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Entry version 161 (03 Jul 2019)
Sequence version 1 (01 Aug 1988)
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Protein

Heat shock cognate 71 kDa protein

Gene

Hspa8

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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 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. 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. 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. Participates in the ER-associated degradation (ERAD) quality control pathway in conjunction with J domain-containing co-chaperones and the E3 ligase STUB1.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei71ATPBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi12 – 15ATPBy similarity4
Nucleotide bindingi202 – 204ATPBy similarity3
Nucleotide bindingi268 – 275ATPBy similarity8
Nucleotide bindingi339 – 342ATPBy similarity4

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

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

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-MMU-3371453 Regulation of HSF1-mediated heat shock response
R-MMU-3371497 HSP90 chaperone cycle for steroid hormone receptors (SHR)
R-MMU-3371568 Attenuation phase
R-MMU-3371571 HSF1-dependent transactivation
R-MMU-432720 Lysosome Vesicle Biogenesis
R-MMU-432722 Golgi Associated Vesicle Biogenesis
R-MMU-450408 AUF1 (hnRNP D0) binds and destabilizes mRNA
R-MMU-6798695 Neutrophil degranulation
R-MMU-72163 mRNA Splicing - Major Pathway
R-MMU-8856828 Clathrin-mediated endocytosis
R-MMU-8876725 Protein methylation
R-MMU-888590 GABA synthesis, release, reuptake and degradation

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Heat shock cognate 71 kDa protein
Alternative name(s):
Heat shock 70 kDa protein 8
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:Hspa8
Synonyms:Hsc70, Hsc73
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiMus musculus (Mouse)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri10090 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000589 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 9

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

More...
MGIi
MGI:105384 Hspa8

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>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 & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane, Nucleus, Spliceosome

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemovedBy similarity
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000782712 – 646Heat shock cognate 71 kDa proteinAdd BLAST645

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei2N-acetylserineBy similarity1
Modified residuei108N6-acetyllysineCombined sources1
Modified residuei153PhosphoserineBy similarity1
Modified residuei246N6-acetyllysineCombined sources1
Modified residuei319N6-acetyllysine; alternateCombined sources1
Modified residuei319N6-succinyllysine; alternateCombined sources1
Modified residuei328N6-acetyllysineCombined sources1
Modified residuei329PhosphoserineBy similarity1
Modified residuei362PhosphoserineBy similarity1
Modified residuei469Omega-N-methylarginineCombined sources1
Modified residuei512N6-acetyllysine; alternateCombined sources1
Modified residuei512N6-succinyllysine; alternateCombined sources1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki512Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateBy similarity
Cross-linki512Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei524N6-acetyllysineCombined sources1
Modified residuei541PhosphoserineBy similarity1
Modified residuei561N6,N6,N6-trimethyllysine; alternate1 Publication1
Modified residuei561N6,N6,N6-trimethyllysine; by METTL21A; alternateBy similarity1
Modified residuei561N6,N6-dimethyllysine; alternateBy similarity1
Modified residuei589N6-acetyllysineBy similarity1
Modified residuei597N6-acetyllysineBy similarity1
Modified residuei601N6-acetyllysineCombined sources1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Acetylated.By similarity
ISGylated.1 Publication
Trimethylation at Lys-561 reduces fibrillar SNCA binding.By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
P63017

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
P63017

MaxQB - The MaxQuant DataBase

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MaxQBi
P63017

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
P63017

PeptideAtlas

More...
PeptideAtlasi
P63017

PRoteomics IDEntifications database

More...
PRIDEi
P63017

2D gel databases

2-DE database at Universidad Complutense de Madrid

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COMPLUYEAST-2DPAGEi
P63017

REPRODUCTION-2DPAGE

More...
REPRODUCTION-2DPAGEi
IPI00323357
P63017
Q6NZD0

Two-dimensional polyacrylamide gel electrophoresis database from the Geneva University Hospital

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SWISS-2DPAGEi
P63017

University College Dublin 2-DE Proteome Database

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UCD-2DPAGEi
P63017

PTM databases

CarbonylDB database of protein carbonylation sites

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CarbonylDBi
P63017

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P63017

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

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PhosphoSitePlusi
P63017

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
P63017

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Ubiquitous.

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Constitutively synthesized.

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSMUSG00000015656 Expressed in 29 organ(s), highest expression level in female gonad

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P63017 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P63017 MM

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs.

Interacts with PACRG.

Interacts with DNAJC7.

Interacts with DNAJB12 (via J domain).

Interacts with DNAJB14 (via J domain).

Interacts (via C-terminus) with the E3 ligase STUB1 forming a 210 kDa complex of one STUB1 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 IRAK1BP1 and HSPH1/HSP105 (PubMed:9675148, PubMed:15292236, PubMed:17233114).

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. Following LPS binding, may form a complex with CXCR4, GDF5 and HSP90AA1.

Interacts with PRKN.

Interacts with FOXP3.

Interacts with DNAJC9 (via J domain).

Interacts with MLLT11.

Interacts with RNF207.

Interacts with DNAJC21.

Interacts with DNAJB2.

Interacts with TTC1 (via TPR repeats).

Interacts with SGTA (via TPR repeats).

Interacts with HSF1 (via transactivation domain).

Interacts with HOPX, STUB1, HSP40, HSP90, BAG2 and BAG3 (By similarity).

Interacts with DNAJC12 (By similarity).

Interacts with HSPC138 (By similarity).

Interacts with ZMYND10 (By similarity).

Interacts with VGF-derived peptide TLQP-21 (By similarity).

Interacts with BCL2L1, GIMAP5 and MCL1; the interaction with BCL2L1 or MCL1 is impaired in the absence of GIMAP5 (PubMed:21502331).

Interacts with NLPR12 (By similarity).

By similarity4 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
200428, 55 interactors

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
P63017

Database of interacting proteins

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DIPi
DIP-32353N

Protein interaction database and analysis system

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IntActi
P63017, 50 interactors

Molecular INTeraction database

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MINTi
P63017

STRING: functional protein association networks

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STRINGi
10090.ENSMUSP00000015800

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

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

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
P63017

Database of comparative protein structure models

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ModBasei
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
P63017

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni2 – 386Nucleotide-binding domain (NBD)By similarityAdd BLAST385
Regioni186 – 377Interaction with BAG1By similarityAdd BLAST192
Regioni394 – 509Substrate-binding domain (SBD)By similarityAdd BLAST116

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>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.By similarity

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the heat shock protein 70 family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG0101 Eukaryota
COG0443 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00950000183206

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P63017

KEGG Orthology (KO)

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KOi
K03283

Identification of Orthologs from Complete Genome Data

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OMAi
IFREDRC

Database of Orthologous Groups

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OrthoDBi
288077at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
P63017

TreeFam database of animal gene trees

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TreeFami
TF105042

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
1.20.1270.10, 1 hit
2.60.34.10, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR018181 Heat_shock_70_CS
IPR029048 HSP70_C_sf
IPR029047 HSP70_peptide-bd_sf
IPR013126 Hsp_70_fam

The PANTHER Classification System

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PANTHERi
PTHR19375 PTHR19375, 1 hit

Pfam protein domain database

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Pfami
View protein in Pfam
PF00012 HSP70, 1 hit

Protein Motif fingerprint database; a protein domain database

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PRINTSi
PR00301 HEATSHOCK70

Superfamily database of structural and functional annotation

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SUPFAMi
SSF100920 SSF100920, 1 hit
SSF100934 SSF100934, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00297 HSP70_1, 1 hit
PS00329 HSP70_2, 1 hit
PS01036 HSP70_3, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry has 1 described isoform and 2 potential isoforms that are computationally mapped.Show allAlign All

P63017-1 [UniParc]FASTAAdd to basket
« 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 LDKCNEIISW LDKNQTAEKE EFEHQQKELE
610 620 630 640
KVCNPIITKL YQSAGGMPGG MPGGFPGGGA PPSGGASSGP TIEEVD
Length:646
Mass (Da):70,871
Last modified:August 1, 1988 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i03A27B30E6C076ED
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
Q504P4Q504P4_MOUSE
Heat shock cognate 71 kDa protein
Hspa8
627Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
D3Z5E2D3Z5E2_MOUSE
Heat shock cognate 71 kDa protein
Hspa8
116Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence BAE31508 differs from that shown. Reason: Frameshift at positions 256 and 269.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti9I → V in BAE28187 (PubMed:16141072).Curated1
Sequence conflicti35N → K in BAE30081 (PubMed:16141072).Curated1
Sequence conflicti35N → K in BAE30861 (PubMed:16141072).Curated1
Sequence conflicti35N → K in BAE30753 (PubMed:16141072).Curated1
Sequence conflicti268E → G in BAE31432 (PubMed:16141072).Curated1
Sequence conflicti268E → G in BAE31346 (PubMed:16141072).Curated1
Sequence conflicti269R → G in BAE31508 (PubMed:16141072).Curated1
Sequence conflicti353F → C in BAE31664 (PubMed:16141072).Curated1
Sequence conflicti428F → L in AAA37869 (PubMed:3334718).Curated1
Sequence conflicti428F → L in AAB18391 (PubMed:10095055).Curated1
Sequence conflicti432S → Y in BAE30707 (PubMed:16141072).Curated1
Sequence conflicti589K → E in AAH66191 (PubMed:15489334).Curated1
Sequence conflicti645V → M in BAE30272 (PubMed:16141072).Curated1
Sequence conflicti645V → M in BAE31427 (PubMed:16141072).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
M19141 mRNA Translation: AAA37869.1
U27129 mRNA Translation: AAC52836.1
U73744 Genomic DNA Translation: AAB18391.1
AK035286 mRNA Translation: BAC29016.1
AK075935 mRNA Translation: BAC36065.1
AK145579 mRNA Translation: BAE26523.1
AK146708 mRNA Translation: BAE27374.1
AK146985 mRNA Translation: BAE27588.1
AK147864 mRNA Translation: BAE28187.1
AK150474 mRNA Translation: BAE29591.1
AK150498 mRNA Translation: BAE29612.1
AK150701 mRNA Translation: BAE29780.1
AK150958 mRNA Translation: BAE29990.1
AK151065 mRNA Translation: BAE30081.1
AK151127 mRNA Translation: BAE30135.1
AK151287 mRNA Translation: BAE30272.1
AK151435 mRNA Translation: BAE30398.1
AK151516 mRNA Translation: BAE30465.1
AK151537 mRNA Translation: BAE30484.1
AK151775 mRNA Translation: BAE30681.1
AK151808 mRNA Translation: BAE30707.1
AK151865 mRNA Translation: BAE30753.1
AK151892 mRNA Translation: BAE30776.1
AK151948 mRNA Translation: BAE30822.1
AK151997 mRNA Translation: BAE30861.1
AK152598 mRNA Translation: BAE31346.1
AK152697 mRNA Translation: BAE31427.1
AK152703 mRNA Translation: BAE31432.1
AK152803 mRNA Translation: BAE31508.1 Frameshift.
AK153032 mRNA Translation: BAE31664.1
AK153834 mRNA Translation: BAE32204.1
AK159479 mRNA Translation: BAE35116.1
AK164000 mRNA Translation: BAE37581.1
AK166643 mRNA Translation: BAE38912.1
AK166721 mRNA Translation: BAE38970.1
AK166767 mRNA Translation: BAE39005.1
AK166776 mRNA Translation: BAE39012.1
AK166808 mRNA Translation: BAE39036.1
AK166830 mRNA Translation: BAE39053.1
AK166846 mRNA Translation: BAE39065.1
AK166861 mRNA Translation: BAE39076.1
AK166873 mRNA Translation: BAE39084.1
AK166908 mRNA Translation: BAE39109.1
AK166910 mRNA Translation: BAE39111.1
AK166913 mRNA Translation: BAE39113.1
AK166933 mRNA Translation: BAE39127.1
AK167043 mRNA Translation: BAE39211.1
AK167121 mRNA Translation: BAE39269.1
AK167122 mRNA Translation: BAE39270.1
AK167134 mRNA Translation: BAE39280.1
AK167163 mRNA Translation: BAE39304.1
AK167218 mRNA Translation: BAE39344.1
AK167229 mRNA Translation: BAE39353.1
AK167845 mRNA Translation: BAE39865.1
AK167910 mRNA Translation: BAE39917.1
AK168492 mRNA Translation: BAE40379.1
AK168519 mRNA Translation: BAE40398.1
AK168542 mRNA Translation: BAE40419.1
AK168711 mRNA Translation: BAE40553.1
AK168750 mRNA Translation: BAE40590.1
AK168776 mRNA Translation: BAE40612.1
AK168887 mRNA Translation: BAE40704.1
AK168934 mRNA Translation: BAE40745.1
AK169093 mRNA Translation: BAE40876.1
AK169179 mRNA Translation: BAE40957.1
AK169236 mRNA Translation: BAE41004.1
AK169293 mRNA Translation: BAE41049.1
BC006722 mRNA Translation: AAH06722.1
BC066191 mRNA Translation: AAH66191.1
BC085486 mRNA Translation: AAH85486.1
BC089322 mRNA Translation: AAH89322.1
BC089457 mRNA Translation: AAH89457.1
BC106193 mRNA Translation: AAI06194.1
X54401 Genomic DNA Translation: CAA38267.1
X54402 Genomic DNA Translation: CAA38268.1
X54403 Genomic DNA Translation: CAA38269.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS23083.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A45935
JC4853

NCBI Reference Sequences

More...
RefSeqi
NP_112442.2, NM_031165.4

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSMUST00000015800; ENSMUSP00000015800; ENSMUSG00000015656

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
15481

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
mmu:15481

UCSC genome browser

More...
UCSCi
uc009ozx.3 mouse

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M19141 mRNA Translation: AAA37869.1
U27129 mRNA Translation: AAC52836.1
U73744 Genomic DNA Translation: AAB18391.1
AK035286 mRNA Translation: BAC29016.1
AK075935 mRNA Translation: BAC36065.1
AK145579 mRNA Translation: BAE26523.1
AK146708 mRNA Translation: BAE27374.1
AK146985 mRNA Translation: BAE27588.1
AK147864 mRNA Translation: BAE28187.1
AK150474 mRNA Translation: BAE29591.1
AK150498 mRNA Translation: BAE29612.1
AK150701 mRNA Translation: BAE29780.1
AK150958 mRNA Translation: BAE29990.1
AK151065 mRNA Translation: BAE30081.1
AK151127 mRNA Translation: BAE30135.1
AK151287 mRNA Translation: BAE30272.1
AK151435 mRNA Translation: BAE30398.1
AK151516 mRNA Translation: BAE30465.1
AK151537 mRNA Translation: BAE30484.1
AK151775 mRNA Translation: BAE30681.1
AK151808 mRNA Translation: BAE30707.1
AK151865 mRNA Translation: BAE30753.1
AK151892 mRNA Translation: BAE30776.1
AK151948 mRNA Translation: BAE30822.1
AK151997 mRNA Translation: BAE30861.1
AK152598 mRNA Translation: BAE31346.1
AK152697 mRNA Translation: BAE31427.1
AK152703 mRNA Translation: BAE31432.1
AK152803 mRNA Translation: BAE31508.1 Frameshift.
AK153032 mRNA Translation: BAE31664.1
AK153834 mRNA Translation: BAE32204.1
AK159479 mRNA Translation: BAE35116.1
AK164000 mRNA Translation: BAE37581.1
AK166643 mRNA Translation: BAE38912.1
AK166721 mRNA Translation: BAE38970.1
AK166767 mRNA Translation: BAE39005.1
AK166776 mRNA Translation: BAE39012.1
AK166808 mRNA Translation: BAE39036.1
AK166830 mRNA Translation: BAE39053.1
AK166846 mRNA Translation: BAE39065.1
AK166861 mRNA Translation: BAE39076.1
AK166873 mRNA Translation: BAE39084.1
AK166908 mRNA Translation: BAE39109.1
AK166910 mRNA Translation: BAE39111.1
AK166913 mRNA Translation: BAE39113.1
AK166933 mRNA Translation: BAE39127.1
AK167043 mRNA Translation: BAE39211.1
AK167121 mRNA Translation: BAE39269.1
AK167122 mRNA Translation: BAE39270.1
AK167134 mRNA Translation: BAE39280.1
AK167163 mRNA Translation: BAE39304.1
AK167218 mRNA Translation: BAE39344.1
AK167229 mRNA Translation: BAE39353.1
AK167845 mRNA Translation: BAE39865.1
AK167910 mRNA Translation: BAE39917.1
AK168492 mRNA Translation: BAE40379.1
AK168519 mRNA Translation: BAE40398.1
AK168542 mRNA Translation: BAE40419.1
AK168711 mRNA Translation: BAE40553.1
AK168750 mRNA Translation: BAE40590.1
AK168776 mRNA Translation: BAE40612.1
AK168887 mRNA Translation: BAE40704.1
AK168934 mRNA Translation: BAE40745.1
AK169093 mRNA Translation: BAE40876.1
AK169179 mRNA Translation: BAE40957.1
AK169236 mRNA Translation: BAE41004.1
AK169293 mRNA Translation: BAE41049.1
BC006722 mRNA Translation: AAH06722.1
BC066191 mRNA Translation: AAH66191.1
BC085486 mRNA Translation: AAH85486.1
BC089322 mRNA Translation: AAH89322.1
BC089457 mRNA Translation: AAH89457.1
BC106193 mRNA Translation: AAI06194.1
X54401 Genomic DNA Translation: CAA38267.1
X54402 Genomic DNA Translation: CAA38268.1
X54403 Genomic DNA Translation: CAA38269.1
CCDSiCCDS23083.1
PIRiA45935
JC4853
RefSeqiNP_112442.2, NM_031165.4

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3CQXX-ray2.30A/B1-381[»]
SMRiP63017
ModBaseiSearch...

Protein-protein interaction databases

BioGridi200428, 55 interactors
CORUMiP63017
DIPiDIP-32353N
IntActiP63017, 50 interactors
MINTiP63017
STRINGi10090.ENSMUSP00000015800

PTM databases

CarbonylDBiP63017
iPTMnetiP63017
PhosphoSitePlusiP63017
SwissPalmiP63017

2D gel databases

COMPLUYEAST-2DPAGEiP63017
REPRODUCTION-2DPAGEiIPI00323357
P63017
Q6NZD0
SWISS-2DPAGEiP63017
UCD-2DPAGEiP63017

Proteomic databases

EPDiP63017
jPOSTiP63017
MaxQBiP63017
PaxDbiP63017
PeptideAtlasiP63017
PRIDEiP63017

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000015800; ENSMUSP00000015800; ENSMUSG00000015656
GeneIDi15481
KEGGimmu:15481
UCSCiuc009ozx.3 mouse

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
3312
MGIiMGI:105384 Hspa8

Phylogenomic databases

eggNOGiKOG0101 Eukaryota
COG0443 LUCA
GeneTreeiENSGT00950000183206
InParanoidiP63017
KOiK03283
OMAiIFREDRC
OrthoDBi288077at2759
PhylomeDBiP63017
TreeFamiTF105042

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTraceiP63017

Protein Ontology

More...
PROi
PR:P63017

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSMUSG00000015656 Expressed in 29 organ(s), highest expression level in female gonad
ExpressionAtlasiP63017 baseline and differential
GenevisibleiP63017 MM

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

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiHSP7C_MOUSE
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P63017
Secondary accession number(s): P08109
, P12225, Q3U6R0, Q3U764, Q3U7D7, Q3U7E2, Q3U9B4, Q3U9G0, Q3UGM0, Q5FWJ6, Q62373, Q62374, Q62375, Q6NZD0
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: August 1, 1988
Last modified: July 3, 2019
This is version 161 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

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

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
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