH
33.48Phosphositeplus
Link
138N6-acetyllysineGGQTKTFAP
CCCCCEECH
33.48Phosphositeplus
Link
152Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)MVLTKMKET
HHHHHHHHH
43.76Phosphositeplus
Link
152N6-acetyllysineMVLTKMKET
HHHHHHHHH
43.76Phosphositeplus
Link
154N6-acetyllysineLTKMKETAE
HHHHHHHHH
54.17Phosphositeplus
Link
163Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)AYLGKKVTH
HHHCCCCCC
41.28Phosphositeplus
Link
185Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)RQATKDAGT
HHHHHHHHH
48.90Phosphositeplus
Link
189PhosphothreonineKDAGTIAGL
HHHHHHCCC
14.90Phosphositeplus
Link
203PhosphothreonineINEPTAAAI
EECHHHHHH
23.81Phosphositeplus
Link
213Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)YGLDKREGE
HCCCCCCCC
58.34Phosphositeplus
Link
229PhosphothreonineLGGGTFDVS
CCCCEEEEE
21.67Phosphositeplus
Link
268Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)EHFIKLYKK
HHHHHHHHH
44.83Phosphositeplus
Link
268N6-acetyllysineEHFIKLYKK
HHHHHHHHH
44.83HPRD
Link
268N6-acetyllysineEHFIKLYKK
HHHHHHHHH
44.83Phosphositeplus
Link
268N6-acetyllysine.EHFIKLYKK
HHHHHHHHH
44.83UniProtKB
Link
326Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)LTRAKFEEL
ECHHHHHHH
50.44Phosphositeplus
Link
340Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)RSTMKPVQK
HHHHHHHHH
41.97Phosphositeplus
Link
352Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)DSDLKKSDI
HCCCCHHHC
56.04Phosphositeplus
Link
352N6-acetyllysineDSDLKKSDI
HCCCCHHHC
56.04Phosphositeplus
Link
353N6-acetyllysineSDLKKSDID
CCCCHHHCC
61.74Phosphositeplus
Link
370Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)TRIPKIQQL
HHHHHHHHH
51.26Phosphositeplus
Link
376Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)QQLVKEFFN
HHHHHHHHC
58.35Phosphositeplus
Link
376N6-acetyllysineQQLVKEFFN
HHHHHHHHC
58.35Phosphositeplus
Link
441PhosphothreonineIPRNTVVPT
ECCCCCCCC
24.94Phosphositeplus
Link-
464Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)TVTIKVYEG
EEEEEEECC
29.42Phosphositeplus
Link-
466PhosphotyrosineTIKVYEGER
EEEEECCCC
17.14HPRD
Link-
466PhosphotyrosineTIKVYEGER
EEEEECCCC
17.14PhosphoELM
Link-
466PhosphotyrosineTIKVYEGER
EEEEECCCC
17.14Phosphositeplus
Link-
466PhosphotyrosineTIKVYEGER
EEEEECCCC
17.14SysPTM
Link-
466Phosphotyrosine.TIKVYEGER
EEEEECCCC
17.14UniProtKB
Link-
518PhosphothreonineEDKGTGNKN
EECCCCEEE
43.23HPRD
Link-
518PhosphothreonineEDKGTGNKN
EECCCCEEE
43.23Phosphositeplus
Link-
523Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)GNKNKITIT
CEEEEEEEE
42.72Phosphositeplus
Link-
547Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)NDAEKFAEE
HHHHHHHHH
52.15Phosphositeplus
Link-
573Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)AYSLKNQIG
HHHHHHHHH
40.65Phosphositeplus
Link-
585N6-acetyllysineKLGGKLSSE
HHHCCCCHH
43.32Phosphositeplus
Link-
601Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)AVEEKIEWL
HHHHHHHHH
32.21Phosphositeplus
Link-
633N6-acetyllysinePIISKLYGS
HHHHHHHHH
35.01Phosphositeplus
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
P53_HUMANphysical interactionMINT-4052873MINT17184779
CH60_HUMANcolocalizationMINT-4054731MINT17174955
TNR1A_HUMANphysical interactionMINT-49298MINT14743216
NFKB1_HUMANphysical interactionMINT-48531MINT14743216
NFKB1_HUMANphysical interactionMINT-48640MINT14743216
TNR1B_HUMANphysical interactionMINT-49372MINT14743216
VDAC1_HUMANcolocalizationMINT-4054731MINT17174955
PSME3_HUMANphysical interactionMINT-63936MINT16169070
NFKB2_HUMANphysical interactionMINT-48694MINT14743216
M3K1_HUMANphysical interactionMINT-48276MINT14743216
TANK_HUMANphysical interactionMINT-48248MINT14743216
M3K14_HUMANphysical interactionMINT-48786MINT14743216
M3K3_HUMANphysical interactionMINT-48377MINT14743216
DPYL5_HUMANphysical interactionMINT-65304MINT16169070
TAB2_HUMANphysical interactionMINT-49184MINT14743216
TBK1_HUMANphysical interactionMINT-49252MINT14743216
RIPK3_HUMANphysical interactionMINT-49083MINT14743216
NEMO_HUMANphysical interactionMINT-48132MINT14743216
RAF1_HUMANcolocalization
physical interaction
physical interaction
physical interaction
EBI-1578685
EBI-1578641
EBI-1
intact18064632
18064632
18064632
18064632
PSME3_HUMANphysical interactionEBI-733001
intact16169070
TMM62_HUMANphysical interactionEBI-736925
intact16169070
A2MG_HUMANin vivoHPRD:00682HPRD12194978
APOB_HUMANin vitro
in vivo
HPRD:00682HPRD12397072
BCAR1_HUMANyeast 2-hybridHPRD:00682HPRD16169070
MUC_HUMANin vivoHPRD:00682HPRD3122216
PSME3_HUMANyeast 2-hybridHPRD:00682HPRD16169070
DDX24_HUMANyeast 2-hybridHPRD:00682HPRD16169070
TMM62_HUMANyeast 2-hybridHPRD:00682HPRD16169070
DPYL5_HUMANyeast 2-hybridHPRD:00682HPRD16169070
DNJA3_HUMANENSP00000324173STRING
DJB11_HUMANENSP00000324173STRING
DNJA2_HUMANENSP00000324173STRING
DNJA4_HUMANENSP00000324173STRING
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
DrugBank
DB00945Acetylsalicylic acid
DB00025Antihemophilic Factor
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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-268, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry.";
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-466, AND MASSSPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures