UniProtKB - P34217 (PIN4_YEAST)
Your basket is currently empty. i <p>When browsing through different UniProt proteins, you can use the ‘basket’ to save them, so that you can back to find or analyse them later.<p><a href='/help/basket' target='_top'>More...</a></p>
Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)
- BLAST>sp|P34217|PIN4_YEAST RNA-binding protein PIN4 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=PIN4 PE=1 SV=1 METSSFENAPPAAINDAQDNNINTETNDQETNQQSIETRDAIDKENGVQTETGENSAKNA EQNVSSTNLNNAPTNGALDDDVIPNAIVIKNIPFAIKKEQLLDIIEEMDLPLPYAFNYHF DNGIFRGLAFANFTTPEETTQVITSLNGKEISGRKLKVEYKKMLPQAERERIEREKREKR GQLEEQHRSSSNLSLDSLSKMSGSGNNNTSNNQLFSTLMNGINANSMMNSPMNNTINNNS SNNNNSGNIILNQPSLSAQHTSSSLYQTNVNNQAQMSTERFYAPLPSTSTLPLPPQQLDF NDPDTLEIYSQLLLFKDREKYYYELAYPMGISASHKRIINVLCSYLGLVEVYDPRFIIIR RKILDHANLQSHLQQQGQMTSAHPLQPNSTGGSMNRSQSYTSLLQAHAAAAANSISNQAV NNSSNSNTINSNNGNGNNVIINNNSASSTPKISSQGQFSMQPTLTSPKMNIHHSSQYNSA DQPQQPQPQTQQNVQSAAQQQQSFLRQQATLTPSSRIPSGYSANHYQINSVNPLLRNSQI SPPNSQIPINSQTLSQAQPPAQSQTQQRVPVAYQNASLSSQQLYNLNGPSSANSQSQLLP QHTNGSVHSNFSYQSYHDESMLSAHNLNSADLIYKSLSHSGLDDGLEQGLNRSLSGLDLQ NQNKKNLW
- Align
- Format
- Add to basketAdded to basket
- History
- Other tutorials and videos
- Help video
- Feedback
RNA-binding protein PIN4
PIN4
Annotation score:4 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.6"Mdt1, a novel Rad53 FHA1 domain-interacting protein, modulates DNA damage tolerance and G(2)/M cell cycle progression in Saccharomyces cerevisiae."
Pike B.L., Yongkiettrakul S., Tsai M.-D., Heierhorst J.
Mol. Cell. Biol. 24:2779-2788(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH RAD53, PHOSPHORYLATION AT THR-305, MUTAGENESIS OF THR-305.
Miscellaneous
<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.5"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
<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
- RNA binding Source: UniProtKB-KW
<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
- DNA damage checkpoint Source: SGD <p>Inferred from Genetic Interaction</p> <p>Used to describe “traditional” genetic interactions such as suppressors and synthetic lethals as well as other techniques such as functional complementation, rescue experiments, or inferences about a gene drawn from the phenotype of a mutation in a different gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#igi">GO evidence code guide</a></p> Inferred from genetic interactioni
- G2/M transition of mitotic cell cycle Source: SGD <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
<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 function | RNA-binding |
Enzyme and pathway databases
BioCyc Collection of Pathway/Genome Databases More...BioCyci | YEAST:G3O-28950-MONOMER |
<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: RNA-binding protein PIN4Alternative name(s): Psi inducibility protein 4 |
| <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:PIN4 Synonyms:MDT1 Ordered Locus Names:YBL051C ORF Names:YBL0506, YBL0516 |
| <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 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
| <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 | 559292 [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 › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae |
| <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 | FungiDB:YBL051C |
Saccharomyces Genome Database More...SGDi | S000000147 PIN4 |
<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
Other locations
- Cytoplasm 1 Publication
<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.4"Global analysis of protein localization in budding yeast."
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.
Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
- Cytoplasm 1 Publication
Other locations
- cytoplasm Source: SGD <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
<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 - Cellular componenti
Cytoplasm<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 key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <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>Mutagenesisi | 305 | T → A: No interaction with RAD53. 1 Publication <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
| 1 |
<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_0000082028 | 1 – 668 | RNA-binding protein PIN4Add BLAST | 668 |
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 | 56 | 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 | 189 | 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 | 191 | 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 | 194 | 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 | 197 | 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 | 305 | Phosphothreonine1 Publication <p>Manually curated information which has been inferred by a curator based on his/her scientific knowledge or on the scientific content of an article.</p> <p><a href="/manual/evidences#ECO:0000305">More...</a></p> Manual assertion inferred by curator fromi
| 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 | 393 | 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 | 466 | 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 | 541 | 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 | 636 | 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 | 638 | 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 | 640 | 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 | 653 | 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 | 655 | 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 <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
<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.6"Mdt1, a novel Rad53 FHA1 domain-interacting protein, modulates DNA damage tolerance and G(2)/M cell cycle progression in Saccharomyces cerevisiae."
Pike B.L., Yongkiettrakul S., Tsai M.-D., Heierhorst J.
Mol. Cell. Biol. 24:2779-2788(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH RAD53, PHOSPHORYLATION AT THR-305, MUTAGENESIS OF THR-305.
<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
MaxQB - The MaxQuant DataBase More...MaxQBi | P34217 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | P34217 |
PRoteomics IDEntifications database More...PRIDEi | P34217 |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | P34217 |
<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.6"Mdt1, a novel Rad53 FHA1 domain-interacting protein, modulates DNA damage tolerance and G(2)/M cell cycle progression in Saccharomyces cerevisiae."
Pike B.L., Yongkiettrakul S., Tsai M.-D., Heierhorst J.
Mol. Cell. Biol. 24:2779-2788(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH RAD53, PHOSPHORYLATION AT THR-305, MUTAGENESIS OF THR-305.
<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 |
|---|---|---|---|---|
| RAD53 | P22216 | 3 | EBI-21256,EBI-17843 |
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGrid) More...BioGridi | 32647, 318 interactors |
Database of interacting proteins More...DIPi | DIP-1905N |
The Eukaryotic Linear Motif resource for Functional Sites in Proteins More...ELMi | P34217 |
Protein interaction database and analysis system More...IntActi | P34217, 44 interactors |
Molecular INTeraction database More...MINTi | P34217 |
STRING: functional protein association networks More...STRINGi | 4932.YBL051C |
<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
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | P34217 |
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P34217 |
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 | P34217 |
<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 <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini | 85 – 163 | RRMPROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi Add BLAST | 79 |
Phylogenomic databases
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000115549 |
Identification of Orthologs from Complete Genome Data More...OMAi | KKMLPQA |
Database of Orthologous Groups More...OrthoDBi | EOG092C3WNG |
Family and domain databases
Conserved Domains Database More...CDDi | cd02639 R3H_RRM, 1 hit cd12253 RRM_PIN4_like, 1 hit |
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 3.30.70.330, 1 hit |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR012677 Nucleotide-bd_a/b_plait_sf IPR034186 PIN4-like_RRM IPR034069 R3H_Cip2 IPR035979 RBD_domain_sf IPR000504 RRM_dom |
Pfam protein domain database More...Pfami | View protein in Pfam PF00076 RRM_1, 1 hit |
Simple Modular Architecture Research Tool; a protein domain database More...SMARTi | View protein in SMART SM00360 RRM, 1 hit |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF54928 SSF54928, 1 hit |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS50102 RRM, 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>Sequencei
<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.
10 20 30 40 50
METSSFENAP PAAINDAQDN NINTETNDQE TNQQSIETRD AIDKENGVQT
60 70 80 90 100
ETGENSAKNA EQNVSSTNLN NAPTNGALDD DVIPNAIVIK NIPFAIKKEQ
110 120 130 140 150
LLDIIEEMDL PLPYAFNYHF DNGIFRGLAF ANFTTPEETT QVITSLNGKE
160 170 180 190 200
ISGRKLKVEY KKMLPQAERE RIEREKREKR GQLEEQHRSS SNLSLDSLSK
210 220 230 240 250
MSGSGNNNTS NNQLFSTLMN GINANSMMNS PMNNTINNNS SNNNNSGNII
260 270 280 290 300
LNQPSLSAQH TSSSLYQTNV NNQAQMSTER FYAPLPSTST LPLPPQQLDF
310 320 330 340 350
NDPDTLEIYS QLLLFKDREK YYYELAYPMG ISASHKRIIN VLCSYLGLVE
360 370 380 390 400
VYDPRFIIIR RKILDHANLQ SHLQQQGQMT SAHPLQPNST GGSMNRSQSY
410 420 430 440 450
TSLLQAHAAA AANSISNQAV NNSSNSNTIN SNNGNGNNVI INNNSASSTP
460 470 480 490 500
KISSQGQFSM QPTLTSPKMN IHHSSQYNSA DQPQQPQPQT QQNVQSAAQQ
510 520 530 540 550
QQSFLRQQAT LTPSSRIPSG YSANHYQINS VNPLLRNSQI SPPNSQIPIN
560 570 580 590 600
SQTLSQAQPP AQSQTQQRVP VAYQNASLSS QQLYNLNGPS SANSQSQLLP
610 620 630 640 650
QHTNGSVHSN FSYQSYHDES MLSAHNLNSA DLIYKSLSHS GLDDGLEQGL
660
NRSLSGLDLQ NQNKKNLW
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 | Z23261 Genomic DNA Translation: CAA80795.1 Z35812 Genomic DNA Translation: CAA84871.1 BK006936 Genomic DNA Translation: DAA07068.1 |
Protein sequence database of the Protein Information Resource More...PIRi | S39836 |
NCBI Reference Sequences More...RefSeqi | NP_009502.1, NM_001178291.1 |
Genome annotation databases
Ensembl fungal genome annotation project More...EnsemblFungii | YBL051C; YBL051C; YBL051C |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 852229 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | sce:YBL051C |
<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 | |
|---|---|---|---|---|---|
| P34217 | Uncharacterized protein | 668 | |||
| Pin4p | 561 | ||||
| K7_Pin4p | 668 | ||||
| PIN4p Protein involved in G2/M phase progression and response to DNA damage | 668 | ||||
| Pin4p | 668 | ||||
| +3 | |||||
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| P34217 | PIN4p Protein involved in G2/M phase progression and response to DNA damage | 668 | |||
| Pin4p | 668 | ||||
| Pin4p | 668 | ||||
| K7_Pin4p | 668 | ||||
| Uncharacterized protein | 668 | ||||
| +11 | |||||
<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 | Z23261 Genomic DNA Translation: CAA80795.1 Z35812 Genomic DNA Translation: CAA84871.1 BK006936 Genomic DNA Translation: DAA07068.1 |
Protein sequence database of the Protein Information Resource More...PIRi | S39836 |
NCBI Reference Sequences More...RefSeqi | NP_009502.1, NM_001178291.1 |
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 |
| 2A0T | NMR | - | B | 301-310 | [»] | |
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | P34217 | |||||
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P34217 | |||||
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 | 32647, 318 interactors |
Database of interacting proteins More...DIPi | DIP-1905N |
The Eukaryotic Linear Motif resource for Functional Sites in Proteins More...ELMi | P34217 |
Protein interaction database and analysis system More...IntActi | P34217, 44 interactors |
Molecular INTeraction database More...MINTi | P34217 |
STRING: functional protein association networks More...STRINGi | 4932.YBL051C |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | P34217 |
Proteomic databases
MaxQB - The MaxQuant DataBase More...MaxQBi | P34217 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | P34217 |
PRoteomics IDEntifications database More...PRIDEi | P34217 |
Protocols and materials databases
| Structural Biology Knowledgebase | Search... |
Genome annotation databases
Ensembl fungal genome annotation project More...EnsemblFungii | YBL051C; YBL051C; YBL051C |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 852229 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | sce:YBL051C |
Organism-specific databases
Eukaryotic Pathogen Database Resources More...EuPathDBi | FungiDB:YBL051C |
Saccharomyces Genome Database More...SGDi | S000000147 PIN4 |
Phylogenomic databases
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000115549 |
Identification of Orthologs from Complete Genome Data More...OMAi | KKMLPQA |
Database of Orthologous Groups More...OrthoDBi | EOG092C3WNG |
Enzyme and pathway databases
BioCyc Collection of Pathway/Genome Databases More...BioCyci | YEAST:G3O-28950-MONOMER |
Miscellaneous databases
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | P34217 |
Protein Ontology More...PROi | PR:P34217 |
Family and domain databases
Conserved Domains Database More...CDDi | cd02639 R3H_RRM, 1 hit cd12253 RRM_PIN4_like, 1 hit |
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 3.30.70.330, 1 hit |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR012677 Nucleotide-bd_a/b_plait_sf IPR034186 PIN4-like_RRM IPR034069 R3H_Cip2 IPR035979 RBD_domain_sf IPR000504 RRM_dom |
Pfam protein domain database More...Pfami | View protein in Pfam PF00076 RRM_1, 1 hit |
Simple Modular Architecture Research Tool; a protein domain database More...SMARTi | View protein in SMART SM00360 RRM, 1 hit |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF54928 SSF54928, 1 hit |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS50102 RRM, 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 | PIN4_YEAST | |
| <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 | P34217Primary (citable) accession number: P34217 Secondary accession number(s): D6VPU8 | |
| <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: | February 1, 1994 |
| Last sequence update: | February 1, 1994 | |
| Last modified: | July 18, 2018 | |
| This is version 154 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 | Fungal Protein Annotation Program | |
<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi
<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
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - Yeast
Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD - Yeast chromosome II
Yeast (Saccharomyces cerevisiae) chromosome II: entries and gene names
