UniProtKB - P36873 (PP1G_HUMAN)
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- BLAST>sp|P36873|PP1G_HUMAN Serine/threonine-protein phosphatase PP1-gamma catalytic subunit OS=Homo sapiens OX=9606 GN=PPP1CC PE=1 SV=1 MADLDKLNIDSIIQRLLEVRGSKPGKNVQLQENEIRGLCLKSREIFLSQPILLELEAPLK ICGDIHGQYYDLLRLFEYGGFPPESNYLFLGDYVDRGKQSLETICLLLAYKIKYPENFFL LRGNHECASINRIYGFYDECKRRYNIKLWKTFTDCFNCLPIAAIVDEKIFCCHGGLSPDL QSMEQIRRIMRPTDVPDQGLLCDLLWSDPDKDVLGWGENDRGVSFTFGAEVVAKFLHKHD LDLICRAHQVVEDGYEFFAKRQLVTLFSAPNYCGEFDNAGAMMSVDETLMCSFQILKPAE KKKPNATRPVTPPRGMITKQAKK
- Align
Serine/threonine-protein phosphatase PP1-gamma catalytic subunit
PPP1CC
Annotation score:5 out of 5
<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome.<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.16"S6K1-mediated disassembly of mitochondrial URI/PP1gamma complexes activates a negative feedback program that counters S6K1 survival signaling."
Djouder N., Metzler S.C., Schmidt A., Wirbelauer C., Gstaiger M., Aebersold R., Hess D., Krek W.
Mol. Cell 28:28-40(2007) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN DEPHOSPHORYLATION OF RPS6KB1, ENZYME REGULATION, INTERACTION WITH URI1, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY. - Ref.25"Identification and characterization of a novel human PP1 phosphatase complex."
Lee J.H., You J., Dobrota E., Skalnik D.G.
J. Biol. Chem. 285:24466-24476(2010) [PubMed] [Europe PMC] [Abstract]Cited for: IDENTIFICATION IN THE PTW/PP1 PHOSPHATASE COMPLEX, FUNCTION, INTERACTION WITH PPP1R8. - Ref.27"Protein phosphatase 1 (PP1) is a post-translational regulator of the mammalian circadian clock."
Schmutz I., Wendt S., Schnell A., Kramer A., Mansuy I.M., Albrecht U.
PLoS ONE 6:E21325-E21325(2011) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN CIRCADIAN CLOCK. - Ref.28"Phosphorylation of FOXP3 controls regulatory T cell function and is inhibited by TNF-alpha in rheumatoid arthritis."
Nie H., Zheng Y., Li R., Guo T.B., He D., Fang L., Liu X., Xiao L., Chen X., Wan B., Chin Y.E., Zhang J.Z.
Nat. Med. 19:322-328(2013) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH FOXP3, INDUCTION.
Miscellaneous
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. the chemical reaction it catalyzes. This information usually correlates with the presence of an EC (Enzyme Commission) number in the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi
<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.33"Crystal structure and mutagenesis of a protein phosphatase-1:calcineurin hybrid elucidate the role of the beta12-beta13 loop in inhibitor binding."
Maynes J.T., Perreault K.R., Cherney M.M., Luu H.A., James M.N., Holmes C.F.
J. Biol. Chem. 279:43198-43206(2004) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 6-298 IN COMPLEX WITH MANGANESE, CATALYTIC ACTIVITY, COFACTOR.
<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori
<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.32"Crystal structure of the tumor-promoter okadaic acid bound to protein phosphatase-1."
Maynes J.T., Bateman K.S., Cherney M.M., Das A.K., Luu H.A., Holmes C.F., James M.N.
J. Biol. Chem. 276:44078-44082(2001) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH MANGANESE, COFACTOR. - Ref.33"Crystal structure and mutagenesis of a protein phosphatase-1:calcineurin hybrid elucidate the role of the beta12-beta13 loop in inhibitor binding."
Maynes J.T., Perreault K.R., Cherney M.M., Luu H.A., James M.N., Holmes C.F.
J. Biol. Chem. 279:43198-43206(2004) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 6-298 IN COMPLEX WITH MANGANESE, CATALYTIC ACTIVITY, COFACTOR.
<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.32"Crystal structure of the tumor-promoter okadaic acid bound to protein phosphatase-1."
Maynes J.T., Bateman K.S., Cherney M.M., Das A.K., Luu H.A., Holmes C.F., James M.N.
J. Biol. Chem. 276:44078-44082(2001) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH MANGANESE, COFACTOR. - Ref.33"Crystal structure and mutagenesis of a protein phosphatase-1:calcineurin hybrid elucidate the role of the beta12-beta13 loop in inhibitor binding."
Maynes J.T., Perreault K.R., Cherney M.M., Luu H.A., James M.N., Holmes C.F.
J. Biol. Chem. 279:43198-43206(2004) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 6-298 IN COMPLEX WITH MANGANESE, CATALYTIC ACTIVITY, COFACTOR.
<p>This subsection of the ‘Function’ section describes an enzyme regulatory mechanism and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/enzyme_regulation' target='_top'>More...</a></p>Enzyme regulationi
<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.13"A selective inhibitor of eIF2alpha dephosphorylation protects cells from ER stress."
Boyce M., Bryant K.F., Jousse C., Long K., Harding H.P., Scheuner D., Kaufman R.J., Ma D., Coen D.M., Ron D., Yuan J.
Science 307:935-939(2005) [PubMed] [Europe PMC] [Abstract]Cited for: ENZYME REGULATION. - Ref.16"S6K1-mediated disassembly of mitochondrial URI/PP1gamma complexes activates a negative feedback program that counters S6K1 survival signaling."
Djouder N., Metzler S.C., Schmidt A., Wirbelauer C., Gstaiger M., Aebersold R., Hess D., Krek W.
Mol. Cell 28:28-40(2007) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN DEPHOSPHORYLATION OF RPS6KB1, ENZYME REGULATION, INTERACTION WITH URI1, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
Sites
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi | 64 | Manganese 12 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
| 1 | |
| <p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi | 66 | Manganese 12 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
| 1 | |
| <p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi | 92 | Manganese 12 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
| 1 | |
| <p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi | 92 | Manganese 22 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
| 1 | |
| <p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi | 124 | Manganese 22 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
| 1 | |
| <p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei | 125 | Proton donor1 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 subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi | 173 | Manganese 22 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
| 1 | |
| <p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi | 248 | Manganese 22 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
| 1 | |
| <p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei | 273 | Inhibition by microcystin toxin binding | 1 |
<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
- lamin binding Source: Ensembl
- metal ion binding Source: UniProtKB-KW
- phosphatase activity Source: UniProtKB
- phosphoprotein phosphatase activity Source: Reactome
- protein complex binding Source: Ensembl
- protein C-terminus binding Source: Ensembl
- protein domain specific binding Source: Ensembl
- protein kinase binding Source: UniProtKB <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 N-terminus binding Source: MGI <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 phosphatase 1 binding Source: Ensembl
- protein serine/threonine phosphatase activity Source: UniProtKB <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
- RNA binding Source: UniProtKBInferred from high throughput direct assayi
<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
- cell division Source: UniProtKB-KW
- circadian regulation of gene expression Source: UniProtKB
- entrainment of circadian clock by photoperiod Source: UniProtKB
- glycogen metabolic process Source: UniProtKB-KW
- neuron differentiation Source: Ensembl
- protein dephosphorylation Source: MGI <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
- regulation of circadian rhythm Source: UniProtKB <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
- regulation of nucleocytoplasmic transport Source: Ensembl
- sister chromatid cohesion Source: Reactome
<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 | Hydrolase, Protein phosphatase |
| Biological process | Biological rhythms, Carbohydrate metabolism, Cell cycle, Cell division, Glycogen metabolism |
| Ligand | Manganese, Metal-binding |
Enzyme and pathway databases
BRENDA Comprehensive Enzyme Information System More...BRENDAi | 3.1.3.16. 2681. |
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-HSA-141444. Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal. R-HSA-163560. Triglyceride catabolism. R-HSA-2173788. Downregulation of TGF-beta receptor signaling. R-HSA-2467813. Separation of Sister Chromatids. R-HSA-2500257. Resolution of Sister Chromatid Cohesion. R-HSA-400253. Circadian Clock. R-HSA-5663220. RHO GTPases Activate Formins. R-HSA-68877. Mitotic Prometaphase. |
SignaLink: a signaling pathway resource with multi-layered regulatory networks More...SignaLinki | P36873. |
SIGNOR Signaling Network Open Resource More...SIGNORi | P36873. |
<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: Serine/threonine-protein phosphatase PP1-gamma catalytic subunit (EC:3.1.3.16)Short name: PP-1G Alternative name(s): Protein phosphatase 1C catalytic subunit |
| <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:PPP1CC |
| <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 <span class="caps">NCBI</span> 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:ENSG00000186298.11. |
Human Gene Nomenclature Database More...HGNCi | HGNC:9283. PPP1CC. |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 176914. gene. |
neXtProt; the human protein knowledge platform More...neXtProti | NX_P36873. |
<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
Mitochondrion
- Mitochondrion 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.16"S6K1-mediated disassembly of mitochondrial URI/PP1gamma complexes activates a negative feedback program that counters S6K1 survival signaling."
Djouder N., Metzler S.C., Schmidt A., Wirbelauer C., Gstaiger M., Aebersold R., Hess D., Krek W.
Mol. Cell 28:28-40(2007) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN DEPHOSPHORYLATION OF RPS6KB1, ENZYME REGULATION, INTERACTION WITH URI1, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
- Mitochondrion 1 Publication
Nucleus
- Nucleus
- nucleolus 2 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
- Ref.8"Dynamic targeting of protein phosphatase 1 within the nuclei of living mammalian cells."
Trinkle-Mulcahy L., Sleeman J.E., Lamond A.I.
J. Cell Sci. 114:4219-4228(2001) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION, INTERACTION WITH PPP1R8, MUTAGENESIS OF HIS-125. - Ref.26"RRP1B targets PP1 to mammalian cell nucleoli and is associated with pre-60S ribosomal subunits."
Chamousset D., De Wever V., Moorhead G.B., Chen Y., Boisvert F.M., Lamond A.I., Trinkle-Mulcahy L.
Mol. Biol. Cell 21:4212-4226(2010) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH RRP1B, SUBCELLULAR LOCATION.
- nucleoplasm 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.8"Dynamic targeting of protein phosphatase 1 within the nuclei of living mammalian cells."
Trinkle-Mulcahy L., Sleeman J.E., Lamond A.I.
J. Cell Sci. 114:4219-4228(2001) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION, INTERACTION WITH PPP1R8, MUTAGENESIS OF HIS-125.
- Nucleus speckle 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.8"Dynamic targeting of protein phosphatase 1 within the nuclei of living mammalian cells."
Trinkle-Mulcahy L., Sleeman J.E., Lamond A.I.
J. Cell Sci. 114:4219-4228(2001) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION, INTERACTION WITH PPP1R8, MUTAGENESIS OF HIS-125.
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.8"Dynamic targeting of protein phosphatase 1 within the nuclei of living mammalian cells."
Trinkle-Mulcahy L., Sleeman J.E., Lamond A.I.
J. Cell Sci. 114:4219-4228(2001) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION, INTERACTION WITH PPP1R8, MUTAGENESIS OF HIS-125.
- kinetochore 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.11"Time-lapse imaging reveals dynamic relocalization of PP1gamma throughout the mammalian cell cycle."
Trinkle-Mulcahy L., Andrews P.D., Wickramasinghe S., Sleeman J., Prescott A., Lam Y.W., Lyon C., Swedlow J.R., Lamond A.I.
Mol. Biol. Cell 14:107-117(2003) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION.
- Cleavage furrow 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.11"Time-lapse imaging reveals dynamic relocalization of PP1gamma throughout the mammalian cell cycle."
Trinkle-Mulcahy L., Andrews P.D., Wickramasinghe S., Sleeman J., Prescott A., Lam Y.W., Lyon C., Swedlow J.R., Lamond A.I.
Mol. Biol. Cell 14:107-117(2003) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION.
- Midbody 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.11"Time-lapse imaging reveals dynamic relocalization of PP1gamma throughout the mammalian cell cycle."
Trinkle-Mulcahy L., Andrews P.D., Wickramasinghe S., Sleeman J., Prescott A., Lam Y.W., Lyon C., Swedlow J.R., Lamond A.I.
Mol. Biol. Cell 14:107-117(2003) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION.
Note: Colocalizes with SPZ1 in the nucleus (By similarity). Colocalizes with URI1 at mitochondrion (PubMed:17936702). Rapidly exchanges between the nucleolar, nucleoplasmic and cytoplasmic compartments (PubMed:11739654). Highly mobile in cells and can be relocalized through interaction with targeting subunits (PubMed:17965019). In the presence of PPP1R8 relocalizes from the nucleolus to nuclear speckles (PubMed:11739654). Shows a dynamic targeting to specific sites throughout the cell cycle (PubMed:12529430). Highly concentrated in nucleoli of interphase cells and localizes at kinetochores early in mitosis (PubMed:12529430). Relocalization to chromosome-containing regions occurs at the transition from early to late anaphase (PubMed:12529430). Also accumulates at the cleavage furrow and midbody by telophase (PubMed:12529430).By similarity- Cytoplasm 1 Publication
- Ref.8"Dynamic targeting of protein phosphatase 1 within the nuclei of living mammalian cells."
Trinkle-Mulcahy L., Sleeman J.E., Lamond A.I.
J. Cell Sci. 114:4219-4228(2001) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION, INTERACTION WITH PPP1R8, MUTAGENESIS OF HIS-125. - Ref.11"Time-lapse imaging reveals dynamic relocalization of PP1gamma throughout the mammalian cell cycle."
Trinkle-Mulcahy L., Andrews P.D., Wickramasinghe S., Sleeman J., Prescott A., Lam Y.W., Lyon C., Swedlow J.R., Lamond A.I.
Mol. Biol. Cell 14:107-117(2003) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION. - Ref.16"S6K1-mediated disassembly of mitochondrial URI/PP1gamma complexes activates a negative feedback program that counters S6K1 survival signaling."
Djouder N., Metzler S.C., Schmidt A., Wirbelauer C., Gstaiger M., Aebersold R., Hess D., Krek W.
Mol. Cell 28:28-40(2007) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN DEPHOSPHORYLATION OF RPS6KB1, ENZYME REGULATION, INTERACTION WITH URI1, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY. - Ref.17"NOM1 targets protein phosphatase I to the nucleolus."
Gunawardena S.R., Ruis B.L., Meyer J.A., Kapoor M., Conklin K.F.
J. Biol. Chem. 283:398-404(2008) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION, INTERACTION WITH NOM1.
<p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More…</a></p> Manual assertion inferred from sequence similarity toi
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
Cytosol
- cytosol Source: Reactome
Mitochondrion
- mitochondrial outer membrane Source: Ensembl
- mitochondrion Source: UniProtKB <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
Nucleus
- nuclear speck Source: UniProtKB-SubCell
- nucleolus Source: UniProtKB <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
- nucleus Source: UniProtKB <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
Other locations
- cleavage furrow Source: UniProtKB-SubCell
- condensed chromosome kinetochore Source: UniProtKB-SubCell
- cytoplasm Source: UniProtKB <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
- dendritic spine Source: Ensembl
- focal adhesion Source: UniProtKBInferred from high throughput direct assayi
- midbody Source: UniProtKB-SubCell
- protein complex Source: UniProtKB <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
- protein phosphatase type 1 complex Source: InterPro
- PTW/PP1 phosphatase complex Source: UniProtKB <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
Centromere, Chromosome, Cytoplasm, Kinetochore, Mitochondrion, Nucleus<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 | 125 | H → A: Loss of activity. 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 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 | 273 | C → A, S or L: Abolishes interaction with microcystin toxin. 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 |
Organism-specific databases
DisGeNET More...DisGeNETi | 5501. |
Open Targets More...OpenTargetsi | ENSG00000186298. |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA33611. |
Chemistry databases
ChEMBL database of bioactive drug-like small molecules More...ChEMBLi | CHEMBL4438. |
Drug and drug target database More...DrugBanki | DB02860. Calyculin A. DB04738. Motuporin. |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | PPP1CC. |
Domain mapping of disease mutations (DMDM) More...DMDMi | 548573. |
<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 <a href="http://www.uniprot.org/help/ptm_processing_section"><span class="caps">PTM</span> / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methioninei | RemovedCombined 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
<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
| |||
| <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_0000058787 | 2 – 323 | Serine/threonine-protein phosphatase PP1-gamma catalytic subunitAdd BLAST | 322 |
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 | 2 | N-acetylalanineCombined 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
<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 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 | 307 | PhosphothreonineCombined 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 | 311 | PhosphothreonineCombined 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"><span class="caps">PTM</span>/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.12"Alternatively spliced protein variants as potential therapeutic targets for male infertility and contraception."
Fardilha M., Wu W., Sa R., Fidalgo S., Sousa C., Mota C., da Cruz e Silva O.A., da Cruz e Silva E.F.
Ann. N. Y. Acad. Sci. 1030:468-478(2004) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH NEK2, PHOSPHORYLATION.
<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
Acetylation, Disulfide bond, PhosphoproteinProteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | P36873. |
MaxQB - The MaxQuant DataBase More...MaxQBi | P36873. |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | P36873. |
PeptideAtlas More...PeptideAtlasi | P36873. |
PRoteomics IDEntifications database More...PRIDEi | P36873. |
Consortium for Top Down Proteomics More...TopDownProteomicsi | P36873-1. [P36873-1] P36873-2. [P36873-2] |
PTM databases
CarbonylDB database of protein carbonylation sites More...CarbonylDBi | P36873. |
DEPOD human dephosphorylation database More...DEPODi | P36873. |
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | P36873. |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | P36873. |
SwissPalm database of S-palmitoylation events More...SwissPalmi | P36873. |
<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 reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni
<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.28"Phosphorylation of FOXP3 controls regulatory T cell function and is inhibited by TNF-alpha in rheumatoid arthritis."
Nie H., Zheng Y., Li R., Guo T.B., He D., Fang L., Liu X., Xiao L., Chen X., Wan B., Chin Y.E., Zhang J.Z.
Nat. Med. 19:322-328(2013) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH FOXP3, INDUCTION.
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000186298. |
CleanEx database of gene expression profiles More...CleanExi | HS_PPP1CC. |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | P36873. baseline and differential. |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | P36873. HS. |
Organism-specific databases
Human Protein Atlas More...HPAi | CAB022645. |
<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 which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More…</a></p> Manual assertion inferred from sequence similarity toi
16 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
- Ref.6"The cyanobacterial toxin microcystin binds covalently to cysteine-273 on protein phosphatase 1."
MacKintosh R.W., Dalby K.N., Campbell D.G., Cohen P.T.W., Cohen P., MacKintosh C.
FEBS Lett. 371:236-240(1995) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH MICROCYSTIN, MUTAGENESIS OF CYS-273. - Ref.7"PPP1R6, a novel member of the family of glycogen-targeting subunits of protein phosphatase 1."
Armstrong C.G., Browne G.J., Cohen P., Cohen P.T.W.
FEBS Lett. 418:210-214(1997) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH PPP1R3D. - Ref.8"Dynamic targeting of protein phosphatase 1 within the nuclei of living mammalian cells."
Trinkle-Mulcahy L., Sleeman J.E., Lamond A.I.
J. Cell Sci. 114:4219-4228(2001) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION, INTERACTION WITH PPP1R8, MUTAGENESIS OF HIS-125. - Ref.9"Growth arrest and DNA damage-inducible protein GADD34 assembles a novel signaling complex containing protein phosphatase 1 and inhibitor 1."
Connor J.H., Weiser D.C., Li S., Hallenbeck J.M., Shenolikar S.
Mol. Cell. Biol. 21:6841-6850(2001) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH PPP1R15A. - Ref.10"Binding of the concave surface of the Sds22 superhelix to the alpha 4/alpha 5/alpha 6-triangle of protein phosphatase-1."
Ceulemans H., Vulsteke V., De Maeyer M., Tatchell K., Stalmans W., Bollen M.
J. Biol. Chem. 277:47331-47337(2002) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH PPP1R7. - Ref.12"Alternatively spliced protein variants as potential therapeutic targets for male infertility and contraception."
Fardilha M., Wu W., Sa R., Fidalgo S., Sousa C., Mota C., da Cruz e Silva O.A., da Cruz e Silva E.F.
Ann. N. Y. Acad. Sci. 1030:468-478(2004) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH NEK2, PHOSPHORYLATION. - Ref.14"Repo-Man recruits PP1 gamma to chromatin and is essential for cell viability."
Trinkle-Mulcahy L., Andersen J., Lam Y.W., Moorhead G., Mann M., Lamond A.I.
J. Cell Biol. 172:679-692(2006) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH CDCA2. - Ref.15"Protein phosphatase-1alpha regulates centrosome splitting through Nek2."
Mi J., Guo C., Brautigan D.L., Larner J.M.
Cancer Res. 67:1082-1089(2007) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH NEK2. - Ref.16"S6K1-mediated disassembly of mitochondrial URI/PP1gamma complexes activates a negative feedback program that counters S6K1 survival signaling."
Djouder N., Metzler S.C., Schmidt A., Wirbelauer C., Gstaiger M., Aebersold R., Hess D., Krek W.
Mol. Cell 28:28-40(2007) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN DEPHOSPHORYLATION OF RPS6KB1, ENZYME REGULATION, INTERACTION WITH URI1, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY. - Ref.17"NOM1 targets protein phosphatase I to the nucleolus."
Gunawardena S.R., Ruis B.L., Meyer J.A., Kapoor M., Conklin K.F.
J. Biol. Chem. 283:398-404(2008) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION, INTERACTION WITH NOM1. - Ref.25"Identification and characterization of a novel human PP1 phosphatase complex."
Lee J.H., You J., Dobrota E., Skalnik D.G.
J. Biol. Chem. 285:24466-24476(2010) [PubMed] [Europe PMC] [Abstract]Cited for: IDENTIFICATION IN THE PTW/PP1 PHOSPHATASE COMPLEX, FUNCTION, INTERACTION WITH PPP1R8. - Ref.26"RRP1B targets PP1 to mammalian cell nucleoli and is associated with pre-60S ribosomal subunits."
Chamousset D., De Wever V., Moorhead G.B., Chen Y., Boisvert F.M., Lamond A.I., Trinkle-Mulcahy L.
Mol. Biol. Cell 21:4212-4226(2010) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH RRP1B, SUBCELLULAR LOCATION. - Ref.28"Phosphorylation of FOXP3 controls regulatory T cell function and is inhibited by TNF-alpha in rheumatoid arthritis."
Nie H., Zheng Y., Li R., Guo T.B., He D., Fang L., Liu X., Xiao L., Chen X., Wan B., Chin Y.E., Zhang J.Z.
Nat. Med. 19:322-328(2013) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH FOXP3, INDUCTION. - Ref.29"Ki-67 is a PP1-interacting protein that organises the mitotic chromosome periphery."
Booth D.G., Takagi M., Sanchez-Pulido L., Petfalski E., Vargiu G., Samejima K., Imamoto N., Ponting C.P., Tollervey D., Earnshaw W.C., Vagnarelli P.
Elife 3:E01641-E01641(2014) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH MKI67. - Ref.32"Crystal structure of the tumor-promoter okadaic acid bound to protein phosphatase-1."
Maynes J.T., Bateman K.S., Cherney M.M., Das A.K., Luu H.A., Holmes C.F., James M.N.
J. Biol. Chem. 276:44078-44082(2001) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH MANGANESE, COFACTOR. - Ref.33"Crystal structure and mutagenesis of a protein phosphatase-1:calcineurin hybrid elucidate the role of the beta12-beta13 loop in inhibitor binding."
Maynes J.T., Perreault K.R., Cherney M.M., Luu H.A., James M.N., Holmes C.F.
J. Biol. Chem. 279:43198-43206(2004) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 6-298 IN COMPLEX WITH MANGANESE, CATALYTIC ACTIVITY, COFACTOR.
<p>This subsection of the ‘<a href="http://www.uniprot.org/help/interaction_section">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 |
|---|---|---|---|---|
| A1DRY3 | 2 | EBI-3964623,EBI-4311408 | ||
| BRCA1 | P38398 | 2 | EBI-356283,EBI-349905 | |
| CD2BP2 | O95400 | 3 | EBI-356283,EBI-768015 | |
| Clock | O08785 | 2 | EBI-356283,EBI-79859 | From Mus musculus. |
| CSRNP1 | Q96S65 | 3 | EBI-356283,EBI-4311573 | |
| CSRNP2 | Q9H175 | 5 | EBI-356283,EBI-5235958 | |
| OGT | O15294 | 11 | EBI-356283,EBI-539828 | |
| PPP1CA | P62136 | 7 | EBI-356283,EBI-357253 | |
| PPP1R2 | P41236 | 7 | EBI-356283,EBI-1056517 | |
| PPP1R32 | Q7Z5V6 | 4 | EBI-3964623,EBI-4311771 | |
| PPP1R7 | Q15435 | 6 | EBI-356283,EBI-1024281 | |
| RANBP9 | Q96S59 | 3 | EBI-3964623,EBI-636085 | |
| TCTEX1D4 | Q5JR98 | 3 | EBI-3964623,EBI-4311709 | |
| TP53 | P04637 | 2 | EBI-356289,EBI-366083 | |
| TP53BP2 | Q13625 | 8 | EBI-356283,EBI-77642 | |
| TP53BP2 | Q13625-3 | 3 | EBI-356283,EBI-10175039 | |
| URI1 | O94763 | 17 | EBI-356283,EBI-357067 | |
| URI1 | O94763-1 | 8 | EBI-356283,EBI-12590720 | |
| ZFYVE9 | O95405 | 5 | EBI-356283,EBI-296817 |
<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
- lamin binding Source: Ensembl
- protein complex binding Source: Ensembl
- protein C-terminus binding Source: Ensembl
- protein domain specific binding Source: Ensembl
- protein kinase binding Source: UniProtKB <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 N-terminus binding Source: MGI <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 phosphatase 1 binding Source: Ensembl
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGrid) More...BioGridi | 111495. 306 interactors. |
Database of interacting proteins More...DIPi | DIP-749N. |
Protein interaction database and analysis system More...IntActi | P36873. 235 interactors. |
Molecular INTeraction database More...MINTi | P36873. |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000335084. |
Chemistry databases
BindingDB database of measured binding affinities More...BindingDBi | P36873. |
<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 | 9 – 17 | 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 | 18 – 21 | 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 | 32 – 48 | 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 beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 51 – 55 | 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 | 5 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 57 – 62 | 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 | 69 – 79 | 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 beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 87 – 89 | 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 beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 94 – 98 | 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 | 5 | |
| <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 | 100 – 113 | 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 | |
| <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 <span class="caps">DSSP</span> secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 115 – 117 | 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 beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 118 – 120 | 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 | 128 – 131 | 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 hydrogen-bonded turns within the protein sequence. These elements correspond to the <span class="caps">DSSP</span> secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 132 – 135 | 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 | 136 – 143 | 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 | 146 – 156 | 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 beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 162 – 165 | 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 hydrogen-bonded turns within the protein sequence. These elements correspond to the <span class="caps">DSSP</span> secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 166 – 168 | 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 beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 169 – 174 | 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 | 183 – 187 | 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 | 5 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 197 – 199 | 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 | 200 – 206 | 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 beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 214 – 218 | 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 | 5 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 222 – 227 | 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 | 229 – 239 | 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 beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 243 – 246 | 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 beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 254 – 258 | 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 | 5 | |
| <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 <span class="caps">DSSP</span> secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 259 – 262 | 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 beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 263 – 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 | 5 | |
| <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 | 272 – 274 | 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 beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 280 – 285 | 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 beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 290 – 298 | 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 |
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 |
| 1IT6 | X-ray | 2.00 | A/B | 1-323 | [»] | |
| 1JK7 | X-ray | 1.90 | A | 1-323 | [»] | |
| 1U32 | X-ray | 2.00 | A | 6-298 | [»] | |
| 2BCD | X-ray | 2.10 | A | 1-323 | [»] | |
| 2BDX | X-ray | 2.30 | A | 1-323 | [»] | |
| 4UT2 | X-ray | 1.96 | A/B | 1-323 | [»] | |
| 4UT3 | X-ray | 2.19 | A/B | 1-323 | [»] | |
| 5INB | X-ray | 1.30 | A | 7-308 | [»] | |
| 5J28 | X-ray | 2.00 | A/B | 7-308 | [»] | |
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | P36873. | |||||
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P36873. | |||||
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 | P36873. |
<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
<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
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | ENOG410IN85. Eukaryota. ENOG410XPVF. LUCA. |
Ensembl GeneTree More...GeneTreei | ENSGT00530000062911. |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000172697. |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG000216. |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | P36873. |
KEGG Orthology (KO) More...KOi | K06269. |
Identification of Orthologs from Complete Genome Data More...OMAi | QRGYEFF. |
Database of Orthologous Groups More...OrthoDBi | EOG091G0EKF. |
Database for complete collections of gene phylogenies More...PhylomeDBi | P36873. |
TreeFam database of animal gene trees More...TreeFami | TF354243. |
Family and domain databases
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 3.60.21.10. 1 hit. |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR004843. Calcineurin-like_PHP_ApaH. IPR029052. Metallo-depent_PP-like. IPR037981. PPP1CC. IPR006186. Ser/Thr-sp_prot-phosphatase. IPR031675. STPPase_N. |
The PANTHER Classification System More...PANTHERi | PTHR11668:SF204. PTHR11668:SF204. 1 hit. |
Pfam protein domain database More...Pfami | View protein in Pfam PF00149. Metallophos. 1 hit. PF16891. STPPase_N. 1 hit. |
Protein Motif fingerprint database; a protein domain database More...PRINTSi | PR00114. STPHPHTASE. |
Simple Modular Architecture Research Tool; a protein domain database More...SMARTi | View protein in SMART SM00156. PP2Ac. 1 hit. |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS00125. SER_THR_PHOSPHATASE. 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 (2)i
<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.
<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.
This entry describes 2 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to 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
MADLDKLNID SIIQRLLEVR GSKPGKNVQL QENEIRGLCL KSREIFLSQP
60 70 80 90 100
ILLELEAPLK ICGDIHGQYY DLLRLFEYGG FPPESNYLFL GDYVDRGKQS
110 120 130 140 150
LETICLLLAY KIKYPENFFL LRGNHECASI NRIYGFYDEC KRRYNIKLWK
160 170 180 190 200
TFTDCFNCLP IAAIVDEKIF CCHGGLSPDL QSMEQIRRIM RPTDVPDQGL
210 220 230 240 250
LCDLLWSDPD KDVLGWGEND RGVSFTFGAE VVAKFLHKHD LDLICRAHQV
260 270 280 290 300
VEDGYEFFAK RQLVTLFSAP NYCGEFDNAG AMMSVDETLM CSFQILKPAE
310 320
KKKPNATRPV TPPRGMITKQ AKK
The sequence of this isoform differs from the canonical sequence as follows:
315-323: GMITKQAKK → VASGLNPSIQKASNYRNNTVLYE
10 20 30 40 50
MADLDKLNID SIIQRLLEVR GSKPGKNVQL QENEIRGLCL KSREIFLSQP
60 70 80 90 100
ILLELEAPLK ICGDIHGQYY DLLRLFEYGG FPPESNYLFL GDYVDRGKQS
110 120 130 140 150
LETICLLLAY KIKYPENFFL LRGNHECASI NRIYGFYDEC KRRYNIKLWK
160 170 180 190 200
TFTDCFNCLP IAAIVDEKIF CCHGGLSPDL QSMEQIRRIM RPTDVPDQGL
210 220 230 240 250
LCDLLWSDPD KDVLGWGEND RGVSFTFGAE VVAKFLHKHD LDLICRAHQV
260 270 280 290 300
VEDGYEFFAK RQLVTLFSAP NYCGEFDNAG AMMSVDETLM CSFQILKPAE
310 320 330
KKKPNATRPV TPPRVASGLN PSIQKASNYR NNTVLYE
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_051734 | 152 | F → S. Corresponds to variant dbSNP:rs11558237Ensembl. | 1 |
Alternative sequence
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_005094 | 315 – 323 | GMITKQAKK → VASGLNPSIQKASNYRNNTV LYE in isoform Gamma-2. 1 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More…</a></p> Manual assertion based on opinion ini
| 9 |
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 | X74008 mRNA. Translation: CAA52169.1. BC014073 mRNA. Translation: AAH14073.1. L07395 mRNA. Translation: AAA19823.1. |
The Consensus CDS (CCDS) project More...CCDSi | CCDS58279.1. [P36873-2] CCDS9150.1. [P36873-1] |
Protein sequence database of the Protein Information Resource More...PIRi | S35699. S35700. |
NCBI Reference Sequences More...RefSeqi | NP_001231903.1. NM_001244974.1. [P36873-2] NP_002701.1. NM_002710.3. [P36873-1] |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.79081. |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000335007; ENSP00000335084; ENSG00000186298. [P36873-1] ENST00000340766; ENSP00000341779; ENSG00000186298. [P36873-2] |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 5501. |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:5501. |
UCSC genome browser More...UCSCi | uc001tru.4. human. [P36873-1] |
<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 | Organisms | Length | Cluster ID | Cluster name | Size | |
|---|---|---|---|---|---|---|---|
| P36873 | A0A024RBP2 H9YUD3 F6YKN7 K7A7K5 Q4R4V0 A0A2J8XL20 | Homo sapiens (Human) Macaca mulatta (Rhesus macaque) Callithrix jacchus (White-tufted-ear marmoset) Pan troglodytes (Chimpanzee) Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey) Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii) | 323 | UniRef100_P36873 | Cluster: Serine/threonine-protein phosphatase PP1-gamma catalytic subunit | 7 | |
| P36873-2 | A0A2I3TLI4 H2NIN2 F7GFT6 A0A2I2ZXW3 A0A2K5WK94 A0A2I3NER2 A0A2K5J6K0 | Pan troglodytes (Chimpanzee) Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii) Macaca mulatta (Rhesus macaque) Gorilla gorilla gorilla (Western lowland gorilla) Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey) Papio anubis (Olive baboon) Colobus angolensis palliatus (Peters' Angolan colobus) | 337 | UniRef100_P36873-2 | Cluster: Isoform Gamma-2 of Serine/threonine-protein phosphatase PP1-gamma catalytic subunit | 8 |
<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
<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi
| Protein Spotlight The things we forget - Issue 32 of March 2003 |
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 | X74008 mRNA. Translation: CAA52169.1. BC014073 mRNA. Translation: AAH14073.1. L07395 mRNA. Translation: AAA19823.1. |
The Consensus CDS (CCDS) project More...CCDSi | CCDS58279.1. [P36873-2] CCDS9150.1. [P36873-1] |
Protein sequence database of the Protein Information Resource More...PIRi | S35699. S35700. |
NCBI Reference Sequences More...RefSeqi | NP_001231903.1. NM_001244974.1. [P36873-2] NP_002701.1. NM_002710.3. [P36873-1] |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.79081. |
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 |
| 1IT6 | X-ray | 2.00 | A/B | 1-323 | [»] | |
| 1JK7 | X-ray | 1.90 | A | 1-323 | [»] | |
| 1U32 | X-ray | 2.00 | A | 6-298 | [»] | |
| 2BCD | X-ray | 2.10 | A | 1-323 | [»] | |
| 2BDX | X-ray | 2.30 | A | 1-323 | [»] | |
| 4UT2 | X-ray | 1.96 | A/B | 1-323 | [»] | |
| 4UT3 | X-ray | 2.19 | A/B | 1-323 | [»] | |
| 5INB | X-ray | 1.30 | A | 7-308 | [»] | |
| 5J28 | X-ray | 2.00 | A/B | 7-308 | [»] | |
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | P36873. | |||||
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P36873. | |||||
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 | 111495. 306 interactors. |
Database of interacting proteins More...DIPi | DIP-749N. |
Protein interaction database and analysis system More...IntActi | P36873. 235 interactors. |
Molecular INTeraction database More...MINTi | P36873. |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000335084. |
Chemistry databases
BindingDB database of measured binding affinities More...BindingDBi | P36873. |
ChEMBL database of bioactive drug-like small molecules More...ChEMBLi | CHEMBL4438. |
Drug and drug target database More...DrugBanki | DB02860. Calyculin A. DB04738. Motuporin. |
PTM databases
CarbonylDB database of protein carbonylation sites More...CarbonylDBi | P36873. |
DEPOD human dephosphorylation database More...DEPODi | P36873. |
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | P36873. |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | P36873. |
SwissPalm database of S-palmitoylation events More...SwissPalmi | P36873. |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | PPP1CC. |
Domain mapping of disease mutations (DMDM) More...DMDMi | 548573. |
Proteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | P36873. |
MaxQB - The MaxQuant DataBase More...MaxQBi | P36873. |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | P36873. |
PeptideAtlas More...PeptideAtlasi | P36873. |
PRoteomics IDEntifications database More...PRIDEi | P36873. |
Consortium for Top Down Proteomics More...TopDownProteomicsi | P36873-1. [P36873-1] P36873-2. [P36873-2] |
Protocols and materials databases
The DNASU plasmid repository More...DNASUi | 5501. |
| Structural Biology Knowledgebase | Search... |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000335007; ENSP00000335084; ENSG00000186298. [P36873-1] ENST00000340766; ENSP00000341779; ENSG00000186298. [P36873-2] |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 5501. |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:5501. |
UCSC genome browser More...UCSCi | uc001tru.4. human. [P36873-1] |
Organism-specific databases
Comparative Toxicogenomics Database More...CTDi | 5501. |
DisGeNET More...DisGeNETi | 5501. |
Eukaryotic Pathogen Database Resources More...EuPathDBi | HostDB:ENSG00000186298.11. |
GeneCards: human genes, protein and diseases More...GeneCardsi | PPP1CC. |
Human Gene Nomenclature Database More...HGNCi | HGNC:9283. PPP1CC. |
Human Protein Atlas More...HPAi | CAB022645. |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 176914. gene. |
neXtProt; the human protein knowledge platform More...neXtProti | NX_P36873. |
Open Targets More...OpenTargetsi | ENSG00000186298. |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA33611. |
GenAtlas: human gene database More...GenAtlasi | Search... |
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | ENOG410IN85. Eukaryota. ENOG410XPVF. LUCA. |
Ensembl GeneTree More...GeneTreei | ENSGT00530000062911. |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000172697. |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG000216. |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | P36873. |
KEGG Orthology (KO) More...KOi | K06269. |
Identification of Orthologs from Complete Genome Data More...OMAi | QRGYEFF. |
Database of Orthologous Groups More...OrthoDBi | EOG091G0EKF. |
Database for complete collections of gene phylogenies More...PhylomeDBi | P36873. |
TreeFam database of animal gene trees More...TreeFami | TF354243. |
Enzyme and pathway databases
BRENDA Comprehensive Enzyme Information System More...BRENDAi | 3.1.3.16. 2681. |
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-HSA-141444. Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal. R-HSA-163560. Triglyceride catabolism. R-HSA-2173788. Downregulation of TGF-beta receptor signaling. R-HSA-2467813. Separation of Sister Chromatids. R-HSA-2500257. Resolution of Sister Chromatid Cohesion. R-HSA-400253. Circadian Clock. R-HSA-5663220. RHO GTPases Activate Formins. R-HSA-68877. Mitotic Prometaphase. |
SignaLink: a signaling pathway resource with multi-layered regulatory networks More...SignaLinki | P36873. |
SIGNOR Signaling Network Open Resource More...SIGNORi | P36873. |
Miscellaneous databases
ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data More...ChiTaRSi | PPP1CC. human. |
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | P36873. |
The Gene Wiki collection of pages on human genes and proteins More...GeneWikii | PPP1CC. |
Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens More...GenomeRNAii | 5501. |
Protein Ontology More...PROi | PR:P36873. |
The Stanford Online Universal Resource for Clones and ESTs More...SOURCEi | Search... |
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000186298. |
CleanEx database of gene expression profiles More...CleanExi | HS_PPP1CC. |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | P36873. baseline and differential. |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | P36873. HS. |
Family and domain databases
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 3.60.21.10. 1 hit. |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR004843. Calcineurin-like_PHP_ApaH. IPR029052. Metallo-depent_PP-like. IPR037981. PPP1CC. IPR006186. Ser/Thr-sp_prot-phosphatase. IPR031675. STPPase_N. |
The PANTHER Classification System More...PANTHERi | PTHR11668:SF204. PTHR11668:SF204. 1 hit. |
Pfam protein domain database More...Pfami | View protein in Pfam PF00149. Metallophos. 1 hit. PF16891. STPPase_N. 1 hit. |
Protein Motif fingerprint database; a protein domain database More...PRINTSi | PR00114. STPHPHTASE. |
Simple Modular Architecture Research Tool; a protein domain database More...SMARTi | View protein in SMART SM00156. PP2Ac. 1 hit. |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS00125. SER_THR_PHOSPHATASE. 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 | PP1G_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 | P36873Primary (citable) accession number: P36873 | |
| <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: | June 1, 1994 |
| Last sequence update: | June 1, 1994 | |
| Last modified: | March 28, 2018 | |
| This is version 210 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
Caution
<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.19"GlcNAcylation of a histone methyltransferase in retinoic-acid-induced granulopoiesis."
Fujiki R., Chikanishi T., Hashiba W., Ito H., Takada I., Roeder R.G., Kitagawa H., Kato S.
Nature 459:455-459(2009) [PubMed] [Europe PMC] [Abstract]Cited for: CAUTION. - Ref.24"Retraction: GlcNAcylation of a histone methyltransferase in retinoic-acid-induced granulopoiesis."
Fujiki R., Chikanishi T., Hashiba W., Ito H., Takada I., Roeder R.G., Kitagawa H., Kato S.
Nature 505:574-574(2014) [PubMed] [Europe PMC] [Abstract]Cited for: CAUTION AND RETRACTION.