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UniProtKB - P11142 (HSP7C_HUMAN)

Protein

Heat shock cognate 71 kDa protein

Gene

HSPA8

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. Plays a pivotal role in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation (PubMed:21150129, PubMed:21148293, PubMed:24732912, PubMed:27916661, PubMed:23018488). This is achieved through cycles of ATP binding, ATP hydrolysis and ADP release, mediated by co-chaperones (PubMed:21150129, PubMed:21148293, PubMed:24732912, PubMed:27916661, PubMed:23018488). The co-chaperones have been shown to not only regulate different steps of the ATPase cycle of HSP70, but they also have an individual specificity such that one co-chaperone may promote folding of a substrate while another may promote degradation (PubMed:21150129, PubMed:21148293, PubMed:24732912, PubMed:27916661, PubMed:23018488). The affinity of HSP70 for polypeptides is regulated by its nucleotide bound state. In the ATP-bound form, it has a low affinity for substrate proteins. However, upon hydrolysis of the ATP to ADP, it undergoes a conformational change that increases its affinity for substrate proteins. HSP70 goes through repeated cycles of ATP hydrolysis and nucleotide exchange, which permits cycles of substrate binding and release. The HSP70-associated co-chaperones are of three types: J-domain co-chaperones HSP40s (stimulate ATPase hydrolysis by HSP70), the nucleotide exchange factors (NEF) such as BAG1/2/3 (facilitate conversion of HSP70 from the ADP-bound to the ATP-bound state thereby promoting substrate release), and the TPR domain chaperones such as HOPX and STUB1 (PubMed:24318877, PubMed:27474739, PubMed:24121476, PubMed:26865365). Acts as a repressor of transcriptional activation. Inhibits the transcriptional coactivator activity of CITED1 on Smad-mediated transcription. 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) and mediates LPS-induced inflammatory response, including TNF secretion by monocytes (PubMed:10722728, PubMed:11276205). Participates in the ER-associated degradation (ERAD) quality control pathway in conjunction with J domain-containing co-chaperones and the E3 ligase STUB1 (PubMed:23990462).2 Publications10 Publications

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

View the complete GO annotation on QuickGO ...

GO - Biological processi

View the complete GO annotation on QuickGO ...

Keywordsi

Molecular functionChaperone, Repressor
Biological processHost-virus interaction, mRNA processing, mRNA splicing, Stress response, Transcription, Transcription regulation
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi3.6.3.51 2681
ReactomeiR-HSA-3371453 Regulation of HSF1-mediated heat shock response
R-HSA-3371497 HSP90 chaperone cycle for steroid hormone receptors (SHR)
R-HSA-3371568 Attenuation phase
R-HSA-3371571 HSF1-dependent transactivation
R-HSA-432720 Lysosome Vesicle Biogenesis
R-HSA-432722 Golgi Associated Vesicle Biogenesis
R-HSA-447041 CHL1 interactions
R-HSA-450408 AUF1 (hnRNP D0) binds and destabilizes mRNA
R-HSA-6785807 Interleukin-4 and Interleukin-13 signaling
R-HSA-6798695 Neutrophil degranulation
R-HSA-72163 mRNA Splicing - Major Pathway
R-HSA-8856828 Clathrin-mediated endocytosis
R-HSA-8876725 Protein methylation
R-HSA-888590 GABA synthesis, release, reuptake and degradation
SIGNORiP11142

Protein family/group databases

MoonDBiP11142 Predicted

Names & Taxonomyi

Protein namesi
Recommended name:
Heat shock cognate 71 kDa protein
Alternative name(s):
Heat shock 70 kDa protein 8
Lipopolysaccharide-associated protein 1
Short name:
LAP-1
Short name:
LPS-associated protein 1
Gene namesi
Name:HSPA8
Synonyms:HSC70, HSP73, HSPA10
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
Proteomesi
  • UP000005640 Componenti: Chromosome 11

Organism-specific databases

EuPathDBiHostDB:ENSG00000109971.13
HGNCiHGNC:5241 HSPA8
MIMi600816 gene
neXtProtiNX_P11142

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane, Nucleus, Spliceosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi561K → R: Complete loss of in vitro methylation by METTL21A. 2 Publications1

Organism-specific databases

DisGeNETi3312
OpenTargetsiENSG00000109971
PharmGKBiPA29507

Chemistry databases

ChEMBLiCHEMBL1275223

Polymorphism and mutation databases

DMDMi123648

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources2 Publications
ChainiPRO_00000782702 – 646Heat shock cognate 71 kDa proteinAdd BLAST645

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineCombined sources2 Publications1
Modified residuei108N6-acetyllysineBy similarity1
Modified residuei153PhosphoserineCombined sources1
Modified residuei246N6-acetyllysineCombined sources1
Modified residuei319N6-acetyllysine; alternateCombined sources1
Modified residuei319N6-succinyllysine; alternateBy similarity1
Modified residuei328N6-acetyllysineBy similarity1
Modified residuei329PhosphoserineCombined sources1
Modified residuei362PhosphoserineCombined sources1
Modified residuei469Omega-N-methylarginineCombined sources1
Modified residuei512N6-acetyllysine; alternateBy similarity1
Modified residuei512N6-succinyllysine; alternateBy similarity1
Cross-linki512Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateCombined sources
Cross-linki512Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Modified residuei524N6-acetyllysineBy similarity1
Modified residuei541PhosphoserineCombined sources1
Modified residuei561N6,N6,N6-trimethyllysine; by METTL21A; alternate2 Publications1
Modified residuei561N6,N6-dimethyllysine; alternateCombined sources1
Modified residuei589N6-acetyllysineCombined sources1
Modified residuei597N6-acetyllysineCombined sources1
Modified residuei601N6-acetyllysineCombined sources1

Post-translational modificationi

Acetylated.2 Publications
ISGylated.2 Publications
Trimethylation at Lys-561 reduces fibrillar SNCA binding.

Keywords - PTMi

Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP11142
PaxDbiP11142
PeptideAtlasiP11142
PRIDEiP11142
ProteomicsDBi52698
52699 [P11142-2]
TopDownProteomicsiP11142-1 [P11142-1]
P11142-2 [P11142-2]

2D gel databases

DOSAC-COBS-2DPAGEiP11142
OGPiP11142
REPRODUCTION-2DPAGEiIPI00003865
SWISS-2DPAGEiP11142
UCD-2DPAGEiP11142

PTM databases

GlyConnecti1299
iPTMnetiP11142
PhosphoSitePlusiP11142
SwissPalmiP11142

Miscellaneous databases

PMAP-CutDBiP11142

Expressioni

Tissue specificityi

Ubiquitous.1 Publication

Inductioni

Constitutively synthesized.

Gene expression databases

BgeeiENSG00000109971 Expressed in 91 organ(s), highest expression level in frontal cortex
CleanExiHS_HSPA8
ExpressionAtlasiP11142 baseline and differential
GenevisibleiP11142 HS

Organism-specific databases

HPAiCAB002056
HPA052504

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. Interacts with DNAJB12 (via J domain) (PubMed:21150129, PubMed:21148293, PubMed:24732912, PubMed:27916661). Interacts with DNAJB14 (via J domain) (PubMed:23018488, PubMed:24732912, PubMed:27916661). 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. Interacts with METTL21A. Following LPS binding, may form a complex with CXCR4, GDF5 and HSP90AA1. Interacts with PRKN. Interacts with FOXP3. Interacts with DNAJC9 (via J domain) (PubMed:17182002). Interacts with MLLT11 (PubMed:24880125). Interacts with RNF207 (PubMed:25281747). Interacts with DNAJC21 (PubMed:27346687). Interacts with DNAJB2 (PubMed:15936278). Interacts with TTC1 (via TPR repeats) (PubMed:15708368). Interacts with SGTA (via TPR repeats) (By similarity). Interacts with HSF1 (via transactivation domain) (PubMed:9499401). Interacts with HOPX, HSP40 and HSP90 (PubMed:27708256). Interacts with STUB1 (PubMed:27708256). Interacts with BAG2 (PubMed:24318877). Interacts with BAG3 (PubMed:27474739, PubMed:24318877). Interacts with DNAJC12 (PubMed:24122553). Interacts with ZMYND10 (PubMed:29601588). Interacts with HSPC138 (PubMed:25760597).By similarity33 Publications
(Microbial infection) Interacts with SV40 VP1.1 Publication

Binary interactionsi

GO - Molecular functioni

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridi109544, 575 interactors
CORUMiP11142
DIPiDIP-32874N
IntActiP11142, 219 interactors
MINTiP11142
STRINGi9606.ENSP00000227378

Chemistry databases

BindingDBiP11142

Structurei

Secondary structure

1646
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliP11142
SMRiP11142
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP11142

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni2 – 386Nucleotide-binding domain (NBD)1 PublicationAdd BLAST385
Regioni186 – 377Interaction with BAG1Add BLAST192
Regioni394 – 509Substrate-binding domain (SBD)1 PublicationAdd BLAST116

Domaini

The N-terminal nucleotide binding domain (NBD) (also known as the ATPase domain) is responsible for binding and hydrolyzing ATP. The C-terminal substrate-binding domain (SBD) (also known as peptide-binding domain) binds to the client/substrate proteins. The two domains are allosterically coupled so that, when ATP is bound to the NBD, the SBD binds relatively weakly to clients. When ADP is bound in the NBD, a conformational change enhances the affinity of the SBD for client proteins.1 Publication

Sequence similaritiesi

Belongs to the heat shock protein 70 family.Curated

Phylogenomic databases

eggNOGiKOG0101 Eukaryota
COG0443 LUCA
GeneTreeiENSGT00910000144045
HOGENOMiHOG000228135
HOVERGENiHBG051845
InParanoidiP11142
KOiK03283
OMAiAYTKNQD
OrthoDBiEOG091G03SF
PhylomeDBiP11142
TreeFamiTF105042

Family and domain databases

Gene3Di1.20.1270.10, 1 hit
2.60.34.10, 1 hit
InterProiView protein in InterPro
IPR018181 Heat_shock_70_CS
IPR029048 HSP70_C_sf
IPR029047 HSP70_peptide-bd_sf
IPR013126 Hsp_70_fam
PANTHERiPTHR19375 PTHR19375, 1 hit
PfamiView protein in Pfam
PF00012 HSP70, 1 hit
PRINTSiPR00301 HEATSHOCK70
SUPFAMiSSF100920 SSF100920, 1 hit
SSF100934 SSF100934, 1 hit
PROSITEiView protein in PROSITE
PS00297 HSP70_1, 1 hit
PS00329 HSP70_2, 1 hit
PS01036 HSP70_3, 1 hit

Sequences (2+)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 2 described isoforms and 13 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: P11142-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« 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 
KVCNPIITKL YQSAGGMPGG MPGGFPGGGA PPSGGASSGP TIEEVD
Length:646
Mass (Da):70,898
Last modified:July 1, 1989 - v1
Checksum:i9AA27B210730670C
GO
Isoform 2 (identifier: P11142-2) [UniParc]FASTAAdd to basket
Also known as: HSC54

The sequence of this isoform differs from the canonical sequence as follows:
     464-616: Missing.

Show »
Length:493
Mass (Da):53,518
Checksum:iBA2CFBD68F17784E
GO

Computationally mapped potential isoform sequencesi

There are 13 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A8K7Q2A8K7Q2_HUMAN
Heat shock cognate 71 kDa protein
HSPA8
410Annotation score:
E9PKE3E9PKE3_HUMAN
Heat shock cognate 71 kDa protein
HSPA8
627Annotation score:
E9PNE6E9PNE6_HUMAN
Heat shock cognate 71 kDa protein
HSPA8
500Annotation score:
E9PN89E9PN89_HUMAN
Heat shock cognate 71 kDa protein
HSPA8
312Annotation score:
E9PLF4E9PLF4_HUMAN
Heat shock cognate 71 kDa protein
HSPA8
187Annotation score:
E9PPY6E9PPY6_HUMAN
Heat shock cognate 71 kDa protein
HSPA8
137Annotation score:
E9PN25E9PN25_HUMAN
Heat shock cognate 71 kDa protein
HSPA8
132Annotation score:
E9PQQ4E9PQQ4_HUMAN
Heat shock cognate 71 kDa protein
HSPA8
171Annotation score:
E9PK54E9PK54_HUMAN
Heat shock cognate 71 kDa protein
HSPA8
183Annotation score:
E9PQK7E9PQK7_HUMAN
Heat shock cognate 71 kDa protein
HSPA8
178Annotation score:
There are more potential isoformsShow all

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_04961932D → Y. Corresponds to variant dbSNP:rs11551602Ensembl.1
Natural variantiVAR_049620459F → L. Corresponds to variant dbSNP:rs11551598Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_002427464 – 616Missing in isoform 2. 1 PublicationAdd BLAST153

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y00371 Genomic DNA Translation: CAA68445.1
AB034951 mRNA Translation: BAB18615.1
AF352832 mRNA Translation: AAK17898.1
BC016179 mRNA Translation: AAH16179.1
BC016660 mRNA Translation: AAH16660.1
BC019816 mRNA Translation: AAH19816.1
CCDSiCCDS44754.1 [P11142-2]
CCDS8440.1 [P11142-1]
PIRiA27077
RefSeqiNP_006588.1, NM_006597.5 [P11142-1]
NP_694881.1, NM_153201.3 [P11142-2]
XP_011541100.1, XM_011542798.1 [P11142-1]
UniGeneiHs.180414

Genome annotation databases

EnsembliENST00000227378; ENSP00000227378; ENSG00000109971 [P11142-1]
ENST00000453788; ENSP00000404372; ENSG00000109971 [P11142-2]
ENST00000532636; ENSP00000437125; ENSG00000109971 [P11142-1]
ENST00000534624; ENSP00000432083; ENSG00000109971 [P11142-1]
GeneIDi3312
KEGGihsa:3312
UCSCiuc001pyp.5 human [P11142-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y00371 Genomic DNA Translation: CAA68445.1
AB034951 mRNA Translation: BAB18615.1
AF352832 mRNA Translation: AAK17898.1
BC016179 mRNA Translation: AAH16179.1
BC016660 mRNA Translation: AAH16660.1
BC019816 mRNA Translation: AAH19816.1
CCDSiCCDS44754.1 [P11142-2]
CCDS8440.1 [P11142-1]
PIRiA27077
RefSeqiNP_006588.1, NM_006597.5 [P11142-1]
NP_694881.1, NM_153201.3 [P11142-2]
XP_011541100.1, XM_011542798.1 [P11142-1]
UniGeneiHs.180414

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3AGYX-ray1.85C/D/F639-646[»]
3AGZX-ray2.51C/D/E/F639-646[»]
3ESKX-ray2.05B635-646[»]
3FZFX-ray2.20A4-381[»]
3FZHX-ray2.00A4-381[»]
3FZKX-ray2.10A4-381[»]
3FZLX-ray2.20A4-381[»]
3FZMX-ray2.30A4-381[»]
3LDQX-ray1.90A4-381[»]
3M3ZX-ray2.10A4-381[»]
4H5NX-ray1.86A/B2-384[»]
4H5RX-ray1.64A/B2-384[»]
4H5TX-ray1.90A2-384[»]
4H5VX-ray1.75A2-384[»]
4H5WX-ray1.94A/B2-384[»]
4HWIX-ray2.27A5-381[»]
4KBQX-ray2.91C/D541-646[»]
5AQFX-ray1.88A/C1-381[»]
5AQGX-ray2.24A/C/E1-381[»]
5AQHX-ray2.00A1-381[»]
5AQIX-ray1.98A/C1-381[»]
5AQJX-ray1.96A/C/E1-381[»]
5AQKX-ray2.09A1-381[»]
5AQLX-ray1.69A/C1-381[»]
5AQMX-ray1.63A/C1-381[»]
5AQNX-ray2.45A/C/E1-381[»]
5AQOX-ray2.12A/C/E1-381[»]
5AQPX-ray2.08A/C/E1-381[»]
5AQQX-ray2.72A/C/E1-381[»]
5AQRX-ray1.91A/C/E1-381[»]
5AQSX-ray2.00A/C1-381[»]
5AQTX-ray1.90A1-381[»]
5AQUX-ray1.92A1-381[»]
5AQVX-ray1.75A1-381[»]
6B1IX-ray2.30A/B5-381[»]
6B1MX-ray1.90A/B5-381[»]
6B1NX-ray1.80A/B5-381[»]
ProteinModelPortaliP11142
SMRiP11142
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109544, 575 interactors
CORUMiP11142
DIPiDIP-32874N
IntActiP11142, 219 interactors
MINTiP11142
STRINGi9606.ENSP00000227378

Chemistry databases

BindingDBiP11142
ChEMBLiCHEMBL1275223

Protein family/group databases

MoonDBiP11142 Predicted

PTM databases

GlyConnecti1299
iPTMnetiP11142
PhosphoSitePlusiP11142
SwissPalmiP11142

Polymorphism and mutation databases

DMDMi123648

2D gel databases

DOSAC-COBS-2DPAGEiP11142
OGPiP11142
REPRODUCTION-2DPAGEiIPI00003865
SWISS-2DPAGEiP11142
UCD-2DPAGEiP11142

Proteomic databases

EPDiP11142
PaxDbiP11142
PeptideAtlasiP11142
PRIDEiP11142
ProteomicsDBi52698
52699 [P11142-2]
TopDownProteomicsiP11142-1 [P11142-1]
P11142-2 [P11142-2]

Protocols and materials databases

DNASUi3312
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000227378; ENSP00000227378; ENSG00000109971 [P11142-1]
ENST00000453788; ENSP00000404372; ENSG00000109971 [P11142-2]
ENST00000532636; ENSP00000437125; ENSG00000109971 [P11142-1]
ENST00000534624; ENSP00000432083; ENSG00000109971 [P11142-1]
GeneIDi3312
KEGGihsa:3312
UCSCiuc001pyp.5 human [P11142-1]

Organism-specific databases

CTDi3312
DisGeNETi3312
EuPathDBiHostDB:ENSG00000109971.13
GeneCardsiHSPA8
H-InvDBiHIX0033867
HGNCiHGNC:5241 HSPA8
HPAiCAB002056
HPA052504
MIMi600816 gene
neXtProtiNX_P11142
OpenTargetsiENSG00000109971
PharmGKBiPA29507
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0101 Eukaryota
COG0443 LUCA
GeneTreeiENSGT00910000144045
HOGENOMiHOG000228135
HOVERGENiHBG051845
InParanoidiP11142
KOiK03283
OMAiAYTKNQD
OrthoDBiEOG091G03SF
PhylomeDBiP11142
TreeFamiTF105042

Enzyme and pathway databases

BRENDAi3.6.3.51 2681
ReactomeiR-HSA-3371453 Regulation of HSF1-mediated heat shock response
R-HSA-3371497 HSP90 chaperone cycle for steroid hormone receptors (SHR)
R-HSA-3371568 Attenuation phase
R-HSA-3371571 HSF1-dependent transactivation
R-HSA-432720 Lysosome Vesicle Biogenesis
R-HSA-432722 Golgi Associated Vesicle Biogenesis
R-HSA-447041 CHL1 interactions
R-HSA-450408 AUF1 (hnRNP D0) binds and destabilizes mRNA
R-HSA-6785807 Interleukin-4 and Interleukin-13 signaling
R-HSA-6798695 Neutrophil degranulation
R-HSA-72163 mRNA Splicing - Major Pathway
R-HSA-8856828 Clathrin-mediated endocytosis
R-HSA-8876725 Protein methylation
R-HSA-888590 GABA synthesis, release, reuptake and degradation
SIGNORiP11142

Miscellaneous databases

ChiTaRSiHSPA8 human
EvolutionaryTraceiP11142
GeneWikiiHSPA8
GenomeRNAii3312
PMAP-CutDBiP11142
PROiPR:P11142
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000109971 Expressed in 91 organ(s), highest expression level in frontal cortex
CleanExiHS_HSPA8
ExpressionAtlasiP11142 baseline and differential
GenevisibleiP11142 HS

Family and domain databases

Gene3Di1.20.1270.10, 1 hit
2.60.34.10, 1 hit
InterProiView protein in InterPro
IPR018181 Heat_shock_70_CS
IPR029048 HSP70_C_sf
IPR029047 HSP70_peptide-bd_sf
IPR013126 Hsp_70_fam
PANTHERiPTHR19375 PTHR19375, 1 hit
PfamiView protein in Pfam
PF00012 HSP70, 1 hit
PRINTSiPR00301 HEATSHOCK70
SUPFAMiSSF100920 SSF100920, 1 hit
SSF100934 SSF100934, 1 hit
PROSITEiView protein in PROSITE
PS00297 HSP70_1, 1 hit
PS00329 HSP70_2, 1 hit
PS01036 HSP70_3, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiHSP7C_HUMAN
AccessioniPrimary (citable) accession number: P11142
Secondary accession number(s): Q9H3R6
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: October 10, 2018
This is version 226 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  4. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  5. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  6. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
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