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Protein

Heat shock cognate 71 kDa protein

Gene

HSPA8

Organism
Homo sapiens (Human)
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. 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.3 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei71 – 711ATP

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi12 – 154ATP
Nucleotide bindingi202 – 2043ATP
Nucleotide bindingi268 – 2758ATP
Nucleotide bindingi339 – 3424ATP

GO - Molecular functioni

  • ATPase activity Source: BHF-UCL
  • ATPase activity, coupled Source: UniProtKB
  • ATP binding Source: BHF-UCL
  • C3HC4-type RING finger domain binding Source: BHF-UCL
  • cadherin binding involved in cell-cell adhesion Source: BHF-UCL
  • 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
  • phosphatidylserine binding Source: Ensembl
  • poly(A) 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
  • cellular response to starvation Source: ParkinsonsUK-UCL
  • chaperone-mediated autophagy Source: ParkinsonsUK-UCL
  • chaperone-mediated autophagy translocation complex disassembly Source: ParkinsonsUK-UCL
  • chaperone mediated protein folding requiring cofactor Source: Ensembl
  • chaperone-mediated protein transport involved in chaperone-mediated autophagy Source: ParkinsonsUK-UCL
  • clathrin coat disassembly Source: Ensembl
  • late endosomal microautophagy Source: Ensembl
  • mRNA splicing, via spliceosome Source: Reactome
  • negative regulation of fibril organization Source: BHF-UCL
  • negative regulation of transcription, DNA-templated Source: UniProtKB
  • neurotransmitter secretion Source: Reactome
  • positive regulation of mRNA splicing, via spliceosome Source: Ensembl
  • protein folding Source: UniProtKB
  • protein refolding Source: UniProtKB
  • protein targeting to lysosome Source: ParkinsonsUK-UCL
  • 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 protein complex assembly Source: ParkinsonsUK-UCL
  • regulation of protein complex stability Source: ParkinsonsUK-UCL
  • regulation of protein import Source: ParkinsonsUK-UCL
  • regulation of protein stability Source: ParkinsonsUK-UCL
  • response to unfolded protein Source: UniProtKB
  • transcription, DNA-templated Source: UniProtKB-KW
  • viral process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Chaperone, Repressor

Keywords - Biological processi

Host-virus interaction, mRNA processing, mRNA splicing, Stress response, Transcription, Transcription regulation

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi3.6.3.51. 2681.
ReactomeiR-HSA-3371453. Regulation of HSF1-mediated heat shock response.
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-72163. mRNA Splicing - Major Pathway.
R-HSA-888590. GABA synthesis, release, reuptake and degradation.

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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:5241. HSPA8.

Subcellular locationi

GO - Cellular componenti

  • blood microparticle Source: UniProtKB
  • cell-cell adherens junction Source: BHF-UCL
  • clathrin-sculpted gamma-aminobutyric acid transport vesicle membrane Source: Reactome
  • cytosol Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • extracellular matrix Source: BHF-UCL
  • extracellular space Source: UniProtKB
  • focal adhesion Source: UniProtKB
  • intracellular Source: UniProtKB
  • intracellular ribonucleoprotein complex Source: UniProtKB
  • late endosome Source: Ensembl
  • lumenal side of lysosomal membrane Source: ParkinsonsUK-UCL
  • lysosomal lumen Source: ParkinsonsUK-UCL
  • lysosomal membrane Source: ParkinsonsUK-UCL
  • melanosome Source: UniProtKB-SubCell
  • membrane Source: UniProtKB
  • myelin sheath Source: Ensembl
  • nucleolus Source: UniProtKB-SubCell
  • nucleoplasm Source: Reactome
  • nucleus Source: UniProtKB
  • plasma membrane Source: Reactome
  • presynapse Source: GOC
  • Prp19 complex Source: UniProtKB
  • spliceosomal complex Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane, Nucleus, Spliceosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi561 – 5611K → R: Complete loss of in vitro methylation by METTL21A. 2 Publications

Organism-specific databases

PharmGKBiPA29507.

Chemistry

ChEMBLiCHEMBL1275223.

Polymorphism and mutation databases

DMDMi123648.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources2 Publications
Chaini2 – 646645Heat shock cognate 71 kDa proteinPRO_0000078270Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineCombined sources2 Publications
Modified residuei108 – 1081N6-acetyllysineBy similarity
Modified residuei153 – 1531PhosphoserineCombined sources
Modified residuei246 – 2461N6-acetyllysineCombined sources
Modified residuei319 – 3191N6-acetyllysine; alternateCombined sources
Modified residuei319 – 3191N6-succinyllysine; alternateBy similarity
Modified residuei328 – 3281N6-acetyllysineBy similarity
Modified residuei329 – 3291PhosphoserineCombined sources
Modified residuei362 – 3621PhosphoserineCombined sources
Modified residuei512 – 5121N6-acetyllysine; alternateBy similarity
Modified residuei512 – 5121N6-succinyllysine; alternateBy similarity
Cross-linki512 – 512Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateCombined sources
Cross-linki512 – 512Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Modified residuei524 – 5241N6-acetyllysineBy similarity
Modified residuei541 – 5411PhosphoserineCombined sources
Modified residuei561 – 5611N6,N6,N6-trimethyllysine; by METTL21A2 Publications
Modified residuei589 – 5891N6-acetyllysineCombined sources
Modified residuei597 – 5971N6-acetyllysineCombined sources
Modified residuei601 – 6011N6-acetyllysineCombined sources

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.
TopDownProteomicsiP11142-1. [P11142-1]
P11142-2. [P11142-2]

2D gel databases

DOSAC-COBS-2DPAGEP11142.
OGPiP11142.
REPRODUCTION-2DPAGEIPI00003865.
SWISS-2DPAGEP11142.
UCD-2DPAGEP11142.

PTM databases

iPTMnetiP11142.
PhosphoSiteiP11142.
SwissPalmiP11142.

Miscellaneous databases

PMAP-CutDBP11142.

Expressioni

Tissue specificityi

Ubiquitous.1 Publication

Inductioni

Constitutively synthesized.

Gene expression databases

BgeeiENSG00000109971.
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 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 SV40 VP1. 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 PARK2. Interacts with FOXP3. Interacts with DNAJC9 (via J domain) (PubMed:17182002). Interacts with MLLT11 (PubMed:24880125). Interacts with RNF207 (PubMed:25281747).19 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Q99IB83EBI-351896,EBI-6927928From a different organism.
ACTBP607092EBI-351896,EBI-353944
AICDAQ9GZX72EBI-351896,EBI-3834328
ARRB1P494074EBI-351896,EBI-743313
ARRB2P321214EBI-351896,EBI-714559
ATP13A2Q9NQ112EBI-351896,EBI-6308763
BAG1Q9993310EBI-351896,EBI-1030678
BAG2O958163EBI-351896,EBI-355275
EBNA-LPQ8AZK73EBI-351896,EBI-1185167From a different organism.
EGFRP005335EBI-351896,EBI-297353
GAKO149765EBI-351896,EBI-714707
HSPBP1Q9NZL47EBI-351896,EBI-356763
JUNP054123EBI-351896,EBI-852823
LDHAP003384EBI-351896,EBI-372327
LRRK2Q5S0075EBI-351896,EBI-5323863
MP034854EBI-351896,EBI-2547543From a different organism.
STUB1Q9UNE75EBI-351896,EBI-357085
TRIM38O006353EBI-351896,EBI-2130415

GO - Molecular functioni

  • C3HC4-type RING finger domain binding Source: BHF-UCL
  • cadherin binding involved in cell-cell adhesion Source: BHF-UCL
  • 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
  • ubiquitin protein ligase binding Source: ParkinsonsUK-UCL
  • unfolded protein binding Source: UniProtKB

Protein-protein interaction databases

BioGridi109544. 505 interactions.
DIPiDIP-32874N.
IntActiP11142. 104 interactions.
MINTiMINT-4998609.
STRINGi9606.ENSP00000227378.

Chemistry

BindingDBiP11142.

Structurei

Secondary structure

1
646
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi7 – 104Combined sources
Beta strandi13 – 2210Combined sources
Beta strandi25 – 284Combined sources
Beta strandi36 – 405Combined sources
Beta strandi42 – 443Combined sources
Beta strandi49 – 524Combined sources
Helixi53 – 575Combined sources
Turni58 – 614Combined sources
Helixi63 – 653Combined sources
Helixi70 – 734Combined sources
Helixi81 – 866Combined sources
Helixi87 – 893Combined sources
Beta strandi91 – 977Combined sources
Beta strandi100 – 1078Combined sources
Beta strandi110 – 1145Combined sources
Helixi116 – 13520Combined sources
Beta strandi141 – 1466Combined sources
Helixi152 – 16413Combined sources
Beta strandi168 – 1747Combined sources
Helixi175 – 1828Combined sources
Helixi185 – 1873Combined sources
Beta strandi193 – 2008Combined sources
Beta strandi205 – 2139Combined sources
Beta strandi216 – 22510Combined sources
Helixi230 – 24920Combined sources
Helixi253 – 2553Combined sources
Helixi257 – 27418Combined sources
Beta strandi277 – 28812Combined sources
Beta strandi291 – 2988Combined sources
Helixi299 – 3057Combined sources
Helixi307 – 3126Combined sources
Helixi314 – 32310Combined sources
Helixi328 – 3303Combined sources
Beta strandi333 – 3386Combined sources
Helixi339 – 3424Combined sources
Helixi344 – 35310Combined sources
Turni354 – 3563Combined sources
Beta strandi357 – 3604Combined sources
Turni365 – 3673Combined sources
Helixi368 – 38013Combined sources
Helixi541 – 55616Combined sources
Helixi564 – 58219Combined sources
Helixi594 – 61219Combined sources
Helixi613 – 6164Combined sources
Beta strandi641 – 6444Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP11142.
SMRiP11142. Positions 1-646.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP11142.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni186 – 377192Interaction with BAG1Add
BLAST

Domaini

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

Sequence similaritiesi

Belongs to the heat shock protein 70 family.Curated

Phylogenomic databases

eggNOGiKOG0101. Eukaryota.
COG0443. LUCA.
GeneTreeiENSGT00820000127001.
HOGENOMiHOG000228135.
HOVERGENiHBG051845.
InParanoidiP11142.
KOiK03283.
OMAiRTQCERT.
OrthoDBiEOG091G03SF.
PhylomeDBiP11142.
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]

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

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

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti32 – 321D → Y.
Corresponds to variant rs11551602 [ dbSNP | Ensembl ].
VAR_049619
Natural varianti459 – 4591F → L.
Corresponds to variant rs11551598 [ dbSNP | Ensembl ].
VAR_049620

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei464 – 616153Missing in isoform 2. 1 PublicationVSP_002427Add
BLAST

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

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
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[»]
ProteinModelPortaliP11142.
SMRiP11142. Positions 1-646.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109544. 505 interactions.
DIPiDIP-32874N.
IntActiP11142. 104 interactions.
MINTiMINT-4998609.
STRINGi9606.ENSP00000227378.

Chemistry

BindingDBiP11142.
ChEMBLiCHEMBL1275223.

PTM databases

iPTMnetiP11142.
PhosphoSiteiP11142.
SwissPalmiP11142.

Polymorphism and mutation databases

DMDMi123648.

2D gel databases

DOSAC-COBS-2DPAGEP11142.
OGPiP11142.
REPRODUCTION-2DPAGEIPI00003865.
SWISS-2DPAGEP11142.
UCD-2DPAGEP11142.

Proteomic databases

EPDiP11142.
PaxDbiP11142.
PeptideAtlasiP11142.
PRIDEiP11142.
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.
GeneCardsiHSPA8.
H-InvDBHIX0033867.
HGNCiHGNC:5241. HSPA8.
HPAiCAB002056.
HPA052504.
MIMi600816. gene.
neXtProtiNX_P11142.
PharmGKBiPA29507.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0101. Eukaryota.
COG0443. LUCA.
GeneTreeiENSGT00820000127001.
HOGENOMiHOG000228135.
HOVERGENiHBG051845.
InParanoidiP11142.
KOiK03283.
OMAiRTQCERT.
OrthoDBiEOG091G03SF.
PhylomeDBiP11142.
TreeFamiTF105042.

Enzyme and pathway databases

BRENDAi3.6.3.51. 2681.
ReactomeiR-HSA-3371453. Regulation of HSF1-mediated heat shock response.
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-72163. mRNA Splicing - Major Pathway.
R-HSA-888590. GABA synthesis, release, reuptake and degradation.

Miscellaneous databases

ChiTaRSiHSPA8. human.
EvolutionaryTraceiP11142.
GeneWikiiHSPA8.
GenomeRNAii3312.
PMAP-CutDBP11142.
PROiP11142.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000109971.
CleanExiHS_HSPA8.
ExpressionAtlasiP11142. baseline and differential.
GenevisibleiP11142. HS.

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_HUMAN
AccessioniPrimary (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: September 7, 2016
This is version 203 of the entry and version 1 of the sequence. [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. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.