Q1L994 · PPR37_DANRE
- ProteinProtein phosphatase 1 regulatory subunit 37
- Geneppp1r37
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids919 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score2/5
Function
function
May inhibit phosphatase activity of protein phosphatase 1 (PP1) complexes.
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Molecular Function | protein phosphatase inhibitor activity |
Keywords
- Molecular function
Names & Taxonomy
Protein names
- Recommended nameProtein phosphatase 1 regulatory subunit 37
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Actinopterygii > Neopterygii > Teleostei > Ostariophysi > Cypriniformes > Danionidae > Danioninae > Danio
Accessions
- Primary accessionQ1L994
- Secondary accessions
Proteomes
Organism-specific databases
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000320941 | 1-919 | Protein phosphatase 1 regulatory subunit 37 | |||
Sequence: MNCEDQAVDLCKAIDLCNVSDNTISHPTPAEEILPRDGLQLMDGDQEEQDAAVLTRLKDVHLKDDALHTKNNGSIAVSADPVNGSAGDLQQSTVEEPLATKCSVGDVGDDGEMDIGVDLSLDENGVLEFEPTAQTQSEESASSCENSLISDTVIELHSQEPLEEHSVDVPSETVPAAATPVVEEAGIKHGLKRVTFPSDEDIVSGAVEPKDPWRHAQNVTVEEILNAYRQACQKLNCKPIPKVLKQTQDLKDLTQRNECLDLKGEKLDYKSCESLEEIFKRVQFKLVDLEQTNLDEDGASALFDMIEYYESATHLNISNNKHIGTRGWQAAAHMMRKTNSLQYLDARNTPLLDHSAPFVARALRISSSLTVLHLENSGISGRPLMLLATALKMNMNLRELYLAENKLNGLQDSAQLGNLLKFNYNIQILDLRNNHILDSGLAYVCEGLKEQRKGLVTLVLWNNQLTHNGMGYLAAALPFTQSLETLNLGHNAVGNEGVHKLKDGLISNRSILRLGLASTKLSCEGAVAIAEFIAESPRLLRLDMRENEIKTGGLMALSLAFKVNTSLLRLDLDREPKKETVKSFIETQRALLADIQNGCKRNFILAREKEETEQKMRLSASMAEIATEDQTHEEEEEEEASPLKKIEEETTDALKDATQESSEVSENQEPKDQESTPQDDSDSDTEDEETPTNTSLTSTSPIPIPAAADTSKTIPSTPPIASPAVISGITVTEASIVTPSSPGRCISVSSPGRGHKIFMVTRVESPPEQQQTSIAMLKSIQPSAITDIKAPSQTQNSTQPTEKSHAEKTPDAQQEDSVSTSTPSLDANIDQTQLTESVSEEEQKKAETLNNEADINEDANTGAPLPNGLKPEFALFEFEGAKPASCIMEHVSVTAELSCGQDLEELLLDASLETSRDAP |
Proteomic databases
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for repeat, region, compositional bias, coiled coil.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Repeat | 340-361 | LRR 1 | ||||
Sequence: SLQYLDARNTPLLDHSAPFVAR | ||||||
Repeat | 368-388 | LRR 2 | ||||
Sequence: SLTVLHLENSGISGRPLMLLA | ||||||
Repeat | 396-417 | LRR 3 | ||||
Sequence: NLRELYLAENKLNGLQDSAQLG | ||||||
Repeat | 425-445 | LRR 4 | ||||
Sequence: NIQILDLRNNHILDSGLAYVC | ||||||
Repeat | 454-474 | LRR 5 | ||||
Sequence: GLVTLVLWNNQLTHNGMGYLA | ||||||
Repeat | 482-502 | LRR 6 | ||||
Sequence: SLETLNLGHNAVGNEGVHKLK | ||||||
Region | 626-716 | Disordered | ||||
Sequence: ATEDQTHEEEEEEEASPLKKIEEETTDALKDATQESSEVSENQEPKDQESTPQDDSDSDTEDEETPTNTSLTSTSPIPIPAAADTSKTIPS | ||||||
Compositional bias | 637-656 | Basic and acidic residues | ||||
Sequence: EEEASPLKKIEEETTDALKD | ||||||
Compositional bias | 690-716 | Polar residues | ||||
Sequence: TPTNTSLTSTSPIPIPAAADTSKTIPS | ||||||
Region | 790-866 | Disordered | ||||
Sequence: APSQTQNSTQPTEKSHAEKTPDAQQEDSVSTSTPSLDANIDQTQLTESVSEEEQKKAETLNNEADINEDANTGAPLP | ||||||
Compositional bias | 813-836 | Polar residues | ||||
Sequence: QQEDSVSTSTPSLDANIDQTQLTE | ||||||
Coiled coil | 833-861 | |||||
Sequence: QLTESVSEEEQKKAETLNNEADINEDANT | ||||||
Compositional bias | 837-852 | Basic and acidic residues | ||||
Sequence: SVSEEEQKKAETLNNE |
Sequence similarities
Belongs to the PPP1R37 family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length919
- Mass (Da)100,325
- Last updated2006-05-30 v1
- ChecksumA9D8D98CF8AAB0F4
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
E7FCE5 | E7FCE5_DANRE | ppp1r37 | 919 |
Sequence caution
Features
Showing features for sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 19 | in Ref. 2; AAI41793 | ||||
Sequence: V → A | ||||||
Sequence conflict | 98-99 | in Ref. 2; AAI41793 | ||||
Sequence: LA → PV | ||||||
Sequence conflict | 183 | in Ref. 2; AAI24388 | ||||
Sequence: E → G | ||||||
Sequence conflict | 191 | in Ref. 2; AAI41793 | ||||
Sequence: L → S | ||||||
Sequence conflict | 609 | in Ref. 2; AAI41793 | ||||
Sequence: K → R | ||||||
Sequence conflict | 632 | in Ref. 2; AAI41793 | ||||
Sequence: H → HE | ||||||
Compositional bias | 637-656 | Basic and acidic residues | ||||
Sequence: EEEASPLKKIEEETTDALKD | ||||||
Compositional bias | 690-716 | Polar residues | ||||
Sequence: TPTNTSLTSTSPIPIPAAADTSKTIPS | ||||||
Sequence conflict | 776 | in Ref. 2; AAI41793 | ||||
Sequence: M → L | ||||||
Compositional bias | 813-836 | Polar residues | ||||
Sequence: QQEDSVSTSTPSLDANIDQTQLTE | ||||||
Compositional bias | 837-852 | Basic and acidic residues | ||||
Sequence: SVSEEEQKKAETLNNE | ||||||
Sequence conflict | 842-888 | in Ref. 2; AAI41793 | ||||
Sequence: Missing |
Keywords
- Technical term