UniProtKB - P11142 (HSP7C_HUMAN)
Heat shock cognate 71 kDa protein
HSPA8
Functioni
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 71 | ATP | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 12 – 15 | ATP | 4 | |
Nucleotide bindingi | 202 – 204 | ATP | 3 | |
Nucleotide bindingi | 268 – 275 | ATP | 8 | |
Nucleotide bindingi | 339 – 342 | ATP | 4 |
GO - Molecular functioni
- ATPase activity Source: BHF-UCL
- ATP binding Source: BHF-UCL
- C3HC4-type RING finger domain binding Source: BHF-UCL
- cadherin binding Source: BHF-UCL
- chaperone binding Source: ARUK-UCL
- clathrin-uncoating ATPase activity Source: GO_Central
- enzyme binding Source: BHF-UCL
- G protein-coupled receptor binding Source: ParkinsonsUK-UCL
- heat shock protein binding Source: UniProtKB
- MHC class II protein complex binding Source: UniProtKB
- misfolded protein binding Source: GO_Central
- phosphatidylserine binding Source: Ensembl
- protein folding chaperone Source: GO_Central
- protein-macromolecule adaptor activity Source: ARUK-UCL
- RNA binding Source: UniProtKB
- ubiquitin protein ligase binding Source: ParkinsonsUK-UCL
- unfolded protein binding Source: UniProtKB
GO - Biological processi
- ATP metabolic process Source: BHF-UCL
- axo-dendritic transport Source: GO_Central
- cellular response to starvation Source: ParkinsonsUK-UCL
- cellular response to unfolded protein Source: GO_Central
- chaperone cofactor-dependent protein refolding Source: GO_Central
- chaperone-mediated autophagy Source: ParkinsonsUK-UCL
- chaperone-mediated autophagy translocation complex disassembly Source: ParkinsonsUK-UCL
- chaperone-mediated protein transport involved in chaperone-mediated autophagy Source: GO_Central
- cytokine-mediated signaling pathway Source: Reactome
- late endosomal microautophagy Source: GO_Central
- membrane organization Source: Reactome
- mRNA splicing, via spliceosome Source: Reactome
- negative regulation of supramolecular fiber organization Source: BHF-UCL
- negative regulation of transcription, DNA-templated Source: UniProtKB
- neurotransmitter secretion Source: Reactome
- neutrophil degranulation Source: Reactome
- positive regulation by host of viral genome replication Source: Ensembl
- positive regulation of mRNA splicing, via spliceosome Source: Ensembl
- protein folding Source: UniProtKB
- protein refolding Source: UniProtKB
- protein targeting to lysosome involved in chaperone-mediated autophagy Source: ParkinsonsUK-UCL
- regulation of cell cycle Source: Ensembl
- regulation of cellular response to heat Source: Reactome
- regulation of mRNA stability Source: Reactome
- regulation of postsynapse organization Source: Ensembl
- regulation of protein complex stability Source: ParkinsonsUK-UCL
- regulation of protein-containing complex assembly Source: ParkinsonsUK-UCL
- regulation of protein import Source: ParkinsonsUK-UCL
- regulation of protein stability Source: ParkinsonsUK-UCL
- response to unfolded protein Source: GO_Central
- slow axonal transport Source: GO_Central
- vesicle-mediated transport Source: GO_Central
- viral process Source: UniProtKB-KW
Keywordsi
Molecular function | Chaperone, Repressor |
Biological process | Host-virus interaction, mRNA processing, mRNA splicing, Stress response, Transcription, Transcription regulation |
Ligand | ATP-binding, Nucleotide-binding |
Enzyme and pathway databases
BRENDAi | 3.6.3.51, 2681 |
PathwayCommonsi | P11142 |
Reactomei | R-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 R-HSA-9613354, Lipophagy R-HSA-9613829, Chaperone Mediated Autophagy R-HSA-9615710, Late endosomal microautophagy |
SIGNORi | P11142 |
Protein family/group databases
MoonDBi | P11142, Predicted |
Names & Taxonomyi
Protein namesi | Recommended name: Heat shock cognate 71 kDa proteinAlternative 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 |
Organismi | Homo sapiens (Human) |
Taxonomic identifieri | 9606 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Proteomesi |
|
Organism-specific databases
EuPathDBi | HostDB:ENSG00000109971.13 |
HGNCi | HGNC:5241, HSPA8 |
MIMi | 600816, gene |
neXtProti | NX_P11142 |
Subcellular locationi
Plasma membrane
Nucleus
Other locations
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.
Cytosol
- cytosol Source: UniProtKB
- postsynaptic cytosol Source: GO_Central
- presynaptic cytosol Source: GO_Central
Endosome
- late endosome Source: Ensembl
Extracellular region or secreted
- blood microparticle Source: UniProtKB
- extracellular exosome Source: UniProtKB
- extracellular region Source: Reactome
- extracellular space Source: UniProtKB
Lysosome
- lumenal side of lysosomal membrane Source: ParkinsonsUK-UCL
- lysosomal lumen Source: ParkinsonsUK-UCL
- lysosomal membrane Source: ParkinsonsUK-UCL
- lysosome Source: GO_Central
Nucleus
- nucleolus Source: UniProtKB-SubCell
- nucleoplasm Source: Reactome
- nucleus Source: UniProtKB
- spliceosomal complex Source: UniProtKB-KW
Plasma Membrane
- plasma membrane Source: GO_Central
Other locations
- autophagosome Source: GO_Central
- axon Source: GO_Central
- chaperone complex Source: ARUK-UCL
- clathrin-sculpted gamma-aminobutyric acid transport vesicle membrane Source: Reactome
- cytoplasm Source: GO_Central
- dendrite Source: GO_Central
- ficolin-1-rich granule lumen Source: Reactome
- focal adhesion Source: UniProtKB
- glutamatergic synapse Source: Ensembl
- melanosome Source: UniProtKB-SubCell
- membrane Source: UniProtKB
- perinuclear region of cytoplasm Source: Ensembl
- photoreceptor ribbon synapse Source: Ensembl
- Prp19 complex Source: UniProtKB
- ribonucleoprotein complex Source: UniProtKB
- secretory granule lumen Source: Reactome
- terminal bouton Source: GO_Central
Keywords - Cellular componenti
Cell membrane, Cytoplasm, Membrane, Nucleus, SpliceosomePathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 561 | K → R: Complete loss of in vitro methylation by METTL21A. 2 Publications | 1 |
Organism-specific databases
DisGeNETi | 3312 |
OpenTargetsi | ENSG00000109971 |
PharmGKBi | PA29507 |
Miscellaneous databases
Pharosi | P11142, Tchem |
Chemistry databases
ChEMBLi | CHEMBL1275223 |
DrugBanki | DB07045, (2R,3R,4S,5R)-2-[6-amino-8-[(3,4-dichlorophenyl)methylamino]purin-9-yl]-5-(hydroxymethyl)oxolane-3,4-diol DB11638, Artenimol DB09130, Copper DB01254, Dasatinib |
DrugCentrali | P11142 |
Polymorphism and mutation databases
BioMutai | HSPA8 |
DMDMi | 123648 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Initiator methioninei | RemovedCombined sources2 Publications | |||
ChainiPRO_0000078270 | 2 – 646 | Heat shock cognate 71 kDa proteinAdd BLAST | 645 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 2 | N-acetylserineCombined sources2 Publications | 1 | |
Modified residuei | 108 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 153 | PhosphoserineCombined sources | 1 | |
Modified residuei | 246 | N6-acetyllysineCombined sources | 1 | |
Modified residuei | 319 | N6-acetyllysine; alternateCombined sources | 1 | |
Modified residuei | 319 | N6-succinyllysine; alternateBy similarity | 1 | |
Modified residuei | 328 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 329 | PhosphoserineCombined sources | 1 | |
Modified residuei | 362 | PhosphoserineCombined sources | 1 | |
Modified residuei | 469 | Omega-N-methylarginineCombined sources | 1 | |
Modified residuei | 512 | N6-acetyllysine; alternateBy similarity | 1 | |
Modified residuei | 512 | N6-succinyllysine; alternateBy similarity | 1 | |
Cross-linki | 512 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateCombined sources | ||
Cross-linki | 512 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources | ||
Modified residuei | 524 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 541 | PhosphoserineCombined sources | 1 | |
Modified residuei | 561 | N6,N6,N6-trimethyllysine; by METTL21A; alternate2 Publications | 1 | |
Modified residuei | 561 | N6,N6-dimethyllysine; alternateCombined sources | 1 | |
Modified residuei | 589 | N6-acetyllysineCombined sources | 1 | |
Modified residuei | 597 | N6-acetyllysineCombined sources | 1 | |
Modified residuei | 601 | N6-acetyllysineCombined sources | 1 |
Post-translational modificationi
Keywords - PTMi
Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugationProteomic databases
EPDi | P11142 |
jPOSTi | P11142 |
MassIVEi | P11142 |
PaxDbi | P11142 |
PeptideAtlasi | P11142 |
PRIDEi | P11142 |
ProteomicsDBi | 52698 [P11142-1] 52699 [P11142-2] |
TopDownProteomicsi | P11142-1 [P11142-1] P11142-2 [P11142-2] |
2D gel databases
DOSAC-COBS-2DPAGEi | P11142 |
OGPi | P11142 |
REPRODUCTION-2DPAGEi | IPI00003865 |
SWISS-2DPAGEi | P11142 |
UCD-2DPAGEi | P11142 |
PTM databases
GlyConnecti | 1299, 1 N-Linked glycan (1 site) |
GlyGeni | P11142, 1 site |
iPTMneti | P11142 |
MetOSitei | P11142 |
PhosphoSitePlusi | P11142 |
SwissPalmi | P11142 |
Expressioni
Tissue specificityi
Inductioni
Gene expression databases
Bgeei | ENSG00000109971, Expressed in frontal cortex and 116 other tissues |
ExpressionAtlasi | P11142, baseline and differential |
Genevisiblei | P11142, HS |
Organism-specific databases
HPAi | ENSG00000109971, Low tissue specificity |
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).
Interacts with BCL2L1, GIMAP5 and MCL1; the interaction with BCL2L1 or MCL1 is impaired in the absence of GIMAP5 (By similarity).
Interacts with NLPR12 (PubMed:17947705).
Interacts with TTC4 (PubMed:18320024).
By similarity35 Publications(Microbial infection) Interacts with SV40 VP1.
1 PublicationBinary interactionsi
Hide detailsP11142
Isoform 1 [P11142-1]
With | #Exp. | IntAct |
---|---|---|
STUB1 - isoform 1 [Q9UNE7-1] | 4 | EBI-351908,EBI-15687717 |
GO - Molecular functioni
- C3HC4-type RING finger domain binding Source: BHF-UCL
- cadherin binding Source: BHF-UCL
- chaperone binding Source: ARUK-UCL
- enzyme binding Source: BHF-UCL
- G protein-coupled receptor binding Source: ParkinsonsUK-UCL
- heat shock protein binding Source: UniProtKB
- misfolded protein binding Source: GO_Central
- ubiquitin protein ligase binding Source: ParkinsonsUK-UCL
- unfolded protein binding Source: UniProtKB
Protein-protein interaction databases
BioGRIDi | 109544, 907 interactors |
ComplexPortali | CPX-5824, PRP19-CDC5L complex |
CORUMi | P11142 |
DIPi | DIP-32874N |
IntActi | P11142, 476 interactors |
MINTi | P11142 |
STRINGi | 9606.ENSP00000432083 |
Chemistry databases
BindingDBi | P11142 |
Miscellaneous databases
RNActi | P11142, protein |
Structurei
Secondary structure
3D structure databases
BMRBi | P11142 |
SMRi | P11142 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P11142 |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 2 – 386 | Nucleotide-binding domain (NBD)1 PublicationAdd BLAST | 385 | |
Regioni | 186 – 377 | Interaction with BAG1Add BLAST | 192 | |
Regioni | 394 – 509 | Substrate-binding domain (SBD)1 PublicationAdd BLAST | 116 |
Domaini
Sequence similaritiesi
Phylogenomic databases
eggNOGi | KOG0101, Eukaryota |
GeneTreei | ENSGT00950000183206 |
HOGENOMi | CLU_005965_3_0_1 |
InParanoidi | P11142 |
OMAi | IFREDRC |
PhylomeDBi | P11142 |
TreeFami | TF105042 |
Family and domain databases
Gene3Di | 1.20.1270.10, 1 hit 2.60.34.10, 1 hit |
IDEALi | IID00440 |
InterProi | View protein in InterPro IPR043129, ATPase_NBD IPR018181, Heat_shock_70_CS IPR029048, HSP70_C_sf IPR029047, HSP70_peptide-bd_sf IPR013126, Hsp_70_fam |
PANTHERi | PTHR19375, PTHR19375, 1 hit |
Pfami | View protein in Pfam PF00012, HSP70, 1 hit |
SUPFAMi | SSF100920, SSF100920, 1 hit SSF100934, SSF100934, 1 hit SSF53067, SSF53067, 2 hits |
PROSITEi | View protein in PROSITE PS00297, HSP70_1, 1 hit PS00329, HSP70_2, 1 hit PS01036, HSP70_3, 1 hit |
s (2+)i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
This entry describes 2 produced by isoformsialternative splicing. AlignAdd to basketThis entry has 2 described isoforms and 13 potential isoforms that are computationally mapped.Show allAlign All
This isoform has been chosen as the sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. canonicali
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
Computationally mapped potential isoform sequencesi
There are 13 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basketA8K7Q2 | A8K7Q2_HUMAN | Heat shock cognate 71 kDa protein | HSPA8 | 410 | Annotation score: | ||
E9PNE6 | E9PNE6_HUMAN | Heat shock cognate 71 kDa protein | HSPA8 | 500 | Annotation score: | ||
E9PKE3 | E9PKE3_HUMAN | Heat shock cognate 71 kDa protein | HSPA8 | 627 | Annotation score: | ||
E9PM13 | E9PM13_HUMAN | Heat shock cognate 71 kDa protein | HSPA8 | 150 | Annotation score: | ||
E9PS65 | E9PS65_HUMAN | Heat shock cognate 71 kDa protein | HSPA8 | 223 | Annotation score: | ||
E9PI65 | E9PI65_HUMAN | Heat shock cognate 71 kDa protein | HSPA8 | 168 | Annotation score: | ||
E9PN89 | E9PN89_HUMAN | Heat shock cognate 71 kDa protein | HSPA8 | 312 | Annotation score: | ||
E9PK54 | E9PK54_HUMAN | Heat shock cognate 71 kDa protein | HSPA8 | 183 | Annotation score: | ||
E9PLF4 | E9PLF4_HUMAN | Heat shock cognate 71 kDa protein | HSPA8 | 187 | Annotation score: | ||
E9PN25 | E9PN25_HUMAN | Heat shock cognate 71 kDa protein | HSPA8 | 132 | Annotation score: | ||
There are more potential isoformsShow all |
Natural variant
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural variantiVAR_049619 | 32 | D → Y. Corresponds to variant dbSNP:rs11551602Ensembl. | 1 | |
Natural variantiVAR_049620 | 459 | F → L. Corresponds to variant dbSNP:rs11551598Ensembl. | 1 |
Alternative sequence
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Alternative sequenceiVSP_002427 | 464 – 616 | Missing in isoform 2. 1 PublicationAdd BLAST | 153 |
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 |
CCDSi | CCDS44754.1 [P11142-2] CCDS8440.1 [P11142-1] |
PIRi | A27077 |
RefSeqi | NP_006588.1, NM_006597.5 [P11142-1] NP_694881.1, NM_153201.3 [P11142-2] XP_011541100.1, XM_011542798.1 [P11142-1] |
Genome annotation databases
Ensembli | ENST00000227378; ENSP00000227378; ENSG00000109971 [P11142-1] ENST00000453788; ENSP00000404372; ENSG00000109971 [P11142-2] ENST00000532636; ENSP00000437125; ENSG00000109971 [P11142-1] ENST00000534624; ENSP00000432083; ENSG00000109971 [P11142-1] |
GeneIDi | 3312 |
KEGGi | hsa:3312 |
UCSCi | uc001pyp.5, human [P11142-1] |
Keywords - Coding sequence diversityi
Alternative splicing, PolymorphismSimilar 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 |
CCDSi | CCDS44754.1 [P11142-2] CCDS8440.1 [P11142-1] |
PIRi | A27077 |
RefSeqi | NP_006588.1, NM_006597.5 [P11142-1] NP_694881.1, NM_153201.3 [P11142-2] XP_011541100.1, XM_011542798.1 [P11142-1] |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
3AGY | X-ray | 1.85 | C/D/F | 639-646 | [»] | |
3AGZ | X-ray | 2.51 | C/D/E/F | 639-646 | [»] | |
3ESK | X-ray | 2.05 | B | 635-646 | [»] | |
3FZF | X-ray | 2.20 | A | 4-381 | [»] | |
3FZH | X-ray | 2.00 | A | 4-381 | [»] | |
3FZK | X-ray | 2.10 | A | 4-381 | [»] | |
3FZL | X-ray | 2.20 | A | 4-381 | [»] | |
3FZM | X-ray | 2.30 | A | 4-381 | [»] | |
3LDQ | X-ray | 1.90 | A | 4-381 | [»] | |
3M3Z | X-ray | 2.10 | A | 4-381 | [»] | |
4H5N | X-ray | 1.86 | A/B | 2-384 | [»] | |
4H5R | X-ray | 1.64 | A/B | 2-384 | [»] | |
4H5T | X-ray | 1.90 | A | 2-384 | [»] | |
4H5V | X-ray | 1.75 | A | 2-384 | [»] | |
4H5W | X-ray | 1.94 | A/B | 2-384 | [»] | |
4HWI | X-ray | 2.27 | A | 5-381 | [»] | |
4KBQ | X-ray | 2.91 | C/D | 541-646 | [»] | |
5AQF | X-ray | 1.88 | A/C | 1-381 | [»] | |
5AQG | X-ray | 2.24 | A/C/E | 1-381 | [»] | |
5AQH | X-ray | 2.00 | A | 1-381 | [»] | |
5AQI | X-ray | 1.98 | A/C | 1-381 | [»] | |
5AQJ | X-ray | 1.96 | A/C/E | 1-381 | [»] | |
5AQK | X-ray | 2.09 | A | 1-381 | [»] | |
5AQL | X-ray | 1.69 | A/C | 1-381 | [»] | |
5AQM | X-ray | 1.63 | A/C | 1-381 | [»] | |
5AQN | X-ray | 2.45 | A/C/E | 1-381 | [»] | |
5AQO | X-ray | 2.12 | A/C/E | 1-381 | [»] | |
5AQP | X-ray | 2.08 | A/C/E | 1-381 | [»] | |
5AQQ | X-ray | 2.72 | A/C/E | 1-381 | [»] | |
5AQR | X-ray | 1.91 | A/C/E | 1-381 | [»] | |
5AQS | X-ray | 2.00 | A/C | 1-381 | [»] | |
5AQT | X-ray | 1.90 | A | 1-381 | [»] | |
5AQU | X-ray | 1.92 | A | 1-381 | [»] | |
5AQV | X-ray | 1.75 | A | 1-381 | [»] | |
6B1I | X-ray | 2.30 | A/B | 5-381 | [»] | |
6B1M | X-ray | 1.90 | A/B | 5-381 | [»] | |
6B1N | X-ray | 1.80 | A/B | 5-381 | [»] | |
BMRBi | P11142 | |||||
SMRi | P11142 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 109544, 907 interactors |
ComplexPortali | CPX-5824, PRP19-CDC5L complex |
CORUMi | P11142 |
DIPi | DIP-32874N |
IntActi | P11142, 476 interactors |
MINTi | P11142 |
STRINGi | 9606.ENSP00000432083 |
Chemistry databases
BindingDBi | P11142 |
ChEMBLi | CHEMBL1275223 |
DrugBanki | DB07045, (2R,3R,4S,5R)-2-[6-amino-8-[(3,4-dichlorophenyl)methylamino]purin-9-yl]-5-(hydroxymethyl)oxolane-3,4-diol DB11638, Artenimol DB09130, Copper DB01254, Dasatinib |
DrugCentrali | P11142 |
Protein family/group databases
MoonDBi | P11142, Predicted |
PTM databases
GlyConnecti | 1299, 1 N-Linked glycan (1 site) |
GlyGeni | P11142, 1 site |
iPTMneti | P11142 |
MetOSitei | P11142 |
PhosphoSitePlusi | P11142 |
SwissPalmi | P11142 |
Polymorphism and mutation databases
BioMutai | HSPA8 |
DMDMi | 123648 |
2D gel databases
DOSAC-COBS-2DPAGEi | P11142 |
OGPi | P11142 |
REPRODUCTION-2DPAGEi | IPI00003865 |
SWISS-2DPAGEi | P11142 |
UCD-2DPAGEi | P11142 |
Proteomic databases
EPDi | P11142 |
jPOSTi | P11142 |
MassIVEi | P11142 |
PaxDbi | P11142 |
PeptideAtlasi | P11142 |
PRIDEi | P11142 |
ProteomicsDBi | 52698 [P11142-1] 52699 [P11142-2] |
TopDownProteomicsi | P11142-1 [P11142-1] P11142-2 [P11142-2] |
Protocols and materials databases
Antibodypediai | 3675, 1105 antibodies |
DNASUi | 3312 |
Genome annotation databases
Ensembli | ENST00000227378; ENSP00000227378; ENSG00000109971 [P11142-1] ENST00000453788; ENSP00000404372; ENSG00000109971 [P11142-2] ENST00000532636; ENSP00000437125; ENSG00000109971 [P11142-1] ENST00000534624; ENSP00000432083; ENSG00000109971 [P11142-1] |
GeneIDi | 3312 |
KEGGi | hsa:3312 |
UCSCi | uc001pyp.5, human [P11142-1] |
Organism-specific databases
CTDi | 3312 |
DisGeNETi | 3312 |
EuPathDBi | HostDB:ENSG00000109971.13 |
GeneCardsi | HSPA8 |
HGNCi | HGNC:5241, HSPA8 |
HPAi | ENSG00000109971, Low tissue specificity |
MIMi | 600816, gene |
neXtProti | NX_P11142 |
OpenTargetsi | ENSG00000109971 |
PharmGKBi | PA29507 |
GenAtlasi | Search... |
Phylogenomic databases
eggNOGi | KOG0101, Eukaryota |
GeneTreei | ENSGT00950000183206 |
HOGENOMi | CLU_005965_3_0_1 |
InParanoidi | P11142 |
OMAi | IFREDRC |
PhylomeDBi | P11142 |
TreeFami | TF105042 |
Enzyme and pathway databases
BRENDAi | 3.6.3.51, 2681 |
PathwayCommonsi | P11142 |
Reactomei | R-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 R-HSA-9613354, Lipophagy R-HSA-9613829, Chaperone Mediated Autophagy R-HSA-9615710, Late endosomal microautophagy |
SIGNORi | P11142 |
Miscellaneous databases
BioGRID-ORCSi | 3312, 410 hits in 859 CRISPR screens |
ChiTaRSi | HSPA8, human |
EvolutionaryTracei | P11142 |
GeneWikii | HSPA8 |
GenomeRNAii | 3312 |
Pharosi | P11142, Tchem |
PROi | PR:P11142 |
RNActi | P11142, protein |
SOURCEi | Search... |
Gene expression databases
Bgeei | ENSG00000109971, Expressed in frontal cortex and 116 other tissues |
ExpressionAtlasi | P11142, baseline and differential |
Genevisiblei | P11142, HS |
Family and domain databases
Gene3Di | 1.20.1270.10, 1 hit 2.60.34.10, 1 hit |
IDEALi | IID00440 |
InterProi | View protein in InterPro IPR043129, ATPase_NBD IPR018181, Heat_shock_70_CS IPR029048, HSP70_C_sf IPR029047, HSP70_peptide-bd_sf IPR013126, Hsp_70_fam |
PANTHERi | PTHR19375, PTHR19375, 1 hit |
Pfami | View protein in Pfam PF00012, HSP70, 1 hit |
SUPFAMi | SSF100920, SSF100920, 1 hit SSF100934, SSF100934, 1 hit SSF53067, SSF53067, 2 hits |
PROSITEi | View protein in PROSITE PS00297, HSP70_1, 1 hit PS00329, HSP70_2, 1 hit PS01036, HSP70_3, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | HSP7C_HUMAN | |
Accessioni | P11142Primary (citable) accession number: P11142 Secondary accession number(s): Q9H3R6 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | July 1, 1989 |
Last sequence update: | July 1, 1989 | |
Last modified: | December 2, 2020 | |
This is version 245 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program | |
Disclaimer | Any 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, Direct protein sequencing, Reference proteomeDocuments
- Human polymorphisms and disease mutations
Index of human polymorphisms and disease mutations - MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families - Human chromosome 11
Human chromosome 11: entries, gene names and cross-references to MIM - Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or disease mutations