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Entry version 164 (12 Aug 2020)
Sequence version 2 (05 Jul 2004)
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Protein

Endoplasmic reticulum chaperone BiP

Gene

Hsc70-3

Organism
Drosophila melanogaster (Fruit fly)
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

Endoplasmic reticulum chaperone that plays a key role in protein folding and quality control in the endoplasmic reticulum lumen. Involved in the correct folding of proteins and degradation of misfolded proteins (By similarity). Acts as a key repressor of the unfolded protein response (UPR) (By similarity).By similarity

Caution

Was initially thought to be AMPylated at 'Thr-366' by Fic (PubMed:25395623). However, it was later shown to be AMPylated at 'Thr-518'.2 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

The chaperone activity is regulated by ATP-induced allosteric coupling of the nucleotide-binding (NBD) and substrate-binding (SBD) domains. In the ADP-bound and nucleotide-free (apo) states, the two domains have little interaction. In contrast, in the ATP-bound state the two domains are tightly coupled, which results in drastically accelerated kinetics in both binding and release of polypeptide substrates. J domain-containing co-chaperones stimulate the ATPase activity and are required for efficient substrate recognition by HSPA5/BiP.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 sitei97ATPBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 bindingi37 – 40ATPBy similarity4
Nucleotide bindingi227 – 229ATPBy similarity3
Nucleotide bindingi293 – 300ATPBy similarity8
Nucleotide bindingi364 – 367ATPBy 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, Hydrolase
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-DME-3371453, Regulation of HSF1-mediated heat shock response

<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%5Fand%5Ftaxonomy%5Fsection">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:
Endoplasmic reticulum chaperone BiPCurated (EC:3.6.4.10)
Alternative name(s):
78 kDa glucose-regulated protein homologBy similarity
Short name:
GRP-78 homologBy similarity
Binding-immunoglobulin protein homologBy similarity
Short name:
BiPBy similarity
Heat shock 70 kDa protein cognate 3Curated
Heat shock protein cognate 72
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:Hsc70-3Imported
Synonyms:Hsc3
ORF Names:CG4147
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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>OrganismiDrosophila melanogaster (Fruit fly)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 identifieri7227 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraHolometabolaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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
  • UP000000803 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">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 X

Organism-specific databases

Drosophila genome database

More...
FlyBasei
FBgn0001218, Hsc70-3

<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

Endoplasmic reticulum

<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 'PTM / Processing' section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 18Sequence analysisAdd BLAST18
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000001354619 – 656Endoplasmic reticulum chaperone BiPAdd BLAST638

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 residuei518O-AMP-threonine2 Publications1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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

AMPylation at Thr-518 by Fic inactivates the chaperome activity (PubMed:25395623, PubMed:29089387). In response to endoplasmic reticulum stress, de-AMPylation by the same protein, Fic, restores the chaperone activity (PubMed:29089387).2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

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

More...
PaxDbi
P29844

PRoteomics IDEntifications database

More...
PRIDEi
P29844

<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

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
FBgn0001218, Expressed in arthropod fat body and 33 other tissues

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
P29844, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
P29844, DM

<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

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
58539, 51 interactors

Database of interacting proteins

More...
DIPi
DIP-19696N

Protein interaction database and analysis system

More...
IntActi
P29844, 3 interactors

Molecular INTeraction database

More...
MINTi
P29844

STRING: functional protein association networks

More...
STRINGi
7227.FBpp0073445

<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

3D structure databases

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

More...
SMRi
P29844

Database of comparative protein structure models

More...
ModBasei
Search...

<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>Regioni126 – 280Nucleotide-binding (NBD)By similarityAdd BLAST155
Regioni420 – 500Substrate-binding (SBD)By similarityAdd BLAST81

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi653 – 656Prevents secretion from ERPROSITE-ProRule annotation4

<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

Keywords - Domaini

Signal

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG0100, Eukaryota

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000154787

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_005965_3_0_1

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P29844

KEGG Orthology (KO)

More...
KOi
K09490

Identification of Orthologs from Complete Genome Data

More...
OMAi
CVGVMQK

Database of Orthologous Groups

More...
OrthoDBi
288077at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P29844

Family and domain databases

Conserved Domains Database

More...
CDDi
cd10241, HSPA5-like_NBD, 1 hit

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
IPR043129, ATPase_NBD
IPR042050, BIP_NBD
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

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF100920, SSF100920, 1 hit
SSF100934, SSF100934, 1 hit
SSF53067, SSF53067, 2 hits

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00014, ER_TARGET, 1 hit
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%5Flength">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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 1 potential isoform that is computationally mapped.Show allAlign All

P29844-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MKLCILLAVV AFVGLSLGEE KKEKDKELGT VIGIDLGTTY SCVGVYKNGR
60 70 80 90 100
VEIIANDQGN RITPSYVAFT ADGERLIGDA AKNQLTTNPE NTVFDAKRLI
110 120 130 140 150
GREWSDTNVQ HDIKFFPFKV VEKNSKPHIS VDTSQGAKVF APEEISAMVL
160 170 180 190 200
GKMKETAEAY LGKKVTHAVV TVPAYFNDAQ RQATKDAGVI AGLQVMRIIN
210 220 230 240 250
EPTAAAIAYG LDKKEGEKNV LVFDLGGGTF DVSLLTIDNG VFEVVATNGD
260 270 280 290 300
THLGGEDFDQ RVMDHFIKLY KKKKGKDIRK DNRAVQKLRR EVEKAKRALS
310 320 330 340 350
GSHQVRIEIE SFFEGDDFSE TLTRAKFEEL NLDLFRSTLK PVQKVLEDAD
360 370 380 390 400
MNKKDVHEIV LVGGSTRIPK VQQLVKDFFG GKEPSRGINP DEAVAYGAAV
410 420 430 440 450
QAGVLSGEQD TDAIVLLDVN PLTMGIETVG GVMTKLIPRN TVIPTKKSQV
460 470 480 490 500
FSTASDNQHT VTIQVYEGER PMTKDNHLLG KFDLTGIPPA PRGIPQIEVS
510 520 530 540 550
FEIDANGILQ VSAEDKGTGN KEKIVITNDQ NRLTPEDIDR MIRDAEKFAD
560 570 580 590 600
EDKKLKERVE SRNELESYAY SLKNQIGDKD KLGAKLSDDE KNKLESAIDE
610 620 630 640 650
SIKWLEQNPD ADPEEYKKQK KDLEAIVQPV IAKLYQGAGG APPPEGGDDA

DLKDEL
Length:656
Mass (Da):72,261
Last modified:July 5, 2004 - v2
<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:i06A68F839A06337D
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 is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
F3YDH0F3YDH0_DROME
Heat shock 70-kDa protein cognate 3...
Hsc70-3 A4V4C4_DROME, anon-WO0138581.7, BiP, Bip, bip
656Annotation 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 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 conflicti313Missing in AAO45194 (Ref. 4) Curated1
Sequence conflicti507G → A in AAA28626 (PubMed:8514184).Curated1
Sequence conflicti510Q → T in AAA28626 (PubMed:8514184).Curated1
Sequence conflicti592N → T in AAA28626 (PubMed:8514184).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
L01498 mRNA Translation: AAA28626.1
AE014298 Genomic DNA Translation: AAF48095.1
AE014298 Genomic DNA Translation: AAN09299.1
AE014298 Genomic DNA Translation: AAN09300.1
AE014298 Genomic DNA Translation: AAN09301.1
BT004838 mRNA Translation: AAO45194.1

Protein sequence database of the Protein Information Resource

More...
PIRi
JN0666

NCBI Reference Sequences

More...
RefSeqi
NP_001285139.1, NM_001298210.1
NP_511132.2, NM_078577.3
NP_727563.1, NM_167306.2
NP_727564.1, NM_167307.2
NP_727565.1, NM_167308.2

Genome annotation databases

Ensembl metazoan genome annotation project

More...
EnsemblMetazoai
FBtr0073608; FBpp0073445; FBgn0001218
FBtr0073609; FBpp0073446; FBgn0001218
FBtr0073610; FBpp0073447; FBgn0001218
FBtr0073611; FBpp0073448; FBgn0001218
FBtr0345166; FBpp0311376; FBgn0001218

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
32133

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
dme:Dmel_CG4147

UCSC genome browser

More...
UCSCi
CG4147-RB, d. melanogaster

<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
L01498 mRNA Translation: AAA28626.1
AE014298 Genomic DNA Translation: AAF48095.1
AE014298 Genomic DNA Translation: AAN09299.1
AE014298 Genomic DNA Translation: AAN09300.1
AE014298 Genomic DNA Translation: AAN09301.1
BT004838 mRNA Translation: AAO45194.1
PIRiJN0666
RefSeqiNP_001285139.1, NM_001298210.1
NP_511132.2, NM_078577.3
NP_727563.1, NM_167306.2
NP_727564.1, NM_167307.2
NP_727565.1, NM_167308.2

3D structure databases

SMRiP29844
ModBaseiSearch...

Protein-protein interaction databases

BioGRIDi58539, 51 interactors
DIPiDIP-19696N
IntActiP29844, 3 interactors
MINTiP29844
STRINGi7227.FBpp0073445

Proteomic databases

PaxDbiP29844
PRIDEiP29844

Genome annotation databases

EnsemblMetazoaiFBtr0073608; FBpp0073445; FBgn0001218
FBtr0073609; FBpp0073446; FBgn0001218
FBtr0073610; FBpp0073447; FBgn0001218
FBtr0073611; FBpp0073448; FBgn0001218
FBtr0345166; FBpp0311376; FBgn0001218
GeneIDi32133
KEGGidme:Dmel_CG4147
UCSCiCG4147-RB, d. melanogaster

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
32133
FlyBaseiFBgn0001218, Hsc70-3

Phylogenomic databases

eggNOGiKOG0100, Eukaryota
GeneTreeiENSGT00940000154787
HOGENOMiCLU_005965_3_0_1
InParanoidiP29844
KOiK09490
OMAiCVGVMQK
OrthoDBi288077at2759
PhylomeDBiP29844

Enzyme and pathway databases

ReactomeiR-DME-3371453, Regulation of HSF1-mediated heat shock response

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...
BioGRID-ORCSi
32133, 2 hits in 5 CRISPR screens

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

More...
ChiTaRSi
Hsc70-3, fly

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

More...
GenomeRNAii
32133

Protein Ontology

More...
PROi
PR:P29844

Gene expression databases

BgeeiFBgn0001218, Expressed in arthropod fat body and 33 other tissues
ExpressionAtlasiP29844, baseline and differential
GenevisibleiP29844, DM

Family and domain databases

CDDicd10241, HSPA5-like_NBD, 1 hit
Gene3Di1.20.1270.10, 1 hit
2.60.34.10, 1 hit
InterProiView protein in InterPro
IPR043129, ATPase_NBD
IPR042050, BIP_NBD
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
SUPFAMiSSF100920, SSF100920, 1 hit
SSF100934, SSF100934, 1 hit
SSF53067, SSF53067, 2 hits
PROSITEiView protein in PROSITE
PS00014, ER_TARGET, 1 hit
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
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<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 nameiBIP_DROME
<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: P29844
Secondary accession number(s): A4V4C4
, Q86NM3, Q9VYU2, Q9VYU3
<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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: July 5, 2004
Last modified: August 12, 2020
This is version 164 of the entry and version 2 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 programDrosophila annotation project

<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

Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. SIMILARITY comments
    Index of protein domains and families
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