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P19120 (HSP7C_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 136. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Heat shock cognate 71 kDa protein
Alternative name(s):
Heat shock 70 kDa protein 8
Gene names
Name:HSPA8
Synonyms:HSC70
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length650 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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 By similarity. Binds bacterial lipopolysaccharide (LPS) et mediates LPS-induced inflammatory response, including TNF secretion By similarity.

Subunit structure

Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs. Interacts with PACRG. Interacts with HSPH1/HSP105. Interacts with IRAK1BP1 and BAG1. Interacts with DNAJC7. Interacts with CITED1 (via N-terminus); the interaction suppresses the association of CITED1 to p300/CBP and SMAD-mediated transcription transactivation. Component of the PRP19-CDC5L splicing complex composed of a core complex comprising a homotetramer of PRPF19, CDC5L, PLRG1 and BCAS2, and at least three less stably associated proteins CTNNBL1, CWC15 and HSPA8. Interacts with TRIM5 By similarity. Part of a complex composed at least of ASCL2, EMSY, HCFC1, HSPA8, CCAR2, MATR3, MKI67, RBBP5, TUBB2A, WDR5 and ZNF335; this complex may have a histone H3-specific methyltransferase activity By similarity. Following LPS binding, may form a complex with CXCR4, GDF5 and HSP90AA1 By similarity. Interacts with PARK2 By similarity.

Subcellular location

Cytoplasm By similarity. Melanosome By similarity. Nucleusnucleolus By similarity. Cell membrane By similarity. 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 By similarity.

Tissue specificity

Ubiquitous.

Induction

Constitutively synthesized.

Domain

The N-terminal 1-386 residues constitute the ATPase domain, while residues 387-646 form the peptide-binding domain By similarity.

Post-translational modification

Acetylated By similarity.

ISGylated By similarity.

Trimethylation at Lys-561 reduces fibrillar SNCA binding By similarity.

Sequence similarities

Belongs to the heat shock protein 70 family.

Ontologies

Keywords
   Biological processmRNA processing
mRNA splicing
Stress response
Transcription
Transcription regulation
   Cellular componentCell membrane
Cytoplasm
Membrane
Nucleus
Spliceosome
   LigandATP-binding
Nucleotide-binding
   Molecular functionChaperone
Repressor
   PTMAcetylation
Methylation
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processRNA splicing

Inferred from electronic annotation. Source: UniProtKB-KW

chaperone mediated protein folding requiring cofactor

Inferred from electronic annotation. Source: Ensembl

mRNA processing

Inferred from electronic annotation. Source: UniProtKB-KW

negative regulation of transcription, DNA-templated

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of cell cycle

Inferred from electronic annotation. Source: Ensembl

response to stress

Inferred from electronic annotation. Source: UniProtKB-KW

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentPrp19 complex

Inferred from sequence or structural similarity. Source: UniProtKB

cytosol

Inferred from electronic annotation. Source: Ensembl

extracellular vesicular exosome

Inferred from electronic annotation. Source: Ensembl

melanosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleolus

Inferred from sequence or structural similarity. Source: UniProtKB

nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

ribonucleoprotein complex

Inferred from sequence or structural similarity. Source: UniProtKB

spliceosomal complex

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

ATPase activity, coupled

Inferred from electronic annotation. Source: Ensembl

protein binding

Inferred from physical interaction PubMed 19878303. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

CFTRP135692EBI-907802,EBI-349854From a different organism.
CftrP263615EBI-907802,EBI-6115317From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 650649Heat shock cognate 71 kDa protein
PRO_0000078268

Regions

Nucleotide binding12 – 154ATP
Nucleotide binding202 – 2043ATP
Nucleotide binding268 – 2758ATP
Nucleotide binding339 – 3424ATP
Region186 – 377192Interaction with BAG1 By similarity

Sites

Binding site711ATP

Amino acid modifications

Modified residue21N-acetylserine By similarity
Modified residue1081N6-acetyllysine By similarity
Modified residue1531Phosphoserine By similarity
Modified residue2461N6-acetyllysine By similarity
Modified residue3191N6-acetyllysine; alternate By similarity
Modified residue3191N6-succinyllysine; alternate By similarity
Modified residue3281N6-acetyllysine By similarity
Modified residue3621Phosphoserine By similarity
Modified residue5121N6-acetyllysine; alternate By similarity
Modified residue5121N6-succinyllysine; alternate By similarity
Modified residue5241N6-acetyllysine By similarity
Modified residue5611N6,N6,N6-trimethyllysine; by METTL21A By similarity
Modified residue5891N6-acetyllysine By similarity
Modified residue5971N6-acetyllysine By similarity
Modified residue6011N6-acetyllysine By similarity

Experimental info

Sequence conflict1801A → T in AAI05183. Ref.3
Sequence conflict5431E → K in CAA37422. Ref.1
Sequence conflict5431E → K in CAA37823. Ref.1

Secondary structure

..................................................................................................... 650
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P19120 [UniParc].

Last modified May 29, 2007. Version 2.
Checksum: FBE109C14A28B925

FASTA65071,241
        10         20         30         40         50         60 
MSKGPAVGID LGTTYSCVGV FQHGKVEIIA NDQGNRTTPS YVAFTDTERL IGDAAKNQVA 

        70         80         90        100        110        120 
MNPTNTVFDA KRLIGRRFDD AVVQSDMKHW PFMVVNDAGR PKVQVEYKGE TKSFYPEEVS 

       130        140        150        160        170        180 
SMVLTKMKEI AEAYLGKTVT NAVVTVPAYF NDSQRQATKD AGTIAGLNVL RIINEPTAAA 

       190        200        210        220        230        240 
IAYGLDKKVG AERNVLIFDL GGGTFDVSIL TIEDGIFEVK STAGDTHLGG EDFDNRMVNH 

       250        260        270        280        290        300 
FIAEFKRKHK KDISENKRAV RRLRTACERA KRTLSSSTQA SIEIDSLYEG IDFYTSITRA 

       310        320        330        340        350        360 
RFEELNADLF RGTLDPVEKA LRDAKLDKSQ IHDIVLVGGS TRIPKIQKLL QDFFNGKELN 

       370        380        390        400        410        420 
KSINPDEAVA YGAAVQAAIL SGDKSENVQD LLLLDVTPLS LGIETAGGVM TVLIKRNTTI 

       430        440        450        460        470        480 
PTKQTQTFTT YSDNQPGVLI QVYEGERAMT KDNNLLGKFE LTGIPPAPRG VPQIEVTFDI 

       490        500        510        520        530        540 
DANGILNVSA VDKSTGKENK ITITNDKGRL SKEDIERMVQ EAEKYKAEDE KQRDKVSSKN 

       550        560        570        580        590        600 
SLESYAFNMK ATVEDEKLQG KINDEDKQKI LDKCNEIINW LDKNQTAEKE EFEHQQKELE 

       610        620        630        640        650 
KVCNPIITKL YQSAGGMPGG MPGGMPGGFP GGGAPPSGGA SSGPTIEEVD 

« Hide

References

« Hide 'large scale' references
[1]"Nucleotide sequence of the cDNA of a bovine 70 kilodalton heat shock cognate protein."
Deluca-Flaherty C., McKay D.B.
Nucleic Acids Res. 18:5569-5569(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Brain cortex.
[2]"Characterization of 954 bovine full-CDS cDNA sequences."
Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L., Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.
BMC Genomics 6:166-166(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]NIH - Mammalian Gene Collection (MGC) project
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Crossbred X Angus.
Tissue: Ileum.
[4]"Three-dimensional structure of the ATPase fragment of a 70K heat-shock cognate protein."
Flaherty K.M., de Luca-Flaherty C., McKay D.B.
Nature 346:623-628(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1-385 IN COMPLEX WITH ADP.
[5]"Structural basis of the 70-kilodalton heat shock cognate protein ATP hydrolytic activity. II. Structure of the active site with ADP or ATP bound to wild type and mutant ATPase fragment."
Flaherty K.M., Wilbanks S.M., Deluca-Flaherty C., McKay D.B.
J. Biol. Chem. 269:12899-12907(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1-385 IN COMPLEXES WITH ADP AND ATP.
[6]"Structural replacement of active site monovalent cations by the epsilon-amino group of lysine in the ATPase fragment of bovine Hsc70."
Wilbanks S.M., McKay D.B.
Biochemistry 37:7456-7462(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1-385 IN COMPLEX WITH ADP.
[7]"The hydroxyl of threonine 13 of the bovine 70-kDa heat shock cognate protein is essential for transducing the ATP-induced conformational change."
Sousa M.C., McKay D.B.
Biochemistry 37:15392-15399(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 1-381 IN COMPLEX WITH ADP.
[8]"Mapping the role of active site residues for transducing an ATP-induced conformational change in the bovine 70-kDa heat shock cognate protein."
Johnson E.R., McKay D.B.
Biochemistry 38:10823-10830(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1-381 OF MUTANTS.
[9]"Structure of the Hsp110:Hsc70 nucleotide exchange machine."
Schuermann J.P., Jiang J., Cuellar J., Llorca O., Wang L., Gimenez L.E., Jin S., Taylor A.B., Demeler B., Morano K.A., Hart P.J., Valpuesta J.M., Lafer E.M., Sousa R.
Mol. Cell 31:232-243(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.12 ANGSTROMS) OF 2-554 IN COMPLEX WITH ADP.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X53827 mRNA. Translation: CAA37823.1.
X53335 mRNA. Translation: CAA37422.1.
BT030487 mRNA. Translation: ABQ12927.1.
BC105182 mRNA. Translation: AAI05183.1.
PIRS11456.
RefSeqNP_776770.2. NM_174345.4.
UniGeneBt.12309.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1ATRX-ray2.34A1-386[»]
1ATSX-ray2.43A1-386[»]
1BA0X-ray1.90A1-386[»]
1BA1X-ray1.70A1-386[»]
1BUPX-ray1.70A1-386[»]
1HPMX-ray1.70A1-386[»]
1HX1X-ray1.90A4-381[»]
1KAXX-ray1.70A1-381[»]
1KAYX-ray1.70A1-381[»]
1KAZX-ray1.70A1-381[»]
1NGAX-ray2.18A1-386[»]
1NGBX-ray2.18A1-386[»]
1NGCX-ray2.20A1-386[»]
1NGDX-ray2.18A1-386[»]
1NGEX-ray2.05A1-386[»]
1NGFX-ray2.17A1-386[»]
1NGGX-ray2.19A1-386[»]
1NGHX-ray2.23A1-386[»]
1NGIX-ray2.15A1-386[»]
1NGJX-ray2.10A1-386[»]
1Q2Gmodel-B4-381[»]
1QQMX-ray1.90A4-381[»]
1QQNX-ray1.90A4-381[»]
1QQOX-ray1.90A4-381[»]
1YUWX-ray2.60A1-554[»]
2BUPX-ray1.70A1-381[»]
2QW9X-ray1.85A/B1-394[»]
2QWLX-ray1.75A/B1-394[»]
2QWMX-ray1.86A/B1-394[»]
2QWNX-ray2.40A1-394[»]
2QWOX-ray1.70A1-394[»]
2QWPX-ray1.75A1-394[»]
2QWQX-ray2.21A1-394[»]
2QWRX-ray2.21A1-394[»]
3C7NX-ray3.12B1-554[»]
3HSCX-ray1.93A1-386[»]
4FL9X-ray1.90A1-554[»]
ProteinModelPortalP19120.
SMRP19120. Positions 1-621.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid159144. 2 interactions.
DIPDIP-35481N.
IntActP19120. 6 interactions.
MINTMINT-157582.
STRING9913.ENSBTAP00000017497.

Chemistry

BindingDBP19120.
ChEMBLCHEMBL1275213.

Proteomic databases

PaxDbP19120.
PRIDEP19120.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSBTAT00000017497; ENSBTAP00000017497; ENSBTAG00000013162.
GeneID281831.
KEGGbta:281831.

Organism-specific databases

CTD3312.

Phylogenomic databases

eggNOGCOG0443.
GeneTreeENSGT00750000117237.
HOGENOMHOG000228135.
HOVERGENHBG051845.
InParanoidP19120.
KOK03283.
OMAGENKIFT.
OrthoDBEOG7PCJGF.
TreeFamTF105042.

Family and domain databases

Gene3D1.20.1270.10. 1 hit.
2.60.34.10. 1 hit.
InterProIPR018181. Heat_shock_70_CS.
IPR029048. HSP70_C.
IPR029047. HSP70_peptide-bd.
IPR013126. Hsp_70_fam.
[Graphical view]
PfamPF00012. HSP70. 1 hit.
[Graphical view]
PRINTSPR00301. HEATSHOCK70.
SUPFAMSSF100920. SSF100920. 1 hit.
SSF100934. SSF100934. 1 hit.
PROSITEPS00297. HSP70_1. 1 hit.
PS00329. HSP70_2. 1 hit.
PS01036. HSP70_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP19120.
NextBio20805740.
PROP19120.

Entry information

Entry nameHSP7C_BOVIN
AccessionPrimary (citable) accession number: P19120
Secondary accession number(s): A5D968, Q3MHM4
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: May 29, 2007
Last modified: June 11, 2014
This is version 136 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references