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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

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

  • ATPase activity Source: BHF-UCL
  • ATPase activity, coupled Source: Reactome
  • ATP binding Source: BHF-UCL
  • C3HC4-type RING finger domain binding Source: BHF-UCL
  • cadherin binding 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
  • 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
  • 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 methylation Source: Reactome
  • 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 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

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 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.

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

EuPathDBiHostDB:ENSG00000109971.13.
HGNCiHGNC:5241. HSPA8.

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

2D gel databases

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

PTM databases

iPTMnetiP11142.
PhosphoSitePlusiP11142.
SwissPalmiP11142.

Miscellaneous databases

PMAP-CutDBiP11142.

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. 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 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 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).By similarity32 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • C3HC4-type RING finger domain binding Source: BHF-UCL
  • cadherin binding 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. 560 interactors.
CORUMiP11142.
DIPiDIP-32874N.
IntActiP11142. 126 interactors.
MINTiMINT-4998609.
STRINGi9606.ENSP00000227378.

Chemistry databases

BindingDBiP11142.

Structurei

Secondary structure

1646
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 – 57Combined sources5
Turni58 – 61Combined sources4
Helixi63 – 65Combined 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 strandi136 – 138Combined sources3
Beta strandi141 – 146Combined sources6
Helixi152 – 164Combined sources13
Beta strandi168 – 174Combined sources7
Helixi175 – 182Combined sources8
Helixi185 – 187Combined sources3
Beta strandi188 – 191Combined sources4
Beta strandi193 – 201Combined sources9
Beta strandi204 – 213Combined sources10
Beta strandi216 – 225Combined sources10
Helixi230 – 249Combined sources20
Helixi253 – 255Combined sources3
Helixi257 – 276Combined sources20
Beta strandi278 – 288Combined sources11
Beta strandi291 – 298Combined sources8
Helixi299 – 305Combined sources7
Helixi307 – 312Combined sources6
Helixi314 – 324Combined sources11
Helixi328 – 330Combined sources3
Beta strandi333 – 338Combined sources6
Helixi339 – 342Combined sources4
Helixi344 – 353Combined sources10
Turni354 – 356Combined sources3
Beta strandi357 – 360Combined sources4
Turni365 – 367Combined sources3
Helixi368 – 380Combined sources13
Helixi541 – 556Combined sources16
Helixi564 – 582Combined sources19
Helixi594 – 612Combined sources19
Helixi613 – 616Combined sources4
Beta strandi641 – 644Combined sources4

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[»]
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.
GeneTreeiENSGT00900000140908.
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.
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

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)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

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: November 22, 2017
This is version 217 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. 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