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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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei97 – 971ATPBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi37 – 404ATPBy similarity
Nucleotide bindingi228 – 2303ATPBy similarity
Nucleotide bindingi294 – 3018ATPBy similarity
Nucleotide bindingi365 – 3684ATPBy similarity

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
ProteomesiUP000009136 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919By similarityAdd
BLAST
Chaini20 – 65563678 kDa glucose-regulated proteinPRO_0000288774Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei126 – 1261N6-acetyllysineBy similarity
Modified residuei161 – 1611Nitrated tyrosineBy similarity
Modified residuei214 – 2141N6-acetyllysineBy similarity
Modified residuei327 – 3271N6-acetyllysineBy similarity
Modified residuei354 – 3541N6-acetyllysineBy similarity
Modified residuei448 – 4481N6-succinyllysineBy similarity
Modified residuei519 – 5191PhosphothreonineBy similarity
Modified residuei586 – 5861N6,N6,N6-trimethyllysine; by METTL21A; in vitroBy similarity

Keywords - PTMi

Acetylation, Methylation, Nitration, Phosphoprotein

Proteomic databases

PRIDEiQ0VCX2.

Interactioni

Subunit structurei

Interacts with DNAJC1 (via J domain) (By similarity). 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 (By similarity). Interacts with MX1. Interacts with METTL23 and DNAJC10. Interacts with CEMIP; the interaction induces calcium leakage from the endoplamic reticulum and cell migration (By similarity).By similarity

Protein-protein interaction databases

DIPiDIP-60411N.
IntActiQ0VCX2. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliQ0VCX2.
SMRiQ0VCX2. Positions 29-571.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi652 – 6554Prevents secretion from ERPROSITE-ProRule annotation

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.
SMRiQ0VCX2. Positions 29-571.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-60411N.
IntActiQ0VCX2. 1 interaction.

Proteomic databases

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

NextBioi20818797.
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...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  2. NIH - Mammalian Gene Collection (MGC) project
    Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Hereford.
    Tissue: Fetal skin.

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: July 22, 2015
This is version 68 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

External Data

Dasty 3

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 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.