about
Thiopurine methyltransferaseCystathionine beta-synthaseBase methyltransferase of 25S rRNA 2 homologMethyltransferase like 14Methyltransferase like 3Protein arginine methyltransferase 8Suppressor of variegation 3-9 homolog 2Protein arginine methyltransferase 17-carboxy-7-deazaguanine synthase HP0934Cyclic pyranopterin monophosphate synthase HP0768TRNA methyltransferase HP0388Cyclic pyranopterin monophosphate synthase PA1505TRNA (cmo5U34)-methyltransferase PA0775Radical activating enzyme PA0975Molybdenum cofactor biosynthesis protein A PA3870Protein arginine N-methyltransferase 8Protein arginine N-methyltransferase 1Glycine N-methyltransferaseMethyltransferase like 14Suppressor of variegation 3-9 2Methyltransferase like 3PDX1 C-terminal inhibiting factor 17-cyano-7-deazaguanosine (preQ0) biosynthesis protein QueE ECIAI39_2968AdoMet-dependent methyltransferase ECIAI39_1179Molybdenum cofactor biosynthesis protein A ECIAI39_0757Hypothetical protein NMB0529TRNA (cmo5U34)-methyltransferase Cj0590Cyclic pyranopterin monophosphate synthase Cj0161c7-carboxy-7-deazaguanine synthase Cj0160cCoenzyme PQQ synthesis protein E PP_03767-carboxy-7-deazaguanine synthase PP_1225Cyclic pyranopterin monophosphate synthase PP_4597Radical activating enzyme lpg2041Glycine N-methyltransferaseBase methyltransferase of 25S rRNA 2Coenzyme PQQ synthesis protein E PA1989TRNA 5-methoxyuridine(34)/uridine-5-oxyacetic acid(34) metyltransferase CmoA PP_1441Pyrroloquinoline quinone biosynthesis protein PqqE RSP_0790Cyclic pyranopterin monophosphate synthase subunit MoaA RSP_0235Cyclic pyranopterin monophosphate synthase subunit MoaA RSP_3050
P680
Human cystathionine β-synthase (CBS) contains two classes of binding sites for S-adenosylmethionine (SAM): complex regulation of CBS activity and stability by SAMStructural Basis of Substrate Recognition in Thiopurine S -Methyltransferase † ‡Structural Biology of Human H3K9 MethyltransferasesA novel route to product specificity in the Suv4-20 family of histone H4K20 methyltransferasesNovel helical assembly in arginine methyltransferase 8Human erythrocyte thiopurine methyltransferase: radiochemical microassay and biochemical propertiesStructure and regulation of ZCCHC4 in m6A-methylation of 28S rRNACap-specific terminal N 6-methylation of RNA by an RNA polymerase II-associated methyltransferase
P921
Q14880764-A2C27794-B88D-40A5-94FE-58B3C0B4771CQ14913099-6401C441-F36A-4AC7-A8B9-3361816B5366Q21106716-E4D7652F-0B2D-45F2-B048-014E9A3DB092Q21120849-4A78575D-0E6C-415E-974A-7F233644C6F3Q21124024-A0801C73-882C-4B48-8CBD-F0A30A7A11A3Q21131689-9F773D04-3193-4113-B4E4-2955FBFE7C29Q21132932-9A238981-0991-49D7-91F9-175ACA0D84BEQ21201642-5043F496-6CED-4A9F-94E6-5E367CE91725Q21632014-22E1A2C9-F1B0-4A3D-91D5-F7C61A70BD07Q21632419-036C719A-4713-432F-AEA0-F66A26AFB05DQ21633588-B45F9711-EB17-40C4-B1DA-E54F98C10CB9Q21757950-1DC7F7E0-4CA2-4E0B-96BB-E6F600DF83FEQ21758664-515CD894-A6E4-447E-83B7-1DE5EB326851Q21761981-95420ED9-FF40-4D90-B7B4-7664374021B7Q21763093-0DBE672A-B781-4AF9-851A-AD499FFD0BACQ21981666-1B168043-51F8-47D9-9BA4-F598BD3B2891Q21981666-A640A68F-C55B-469C-9AD3-99C4B70DA765Q21981677-36278F11-B717-4D1E-8377-294EC965C776Q21981677-C5B95433-D1BD-49A6-9AF2-F3EB10949A0AQ21984046-9EBA48D3-DA84-4807-9F59-CCDFBA746CBBQ21985121-C722C848-2179-4AA3-85C5-212D4E419F53Q21986916-409A111E-E6D1-4D73-B9A8-B98E70E40F9EQ21987736-904C3D22-7629-4A48-A147-EF5C92961AE9Q21988884-0B451670-6218-43AC-B729-E0D10002C13BQ21988884-1841E937-15CF-4B0C-BAE0-299477FEC544Q22135701-609D1066-5F16-49DE-BF65-28E5BAA4AAD3Q22160405-CDB64624-E427-4228-9987-321AA2A18903Q22161281-4A26A419-2DB3-4630-B8FB-17FA384A1515Q22270550-FE120DB9-B14C-41B9-86F5-0CDFC3EB643FQ22300374-22275850-6C6A-41AE-B405-C5613E46549FQ22301379-10EA7A37-A19A-43F0-A076-84EB4F14DFB0Q22301856-81065DB4-7D2D-4597-890F-8135E961A3FFQ22314251-A84FF945-9875-4186-9435-A81FF3E88BCFQ22314496-09892583-1A8A-49AF-B4D1-225A2025D685Q22318265-BB7C95B0-D9DB-403B-B84F-911C9701EF43Q22335490-FE515974-1E3C-4305-A761-7F72020551B9Q22679798-8114B5BB-FCB8-4051-A338-FAB2108448A9Q22680291-0508AEFF-F1E1-4EB2-BFFF-ACC9A7E2C9F8Q22990032-2F7640EE-0F1C-4258-88E1-6EFDB3125A3BQ22991449-1E329733-A2C4-4041-8C1E-8BE28B8EB2AB
P680
Q24298897-89F5C99D-7B80-4BF2-A3C5-B7AAACFE6608Q24298897-F4C63F0A-513C-4F97-A5DF-7A179D16850DQ27650629-E64B3FE2-6A92-4291-96B9-211E4FDFA671Q27659033-2AF56A5E-8191-43FF-9C39-78F9EBBF4F8DQ27679986-C2893B2B-6A8C-448D-9437-F5FF988D67BDQ27704022-C615AF45-AAE8-4C92-A448-4A271D1D032CQ52162405-00360F57-65F1-4FFE-A7DF-DAEFDF0DB79CQ91151485-FC00BE0C-A028-48BE-9959-C5448C418C0AQ93358396-C3736AE2-ED4E-403A-B321-9D93F4515F81
P921
description
Interacting selectively and non-covalently with S-adenosyl-L-methionine.
@en
moleculaire functie
@nl
name
S-adenosyl-L-methionine binding
@en
S-adenosyl-L-metioninbinding
@nn
type
label
S-adenosyl-L-methionine binding
@en
S-adenosyl-L-metioninbinding
@nn
altLabel
GO:1904047
@en
prefLabel
S-adenosyl-L-methionine binding
@en
S-adenosyl-L-metioninbinding
@nn
P279
P2888
P686
GO:1904047