about
Insulin degrading enzymeVasodilator stimulated phosphoproteinTransformation related protein 53CatalaseHypoxanthine guanine phosphoribosyl transferaseAldolase A, fructose-bisphosphateAcid phosphatase, prostateGlyceraldehyde-3-phosphate dehydrogenaseTransient receptor potential cation channel, subfamily V, member 6Aquaporin 4Aquaporin 2Potassium inwardly-rectifying channel, subfamily J, member 2Transient receptor potential cation channel, subfamily V, member 1Serine racemaseMucolipin 1Transformation related protein 63Transient receptor potential cation channel, subfamily A, member 1Transient receptor potential cation channel, subfamily M, member 4Transient receptor potential cation channel, subfamily M, member 8Transient receptor potential cation channel subfamily V member 5Superoxide dismutase 2, mitochondrialPotassium inwardly rectifying channel subfamily J member 2Aquaporin 2Acyl-CoA thioesterase 13Actinin alpha 2APAF1 interacting proteinAdaptor protein, phosphotyrosine interacting with PH domain and leucine zipper 22,4-dienoyl-CoA reductase 1Dynamin 1 likeAldehyde dehydrogenase 1 family member A2Aldehyde dehydrogenase 1 family member A3ST13 Hsp70 interacting proteinCD247 moleculeCarbonyl reductase 4Chibby family member 1, beta catenin antagonistHistocompatibility minor 13Pterin-4 alpha-carbinolamine dehydratase 2GlutaminasePolycystin 2, transient receptor potential cation channelEnah/Vasp-like
P682
Full-length human glutaminase in complex with an allosteric inhibitorRegulation of cell cycle progression and gene expression by H2A deubiquitinationCrystal structure of human thioesterase superfamily member 2Binding of ATP to TK1-like enzymes is associated with a conformational change in the quaternary structureGlycine N-methyltransferases: a comparison of the crystal structures and kinetic properties of recombinant human, mouse and rat enzymesCrystal structure of Spot 14, a modulator of fatty acid synthesisThe crystal structure of free human hypoxanthine-guanine phosphoribosyltransferase reveals extensive conformational plasticity throughout the catalytic cycleContribution of human manganese superoxide dismutase tyrosine 34 to structure and catalysisThe mechanisms of human hotdog-fold thioesterase 2 (hTHEM2) substrate recognition and catalysis illuminated by a structure and function based analysisStructural basis of PIP2 activation of the classical inward rectifier K+ channel Kir2.2Structural insight into dGTP-dependent activation of tetrameric SAMHD1 deoxynucleoside triphosphate triphosphohydrolaseCrystal structure of human aquaporin 4 at 1.8 A and its mechanism of conductanceHigh-resolution x-ray structure of human aquaporin 5Membrane Curvature Protein Exhibits Interdomain Flexibility and Binds a Small GTPaseInsight into S -adenosylmethionine biosynthesis from the crystal structures of the human methionine adenosyltransferase catalytic and regulatory subunitsX-ray structure of human aquaporin 2 and its implications for nephrogenic diabetes insipidus and traffickingCrystal structure of human aldehyde dehydrogenase 1A3 complexed with NAD(+) and retinoic acidMolecular basis for catalysis and substrate-mediated cellular stabilization of human tryptophan 2,3-dioxygenaseStructural characterization of partially disordered human Chibby: insights into its function in the Wnt-signaling pathwayMolecular insights into lipid-assisted Ca(2+) regulation of the TRP channel Polycystin-2Structural Basis of ALDH1A2 Inhibition by Irreversible and Reversible Small Molecule Inhibitors.Hypertryptophanemia due to tryptophan 2,3-dioxygenase deficiency.Structural basis of meiotic chromosome synapsis through SYCP1 self-assemblyKinetic and structural analysis of human ALDH9A1
P921
Q1225690-416135F5-EDA1-4CCA-864C-DFE5ECC96690Q1299381-2B04D2A2-EE31-4D84-8C44-133E9D379D29Q14818136-2F2F80AD-478E-4374-9328-ABCE6E964B14Q14818136-830F392C-4BC6-4CA7-9EF2-4143EF76BF60Q14849204-10400B27-532A-47C9-B827-E55F6EDB52F4Q14864609-8E025428-8CD6-458A-BCFB-013EA677A847Q14865094-B385EEDA-9246-4B4F-BCCE-2E382B8EBB2CQ14878292-017D9929-C3A8-4183-A271-C3D72E94A9B1Q14890093-59C099C8-5674-4A5F-8B0E-7547AF962755Q14891589-1AF48C23-A7EE-440E-BC6C-E170F61163BDQ14902507-030FE6A0-FE7B-4A65-8E93-62FD0EC92D87Q14902507-0F6898E5-24A8-47AF-9464-89DA4BC4D12FQ14902532-BF338AF7-4218-4FD6-BE61-F6AC3B63537EQ14905763-B51982CF-93D3-4A47-BF9E-BA8DDB92FFD2Q14908176-9A48D005-049E-482C-8AF9-33A804924C0FQ14914220-B95BA786-A3B5-47CD-96A1-D67FC7F9CCE6Q14914220-DACB9AA2-A613-4135-8AD7-227C297DFE23Q14914273-24120FC8-2F21-4BB8-A569-89BECE71AD42Q15314027-01D05381-714E-4EF2-8148-FC325CB06C87Q15323278-1D4FF7B5-1E41-4AAA-BAC5-DBD9253819C7Q15323770-ACBCFF2F-38A1-4ED1-A530-755EF73BDD95Q15324415-361DEB18-6075-47DB-A228-07C1CA9F276FQ15327766-34CBFB95-5A8A-4479-9DA0-F5AE0045B24AQ15335644-63C185EF-5778-4D00-AAFE-4A8E3F7A49EFQ2004050-934E99A5-CD32-4153-B704-78623E1B0E87Q2045854-9F5EB446-B7A8-404D-97B4-E4D76EEFEC89Q21096343-9C29EE6F-898E-4690-B730-69FE984B1E69Q21096407-3B40F501-36C7-40A4-981C-44CE71AFEC64Q21100690-AA9BFC42-A218-4C81-B67F-1EB06CC5E906Q21100937-4D733C8E-8599-4225-B836-884D51B7B0AAQ21101067-E98AF94F-5F85-490B-A032-5620CF9A7C22Q21101107-AB946750-1DED-4634-A815-F8B60C84E75BQ21101831-A21C5CB7-35C4-410C-8B5B-6403467A1A06Q21101841-D7BF54D7-3069-49C4-BB07-63EF42475BDFQ21101878-9A2CBDA7-8312-46C5-B979-8C230AD72ADFQ21102029-1984D871-A56E-4CCB-A514-554A90459379Q21102252-1660651C-C29F-48DD-B92E-7E73C51F6AE1Q21102252-D3FCB169-94EB-437E-8B8A-4E3B508F0645Q21102283-48AE2848-6D6B-4A22-BBE4-670C86728BD4Q21102548-6AF80C0C-B24E-4524-AB28-E6E93AFD7B49
P682
Q24295587-1E77A9F3-2F92-4C3F-8C9B-AC2726BDD3C8Q24296401-EA1DF0C4-819D-42FF-961D-920ACE20EEAAQ24300727-FC11F945-A560-480D-984A-AEECCAF9DEE3Q24301636-08EEB128-977C-4C93-B5FE-A2612726AFDFQ24302229-2511E62A-A1F4-4725-903D-8CFE96245F68Q24303625-10F19984-0331-4B94-B5B3-452BB891E898Q24306496-9534B4F0-3549-4B44-B172-F3336500DBC2Q24318481-D1C66579-0EF4-47DA-860C-D84E0E49F37CQ24322296-02FE9F87-7030-42D7-86F2-B783EDC6FF3EQ24336573-06A2C574-87B5-43A7-A83A-D26AB3798E9BQ24339547-AC3D7F47-4CC4-420B-8B39-4484451E3B6FQ24648744-1759F459-EED7-4803-BE2F-9E3A7DB4DAEAQ27651968-456689B1-D721-4034-9C07-453385C656B3Q27674406-F7812C2C-64C9-4D19-9A53-21091B62306DQ27676482-3BE761E5-E057-42A8-B12D-6CD26F068D55Q27683366-54F92BE7-3C93-457E-B547-4989AEC4B62EQ28115266-EE176B7A-8CCB-4949-95A3-85616FA6405EQ28115713-E401626E-F8A3-4A2D-86C1-E016E3B7D265Q28910332-98CDC5CE-AF35-43C1-A1B2-E92A17B5332AQ29147506-4A867D84-FCCD-4FCC-9097-4BDA9C2F82B5Q48117853-8C9A7079-B8FA-44ED-BB4E-44E06600B8F7Q50320385-2E370C23-E8A3-4420-96E0-3DBB5FB1AB70Q63383698-CA3AE201-6476-4C5F-A758-37B9524447EAQ64084262-2B6F88E4-2F3D-4700-B590-AC185510BC11
P921
description
The formation of a protein hom ...... associated identical subunits.
@en
biologisch proces
@nl
name
protein homotetramerization
@en
type
label
protein homotetramerization
@en
altLabel
GO:0051289
@en
protein homotetramer assembly
@en
protein homotetramer biosynthesis
@en
protein homotetramer biosynthetic process
@en
protein homotetramer formation
@en
prefLabel
protein homotetramerization
@en
P2888
P686
GO:0051289