about
Insulin degrading enzymeSolute carrier family 6 (neurotransmitter transporter, serotonin), member 4Von Willebrand factorAdiponectin, C1Q and collagen domain containingMicrotubule-associated protein tauAmyloid beta (A4) precursor proteinGTP cyclohydrolase 1PhospholambanPrion proteinHeme oxygenase 1Aquaporin 4Transglutaminase 2, C polypeptideBCL2-associated X proteinTumor necrosis factor (ligand) superfamily, member 11Potassium voltage-gated channel, shaker-related subfamily, member 1RAD51 recombinaseAnnexin A5Amelogenin, X-linkedAngiopoietin 1Acetyl-Coenzyme A acetyltransferase 1GTP cyclohydrolase 1Superoxide dismutase 2, mitochondrialFas cell surface death receptorMajor prion proteinPotassium voltage-gated channel subfamily A member 5Potassium channel tetramerization domain containing 6Angiopoietin like 4EH domain containing 1Fission, mitochondrial 1Crystallin alpha BDNA fragmentation factor subunit betaDynamin 1 likeDNA polymerase thetaTRNA methyltransferase 61BFc fragment of IgE receptor IgReceptor interacting serine/threonine kinase 1ST13 Hsp70 interacting proteinComplement C9Diacylglycerol kinase deltaPotassium channel tetramerization domain containing 17
P682
The molecular mechanism of lead inhibition of human porphobilinogen synthaseCellular localization, oligomerization, and membrane association of the hereditary spastic paraplegia 3A (SPG3A) protein atlastinSite-specific identification of SUMO-2 targets in cells reveals an inverted SUMOylation motif and a hydrophobic cluster SUMOylation motifHuman perforin employs different avenues to damage membranesStructural and functional similarities of calcium homeostasis modulator 1 (CALHM1) ion channel with connexins, pannexins, and innexinsThe tandem BRCT domains of Ect2 are required for both negative and positive regulation of Ect2 in cytokinesisStructural and mechanistic insights into MICU1 regulation of mitochondrial calcium uptakeCrystal structure of human glycine receptor-α3 bound to antagonist strychnineMoyamoya disease-associated protein mysterin/RNF213 is a novel AAA+ ATPase, which dynamically changes its oligomeric stateStructure of the poly-C9 component of the complement membrane attack complexBiochemical and Functional Characterization of RNF213 (Mysterin) R4810K, a Susceptibility Mutation of Moyamoya Disease, in Angiogenesis In Vitro and In VivoWild-type and missense mutants of retinoschisin co-assemble resulting in either intracellular retention or incorrect assembly of the functionally active octamer.A helical bundle in the N-terminal domain of the BLM helicase mediates dimer and potentially hexamer formation.Self-assembled FUS binds active chromatin and regulates gene transcription.Intermolecular binding between TIFA-FHA and TIFA-pT mediates tumor necrosis factor alpha stimulation and NF-κB activationThe role of Cysteine 227 in subcellular localization, water permeability, and multimerization of aquaporin-11.ß-ureidopropionase deficiency: phenotype, genotype and protein structural consequences in 16 patients.The first transmembrane region of complement component-9 acts as a brake on its self-assembly
P921
Q1225690-7C663103-0EBF-4EEB-8089-6F768CDA6BD3Q14860827-8CD4458D-7250-4BF9-9C21-A378F8D38EE1Q14863680-5FDA3729-0EB0-4D73-8ECE-7DC1DC8C9D21Q14864062-0CC59503-7EC2-47A3-8D97-0031C8CB5A9CQ14865311-10E80353-663A-4ECC-82A7-45C06DA534F9Q14865884-05FB7740-CAFE-49F9-9152-B93C5EE5882FQ1487359-980C368A-0D42-423A-9574-A1368F87C50FQ14873917-88E1697E-902A-4989-8A13-ADE212A842C3Q14881308-2CAAA4A2-7B0E-46F1-AD9F-BB8BB202FF16Q14881308-53F87D85-0934-4BF0-8FE0-EF6ADFA14185Q14882925-2AAFD7BB-7197-41D3-9689-E9349C45E757Q14902507-DE00E0B8-9293-48FC-8DD1-EA33D1DFC70FQ14903612-1ED7586C-89AA-4B32-8261-7901701E54AEQ14905404-C4C6A70E-A8EC-4472-BCAB-2821FC2E594BQ14905570-D27DDC85-3B1F-40D0-A55B-EDD78510F1B2Q14905969-BB932A34-7824-486E-BD83-EA613411DAFEQ14907735-2E9B63FB-8898-4884-B2DD-BED1B043AC1BQ14908242-21302B25-1D0E-4C7B-88D4-B87CDA6607BFQ14908242-F8522DE9-B18F-49DD-9949-F795E7475CB7Q14911774-43D82294-A159-4CA1-8F03-9F2C54566861Q14912180-AA606502-A126-4831-AE0A-2FBC6D4BB293Q14913203-9D87B611-E5E9-4AD1-8754-3A4B8DB62CB2Q14913203-EF21D2B7-FE75-415B-950E-DD18E1D4A815Q14916170-628D6D94-0FA1-476F-BD9F-D3892BC78F89Q15335644-7AD37853-32A5-4CBF-BB15-91ABB41AC654Q15335644-DB687C12-F1FF-473A-972C-E6C93898A787Q1649375-E500A718-3A17-49F6-9190-F07D1311407AQ21096129-D0618C56-CBD0-4FA1-AB4C-4993318FA4EBQ21096129-DF9AC992-BF3C-44A6-AB4C-9FA5F344556AQ21096394-68CB8134-DCCA-4DA6-9F1E-A39F787BB319Q21096446-393B393C-6F4B-487E-84A6-C5A776616A52Q21097344-7B4D843E-44A5-41AC-BE91-CD79F4B21204Q21097347-4F92BBAB-7069-4744-A734-9E6961EF0735Q21100434-154B2879-6492-4F39-A907-7BAD616686FAQ21100907-86085EA0-23DB-4A39-9813-2D0A6B0572F0Q21101094-58369601-D956-43E2-8865-E099AC557F5FQ21101107-D24D1A2F-C7B2-4CFC-8EF4-CFE4AAD82717Q21101126-4162CE42-D0D4-437C-ABE5-8C3120ACFA52Q21101315-F782E900-DDFB-4F5D-A682-C2A8592A16A9Q21101408-54836E52-4276-4E07-BD71-C733BDB0FEB1
P682
Q24290407-B1984CD1-9FD1-413B-8D91-62CEEC2E6E54Q24295115-697186F1-D64E-4CC5-B814-EDA2AF872C51Q24297572-EF5953D6-0CC5-44B3-9645-5945C7DB2024Q24301586-EADF9130-80A4-4AC9-8896-7FFD2DBED3DEQ24307848-A1C2772F-CEA1-4EBC-8506-9A622EA7E9AFQ24315138-DDC445C3-766D-4C07-8F7C-F47802008122Q24336668-A3F5EFA7-069E-42B3-8A9B-1F8F73C3A429Q27702217-D373449C-0704-4F03-83E2-F437F867811FQ28115492-089380F1-BCA2-4518-93B8-187F5AD66AFAQ28115911-F82B3845-FD5C-4DEF-9A0C-53FBBC068122Q28118678-2B73311F-2D1F-4EAA-B8E2-346B87B8D659Q29465813-76783782-8B71-43F0-8CEC-BF2BB9D123C2Q31814841-53925C2B-5916-426E-BA6F-822F69746C86Q34752975-C892EA32-EA8D-414B-8895-F57D4BBBAA57Q36155061-B3756E64-5712-4CC7-80B5-9FFBD61680E1Q40419784-158FCAF2-FC00-4D61-B741-8A15E56A7D4EQ41934023-1BC48951-69B7-438A-B3C3-7D659952B269Q57651515-06538383-6C63-4F14-82E2-FF4DA3EE29C8
P921
description
The process of creating protei ...... he depolymerization of a large
@en
biologisch proces
@nl
name
protein homooligomerization
@en
type
label
protein homooligomerization
@en
altLabel
GO:0051260
@en
protein homooligomer assembly
@en
protein homooligomer biosynthesis
@en
protein homooligomer biosynthetic process
@en
protein homooligomer formation
@en
prefLabel
protein homooligomerization
@en
P2888
P686
GO:0051260