Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Heat shock 70 kDa protein 1A

Gene

HSPA1A

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. This is achieved through cycles of ATP binding, ATP hydrolysis and ADP release, mediated by co-chaperones. The co-chaperones have been shown to not only regulate different steps of the ATPase cycle, but they also have an individual specificity such that one co-chaperone may promote folding of a substrate while another may promote degradation. The affinity 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. It goes through repeated cycles of ATP hydrolysis and nucleotide exchange, which permits cycles of substrate binding and release. The co-chaperones are of three types: J-domain co-chaperones such as 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:24012426, PubMed:26865365, PubMed:24318877). Maintains protein homeostasis during cellular stress through two opposing mechanisms: protein refolding and degradation. Its acetylation/deacetylation state determines whether it functions in protein refolding or protein degradation by controlling the competitive binding of co-chaperones HOPX and STUB1. During the early stress response, the acetylated form binds to HOPX which assists in chaperone-mediated protein refolding, thereafter, it is deacetylated and binds to ubiquitin ligase STUB1 that promotes ubiquitin-mediated protein degradation (PubMed:27708256). Regulates centrosome integrity during mitosis, and is required for the maintenance of a functional mitotic centrosome that supports the assembly of a bipolar mitotic spindle (PubMed:27137183). Enhances STUB1-mediated SMAD3 ubiquitination and degradation and facilitates STUB1-mediated inhibition of TGF-beta signaling (PubMed:24613385). Essential for STUB1-mediated ubiquitination and degradation of FOXP3 in regulatory T-cells (Treg) during inflammation (PubMed:23973223). Negatively regulates heat shock-induced HSF1 transcriptional activity during the attenuation and recovery phase period of the heat shock response (PubMed:9499401).2 Publications7 Publications
(Microbial infection) In case of rotavirus A infection, serves as a post-attachment receptor for the virus to facilitate entry into the cell.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei71ATP1

Regions

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

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionChaperone, Host cell receptor for virus entry, Receptor
Biological processStress response
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-HSA-168330 Viral RNP Complexes in the Host Cell Nucleus
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-450408 AUF1 (hnRNP D0) binds and destabilizes mRNA
R-HSA-6798695 Neutrophil degranulation
SIGNORiP0DMV8

Names & Taxonomyi

Protein namesi
Recommended name:
Heat shock 70 kDa protein 1AImported
Alternative name(s):
Heat shock 70 kDa protein 1
Short name:
HSP70-12 Publications
Short name:
HSP70.1
Gene namesi
Name:HSPA1A
Synonyms:HSP721 Publication, HSPA1, HSX70
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 6

Organism-specific databases

EuPathDBiHostDB:ENSG00000204389.9
HGNCiHGNC:5232 HSPA1A
MIMi140550 gene
603012 gene
neXtProtiNX_P0DMV8

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

Cytoplasm, Cytoskeleton, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi10D → A: Reduces affinity for ADP. 1 Publication1
Mutagenesisi77K → Q: No loss of acetylation and ATPase activity. Exhibits normal protein refolding activity during the early phase but exhibits defects in ubiquitin-mediated protein degradation during the later phase. 1 Publication1
Mutagenesisi77K → R: Significant loss of acetylation and ATPase activity. Decreased binding to HOPX and HSP90 and increased binding to STUB1 and NAA10. Impaired capacity for protein refolding during the early phase after stress but shows normal protein degradation activity in the late phase. 1 Publication1
Mutagenesisi199D → A: Reduces affinity for ADP. 1 Publication1
Mutagenesisi561K → R: Complete loss of in vitro methylation by METTL21A. 2 Publications1

Organism-specific databases

DisGeNETi3303
3304
OpenTargetsiENSG00000204388
ENSG00000204389

Chemistry databases

ChEMBLiCHEMBL5460

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00000782492 – 641Heat shock 70 kDa protein 1AAdd BLAST640

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineCombined sources1
Modified residuei77N6-acetyllysine1 Publication1
Modified residuei108N6-acetyllysineCombined sources1
Modified residuei246N6-acetyllysineCombined sources1
Modified residuei348N6-acetyllysineCombined sources1
Modified residuei469Omega-N-methylarginineCombined sources1
Modified residuei561N6,N6,N6-trimethyllysine; by METTL21A; alternateCombined sources2 Publications1
Modified residuei561N6,N6-dimethyllysine; alternateCombined sources1
Modified residuei631PhosphoserineCombined sources1
Modified residuei633PhosphoserineCombined sources1
Modified residuei636PhosphothreonineCombined sources1

Post-translational modificationi

In response to cellular stress, acetylated at Lys-77 by NA110 and then gradually deacetylated by HDAC4 at later stages. Acetylation enhances its chaperone activity and also determines whether it will function as a chaperone for protein refolding or degradation by controlling its binding to co-chaperones HOPX and STUB1. The acetylated form and the non-acetylated form bind to HOPX and STUB1 respectively. Acetylation also protects cells against various types of cellular stress.1 Publication

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein

Proteomic databases

PaxDbiP0DMV8
PeptideAtlasiP0DMV8
PRIDEiP0DMV8

2D gel databases

REPRODUCTION-2DPAGEiIPI00304925

PTM databases

CarbonylDBiP0DMV8
GlyConnecti1295
iPTMnetiP0DMV8
PhosphoSitePlusiP0DMV8
SwissPalmiP0DMV8

Expressioni

Inductioni

By heat shock.

Gene expression databases

BgeeiENSG00000204389 Expressed in 237 organ(s), highest expression level in endothelial cell
CleanExiHS_HSPA1A
ExpressionAtlasiP0DMV8 baseline and differential

Organism-specific databases

HPAiCAB017451
CAB032815
HPA052504

Interactioni

Subunit structurei

Component of the CatSper complex. Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs (PubMed:17289661). Interacts with CHCHD3, DNAJC7, IRAK1BP1, PPP5C and TSC2 (PubMed:21081504, PubMed:12853476, PubMed:18620420, PubMed:17233114, PubMed:15383005, PubMed:15963462). Interacts with TERT; the interaction occurs in the absence of the RNA component, TERC, and dissociates once the TERT complex has formed (PubMed:11274138). Interacts with TRIM5 (via B30.2/SPRY domain) (PubMed:20053985). Interacts with METTL21A (PubMed:23921388). Interacts with DNAAF2 (By similarity). Interacts with PRKN (PubMed:24270810). Interacts with FOXP3 (PubMed:23973223). Interacts with NOD2; the interaction enhances NOD2 stability (PubMed:24790089). Interacts with DNAJC9 (via J domain) (PubMed:17182002). Interacts with ATF5; the interaction protects ATF5 from degradation via proteasome-dependent and caspase-dependent processes (PubMed:22528486). Interacts with RNF207 (via the C-terminus); this interaction additively increases KCNH2 expression (PubMed:25281747). Interacts with HSF1 (via transactivation domain); this interaction results in the inhibition of heat shock- and HSF1-induced transcriptional activity during the attenuation and recovery phase period of the heat shock response (PubMed:7935376, PubMed:9499401). Interacts with NAA10, HSP40, HSP90 and HDAC4. The acetylated form and the non-acetylated form interact with HOPX and STUB1 respectively (PubMed:27708256). Interacts with NEDD1 (PubMed:27137183). Interacts (via NBD) with BAG1, BAG2, BAG3 and HSPH1/HSP105 (PubMed:24318877). Interacts with SMAD3 (PubMed:24613385). Interacts with DNAJC8 (PubMed:27133716).By similarity27 Publications

Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

CORUMiP0DMV8
IntActiP0DMV8, 54 interactors
MINTiP0DMV8
STRINGi9606.ENSP00000364802

Chemistry databases

BindingDBiP0DMV8

Structurei

Secondary structure

1641
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliP0DMV8
SMRiP0DMV8
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni2 – 386Nucleotide-binding domain (NBD)By similarityAdd BLAST385
Regioni394 – 509Substrate-binding domain (SBD)By similarityAdd 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.2 Publications

Sequence similaritiesi

Belongs to the heat shock protein 70 family.Curated

Phylogenomic databases

KOiK03283
OMAiFRGEEKQ
OrthoDBiEOG093705LK
PhylomeDBiP0DMV8

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 1 potential isoform that is computationally mapped.Show allAlign All

Isoform 1 (identifier: P0DMV8-1) [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
MAKAAAIGID LGTTYSCVGV FQHGKVEIIA NDQGNRTTPS YVAFTDTERL
60 70 80 90 100
IGDAAKNQVA LNPQNTVFDA KRLIGRKFGD PVVQSDMKHW PFQVINDGDK
110 120 130 140 150
PKVQVSYKGE TKAFYPEEIS SMVLTKMKEI AEAYLGYPVT NAVITVPAYF
160 170 180 190 200
NDSQRQATKD AGVIAGLNVL RIINEPTAAA IAYGLDRTGK GERNVLIFDL
210 220 230 240 250
GGGTFDVSIL TIDDGIFEVK ATAGDTHLGG EDFDNRLVNH FVEEFKRKHK
260 270 280 290 300
KDISQNKRAV RRLRTACERA KRTLSSSTQA SLEIDSLFEG IDFYTSITRA
310 320 330 340 350
RFEELCSDLF RSTLEPVEKA LRDAKLDKAQ IHDLVLVGGS TRIPKVQKLL
360 370 380 390 400
QDFFNGRDLN KSINPDEAVA YGAAVQAAIL MGDKSENVQD LLLLDVAPLS
410 420 430 440 450
LGLETAGGVM TALIKRNSTI PTKQTQIFTT YSDNQPGVLI QVYEGERAMT
460 470 480 490 500
KDNNLLGRFE LSGIPPAPRG VPQIEVTFDI DANGILNVTA TDKSTGKANK
510 520 530 540 550
ITITNDKGRL SKEEIERMVQ EAEKYKAEDE VQRERVSAKN ALESYAFNMK
560 570 580 590 600
SAVEDEGLKG KISEADKKKV LDKCQEVISW LDANTLAEKD EFEHKRKELE
610 620 630 640
QVCNPIISGL YQGAGGPGPG GFGAQGPKGG SGSGPTIEEV D
Length:641
Mass (Da):70,052
Last modified:May 27, 2015 - v1
Checksum:i78F513118C96DE66
GO
Isoform 2 (identifier: P0DMV8-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     96-150: Missing.

Show »
Length:586
Mass (Da):63,937
Checksum:i6FBA863FEACE9DF1
GO

Computationally mapped potential isoform sequencesi

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
V9GZ37V9GZ37_HUMAN
Heat shock 70 kDa protein 1A
HSPA1A
476Annotation score:

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti7I → V in AAA52697 (PubMed:3931075).Curated1
Sequence conflicti7I → V in CAA28381 (PubMed:3786141).Curated1
Sequence conflicti355N → D in BAG65428 (PubMed:14702039).Curated1
Sequence conflicti370A → G in AAA52697 (PubMed:3931075).Curated1
Sequence conflicti469Missing in AAA52697 (PubMed:3931075).Curated1
Sequence conflicti497K → N in BAG65428 (PubMed:14702039).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_029053110E → D2 PublicationsCorresponds to variant dbSNP:rs562047Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_04442796 – 150Missing in isoform 2. 1 PublicationAdd BLAST55

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M11717 Genomic DNA Translation: AAA52697.1
M59828 Genomic DNA Translation: AAA63226.1
BA000025 Genomic DNA Translation: BAB63300.1
AF134726 Genomic DNA Translation: AAD21816.1
AK304652 mRNA Translation: BAG65428.1
DQ451402 Genomic DNA Translation: ABD96830.1
AL671762 Genomic DNA No translation available.
BC002453 mRNA Translation: AAH02453.1
M24743 Genomic DNA Translation: AAA59844.1
X04676 Genomic DNA Translation: CAA28381.1
X04677 Genomic DNA Translation: CAA28382.1
CCDSiCCDS34414.1 [P0DMV8-1]
PIRiA29160
A45871
I59139
I79540
RefSeqiNP_005336.3, NM_005345.5 [P0DMV8-1]
NP_005337.2, NM_005346.4 [P0DMV8-1]
UniGeneiHs.274402
Hs.702139
Hs.719966
Hs.743411

Genome annotation databases

EnsembliENST00000375651; ENSP00000364802; ENSG00000204389 [P0DMV8-1]
ENST00000400040; ENSP00000382915; ENSG00000215328
ENST00000430065; ENSP00000404524; ENSG00000235941 [P0DMV8-1]
ENST00000433487; ENSP00000408907; ENSG00000234475 [P0DMV8-1]
ENST00000441618; ENSP00000406359; ENSG00000237724 [P0DMV8-1]
GeneIDi3303
3304
KEGGihsa:3303
hsa:3304

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Similar proteinsi

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M11717 Genomic DNA Translation: AAA52697.1
M59828 Genomic DNA Translation: AAA63226.1
BA000025 Genomic DNA Translation: BAB63300.1
AF134726 Genomic DNA Translation: AAD21816.1
AK304652 mRNA Translation: BAG65428.1
DQ451402 Genomic DNA Translation: ABD96830.1
AL671762 Genomic DNA No translation available.
BC002453 mRNA Translation: AAH02453.1
M24743 Genomic DNA Translation: AAA59844.1
X04676 Genomic DNA Translation: CAA28381.1
X04677 Genomic DNA Translation: CAA28382.1
CCDSiCCDS34414.1 [P0DMV8-1]
PIRiA29160
A45871
I59139
I79540
RefSeqiNP_005336.3, NM_005345.5 [P0DMV8-1]
NP_005337.2, NM_005346.4 [P0DMV8-1]
UniGeneiHs.274402
Hs.702139
Hs.719966
Hs.743411

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1HJOX-ray2.30A3-382[»]
1S3XX-ray1.84A1-382[»]
1XQSX-ray2.90C/D184-371[»]
2E88X-ray1.80A1-388[»]
2E8AX-ray1.77A1-388[»]
2LMGNMR-A537-610[»]
3A8YX-ray2.30A/B1-388[»]
3ATUX-ray1.65A1-388[»]
3ATVX-ray1.58A1-388[»]
3AY9X-ray1.75A1-388[»]
3D2EX-ray2.35B/D1-382[»]
3D2FX-ray2.30B/D1-382[»]
3JXUX-ray2.14A1-387[»]
3LOFX-ray2.40A/B/C/D/E/F534-641[»]
3Q49X-ray1.54C634-641[»]
4IO8X-ray2.58A1-382[»]
4J8FX-ray2.70A1-382[»]
4PO2X-ray2.00A/B386-613[»]
4WV5X-ray2.04A/B395-543[»]
4WV7X-ray2.42A/B395-543[»]
5AQWX-ray1.53A1-380[»]
5AQXX-ray2.12A1-380[»]
5AQYX-ray1.56A1-380[»]
5AQZX-ray1.65A1-380[»]
5AR0X-ray1.90A1-380[»]
5BN8X-ray1.34A1-388[»]
5BN9X-ray1.69A1-388[»]
5BPLX-ray1.93A1-388[»]
5BPMX-ray1.83A1-388[»]
5BPNX-ray2.10A1-388[»]
5GJJNMR-A385-641[»]
5MKRX-ray1.87A1-380[»]
5MKSX-ray1.99A1-380[»]
5XI9NMR-A381-564[»]
5XIRNMR-A381-564[»]
ProteinModelPortaliP0DMV8
SMRiP0DMV8
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

CORUMiP0DMV8
IntActiP0DMV8, 54 interactors
MINTiP0DMV8
STRINGi9606.ENSP00000364802

Chemistry databases

BindingDBiP0DMV8
ChEMBLiCHEMBL5460

PTM databases

CarbonylDBiP0DMV8
GlyConnecti1295
iPTMnetiP0DMV8
PhosphoSitePlusiP0DMV8
SwissPalmiP0DMV8

2D gel databases

REPRODUCTION-2DPAGEiIPI00304925

Proteomic databases

PaxDbiP0DMV8
PeptideAtlasiP0DMV8
PRIDEiP0DMV8

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000375651; ENSP00000364802; ENSG00000204389 [P0DMV8-1]
ENST00000400040; ENSP00000382915; ENSG00000215328
ENST00000430065; ENSP00000404524; ENSG00000235941 [P0DMV8-1]
ENST00000433487; ENSP00000408907; ENSG00000234475 [P0DMV8-1]
ENST00000441618; ENSP00000406359; ENSG00000237724 [P0DMV8-1]
GeneIDi3303
3304
KEGGihsa:3303
hsa:3304

Organism-specific databases

CTDi3303
3304
DisGeNETi3303
3304
EuPathDBiHostDB:ENSG00000204389.9
GeneCardsiHSPA1A
HGNCiHGNC:5232 HSPA1A
HPAiCAB017451
CAB032815
HPA052504
MIMi140550 gene
603012 gene
neXtProtiNX_P0DMV8
OpenTargetsiENSG00000204388
ENSG00000204389
GenAtlasiSearch...

Phylogenomic databases

KOiK03283
OMAiFRGEEKQ
OrthoDBiEOG093705LK
PhylomeDBiP0DMV8

Enzyme and pathway databases

ReactomeiR-HSA-168330 Viral RNP Complexes in the Host Cell Nucleus
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-450408 AUF1 (hnRNP D0) binds and destabilizes mRNA
R-HSA-6798695 Neutrophil degranulation
SIGNORiP0DMV8

Miscellaneous databases

ChiTaRSiHSPA1A human
PROiPR:P0DMV8
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000204389 Expressed in 237 organ(s), highest expression level in endothelial cell
CleanExiHS_HSPA1A
ExpressionAtlasiP0DMV8 baseline and differential

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 nameiHS71A_HUMAN
AccessioniPrimary (citable) accession number: P0DMV8
Secondary accession number(s): B4E3B6
, P08107, P19790, Q5JQI4, Q5SP17, Q9UQL9, Q9UQM0
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 27, 2015
Last sequence update: May 27, 2015
Last modified: November 7, 2018
This is version 39 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. SIMILARITY comments
    Index of protein domains and families
  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. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again