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Protein

78 kDa glucose-regulated protein

Gene

HSPA5

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Probably plays a role in facilitating the assembly of multimeric protein complexes inside the endoplasmic reticulum. Involved in the correct folding of proteins and degradation of misfolded proteins via its interaction with DNAJC10, probably to facilitate the release of DNAJC10 from its substrate (By similarity).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei97ATPBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi37 – 40ATPBy similarity4
Nucleotide bindingi228 – 230ATPBy similarity3
Nucleotide bindingi294 – 301ATPBy similarity8
Nucleotide bindingi365 – 368ATPBy similarity4

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
78 kDa glucose-regulated protein
Short name:
GRP-78
Alternative name(s):
Heat shock 70 kDa protein 5
Gene namesi
Name:HSPA5
Synonyms:GRP78
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 19By similarityAdd BLAST19
ChainiPRO_000028877420 – 65578 kDa glucose-regulated proteinAdd BLAST636

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei87PhosphoserineBy similarity1
Modified residuei126N6-acetyllysineBy similarity1
Modified residuei161Nitrated tyrosineBy similarity1
Modified residuei214N6-acetyllysineBy similarity1
Modified residuei272N6-acetyllysineBy similarity1
Modified residuei327N6-acetyllysineBy similarity1
Cross-linki353Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei354N6-acetyllysine; alternateBy similarity1
Cross-linki354Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateBy similarity
Modified residuei448N6-succinyllysineBy similarity1
Modified residuei493Omega-N-methylarginineBy similarity1
Modified residuei519PhosphothreonineBy similarity1
Modified residuei586N6,N6,N6-trimethyllysine; by METTL21A; in vitroBy similarity1
Modified residuei586N6,N6-dimethyllysine; alternateBy similarity1
Modified residuei586N6-methyllysine; alternateBy similarity1
Modified residuei592N6-methyllysineBy similarity1
Modified residuei644PhosphothreonineBy similarity1

Keywords - PTMi

Acetylation, Isopeptide bond, Methylation, Nitration, Phosphoprotein, Ubl conjugation

Proteomic databases

PeptideAtlasiQ0VCX2.
PRIDEiQ0VCX2.

Interactioni

Subunit structurei

Interacts with DNAJC1 (via J domain). Component of an EIF2 complex at least composed of CELF1/CUGBP1, CALR, CALR3, EIF2S1, EIF2S2, HSP90B1 and HSPA5. 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 TMEM132A and TRIM21. May form a complex with ERLEC1, OS9, SEL1L and SYVN1. Interacts with DNAJC10. Interacts with MX1. Interacts with METTL23. Interacts with CEMIP; the interaction induces calcium leakage from the endoplasmic reticulum and cell migration. Interacts with PCSK4 form; the interaction takes place in the endoplasmic reticulum. Interacts with CIPC. Interacts with CCDC88B (via C-terminus); the interaction opposes ERN1-mediated JNK activation, protecting against apoptosis.By similarity

Protein-protein interaction databases

DIPiDIP-60411N.
IntActiQ0VCX2. 1 interactor.

Structurei

3D structure databases

ProteinModelPortaliQ0VCX2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi652 – 655Prevents secretion from ERPROSITE-ProRule annotation4

Sequence similaritiesi

Belongs to the heat shock protein 70 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

HOVERGENiHBG051845.
InParanoidiQ0VCX2.
KOiK09490.

Family and domain databases

Gene3Di1.20.1270.10. 1 hit.
2.60.34.10. 1 hit.
InterProiIPR018181. Heat_shock_70_CS.
IPR029048. HSP70_C.
IPR029047. HSP70_peptide-bd.
IPR013126. Hsp_70_fam.
[Graphical view]
PfamiPF00012. HSP70. 1 hit.
[Graphical view]
PRINTSiPR00301. HEATSHOCK70.
SUPFAMiSSF100920. SSF100920. 1 hit.
SSF100934. SSF100934. 1 hit.
PROSITEiPS00014. ER_TARGET. 1 hit.
PS00297. HSP70_1. 1 hit.
PS00329. HSP70_2. 1 hit.
PS01036. HSP70_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q0VCX2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKLSLVAAVL LLLLGTARAE EEDKKEDVGT VVGIDLGTTY SCVGVFKNGR
60 70 80 90 100
VEIIANDQGN RITPSYVAFT PEGERLIGDA AKNQLTSNPE NTVFDAKRLI
110 120 130 140 150
GRTWNDPSVQ QDIKFLPFKV VEKKTKPYIQ VDVGGGQTKT FAPEEISAMV
160 170 180 190 200
LTKMKETAEA YLGKKVTHAV VTVPAYFNDA QRQATKDAGT IAGLNVMRII
210 220 230 240 250
NEPTAAAIAY GLDKREGEKN ILVFDLGGGT FDVSLLTIDN GVFEVVATNG
260 270 280 290 300
DTHLGGEDFD QRVMEHFIKL YKKKTGKDVR KDNRAVQKLR REVEKAKRAL
310 320 330 340 350
SSQHQARIEI ESFYEGEDFS ETLTRAKFEE LNMDLFRSTM KPVQKVLEDS
360 370 380 390 400
DLKKSDIDEI VLVGGSTRIP KIQQLVKEFF NGKEPSRGIN PDEAVAYGAA
410 420 430 440 450
VQAGVLSGDQ DTGDLVLLDV CPLTLGIETV GGVMTKLIPR NTVVPTKKSQ
460 470 480 490 500
IFSTASDNQP TVTIKVYEGE RPLTKDNHLL GTFDLTGIPP APRGVPQIEV
510 520 530 540 550
TFEIDVNGIL RVTAEDKGTG NKNKITITND QNRLTPEEIE RMVNDAEKFA
560 570 580 590 600
EEDKKLKERI DTRNELESYA YSLKNQIGDK EKLGGKLSSE DKETMEKAVE
610 620 630 640 650
EKIEWLESHQ DADIEDFKAK KKELEEIVQP IISKLYGSAG PPPTSEEEAA

DKDEL
Length:655
Mass (Da):72,400
Last modified:September 5, 2006 - v1
Checksum:i93B4C3D46A441066
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BT030726 mRNA. Translation: ABS45042.1.
BC119953 mRNA. Translation: AAI19954.1.
RefSeqiNP_001068616.1. NM_001075148.1.
UniGeneiBt.65104.

Genome annotation databases

GeneIDi415113.
KEGGibta:415113.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BT030726 mRNA. Translation: ABS45042.1.
BC119953 mRNA. Translation: AAI19954.1.
RefSeqiNP_001068616.1. NM_001075148.1.
UniGeneiBt.65104.

3D structure databases

ProteinModelPortaliQ0VCX2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-60411N.
IntActiQ0VCX2. 1 interactor.

Proteomic databases

PeptideAtlasiQ0VCX2.
PRIDEiQ0VCX2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi415113.
KEGGibta:415113.

Organism-specific databases

CTDi3309.

Phylogenomic databases

HOVERGENiHBG051845.
InParanoidiQ0VCX2.
KOiK09490.

Miscellaneous databases

PROiQ0VCX2.

Family and domain databases

Gene3Di1.20.1270.10. 1 hit.
2.60.34.10. 1 hit.
InterProiIPR018181. Heat_shock_70_CS.
IPR029048. HSP70_C.
IPR029047. HSP70_peptide-bd.
IPR013126. Hsp_70_fam.
[Graphical view]
PfamiPF00012. HSP70. 1 hit.
[Graphical view]
PRINTSiPR00301. HEATSHOCK70.
SUPFAMiSSF100920. SSF100920. 1 hit.
SSF100934. SSF100934. 1 hit.
PROSITEiPS00014. ER_TARGET. 1 hit.
PS00297. HSP70_1. 1 hit.
PS00329. HSP70_2. 1 hit.
PS01036. HSP70_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiGRP78_BOVIN
AccessioniPrimary (citable) accession number: Q0VCX2
Secondary accession number(s): A7E3V5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 29, 2007
Last sequence update: September 5, 2006
Last modified: November 30, 2016
This is version 76 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. 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.