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UniProtKB - P11142 (HSP7C_HUMAN)

Entry version 233 (05 Jun 2019)
Sequence version 1 (01 Jul 1989)
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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

<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 (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). Interacts with VGF-derived peptide TLQP-21 (PubMed:28934328).2 Publications11 Publications

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 sitei71ATP1

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 – 15ATP4
Nucleotide bindingi202 – 204ATP3
Nucleotide bindingi268 – 275ATP8
Nucleotide bindingi339 – 342ATP4

<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

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<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 processHost-virus interaction, mRNA processing, mRNA splicing, Stress response, Transcription, Transcription regulation
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		3.6.3.51 2681

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-HSA-3371453 Regulation of HSF1-mediated heat shock response
R-HSA-3371497 HSP90 chaperone cycle for steroid hormone receptors (SHR)
R-HSA-3371568 Attenuation phase
R-HSA-3371571 HSF1-dependent transactivation
R-HSA-432720 Lysosome Vesicle Biogenesis
R-HSA-432722 Golgi Associated Vesicle Biogenesis
R-HSA-447041 CHL1 interactions
R-HSA-450408 AUF1 (hnRNP D0) binds and destabilizes mRNA
R-HSA-6785807 Interleukin-4 and Interleukin-13 signaling
R-HSA-6798695 Neutrophil degranulation
R-HSA-72163 mRNA Splicing - Major Pathway
R-HSA-8856828 Clathrin-mediated endocytosis
R-HSA-8876725 Protein methylation
R-HSA-888590 GABA synthesis, release, reuptake and degradation

SIGNOR Signaling Network Open Resource

More...SIGNORi		P11142

Protein family/group databases

MoonDB Database of extreme multifunctional and moonlighting proteins

More...MoonDBi		P11142 Predicted

<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
Lipopolysaccharide-associated protein 1
Short name:
LAP-1
Short name:
LPS-associated protein 1
<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, HSP73, HSPA10
<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>OrganismiHomo sapiens (Human)
<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 identifieri9606 [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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
<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
  • UP000005640 <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 11

Organism-specific databases

Human Gene Nomenclature Database

More...HGNCi		HGNC:5241 HSPA8

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		600816 gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_P11142

<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 provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi561K → R: Complete loss of in vitro methylation by METTL21A. 2 Publications1

Organism-specific databases

DisGeNET

More...DisGeNETi		3312

Open Targets

More...OpenTargetsi		ENSG00000109971

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA29507

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL1275223

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		HSPA8

Domain mapping of disease mutations (DMDM)

More...DMDMi		123648

<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 methionineiRemovedCombined sources2 Publications
<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_00000782702 – 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-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
<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); 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

<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.2 Publications
ISGylated.2 Publications
Trimethylation at Lys-561 reduces fibrillar SNCA binding.

Keywords - PTMi

Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		P11142

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P11142

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

More...PaxDbi		P11142

PeptideAtlas

More...PeptideAtlasi		P11142

PRoteomics IDEntifications database

More...PRIDEi		P11142

ProteomicsDB human proteome resource

More...ProteomicsDBi		52698
52699 [P11142-2]

Consortium for Top Down Proteomics

More...TopDownProteomicsi		P11142-1 [P11142-1]
P11142-2 [P11142-2]

2D gel databases

DOSAC-COBS 2D-PAGE database

More...DOSAC-COBS-2DPAGEi		P11142

USC-OGP 2-DE database

More...OGPi		P11142

REPRODUCTION-2DPAGE

More...REPRODUCTION-2DPAGEi		IPI00003865

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

More...SWISS-2DPAGEi		P11142

University College Dublin 2-DE Proteome Database

More...UCD-2DPAGEi		P11142

PTM databases

GlyConnect protein glycosylation platform

More...GlyConnecti		1299

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P11142

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

More...PhosphoSitePlusi		P11142

SwissPalm database of S-palmitoylation events

More...SwissPalmi		P11142

Miscellaneous databases

CutDB - Proteolytic event database

More...PMAP-CutDBi		P11142

<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.1 Publication

<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

More...Bgeei		ENSG00000109971 Expressed in 91 organ(s), highest expression level in frontal cortex

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		P11142 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P11142 HS

Organism-specific databases

Human Protein Atlas

More...HPAi		CAB002056
HPA052504

<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 HSPH1/HSP105. Interacts with IRAK1BP1 and BAG1. Interacts with DNAJC7. Interacts with DNAJB12 (via J domain) (PubMed:21150129, PubMed:21148293, PubMed:24732912, PubMed:27916661). Interacts with DNAJB14 (via J domain) (PubMed:23018488, PubMed:24732912, PubMed:27916661). Interacts (via C-terminus) with the E3 ligase CHIP forming a 210 kDa complex of one CHIP and two HSPA8 molecules. Interacts with CITED1 (via N-terminus); the interaction suppresses the association of CITED1 to p300/CBP and Smad-mediated transcription transactivation. Component of the PRP19-CDC5L splicing complex composed of a core complex comprising a homotetramer of PRPF19, CDC5L, PLRG1 and BCAS2, and at least three less stably associated proteins CTNNBL1, CWC15 and HSPA8. Interacts with TRIM5. Part of a complex composed at least of ASCL2, EMSY, HCFC1, HSPA8, CCAR2, MATR3, MKI67, RBBP5, TUBB2A, WDR5 and ZNF335; this complex may have a histone H3-specific methyltransferase activity. Interacts with METTL21A. Following LPS binding, may form a complex with CXCR4, GDF5 and HSP90AA1. Interacts with PRKN. Interacts with FOXP3. Interacts with DNAJC9 (via J domain) (PubMed:17182002). Interacts with MLLT11 (PubMed:24880125). Interacts with RNF207 (PubMed:25281747). Interacts with DNAJC21 (PubMed:27346687). Interacts with DNAJB2 (PubMed:15936278). Interacts with TTC1 (via TPR repeats) (PubMed:15708368). Interacts with SGTA (via TPR repeats) (By similarity). Interacts with HSF1 (via transactivation domain) (PubMed:9499401). Interacts with HOPX, HSP40 and HSP90 (PubMed:27708256). Interacts with STUB1 (PubMed:27708256). Interacts with BAG2 (PubMed:24318877). Interacts with BAG3 (PubMed:27474739, PubMed:24318877). Interacts with DNAJC12 (PubMed:24122553). Interacts with ZMYND10 (PubMed:29601588). Interacts with HSPC138 (PubMed:25760597). Interacts with BCL2L1, GIMAP5 and MCL1; the interaction with BCL2L1 or MCL1 is impaired in the absence of GIMAP5 (By similarity). Interacts with NLPR12 (PubMed:17947705).By similarity34 Publications
(Microbial infection) Interacts with SV40 VP1.1 Publication

<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

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		109544, 766 interactors

CORUM comprehensive resource of mammalian protein complexes

More...CORUMi		P11142

Database of interacting proteins

More...DIPi		DIP-32874N

Protein interaction database and analysis system

More...IntActi		P11142, 251 interactors

Molecular INTeraction database

More...MINTi		P11142

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000432083

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		P11142

<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

More...SMRi		P11142

Database of comparative protein structure models

More...ModBasei		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P11142

<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)1 PublicationAdd BLAST385
Regioni186 – 377Interaction with BAG1Add BLAST192
Regioni394 – 509Substrate-binding domain (SBD)1 PublicationAdd 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.1 Publication

<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

More...eggNOGi		KOG0101 Eukaryota
COG0443 LUCA

Ensembl GeneTree

More...GeneTreei		ENSGT00950000183206

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000228135

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P11142

KEGG Orthology (KO)

More...KOi		K03283

Identification of Orthologs from Complete Genome Data

More...OMAi		IFREDRC

Database of Orthologous Groups

More...OrthoDBi		288077at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		P11142

TreeFam database of animal gene trees

More...TreeFami		TF105042

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		1.20.1270.10, 1 hit
2.60.34.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...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

More...PANTHERi		PTHR19375 PTHR19375, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00012 HSP70, 1 hit

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR00301 HEATSHOCK70

Superfamily database of structural and functional annotation

More...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>Sequences (2+)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 describes 2 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 2 described isoforms and 13 potential isoforms that are computationally mapped.Show allAlign All

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
<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: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

<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 13 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A8K7Q2A8K7Q2_HUMAN
Heat shock cognate 71 kDa protein
HSPA8
410Annotation 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>
E9PKE3E9PKE3_HUMAN
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>
E9PNE6E9PNE6_HUMAN
Heat shock cognate 71 kDa protein
HSPA8
500Annotation 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>
E9PLF4E9PLF4_HUMAN
Heat shock cognate 71 kDa protein
HSPA8
187Annotation 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>
E9PN89E9PN89_HUMAN
Heat shock cognate 71 kDa protein
HSPA8
312Annotation 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>
E9PK54E9PK54_HUMAN
Heat shock cognate 71 kDa protein
HSPA8
183Annotation 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>
E9PN25E9PN25_HUMAN
Heat shock cognate 71 kDa protein
HSPA8
132Annotation 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>
E9PQK7E9PQK7_HUMAN
Heat shock cognate 71 kDa protein
HSPA8
178Annotation 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>
E9PPY6E9PPY6_HUMAN
Heat shock cognate 71 kDa protein
HSPA8
137Annotation 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>
E9PI65E9PI65_HUMAN
Heat shock cognate 71 kDa protein
HSPA8
168Annotation 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>
There are more potential isoformsShow all

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>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
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_002427464 – 616Missing in isoform 2. 1 PublicationAdd BLAST153

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...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

The Consensus CDS (CCDS) project

More...CCDSi		CCDS44754.1 [P11142-2]
CCDS8440.1 [P11142-1]

Protein sequence database of the Protein Information Resource

More...PIRi		A27077

NCBI Reference Sequences

More...RefSeqi		NP_006588.1, NM_006597.5 [P11142-1]
NP_694881.1, NM_153201.3 [P11142-2]
XP_011541100.1, XM_011542798.1 [P11142-1]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000227378; ENSP00000227378; ENSG00000109971 [P11142-1]
ENST00000453788; ENSP00000404372; ENSG00000109971 [P11142-2]
ENST00000532636; ENSP00000437125; ENSG00000109971 [P11142-1]
ENST00000534624; ENSP00000432083; ENSG00000109971 [P11142-1]

Database of genes from NCBI RefSeq genomes

More...GeneIDi		3312

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:3312

UCSC genome browser

More...UCSCi		uc001pyp.5 human [P11142-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

<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
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]

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...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[»]
6B1IX-ray2.30A/B5-381[»]
6B1MX-ray1.90A/B5-381[»]
6B1NX-ray1.80A/B5-381[»]
SMRiP11142
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109544, 766 interactors
CORUMiP11142
DIPiDIP-32874N
IntActiP11142, 251 interactors
MINTiP11142
STRINGi9606.ENSP00000432083

Chemistry databases

BindingDBiP11142
ChEMBLiCHEMBL1275223

Protein family/group databases

MoonDBiP11142 Predicted

PTM databases

GlyConnecti1299
iPTMnetiP11142
PhosphoSitePlusiP11142
SwissPalmiP11142

Polymorphism and mutation databases

BioMutaiHSPA8
DMDMi123648

2D gel databases

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

Proteomic databases

EPDiP11142
jPOSTiP11142
PaxDbiP11142
PeptideAtlasiP11142
PRIDEiP11142
ProteomicsDBi52698
52699 [P11142-2]
TopDownProteomicsiP11142-1 [P11142-1]
P11142-2 [P11142-2]

Protocols and materials databases

The DNASU plasmid repository

More...DNASUi		3312
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

Comparative Toxicogenomics Database

More...CTDi		3312
DisGeNETi3312

GeneCards: human genes, protein and diseases

More...GeneCardsi		HSPA8

H-Invitational Database, human transcriptome db

More...H-InvDBi		HIX0033867
HGNCiHGNC:5241 HSPA8
HPAiCAB002056
HPA052504
MIMi600816 gene
neXtProtiNX_P11142
OpenTargetsiENSG00000109971
PharmGKBiPA29507

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG0101 Eukaryota
COG0443 LUCA
GeneTreeiENSGT00950000183206
HOGENOMiHOG000228135
InParanoidiP11142
KOiK03283
OMAiIFREDRC
OrthoDBi288077at2759
PhylomeDBiP11142
TreeFamiTF105042

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 Interleukin-13 signaling
R-HSA-6798695 Neutrophil degranulation
R-HSA-72163 mRNA Splicing - Major Pathway
R-HSA-8856828 Clathrin-mediated endocytosis
R-HSA-8876725 Protein methylation
R-HSA-888590 GABA synthesis, release, reuptake and degradation
SIGNORiP11142

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...ChiTaRSi		HSPA8 human
EvolutionaryTraceiP11142

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		HSPA8

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...GenomeRNAii		3312
PMAP-CutDBiP11142

Protein Ontology

More...PROi		PR:P11142

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000109971 Expressed in 91 organ(s), highest expression level in frontal cortex
ExpressionAtlasiP11142 baseline and differential
GenevisibleiP11142 HS

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...

<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_HUMAN
<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: P11142
Secondary accession number(s): Q9H3R6
<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: July 1, 1989
Last sequence update: July 1, 1989
Last modified: June 5, 2019
This is version 233 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
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.

<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. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  4. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  5. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  6. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
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