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Protein

Heat shock cognate 71 kDa protein

Gene

HSPA8

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

Functioni

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. Participates in the ER-associated degradation (ERAD) quality control pathway in conjunction with J domain-containing co-chaperones and the E3 ligase CHIP (By similarity).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei71ATP1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi12 – 15ATP4
Nucleotide bindingi202 – 204ATP3
Nucleotide bindingi268 – 275ATP8
Nucleotide bindingi339 – 342ATP4

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Chaperone, Repressor

Keywords - Biological processi

mRNA processing, mRNA splicing, Stress response, Transcription, Transcription regulation

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-BTA-3371453. Regulation of HSF1-mediated heat shock response.
R-BTA-3371568. Attenuation phase.
R-BTA-3371571. HSF1-dependent transactivation.
R-BTA-450408. AUF1 (hnRNP D0) binds and destabilizes mRNA.
R-BTA-6798695. Neutrophil degranulation.
R-BTA-72163. mRNA Splicing - Major Pathway.
R-BTA-8856828. Clathrin-mediated endocytosis.

Names & Taxonomyi

Protein namesi
Recommended name:
Heat shock cognate 71 kDa protein
Alternative name(s):
Heat shock 70 kDa protein 8
Gene namesi
Name:HSPA8
Synonyms:HSC70
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 15

Subcellular locationi

  • 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).By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane, Nucleus, Spliceosome

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL1275213.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00000782682 – 650Heat shock cognate 71 kDa proteinAdd BLAST649

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineBy similarity1
Modified residuei108N6-acetyllysineBy similarity1
Modified residuei153PhosphoserineBy similarity1
Modified residuei246N6-acetyllysineBy similarity1
Modified residuei319N6-acetyllysine; alternateBy similarity1
Modified residuei319N6-succinyllysine; alternateBy similarity1
Modified residuei328N6-acetyllysineBy similarity1
Modified residuei329PhosphoserineBy similarity1
Modified residuei362PhosphoserineBy similarity1
Modified residuei469Omega-N-methylarginineBy similarity1
Modified residuei512N6-acetyllysine; alternateBy similarity1
Modified residuei512N6-succinyllysine; alternateBy similarity1
Cross-linki512Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateBy similarity
Cross-linki512Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei524N6-acetyllysineBy similarity1
Modified residuei541PhosphoserineBy similarity1
Modified residuei561N6,N6,N6-trimethyllysine; by METTL21A; alternateBy similarity1
Modified residuei561N6,N6-dimethyllysine; alternateBy similarity1
Modified residuei589N6-acetyllysineBy similarity1
Modified residuei597N6-acetyllysineBy similarity1
Modified residuei601N6-acetyllysineBy similarity1

Post-translational modificationi

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

Keywords - PTMi

Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiP19120.
PeptideAtlasiP19120.
PRIDEiP19120.

Expressioni

Tissue specificityi

Ubiquitous.

Inductioni

Constitutively synthesized.

Gene expression databases

BgeeiENSBTAG00000013162.

Interactioni

Subunit structurei

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 and DNAJB14 (via J domain). Interacts (via C-terminus) with the E3 ligase CHIP forming a 210 kDa complex of one CHIP and two HSPA8 molecules. 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. 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. Following LPS binding, may form a complex with CXCR4, GDF5 and HSP90AA1. Interacts with PARK2. Interacts with FOXP3. Interacts with DNAJC9 (via J domain). Interacts with MLLT11. Interacts with RNF207 (By similarity). Interacts with DNAJC21 (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
CFTRP135692EBI-907802,EBI-349854From a different organism.
CftrP263615EBI-907802,EBI-6115317From a different organism.

Protein-protein interaction databases

BioGridi159144. 2 interactors.
DIPiDIP-35481N.
IntActiP19120. 6 interactors.
MINTiMINT-157582.
STRINGi9913.ENSBTAP00000017497.

Chemistry databases

BindingDBiP19120.

Structurei

Secondary structure

1650
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi7 – 10Combined sources4
Beta strandi13 – 22Combined sources10
Beta strandi25 – 28Combined sources4
Beta strandi36 – 39Combined sources4
Beta strandi42 – 44Combined sources3
Beta strandi49 – 51Combined sources3
Helixi53 – 56Combined sources4
Turni57 – 61Combined sources5
Helixi63 – 65Combined sources3
Beta strandi66 – 68Combined sources3
Helixi70 – 72Combined sources3
Turni73 – 75Combined sources3
Helixi81 – 87Combined sources7
Beta strandi91 – 97Combined sources7
Beta strandi100 – 107Combined sources8
Beta strandi110 – 114Combined sources5
Helixi116 – 135Combined sources20
Beta strandi141 – 146Combined sources6
Helixi152 – 164Combined sources13
Beta strandi168 – 174Combined sources7
Helixi175 – 182Combined sources8
Turni183 – 186Combined sources4
Beta strandi187 – 191Combined sources5
Beta strandi193 – 200Combined sources8
Beta strandi205 – 213Combined sources9
Beta strandi216 – 225Combined sources10
Helixi230 – 249Combined sources20
Helixi253 – 255Combined sources3
Helixi257 – 273Combined sources17
Turni274 – 276Combined sources3
Beta strandi277 – 288Combined sources12
Beta strandi291 – 298Combined sources8
Helixi299 – 312Combined sources14
Helixi314 – 323Combined sources10
Helixi328 – 330Combined sources3
Beta strandi333 – 338Combined sources6
Helixi339 – 342Combined sources4
Helixi344 – 353Combined sources10
Turni354 – 356Combined sources3
Helixi365 – 367Combined sources3
Helixi368 – 380Combined sources13
Beta strandi386 – 388Combined sources3
Beta strandi392 – 396Combined sources5
Beta strandi401 – 405Combined sources5
Turni406 – 408Combined sources3
Beta strandi409 – 414Combined sources6
Beta strandi419 – 432Combined sources14
Beta strandi438 – 446Combined sources9
Helixi450 – 452Combined sources3
Beta strandi453 – 461Combined sources9
Beta strandi474 – 480Combined sources7
Beta strandi486 – 492Combined sources7
Turni493 – 495Combined sources3
Beta strandi498 – 503Combined sources6
Helixi512 – 524Combined sources13
Helixi526 – 534Combined sources9
Beta strandi539 – 542Combined sources4
Helixi547 – 549Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
ProteinModelPortaliP19120.
SMRiP19120.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP19120.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni186 – 377Interaction with BAG1By similarityAdd BLAST192

Domaini

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

Sequence similaritiesi

Belongs to the heat shock protein 70 family.Curated

Phylogenomic databases

eggNOGiKOG0101. Eukaryota.
COG0443. LUCA.
GeneTreeiENSGT00820000127001.
HOGENOMiHOG000228135.
HOVERGENiHBG051845.
InParanoidiP19120.
KOiK03283.
OMAiCFNIKST.
OrthoDBiEOG091G03SF.
TreeFamiTF105042.

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.
PROSITEiPS00297. 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.

P19120-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSKGPAVGID LGTTYSCVGV FQHGKVEIIA NDQGNRTTPS YVAFTDTERL
60 70 80 90 100
IGDAAKNQVA MNPTNTVFDA KRLIGRRFDD AVVQSDMKHW PFMVVNDAGR
110 120 130 140 150
PKVQVEYKGE TKSFYPEEVS SMVLTKMKEI AEAYLGKTVT NAVVTVPAYF
160 170 180 190 200
NDSQRQATKD AGTIAGLNVL RIINEPTAAA IAYGLDKKVG AERNVLIFDL
210 220 230 240 250
GGGTFDVSIL TIEDGIFEVK STAGDTHLGG EDFDNRMVNH FIAEFKRKHK
260 270 280 290 300
KDISENKRAV RRLRTACERA KRTLSSSTQA SIEIDSLYEG IDFYTSITRA
310 320 330 340 350
RFEELNADLF RGTLDPVEKA LRDAKLDKSQ IHDIVLVGGS TRIPKIQKLL
360 370 380 390 400
QDFFNGKELN KSINPDEAVA YGAAVQAAIL SGDKSENVQD LLLLDVTPLS
410 420 430 440 450
LGIETAGGVM TVLIKRNTTI PTKQTQTFTT YSDNQPGVLI QVYEGERAMT
460 470 480 490 500
KDNNLLGKFE LTGIPPAPRG VPQIEVTFDI DANGILNVSA VDKSTGKENK
510 520 530 540 550
ITITNDKGRL SKEDIERMVQ EAEKYKAEDE KQRDKVSSKN SLESYAFNMK
560 570 580 590 600
ATVEDEKLQG KINDEDKQKI LDKCNEIINW LDKNQTAEKE EFEHQQKELE
610 620 630 640 650
KVCNPIITKL YQSAGGMPGG MPGGMPGGFP GGGAPPSGGA SSGPTIEEVD
Length:650
Mass (Da):71,241
Last modified:May 29, 2007 - v2
Checksum:iFBE109C14A28B925
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti180A → T in AAI05183 (Ref. 3) Curated1
Sequence conflicti543E → K in CAA37422 (PubMed:2216746).Curated1
Sequence conflicti543E → K in CAA37823 (PubMed:2216746).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X53827 mRNA. Translation: CAA37823.1.
X53335 mRNA. Translation: CAA37422.1.
BT030487 mRNA. Translation: ABQ12927.1.
BC105182 mRNA. Translation: AAI05183.1.
PIRiS11456.
RefSeqiNP_776770.2. NM_174345.4.
UniGeneiBt.12309.

Genome annotation databases

EnsembliENSBTAT00000017497; ENSBTAP00000017497; ENSBTAG00000013162.
GeneIDi281831.
KEGGibta:281831.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X53827 mRNA. Translation: CAA37823.1.
X53335 mRNA. Translation: CAA37422.1.
BT030487 mRNA. Translation: ABQ12927.1.
BC105182 mRNA. Translation: AAI05183.1.
PIRiS11456.
RefSeqiNP_776770.2. NM_174345.4.
UniGeneiBt.12309.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
ProteinModelPortaliP19120.
SMRiP19120.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi159144. 2 interactors.
DIPiDIP-35481N.
IntActiP19120. 6 interactors.
MINTiMINT-157582.
STRINGi9913.ENSBTAP00000017497.

Chemistry databases

BindingDBiP19120.
ChEMBLiCHEMBL1275213.

Proteomic databases

PaxDbiP19120.
PeptideAtlasiP19120.
PRIDEiP19120.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000017497; ENSBTAP00000017497; ENSBTAG00000013162.
GeneIDi281831.
KEGGibta:281831.

Organism-specific databases

CTDi3312.

Phylogenomic databases

eggNOGiKOG0101. Eukaryota.
COG0443. LUCA.
GeneTreeiENSGT00820000127001.
HOGENOMiHOG000228135.
HOVERGENiHBG051845.
InParanoidiP19120.
KOiK03283.
OMAiCFNIKST.
OrthoDBiEOG091G03SF.
TreeFamiTF105042.

Enzyme and pathway databases

ReactomeiR-BTA-3371453. Regulation of HSF1-mediated heat shock response.
R-BTA-3371568. Attenuation phase.
R-BTA-3371571. HSF1-dependent transactivation.
R-BTA-450408. AUF1 (hnRNP D0) binds and destabilizes mRNA.
R-BTA-6798695. Neutrophil degranulation.
R-BTA-72163. mRNA Splicing - Major Pathway.
R-BTA-8856828. Clathrin-mediated endocytosis.

Miscellaneous databases

EvolutionaryTraceiP19120.
PROiP19120.

Gene expression databases

BgeeiENSBTAG00000013162.

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.
PROSITEiPS00297. HSP70_1. 1 hit.
PS00329. HSP70_2. 1 hit.
PS01036. HSP70_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiHSP7C_BOVIN
AccessioniPrimary (citable) accession number: P19120
Secondary accession number(s): A5D968, Q3MHM4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: May 29, 2007
Last modified: November 30, 2016
This is version 157 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.