Names & Taxonomy

Uniprot ID:
P11142
Entry Name:
HSP7C_HUMAN
Status:
reviewed
Protein Names:
Heat shock cognate 71 kDa protein (Heat shock 70 kDa protein 8) (Lipopolysaccharide-associated protein 1) (LAP-1) (LPS-associated protein 1)
Gene Names:
HSPA8 HSC70 HSP73 HSPA10
Gene Names Primary:
HSPA8
Organism:
Homo sapiens (Human)

Structure

Length:
646
Sequence:
MSKGPAVGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPTNTVFDAKRLIGRRFDDAVVQSDMKHWPFMVVNDAGRPKVQVEYKGETKSFYPEEVSSMVLTKMKEIAEAYLGKTVTNAVVTVPAYFNDSQRQATKDAGTIAGLNVLRIINEPTAAAIAYGLDKKVGAERNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVNHFIAEFKRKHKKDISENKRAVRRLRTACERAKRTLSSSTQASIEIDSLYEGIDFYTSITRARFEELNADLFRGTLDPVEKALRDAKLDKSQIHDIVLVGGSTRIPKIQKLLQDFFNGKELNKSINPDEAVAYGAAVQAAILSGDKSENVQDLLLLDVTPLSLGIETAGGVMTVLIKRNTTIPTKQTQTFTTYSDNQPGVLIQVYEGERAMTKDNNLLGKFELTGIPPAPRGVPQIEVTFDIDANGILNVSAVDKSTGKENKITITNDKGRLSKEDIERMVQEAEKYKAEDEKQRDKVSSKNSLESYAFNMKATVEDEKLQGKINDEDKQKILDKCNEIINWLDKNQTAEKEEFEHQQKELEKVCNPIITKLYQSAGGMPGGMPGGFPGGGAPPSGGASSGPTIEEVD
Proteomes:
UP000005640

Subcellular location

Subcellular Location:
Cytoplasm. Melanosome. Nucleus, nucleolus. Cell membrane. Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Translocates rapidly from the cytoplasm to the nuclei, and especially to the nucleoli, upon heat shock.

Function

Function:
Acts as a repressor of transcriptional activation. Inhibits the transcriptional coactivator activity of CITED1 on Smad-mediated transcription. Chaperone. Component of the PRP19-CDC5L complex that forms an integral part of the spliceosome and is required for activating pre-mRNA splicing. May have a scaffolding role in the spliceosome assembly as it contacts all other components of the core complex. Binds bacterial lipopolysaccharide (LPS) et mediates LPS-induced inflammatory response, including TNF secretion by monocytes. Participates in the ER-associated degradation (ERAD) quality control pathway in conjunction with J domain-containing co-chaperones and the E3 ligase CHIP.
Gene Ontology Go:
blood microparticle
clathrin-sculpted gamma-aminobutyric acid transport vesicle membrane
cytosol
extracellular exosome
extracellular space
focal adhesion
intracellular
intracellular ribonucleoprotein complex
late endosome
lumenal side of lysosomal membrane
lysosomal lumen
lysosomal membrane
melanosome
membrane
myelin sheath
nucleolus
nucleoplasm
nucleus
plasma membrane
presynapse
Prp19 complex
spliceosomal complex
ATP binding
ATPase activity
ATPase activity, coupled
C3HC4-type RING finger domain binding
enzyme binding
G-protein coupled receptor binding
heat shock protein binding
MHC class II protein complex binding
phosphatidylserine binding
poly(A) RNA binding
ubiquitin protein ligase binding
unfolded protein binding
ATP metabolic process
axon guidance
cellular response to heat
cellular response to starvation
chaperone mediated protein folding requiring cofactor
chaperone-mediated autophagy
chaperone-mediated autophagy translocation complex disassembly
chaperone-mediated protein transport involved in chaperone-mediated autophagy
clathrin coat disassembly
gene expression
late endosomal microautophagy
membrane organization
mRNA splicing, via spliceosome
negative regulation of fibril organization
negative regulation of transcription, DNA-templated
neurotransmitter secretion
positive regulation of mRNA splicing, via spliceosome
post-Golgi vesicle-mediated transport
protein folding
protein refolding
protein targeting to lysosome
protein targeting to lysosome involved in chaperone-mediated autophagy
regulation of cell cycle
regulation of cellular response to heat
regulation of mRNA stability
regulation of protein complex assembly
regulation of protein complex stability
regulation of protein import
regulation of protein stability
response to unfolded protein
RNA splicing
synaptic transmission
transcription, DNA-templated
viral process
Gene Ontology Biological Process:
ATP metabolic process
axon guidance
cellular response to heat
cellular response to starvation
chaperone-mediated autophagy
chaperone-mediated autophagy translocation complex disassembly
chaperone mediated protein folding requiring cofactor
chaperone-mediated protein transport involved in chaperone-mediated autophagy
clathrin coat disassembly
gene expression
late endosomal microautophagy
membrane organization
mRNA splicing, via spliceosome
negative regulation of fibril organization
negative regulation of transcription, DNA-templated
neurotransmitter secretion
positive regulation of mRNA splicing, via spliceosome
post-Golgi vesicle-mediated transport
protein folding
protein refolding
protein targeting to lysosome
protein targeting to lysosome involved in chaperone-mediated autophagy
regulation of cell cycle
regulation of cellular response to heat
regulation of mRNA stability
regulation of protein complex assembly
regulation of protein complex stability
regulation of protein import
regulation of protein stability
response to unfolded protein
RNA splicing
synaptic transmission
transcription, DNA-templated
viral process
Gene Ontology Molecular Function:
ATPase activity
ATPase activity, coupled
ATP binding
C3HC4-type RING finger domain binding
enzyme binding
G-protein coupled receptor binding
heat shock protein binding
MHC class II protein complex binding
phosphatidylserine binding
poly(A) RNA binding
ubiquitin protein ligase binding
unfolded protein binding
Gene Ontology Cellular Component:
blood microparticle
clathrin-sculpted gamma-aminobutyric acid transport vesicle membrane
cytosol
extracellular exosome
extracellular space
focal adhesion
intracellular
intracellular ribonucleoprotein complex
late endosome
lumenal side of lysosomal membrane
lysosomal lumen
lysosomal membrane
melanosome
membrane
myelin sheath
nucleolus
nucleoplasm
nucleus
plasma membrane
presynapse
Prp19 complex
spliceosomal complex
Keywords:
3D-structure
ATP-binding
Acetylation
Alternative splicing
Cell membrane
Chaperone
Complete proteome
Cytoplasm
Direct protein sequencing
Host-virus interaction
Isopeptide bond
Membrane
Methylation
Nucleotide-binding
Nucleus
Phosphoprotein
Polymorphism
Reference proteome
Repressor
Spliceosome
Stress response
Transcription
Transcription regulation
Ubl conjugation
mRNA processing
mRNA splicing
Interacts With:
Q99IB8; P60709; Q9GZX7; P49407; P32121; Q9NQ11; Q99933; O95816; Q8AZK7; P00533; O14976; Q9NZL4; P05412; P00338; Q5S007; P03485; Q9UNE7; O00635

Publication

PubMed ID:
3037489 11093761 15489334 1286667 8713105 23349634 1586970 9305631 9679980 11147964 10722728 11276205 14532270 16139798 15963462 17081065 16815975 17182002 17289661 17525332 19413330 19131338 19690332 19608861 20053985 20176811 20068231 21269460 22814378 23865999 23973223 23921388 23990462 24270810 24880125 24275569 25218447 25944712 19586912 19256508 21526763