TRX2_YEAST
ID TRX2_YEAST Reviewed; 104 AA.
AC P22803; D6VUZ2;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 214.
DE RecName: Full=Thioredoxin-2;
DE AltName: Full=Thioredoxin II;
DE Short=TR-II;
DE AltName: Full=Thioredoxin-1;
GN Name=TRX2; Synonyms=TRX1; OrderedLocusNames=YGR209C; ORFNames=G7746;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1988444; DOI=10.1016/s0021-9258(18)52350-4;
RA Gan Z.-R.;
RT "Yeast thioredoxin genes.";
RL J. Biol. Chem. 266:1692-1696(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2026619; DOI=10.1016/s0021-9258(18)31570-9;
RA Muller E.G.D.;
RT "Thioredoxin deficiency in yeast prolongs S phase and shortens the G1
RT interval of the cell cycle.";
RL J. Biol. Chem. 266:9194-9202(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=S288c / GRF88;
RA Song J.M., Cheung E., Rabinowitz J.C.;
RT "Analysis of the 15.6-kb fragment encompassing the ADE3 gene.";
RL Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8904340;
RX DOI=10.1002/(sici)1097-0061(19960315)12:3<273::aid-yea898>3.0.co;2-1;
RA Guerreiro P., Barreiros T., Soares H., Cyrne L., Maia e Silva A.,
RA Rodrigues-Pousada C.;
RT "Sequencing of a 17.6 kb segment on the right arm of yeast chromosome VII
RT reveals 12 ORFs, including CCT, ADE3 and TR-I genes, homologues of the
RT yeast PMT and EF1G genes, of the human and bacterial electron-transferring
RT flavoproteins (beta-chain) and of the Escherichia coli phosphoserine
RT phosphohydrolase, and five new ORFs.";
RL Yeast 12:273-280(1996).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
RN [6]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [8]
RP PROTEIN SEQUENCE OF 2-13, AND TSA1 DEPENDENCE ON THIOREDOXIN.
RC STRAIN=ATCC 200358 / YNN 295;
RX PubMed=7961686; DOI=10.1016/s0021-9258(18)47038-x;
RA Chae H.Z., Chung S.J., Rhee S.G.;
RT "Thioredoxin-dependent peroxide reductase from yeast.";
RL J. Biol. Chem. 269:27670-27678(1994).
RN [9]
RP PROTEIN SEQUENCE OF 27-43, AND REDOX-ACTIVE DISULFIDE BOND.
RX PubMed=4945270; DOI=10.1111/j.1432-1033.1971.tb01625.x;
RA Hall D.E., Baldesten A., Holmgren A., Reichard P.;
RT "Yeast thioredoxin. Amino-acid sequence around the active-center disulfide
RT of thioredoxin I and II.";
RL Eur. J. Biochem. 23:328-335(1971).
RN [10]
RP FUNCTION, AND SULFATE ASSIMILATION AND METHIONINE METABOLISM.
RX PubMed=3060034; DOI=10.1007/bf00408300;
RA Schwenn J.D., Krone F.A., Husmann K.;
RT "Yeast PAPS reductase: properties and requirements of the purified
RT enzyme.";
RL Arch. Microbiol. 150:313-319(1988).
RN [11]
RP FUNCTION, AND IDENTIFICATION IN THE LMA1 COMPLEX.
RX PubMed=9015301; DOI=10.1083/jcb.136.2.299;
RA Xu Z., Mayer A., Muller E.G.D., Wickner W.;
RT "A heterodimer of thioredoxin and I(B)2 cooperates with Sec18p (NSF) to
RT promote yeast vacuole inheritance.";
RL J. Cell Biol. 136:299-306(1997).
RN [12]
RP FUNCTION, AND INTERACTION OF THE LMA1 COMPLEX WITH SEC18.
RX PubMed=9657146; DOI=10.1016/s0092-8674(00)81457-9;
RA Xu Z., Sato K., Wickner W.;
RT "LMA1 binds to vacuoles at Sec18p (NSF), transfers upon ATP hydrolysis to a
RT t-SNARE (Vam3p) complex, and is released during fusion.";
RL Cell 93:1125-1134(1998).
RN [13]
RP FUNCTION, AND DOT5 AND TSA2 DEPENDENCE ON THIOREDOXIN.
RX PubMed=10681558; DOI=10.1074/jbc.275.8.5723;
RA Park S.G., Cha M.-K., Jeong W., Kim I.-H.;
RT "Distinct physiological functions of thiol peroxidase isoenzymes in
RT Saccharomyces cerevisiae.";
RL J. Biol. Chem. 275:5723-5732(2000).
RN [14]
RP FUNCTION, AND REDUCTION OF AHP1.
RX PubMed=9988687; DOI=10.1074/jbc.274.8.4537;
RA Lee J., Spector D., Godon C., Labarre J., Toledano M.B.;
RT "A new antioxidant with alkyl hydroperoxide defense properties in yeast.";
RL J. Biol. Chem. 274:4537-4544(1999).
RN [15]
RP FUNCTION, AND REGULATION OF YAP1.
RX PubMed=11013218; DOI=10.1093/emboj/19.19.5157;
RA Delaunay A., Isnard A.D., Toledano M.B.;
RT "H2O2 sensing through oxidation of the Yap1 transcription factor.";
RL EMBO J. 19:5157-5166(2000).
RN [16]
RP FUNCTION, AND REGULATION OF HYR1/GPX3.
RX PubMed=12437921; DOI=10.1016/s0092-8674(02)01048-6;
RA Delaunay A., Pflieger D., Barrault M.-B., Vinh J., Toledano M.B.;
RT "A thiol peroxidase is an H2O2 receptor and redox-transducer in gene
RT activation.";
RL Cell 111:471-481(2002).
RN [17]
RP FUNCTION, AND PROTECTION AGAINST REDUCING STRESS.
RX PubMed=12410842; DOI=10.1046/j.1365-2958.2002.03216.x;
RA Trotter E.W., Grant C.M.;
RT "Thioredoxins are required for protection against a reductive stress in the
RT yeast Saccharomyces cerevisiae.";
RL Mol. Microbiol. 46:869-878(2002).
RN [18]
RP REVIEW, AND OXIDATIVE STRESS.
RX PubMed=11018134; DOI=10.1146/annurev.micro.54.1.439;
RA Carmel-Harel O., Storz G.;
RT "Roles of the glutathione- and thioredoxin-dependent reduction systems in
RT the Escherichia coli and Saccharomyces cerevisiae responses to oxidative
RT stress.";
RL Annu. Rev. Microbiol. 54:439-461(2000).
RN [19]
RP REVIEW.
RX PubMed=11169096; DOI=10.1046/j.1365-2958.2001.02283.x;
RA Grant C.M.;
RT "Role of the glutathione/glutaredoxin and thioredoxin systems in yeast
RT growth and response to stress conditions.";
RL Mol. Microbiol. 39:533-541(2001).
RN [20]
RP REVIEW, AND FUNCTION OF THE LMA1 COMPLEX IN VESICLE FUSION.
RX PubMed=12914955; DOI=10.1016/s0167-4889(03)00086-7;
RA Elazar Z., Scherz-Shouval R., Shorer H.;
RT "Involvement of LMA1 and GATE-16 family members in intracellular membrane
RT dynamics.";
RL Biochim. Biophys. Acta 1641:145-156(2003).
RN [21]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [22]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-62, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [24]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-62, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [25]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-67 AND LYS-97, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22106047; DOI=10.1002/pmic.201100166;
RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL Proteomics 12:236-240(2012).
RN [26]
RP X-RAY CRYSTALLOGRAPHY (2.38 ANGSTROMS), DISULFIDE BOND, AND SUBUNIT.
RX PubMed=17044062; DOI=10.1002/prot.21194;
RA Bao R., Chen Y., Tang Y.-J., Janin J., Zhou C.-Z.;
RT "Crystal structure of the yeast cytoplasmic thioredoxin Trx2.";
RL Proteins 66:246-249(2007).
CC -!- FUNCTION: Participates as a hydrogen donor in redox reactions through
CC the reversible oxidation of its active center dithiol to a disulfide,
CC accompanied by the transfer of 2 electrons and 2 protons. It is
CC involved in many cellular processes, including deoxyribonucleotide
CC synthesis, repair of oxidatively damaged proteins, protein folding,
CC sulfur metabolism, and redox homeostasis. Thioredoxin-dependent enzymes
CC include phosphoadenosine-phosphosulfate reductase MET16, alkyl-
CC hydroperoxide reductase DOT5, thioredoxin peroxidases TSA1 and TSA2,
CC alkyl hydroperoxide reductase AHP1, and peroxiredoxin HYR1. Thioredoxin
CC is also involved in protection against reducing stress. As part of the
CC LMA1 complex, it is involved in the facilitation of vesicle fusion such
CC as homotypic vacuole and ER-derived COPII vesicle fusion with the
CC Golgi. This activity does not require the redox mechanism. Through its
CC capacity to inactivate the stress response transcription factor YAP1
CC and its regulator the hydroperoxide stress sensor HYR1, it is involved
CC in feedback regulation of stress response gene expression upon
CC oxidative stress. {ECO:0000269|PubMed:10681558,
CC ECO:0000269|PubMed:11013218, ECO:0000269|PubMed:12410842,
CC ECO:0000269|PubMed:12437921, ECO:0000269|PubMed:12914955,
CC ECO:0000269|PubMed:3060034, ECO:0000269|PubMed:9015301,
CC ECO:0000269|PubMed:9657146, ECO:0000269|PubMed:9988687}.
CC -!- SUBUNIT: Monomer. Part of the heterodimeric LMA1 complex together with
CC the proteinase inhibitor PBI2. LMA1 binds to the ATPase SEC18.
CC {ECO:0000269|PubMed:17044062, ECO:0000269|PubMed:9015301,
CC ECO:0000269|PubMed:9657146}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Golgi
CC apparatus membrane {ECO:0000269|PubMed:14562095}; Peripheral membrane
CC protein {ECO:0000269|PubMed:14562095}. Nucleus
CC {ECO:0000269|PubMed:14562095}.
CC -!- INDUCTION: Strongly induced by hydrogen peroxide and diamide stress in
CC a YAP1- and SKN7-dependent manner. Also induced by reducing stress by
CC DTT.
CC -!- PTM: Reversible disulfide bond formation between Cys-31 and Cys-34,
CC reverted by thioredoxin reductase TRR1 using NADPH as hydrogen donor.
CC -!- MISCELLANEOUS: Present with 17237 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- MISCELLANEOUS: Yeast has two cytoplasmic thioredoxins, TRX1 and TRX2,
CC and one mitochondrial, TRX3.
CC -!- SIMILARITY: Belongs to the thioredoxin family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M59168; AAA35170.1; -; Genomic_DNA.
DR EMBL; M62648; AAA35178.1; -; Genomic_DNA.
DR EMBL; U40843; AAA85584.1; -; Genomic_DNA.
DR EMBL; Z49133; CAA89002.1; -; Genomic_DNA.
DR EMBL; Z72994; CAA97236.1; -; Genomic_DNA.
DR EMBL; AY557817; AAS56143.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08303.1; -; Genomic_DNA.
DR PIR; S15049; TXBY1.
DR RefSeq; NP_011725.3; NM_001181338.3.
DR PDB; 2FA4; X-ray; 2.38 A; A/B=1-104.
DR PDB; 2HSY; NMR; -; A=1-104.
DR PDB; 3PIN; X-ray; 2.70 A; A=1-104.
DR PDB; 4DSS; X-ray; 2.10 A; B=1-104.
DR PDB; 7BVV; X-ray; 2.12 A; B=1-104.
DR PDBsum; 2FA4; -.
DR PDBsum; 2HSY; -.
DR PDBsum; 3PIN; -.
DR PDBsum; 4DSS; -.
DR PDBsum; 7BVV; -.
DR AlphaFoldDB; P22803; -.
DR BMRB; P22803; -.
DR SMR; P22803; -.
DR BioGRID; 33462; 196.
DR ComplexPortal; CPX-1279; LMA1 complex, TRX2 variant.
DR DIP; DIP-5552N; -.
DR IntAct; P22803; 13.
DR MINT; P22803; -.
DR STRING; 4932.YGR209C; -.
DR CarbonylDB; P22803; -.
DR iPTMnet; P22803; -.
DR MaxQB; P22803; -.
DR PaxDb; P22803; -.
DR PRIDE; P22803; -.
DR TopDownProteomics; P22803; -.
DR EnsemblFungi; YGR209C_mRNA; YGR209C; YGR209C.
DR GeneID; 853123; -.
DR KEGG; sce:YGR209C; -.
DR SGD; S000003441; TRX2.
DR VEuPathDB; FungiDB:YGR209C; -.
DR eggNOG; KOG0907; Eukaryota.
DR GeneTree; ENSGT00940000156170; -.
DR HOGENOM; CLU_090389_14_0_1; -.
DR InParanoid; P22803; -.
DR OMA; QVGVAPK; -.
DR BioCyc; YEAST:MON3O-68; -.
DR EvolutionaryTrace; P22803; -.
DR PRO; PR:P22803; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P22803; protein.
DR GO; GO:0005737; C:cytoplasm; IC:ComplexPortal.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0000324; C:fungal-type vacuole; IC:ComplexPortal.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0120124; C:membrane fusion priming complex; IC:ComplexPortal.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0015036; F:disulfide oxidoreductase activity; ISS:SGD.
DR GO; GO:0015035; F:protein-disulfide reductase activity; IEA:InterPro.
DR GO; GO:0045454; P:cell redox homeostasis; IGI:SGD.
DR GO; GO:0009263; P:deoxyribonucleotide biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IDA:SGD.
DR GO; GO:0006749; P:glutathione metabolic process; IGI:SGD.
DR GO; GO:0080058; P:protein deglutathionylation; IDA:SGD.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; IDA:SGD.
DR GO; GO:0000103; P:sulfate assimilation; IGI:SGD.
DR GO; GO:0042144; P:vacuole fusion, non-autophagic; IDA:SGD.
DR GO; GO:0000011; P:vacuole inheritance; IMP:SGD.
DR InterPro; IPR005746; Thioredoxin.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
DR Pfam; PF00085; Thioredoxin; 1.
DR PIRSF; PIRSF000077; Thioredoxin; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR TIGRFAMs; TIGR01068; thioredoxin; 1.
DR PROSITE; PS00194; THIOREDOXIN_1; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Deoxyribonucleotide synthesis;
KW Direct protein sequencing; Disulfide bond; Electron transport;
KW Golgi apparatus; Isopeptide bond; Membrane; Nucleus; Phosphoprotein;
KW Protein transport; Redox-active center; Reference proteome; Transport;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:7961686"
FT CHAIN 2..104
FT /note="Thioredoxin-2"
FT /id="PRO_0000120045"
FT DOMAIN 2..104
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT ACT_SITE 31
FT /note="Nucleophile"
FT ACT_SITE 34
FT /note="Nucleophile"
FT SITE 25
FT /note="Deprotonates C-terminal active site Cys"
FT SITE 32
FT /note="Contributes to redox potential value"
FT SITE 33
FT /note="Contributes to redox potential value"
FT MOD_RES 62
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT DISULFID 31..34
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691,
FT ECO:0000269|PubMed:17044062"
FT CROSSLNK 67
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CROSSLNK 97
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT STRAND 3..5
FT /evidence="ECO:0007829|PDB:4DSS"
FT HELIX 8..15
FT /evidence="ECO:0007829|PDB:4DSS"
FT STRAND 19..27
FT /evidence="ECO:0007829|PDB:4DSS"
FT HELIX 32..47
FT /evidence="ECO:0007829|PDB:4DSS"
FT STRAND 51..57
FT /evidence="ECO:0007829|PDB:4DSS"
FT TURN 58..60
FT /evidence="ECO:0007829|PDB:4DSS"
FT HELIX 62..67
FT /evidence="ECO:0007829|PDB:4DSS"
FT STRAND 72..80
FT /evidence="ECO:0007829|PDB:4DSS"
FT STRAND 83..91
FT /evidence="ECO:0007829|PDB:4DSS"
FT HELIX 93..101
FT /evidence="ECO:0007829|PDB:4DSS"
SQ SEQUENCE 104 AA; 11204 MW; 071503762C90D451 CRC64;
MVTQLKSASE YDSALASGDK LVVVDFFATW CGPCKMIAPM IEKFAEQYSD AAFYKLDVDE
VSDVAQKAEV SSMPTLIFYK GGKEVTRVVG ANPAAIKQAI ASNV
