%D8%B3%D9%8A%D9%84%D9%8A%D9%86%D9%88%D8%B3%D9%8A%D8%B3%D8%AA%D8%A6%D9%8A%D9%86%D8%B3%D9%84%D9%86%D9%88%D8%B3%DB%8C%D8%B3%D8%AA%D8%A6%DB%8C%D9%86SelenocisteinSelenociste%C3%AFnaCategory:SelenocysteineSelenocysteinSelenocysteinSelenocysteinSelenocysteineSelenocisteinoSelenociste%C3%ADna%D8%B3%D9%84%D9%86%D9%88%D8%B3%DB%8C%D8%B3%D8%AA%D8%A6%DB%8C%D9%86SelenokysteiiniS%C3%A9l%C3%A9nocyst%C3%A9ineSelenociste%C3%ADnaSzelenociszteinSelenocisteina%E3%82%BB%E3%83%AC%E3%83%8E%E3%82%B7%E3%82%B9%E3%83%86%E3%82%A4%E3%83%B3%EC%85%80%EB%A0%88%EB%85%B8%EC%8B%9C%EC%8A%A4%ED%85%8C%EC%9D%B8Selenocisteinas%D0%A1%D0%B5%D0%BB%D0%B5%D0%BD%D1%82_%D1%86%D0%B8%D1%81%D1%82%D0%B5%D0%B8%D0%BDSelenocyste%C3%AFneSelenocysteinSelenocysteinaSelenociste%C3%ADnaSelenocistein%C4%83%D0%A1%D0%B5%D0%BB%D0%B5%D0%BD%D0%BE%D1%86%D0%B8%D1%81%D1%82%D0%B5%D0%B8%D0%BDSelenocisteinSelenocysteineSelenocyste%C3%ADnSelenocisteinSelenocystein%E0%AE%9A%E0%AF%86%E0%AE%B2%E0%AF%80%E0%AE%A9%E0%AF%8B%E0%AE%9A%E0%AE%BF%E0%AE%B8%E0%AF%8D%E0%AE%9F%E0%AF%80%E0%AE%A9%E0%AF%8DSelenosistein%D0%A1%D0%B5%D0%BB%D0%B5%D0%BD%D0%BE%D1%86%D0%B8%D1%81%D1%82%D0%B5%D1%97%D0%BDSelenocysteineSelenocysteine%E7%A1%92%E5%8D%8A%E8%83%B1%E6%B0%A8%E9%85%B8Q408663%E7%A1%92%E5%8D%8A%E8%83%B1%E6%B0%A8%E9%85%B8
about
sameAs
Biosynthesis of selenocysteine on its tRNA in eukaryotesSelenocysteine, pyrrolysine, and the unique energy metabolism of methanogenic archaeaOsteo-chondroprogenitor-specific deletion of the selenocysteine tRNA gene, Trsp, leads to chondronecrosis and abnormal skeletal development: a putative model for Kashin-Beck diseaseRedox regulation of cell signaling by selenocysteine in mammalian thioredoxin reductasesThe 3'-untranslated region of human type 2 iodothyronine deiodinase mRNA contains a functional selenocysteine insertion sequence elementNew mammalian selenocysteine-containing proteins identified with an algorithm that searches for selenocysteine insertion sequence elementscDNA cloning, purification, and characterization of mouse liver selenocysteine lyase. Candidate for selenium delivery protein in selenoprotein synthesisAn improved definition of the RNA-binding specificity of SECIS-binding protein 2, an essential component of the selenocysteine incorporation machineryIdentification of a novel selD homolog from eukaryotes, bacteria, and archaea: is there an autoregulatory mechanism in selenocysteine metabolism?Genetic evidence for an androgen-regulated epididymal secretory glutathione peroxidase whose transcript does not contain a selenocysteine codonA selenocysteine tRNA and SECIS element in Plasmodium falciparumA novel RNA structural motif in the selenocysteine insertion element of eukaryotic selenoprotein mRNAsThe redox state of SECIS binding protein 2 controls its localization and selenocysteine incorporation functionThree-dimensional structure of a mammalian thioredoxin reductase: implications for mechanism and evolution of a selenocysteine-dependent enzymeSelenophosphate synthetase genes from lung adenocarcinoma cells: Sps1 for recycling L-selenocysteine and Sps2 for selenite assimilationChemical characterization of the selenoprotein component of clostridial glycine reductase: identification of selenocysteine as the organoselenium moietyFunctional characterization of the eukaryotic SECIS elements which direct selenocysteine insertion at UGA codonsSECIS-SBP2 interactions dictate selenocysteine incorporation efficiency and selenoprotein hierarchyStaf, a novel zinc finger protein that activates the RNA polymerase III promoter of the selenocysteine tRNA geneCotranslational insertion of selenocysteine into formate dehydrogenase from Escherichia coli directed by a UGA codonNucleotide sequence and expression of the selenocysteine-containing polypeptide of formate dehydrogenase (formate-hydrogen-lyase-linked) from Escherichia coliEvidence for selenocysteine coordination to the active site nickel in the [NiFeSe]hydrogenases from Desulfovibrio baculatusSequence of a cDNA coding for human glutathione peroxidase confirms TGA encodes active site selenocysteineRNA-dependent conversion of phosphoserine forms selenocysteine in eukaryotes and archaeaStructure and mechanism of mammalian thioredoxin reductase: the active site is a redox-active selenolthiol/selenenylsulfide formed from the conserved cysteine-selenocysteine sequenceHigh content of proteins containing 21st and 22nd amino acids, selenocysteine and pyrrolysine, in a symbiotic deltaproteobacterium of gutless worm Olavius algarvensisSelenocysteine insertion directed by the 3'-UTR SECIS element in Escherichia coliProduction of Se-methylselenocysteine in transgenic plants expressing selenocysteine methyltransferaseNematode selenoproteome: the use of the selenocysteine insertion system to decode one codon in an animal genome?Making sense of nonsense: the evolution of selenocysteine usage in proteins.Characterization of the SECIS binding protein 2 complex required for the co-translational insertion of selenocysteine in mammalsDifferent catalytic mechanisms in mammalian selenocysteine- and cysteine-containing methionine-R-sulfoxide reductasesThe molecular biology of selenocysteineSynthesis and decoding of selenocysteine and human healthStructure of a NifS homologue: X-ray structure analysis of CsdB, an Escherichia coli counterpart of mammalian selenocysteine lyaseStructure of external aldimine of Escherichia coli CsdB, an IscS/NifS homolog: implications for its specificity toward selenocysteineSelenomethionine and selenocysteine double labeling strategy for crystallographic phasingStructural basis for dynamic interdomain movement and RNA recognition of the selenocysteine-specific elongation factor SelBThe three-dimensional structure of the Moorella thermoacetica selenocysteine insertion sequence RNA hairpin and its interaction with the elongation factor SelBStructure and catalytic mechanism of eukaryotic selenocysteine synthase
P921
Q21145895-09E10C09-2370-4BAB-AC1D-13EE74AB4134Q21296868-43FF2FF5-C97F-4859-890C-DE95A6CCBB1EQ21563337-12ABAA89-825D-4CF4-8B86-56ABD90711C6Q22003810-7B302DA0-C0D7-4973-8C3F-BFA964F6EED0Q22008463-31736471-073C-48F1-9FAF-A5DCBB206C83Q22010809-41DE43A4-468C-4409-9C4A-9DDD414E3DCEQ22253238-6EA2B004-30F3-40AD-B006-9ED9E10CAFB0Q24298619-7B5B5E82-581F-4397-94B3-C09C31B048BCQ24310900-D1EBD706-7285-48F0-A318-0CBF6FC32BF2Q24528073-85BE60F3-BD83-4D13-B6F5-B007B93BD908Q24537358-75154D70-0947-4BF5-BDB0-13BDEA2338A0Q24539169-6690D925-7B0D-469B-8C5C-164DA2E583A5Q24548981-4689563B-671F-4FCF-9F59-4331AE5C0055Q24555780-844CA3D3-4728-400A-8ECC-36858376F8C2Q24559999-E9680C7F-8E0A-428E-847F-AB190C6C55E1Q24561775-578E3942-1554-40B6-80CA-AAECDE002C1CQ24564454-234E6446-DA22-4D14-9618-736116F4CB4BQ24595047-BE16333E-8FC4-461F-8B50-C9015F637AFBQ24598763-D3DF6E47-BA5C-4033-A70F-7BB8CBC9FD2BQ24610152-BB110AFD-8F56-4CD2-807C-EF6626B483A3Q24628744-0E4097CC-7C35-4606-8105-7DD473B64788Q24628999-6E54CF51-4A65-442B-ABA4-C57E2628D0D4Q24634303-FDF4D8BC-17AC-466B-925C-C77A745F732DQ24678069-18296CD1-CFCA-492B-93DD-1202BAC58BC2Q24683648-03CE238D-9E04-4B6F-B5B5-9E052832B2F0Q24683921-97D32A7E-E83D-4ECD-85CD-BDF66ADF22E8Q24796149-84FE1E02-058A-4844-9074-BFE7E033F144Q24797066-07134A4F-2BB4-4507-8637-4616C64BF131Q24805819-43E531FF-A771-486B-AD54-452D839CB6FBQ24812416-FB07DFF9-845C-4B5C-9124-77562C98BC9DQ24814404-5F63F2DC-66BF-4911-9ACA-B65B38C0291FQ24814982-7D7B26F4-9A27-4823-919C-93B2FA7D967AQ27000485-F4F79FDE-E33E-46D4-BF1C-250B5593F5C9Q27022391-19FD8A8D-3F33-443F-83BD-DD4DA41D08A7Q27621507-36F273C8-6845-4238-BCE5-5986A0DC9B19Q27638920-44F6F9F5-BB2D-4545-9CFA-CCC9CA81485FQ27642497-2E7819D1-6616-4F37-B9FE-65CB3F3B1382Q27644774-865AB11C-16D5-453C-9CD7-FBCAAC492618Q27648629-D0C78FEB-230F-46E2-8DF8-3A1DA591AD35Q27649369-6BB1482A-F335-4ADC-9B77-666CAB4BC9BA
P921
description
chemesch Verbindung
@lb
chemical compound
@en
chemical compound
@en-ca
chemical compound
@en-gb
chemická sloučenina
@cs
chemická zlúčenina
@sk
chemiese verbinding
@af
chemische Verbindung
@de
chemische Verbindung
@de-ch
chemische verbinding
@nl
name
L-Selenocystein
@de
L-selenocysteine
@en
Selenocistein
@bs
Selenocistein
@sh
Selenocistein
@sr-el
Selenocisteina
@it
Selenocisteinas
@lt
Selenocisteino
@eo
Selenocisteină
@ro
Selenocisteína
@es
type
label
L-Selenocystein
@de
L-selenocysteine
@en
Selenocistein
@bs
Selenocistein
@sh
Selenocistein
@sr-el
Selenocisteina
@it
Selenocisteinas
@lt
Selenocisteino
@eo
Selenocisteină
@ro
Selenocisteína
@es
altLabel
10236-58-5
@fr
3-Selanil-L-alanin
@sr
3-Selanyl-2-aminopropanoic acid
@en
3-selenyl-L-alanine
@en
Acido 2(R)-ammino-3-idroselenopropanoico
@it
C3H7NO2Se
@fr
C3H7NO2Se
@it
C3H7NO2Se
@sr
L-Selenocistein
@sr
Se-Cys
@sr
prefLabel
L-Selenocystein
@de
L-selenocysteine
@en
Selenocistein
@bs
Selenocistein
@sh
Selenocistein
@sr-el
Selenocisteina
@it
Selenocisteinas
@lt
Selenocisteino
@eo
Selenocisteină
@ro
Selenocisteína
@es
P527
P486
P592
P6366
P646
P661
P662
P665
P683
P1579
P2017
C([C@@H](C(=O)O)N)[SeH]
P2057
HMDB0003288
P2067
P231
10236-58-5