UniProtKB - Q9NZL4 (HPBP1_HUMAN)
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- BLAST>sp|Q9NZL4|HPBP1_HUMAN Hsp70-binding protein 1 OS=Homo sapiens OX=9606 GN=HSPBP1 PE=1 SV=1 MSDEGSRGSRLPLALPPASQGCSSGGGGGGGGGSSAGGSGNSRPPRNLQGLLQMAITAGS EEPDPPPEPMSEERRQWLQEAMSAAFRGQREEVEQMKSCLRVLSQPMPPTAGEAEQAADQ QEREGALELLADLCENMDNAADFCQLSGMHLLVGRYLEAGAAGLRWRAAQLIGTCSQNVA AIQEQVLGLGALRKLLRLLDRDACDTVRVKALFAISCLVREQEAGLLQFLRLDGFSVLMR AMQQQVQKLKVKSAFLLQNLLVGHPEHKGTLCSMGMVQQLVALVRTEHSPFHEHVLGALC SLVTDFPQGVRECREPELGLEELLRHRCQLLQQHEEYQEELEFCEKLLQTCFSSPADDSM DR
- Align
Hsp70-binding protein 1
HSPBP1
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>Select a section on the left to see content.
<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
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.1"Inhibition of Hsp70 ATPase activity and protein renaturation by a novel Hsp70-binding protein."
Raynes D.A., Guerriero V. Jr.
J. Biol. Chem. 273:32883-32888(1998) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT 25-GLY--GLY-27 DEL, FUNCTION, INTERACTION WITH HSPA1A, TISSUE SPECIFICITY. - Ref.2"Isolation and characterization of isoforms of HspBP1, inhibitors of Hsp70."
Guerriero V. Jr., Raynes D.A.
Biochim. Biophys. Acta 1490:203-207(2000) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, POLYMORPHISM OF POLY-GLY REGION. - Ref.9"HspBP1, an Hsp70 cochaperone, has two structural domains and is capable of altering the conformation of the Hsp70 ATPase domain."
McLellan C.A., Raynes D.A., Guerriero V. Jr.
J. Biol. Chem. 278:19017-19022(2003) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH HSPA1A. - Ref.10"The cochaperone HspBP1 inhibits the CHIP ubiquitin ligase and stimulates the maturation of the cystic fibrosis transmembrane conductance regulator."
Alberti S., Boehse K., Arndt V., Schmitz A., Hoehfeld J.
Mol. Biol. Cell 15:4003-4010(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH HSPA1A AND STUB1.
<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
- enzyme inhibitor activity Source: ProtInc <p>Traceable Author Statement</p> <p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#tas">GO evidence code guide</a></p> Traceable author statementi
- ubiquitin protein ligase binding Source: ARUK-UCL <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
<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 - Biological processi
- positive regulation of proteasomal ubiquitin-dependent protein catabolic process Source: BHF-UCL <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- positive regulation of protein ubiquitination Source: BHF-UCL <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- protein folding Source: ProtInc <p>Traceable Author Statement</p> <p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#tas">GO evidence code guide</a></p> Traceable author statementi
<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: Hsp70-binding protein 1Short name: HspBP1 Alternative name(s): Heat shock protein-binding protein 1 Hsp70-binding protein 2 Short name: HspBP2 Hsp70-interacting protein 1 Hsp70-interacting protein 2 |
| <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:HSPBP1 Synonyms:HSPBP ORF Names:PP1845 |
| <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>Organismi | Homo 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 identifieri | 9606 [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 lineagei | cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › 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 |
|
Organism-specific databases
Eukaryotic Pathogen Database Resources More...EuPathDBi | HostDB:ENSG00000133265.10 |
Human Gene Nomenclature Database More...HGNCi | HGNC:24989 HSPBP1 |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 612939 gene |
neXtProt; the human protein knowledge platform More...neXtProti | NX_Q9NZL4 |
<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
Organism-specific databases
DisGeNET More...DisGeNETi | 23640 |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA164720725 |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | HSPBP1 |
Domain mapping of disease mutations (DMDM) More...DMDMi | 74734730 |
<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 key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <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_0000084035 | 1 – 362 | Hsp70-binding protein 1Add BLAST | 362 |
Amino acid modifications
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <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 residuei | 354 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <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 residuei | 359 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 |
<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>Keywords - PTMi
PhosphoproteinProteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | Q9NZL4 |
MaxQB - The MaxQuant DataBase More...MaxQBi | Q9NZL4 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | Q9NZL4 |
PeptideAtlas More...PeptideAtlasi | Q9NZL4 |
PRoteomics IDEntifications database More...PRIDEi | Q9NZL4 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 83428 83429 [Q9NZL4-2] |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | Q9NZL4 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | Q9NZL4 |
<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
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.1"Inhibition of Hsp70 ATPase activity and protein renaturation by a novel Hsp70-binding protein."
Raynes D.A., Guerriero V. Jr.
J. Biol. Chem. 273:32883-32888(1998) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT 25-GLY--GLY-27 DEL, FUNCTION, INTERACTION WITH HSPA1A, TISSUE SPECIFICITY.
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000133265 |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | Q9NZL4 baseline and differential |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | Q9NZL4 HS |
Organism-specific databases
Human Protein Atlas More...HPAi | CAB005865 HPA071444 |
<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
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.1"Inhibition of Hsp70 ATPase activity and protein renaturation by a novel Hsp70-binding protein."
Raynes D.A., Guerriero V. Jr.
J. Biol. Chem. 273:32883-32888(1998) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT 25-GLY--GLY-27 DEL, FUNCTION, INTERACTION WITH HSPA1A, TISSUE SPECIFICITY. - Ref.9"HspBP1, an Hsp70 cochaperone, has two structural domains and is capable of altering the conformation of the Hsp70 ATPase domain."
McLellan C.A., Raynes D.A., Guerriero V. Jr.
J. Biol. Chem. 278:19017-19022(2003) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH HSPA1A. - Ref.10"The cochaperone HspBP1 inhibits the CHIP ubiquitin ligase and stimulates the maturation of the cystic fibrosis transmembrane conductance regulator."
Alberti S., Boehse K., Arndt V., Schmitz A., Hoehfeld J.
Mol. Biol. Cell 15:4003-4010(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH HSPA1A AND STUB1. - Ref.16"Regulation of Hsp70 function by HspBP1: structural analysis reveals an alternate mechanism for Hsp70 nucleotide exchange."
Shomura Y., Dragovic Z., Chang H.-C., Tzvetkov N., Young J.C., Brodsky J.L., Guerriero V. Jr., Hartl F.U., Bracher A.
Mol. Cell 17:367-379(2005) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 87-362 IN COMPLEX WITH HSPA1A.
<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
| With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| HSF1 | Q00613 | 3 | EBI-356763,EBI-719620 | |
| HSPA2 | P54652 | 6 | EBI-356763,EBI-356991 | |
| HSPA8 | P11142 | 11 | EBI-356763,EBI-351896 | |
| HSPA8 | Q96IS6 | 5 | EBI-356763,EBI-10289199 | |
| NOTCH2NL | Q7Z3S9 | 3 | EBI-356763,EBI-945833 | |
| SSA3 | P09435 | 3 | EBI-356763,EBI-8611 | From Saccharomyces cerevisiae (strain ATCC 204508 / S288c). |
<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
- ubiquitin protein ligase binding Source: ARUK-UCL <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGrid) More...BioGridi | 117168, 93 interactors |
Protein interaction database and analysis system More...IntActi | Q9NZL4, 29 interactors |
Molecular INTeraction database More...MINTi | Q9NZL4 |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000255631 |
<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
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 90 – 104 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 15 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 113 – 134 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 22 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 137 – 145 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 9 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 148 – 154 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 7 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 155 – 158 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 162 – 176 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 15 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 180 – 188 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 9 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 191 – 201 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 11 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 205 – 219 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 15 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 223 – 231 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 9 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 234 – 243 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 10 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 247 – 263 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 17 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 265 – 267 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 268 – 273 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 276 – 284 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 9 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 291 – 303 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 13 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 307 – 314 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 316 – 318 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 320 – 331 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 12 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 335 – 337 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 338 – 351 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 14 |
3D structure databases
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | Q9NZL4 |
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | Q9NZL4 |
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 | Q9NZL4 |
<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
Domains and Repeats
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Family and Domains’ section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati | 135 – 177 | ARM 1Add BLAST | 43 | |
| <p>This subsection of the ‘Family and Domains’ section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati | 180 – 220 | ARM 2Add BLAST | 41 | |
| <p>This subsection of the ‘Family and Domains’ section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati | 223 – 262 | ARM 3Add BLAST | 40 | |
| <p>This subsection of the ‘Family and Domains’ section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati | 265 – 304 | ARM 4Add BLAST | 40 |
Compositional bias
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi | 21 – 40 | Gly-richAdd BLAST | 20 |
<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>Keywords - Domaini
RepeatPhylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | KOG2160 Eukaryota ENOG410Y90B LUCA |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000007740 |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG053282 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | Q9NZL4 |
KEGG Orthology (KO) More...KOi | K09562 |
Database of Orthologous Groups More...OrthoDBi | EOG091G0HDF |
Database for complete collections of gene phylogenies More...PhylomeDBi | Q9NZL4 |
TreeFam database of animal gene trees More...TreeFami | TF324307 |
Family and domain databases
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 1.25.10.10, 1 hit |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR011989 ARM-like IPR016024 ARM-type_fold IPR013918 Nucleotide_exch_fac_Fes1 |
Pfam protein domain database More...Pfami | View protein in Pfam PF08609 Fes1, 1 hit |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF48371 SSF48371, 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>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (3)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.
This entry describes 3 <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 basketAdded 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.
10 20 30 40 50
MSDEGSRGSR LPLALPPASQ GCSSGGGGGG GGGSSAGGSG NSRPPRNLQG
60 70 80 90 100
LLQMAITAGS EEPDPPPEPM SEERRQWLQE AMSAAFRGQR EEVEQMKSCL
110 120 130 140 150
RVLSQPMPPT AGEAEQAADQ QEREGALELL ADLCENMDNA ADFCQLSGMH
160 170 180 190 200
LLVGRYLEAG AAGLRWRAAQ LIGTCSQNVA AIQEQVLGLG ALRKLLRLLD
210 220 230 240 250
RDACDTVRVK ALFAISCLVR EQEAGLLQFL RLDGFSVLMR AMQQQVQKLK
260 270 280 290 300
VKSAFLLQNL LVGHPEHKGT LCSMGMVQQL VALVRTEHSP FHEHVLGALC
310 320 330 340 350
SLVTDFPQGV RECREPELGL EELLRHRCQL LQQHEEYQEE LEFCEKLLQT
360
CFSSPADDSM DR
The sequence of this isoform differs from the canonical sequence as follows:
207-309: Missing.
10 20 30 40 50
MSDEGSRGSR LPLALPPASQ GCSSGGGGGG GGGSSAGGSG NSRPPRNLQG
60 70 80 90 100
LLQMAITAGS EEPDPPPEPM SEERRQWLQE AMSAAFRGQR EEVEQMKSCL
110 120 130 140 150
RVLSQPMPPT AGEAEQAADQ QEREGALELL ADLCENMDNA ADFCQLSGMH
160 170 180 190 200
LLVGRYLEAG AAGLRWRAAQ LIGTCSQNVA AIQEQVLGLG ALRKLLRLLD
210 220 230 240 250
RDACDTVREC REPELGLEEL LRHRCQLLQQ HEEYQEELEF CEKLLQTCFS
SPADDSMDR
The sequence of this isoform differs from the canonical sequence as follows:
1-1: M → MGGRRAPLKRRLLSRPSRIDPSGRQSCFSGDHLLPLTHSSLLHKRPM
25-27: Missing.
10 20 30 40 50
MGGRRAPLKR RLLSRPSRID PSGRQSCFSG DHLLPLTHSS LLHKRPMSDE
60 70 80 90 100
GSRGSRLPLA LPPASQGCSS GGGGGGSSAG GSGNSRPPRN LQGLLQMAIT
110 120 130 140 150
AGSEEPDPPP EPMSEERRQW LQEAMSAAFR GQREEVEQMK SCLRVLSQPM
160 170 180 190 200
PPTAGEAEQA ADQQEREGAL ELLADLCENM DNAADFCQLS GMHLLVGRYL
210 220 230 240 250
EAGAAGLRWR AAQLIGTCSQ NVAAIQEQVL GLGALRKLLR LLDRDACDTV
260 270 280 290 300
RVKALFAISC LVREQEAGLL QFLRLDGFSV LMRAMQQQVQ KLKVKSAFLL
310 320 330 340 350
QNLLVGHPEH KGTLCSMGMV QQLVALVRTE HSPFHEHVLG ALCSLVTDFP
360 370 380 390 400
QGVRECREPE LGLEELLRHR CQLLQQHEEY QEELEFCEKL LQTCFSSPAD
DSMDR
Experimental Info
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <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 conflicti | 276 | M → V in BAG57622 (PubMed:14702039).Curated | 1 |
Natural variant
| Feature key | Position(s) | DescriptionActions | Graphical view | Length | |
|---|---|---|---|---|---|
| <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_023645 | 25 – 27 | Missing 4 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 3 | ||
| Isoform 3 (identifier: Q9NZL4-3) | |||||
| <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 varianti | 71 | G → V. Corresponds to variant dbSNP:rs140649061Ensembl. | 1 | ||
Alternative sequence
Sequence databases
| Select the link destinations: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks Updated | AF093420 mRNA Translation: AAC79703.1 AF187859 mRNA Translation: AAF35833.1 AB020592 mRNA Translation: BAB18742.1 AF217996 mRNA Translation: AAG17238.1 AK130636 mRNA Translation: BAC85399.1 AK294358 mRNA Translation: BAG57622.1 CR457118 mRNA Translation: CAG33399.1 AK075293 mRNA Translation: BAG52102.1 BC001236 mRNA Translation: AAH01236.1 BC002373 mRNA Translation: AAH02373.1 |
NCBI Reference Sequences More...RefSeqi | NP_001123578.1, NM_001130106.1 NP_001284529.1, NM_001297600.1 [Q9NZL4-3] NP_036399.3, NM_012267.4 XP_016882033.1, XM_017026544.1 |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.53066 |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000255631; ENSP00000255631; ENSG00000133265 ENST00000433386; ENSP00000398244; ENSG00000133265 ENST00000587922; ENSP00000467574; ENSG00000133265 |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 23640 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:23640 |
UCSC genome browser More...UCSCi | uc002qkc.4 human [Q9NZL4-1] |
<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>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
| Protein | Similar proteins | Species | Score | Length |
|---|
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| Q9NZL4 | Hsp70-interacting protein, isoform CRA_a | 216 | |||
| UPI0004E00A01 | 423 | ||||
| hsp70-binding protein 1 isoform X1 | 421 | ||||
| hsp70-binding protein 1 isoform X1 | 408 | ||||
| UPI0006D725FF | 405 | ||||
| +99 | |||||
| Q9NZL4-2 | UPI00062A994C | 272 | |||
| Uncharacterized protein | 240 | ||||
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| Q9NZL4 | Hsp70-interacting protein, isoform CRA_a | 216 | |||
| UPI0004E00A01 | 423 | ||||
| hsp70-binding protein 1 isoform X1 | 421 | ||||
| hsp70-binding protein 1 isoform X1 | 408 | ||||
| UPI0006D725FF | 405 | ||||
| +159 | |||||
| Q9NZL4-2 | UPI00062A994C | 272 | |||
| Uncharacterized protein | 240 | ||||
| UPI00073274C9 | 262 | ||||
| Hsp70-binding protein 1 (Fragment) | 218 | ||||
| Hsp70-binding protein 1 (Fragment) | 256 | ||||
<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: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks Updated | AF093420 mRNA Translation: AAC79703.1 AF187859 mRNA Translation: AAF35833.1 AB020592 mRNA Translation: BAB18742.1 AF217996 mRNA Translation: AAG17238.1 AK130636 mRNA Translation: BAC85399.1 AK294358 mRNA Translation: BAG57622.1 CR457118 mRNA Translation: CAG33399.1 AK075293 mRNA Translation: BAG52102.1 BC001236 mRNA Translation: AAH01236.1 BC002373 mRNA Translation: AAH02373.1 |
NCBI Reference Sequences More...RefSeqi | NP_001123578.1, NM_001130106.1 NP_001284529.1, NM_001297600.1 [Q9NZL4-3] NP_036399.3, NM_012267.4 XP_016882033.1, XM_017026544.1 |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.53066 |
3D structure databases
| Select the link destinations: Protein Data Bank Europe More...PDBeiProtein Data Bank RCSB More...RCSB PDBiProtein Data Bank Japan More...PDBjiLinks Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
| 1XQR | X-ray | 2.10 | A/B | 87-362 | [»] | |
| 1XQS | X-ray | 2.90 | A/B | 87-362 | [»] | |
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | Q9NZL4 | |||||
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | Q9NZL4 | |||||
Database of comparative protein structure models More...ModBasei | Search... | |||||
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... | |||||
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGrid) More...BioGridi | 117168, 93 interactors |
Protein interaction database and analysis system More...IntActi | Q9NZL4, 29 interactors |
Molecular INTeraction database More...MINTi | Q9NZL4 |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000255631 |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | Q9NZL4 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | Q9NZL4 |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | HSPBP1 |
Domain mapping of disease mutations (DMDM) More...DMDMi | 74734730 |
Proteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | Q9NZL4 |
MaxQB - The MaxQuant DataBase More...MaxQBi | Q9NZL4 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | Q9NZL4 |
PeptideAtlas More...PeptideAtlasi | Q9NZL4 |
PRoteomics IDEntifications database More...PRIDEi | Q9NZL4 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 83428 83429 [Q9NZL4-2] |
Protocols and materials databases
The DNASU plasmid repository More...DNASUi | 23640 |
| Structural Biology Knowledgebase | Search... |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000255631; ENSP00000255631; ENSG00000133265 ENST00000433386; ENSP00000398244; ENSG00000133265 ENST00000587922; ENSP00000467574; ENSG00000133265 |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 23640 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:23640 |
UCSC genome browser More...UCSCi | uc002qkc.4 human [Q9NZL4-1] |
Organism-specific databases
Comparative Toxicogenomics Database More...CTDi | 23640 |
DisGeNET More...DisGeNETi | 23640 |
Eukaryotic Pathogen Database Resources More...EuPathDBi | HostDB:ENSG00000133265.10 |
GeneCards: human genes, protein and diseases More...GeneCardsi | HSPBP1 |
H-Invitational Database, human transcriptome db More...H-InvDBi | HIX0015460 |
Human Gene Nomenclature Database More...HGNCi | HGNC:24989 HSPBP1 |
Human Protein Atlas More...HPAi | CAB005865 HPA071444 |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 612939 gene |
neXtProt; the human protein knowledge platform More...neXtProti | NX_Q9NZL4 |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA164720725 |
GenAtlas: human gene database More...GenAtlasi | Search... |
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | KOG2160 Eukaryota ENOG410Y90B LUCA |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000007740 |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG053282 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | Q9NZL4 |
KEGG Orthology (KO) More...KOi | K09562 |
Database of Orthologous Groups More...OrthoDBi | EOG091G0HDF |
Database for complete collections of gene phylogenies More...PhylomeDBi | Q9NZL4 |
TreeFam database of animal gene trees More...TreeFami | TF324307 |
Miscellaneous databases
ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data More...ChiTaRSi | HSPBP1 human |
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | Q9NZL4 |
The Gene Wiki collection of pages on human genes and proteins More...GeneWikii | HSPBP1 |
Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens More...GenomeRNAii | 23640 |
Protein Ontology More...PROi | PR:Q9NZL4 |
The Stanford Online Universal Resource for Clones and ESTs More...SOURCEi | Search... |
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000133265 |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | Q9NZL4 baseline and differential |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | Q9NZL4 HS |
Family and domain databases
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 1.25.10.10, 1 hit |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR011989 ARM-like IPR016024 ARM-type_fold IPR013918 Nucleotide_exch_fac_Fes1 |
Pfam protein domain database More...Pfami | View protein in Pfam PF08609 Fes1, 1 hit |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF48371 SSF48371, 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 namei | HPBP1_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>Accessioni | Q9NZL4Primary (citable) accession number: Q9NZL4 Secondary accession number(s): B3KQP0 , B4DG11, O95351, Q6ZNU5 | |
| <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 historyi | Integrated into UniProtKB/Swiss-Prot: | October 25, 2005 |
| Last sequence update: | October 1, 2000 | |
| Last modified: | July 18, 2018 | |
| This is version 138 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 statusi | Reviewed (UniProtKB/Swiss-Prot) | |
| Annotation program | Chordata Protein Annotation Program | |
| Disclaimer | Any 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
<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>Keywords - Technical termi
3D-structure, Complete proteome, Reference proteomeDocuments
- Human chromosome 19
Human chromosome 19: entries, gene names and cross-references to MIM - Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or disease mutations - MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot - PDB cross-references
Index of Protein Data Bank (PDB) cross-references
