EIF3H_HUMAN
ID EIF3H_HUMAN Reviewed; 352 AA.
AC O15372;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 196.
DE RecName: Full=Eukaryotic translation initiation factor 3 subunit H {ECO:0000255|HAMAP-Rule:MF_03007};
DE Short=eIF3h {ECO:0000255|HAMAP-Rule:MF_03007};
DE AltName: Full=Eukaryotic translation initiation factor 3 subunit 3 {ECO:0000255|HAMAP-Rule:MF_03007};
DE AltName: Full=eIF-3-gamma;
DE AltName: Full=eIF3 p40 subunit {ECO:0000255|HAMAP-Rule:MF_03007};
GN Name=EIF3H {ECO:0000255|HAMAP-Rule:MF_03007};
GN Synonyms=EIF3S3 {ECO:0000255|HAMAP-Rule:MF_03007};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=9341143; DOI=10.1074/jbc.272.43.27042;
RA Asano K., Vornlocher H.-P., Richter-Cook N.J., Merrick W.C.,
RA Hinnebusch A.G., Hershey J.W.B.;
RT "Structure of cDNAs encoding human eukaryotic initiation factor 3 subunits.
RT Possible roles in RNA binding and macromolecular assembly.";
RL J. Biol. Chem. 272:27042-27052(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Schmidt O.G., von Holtum D., Gross S., Horsthemke B., Luedecke H.-J.;
RT "The gene encoding the p40 subunit of the translation initiation factor
RT eIF3 has 8 exons, maps to the Langer-Giedion syndrome region on chromosome
RT 8q24, but is not the TRPS gene.";
RL Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP INTERACTION WITH RPS6KB1, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=16286006; DOI=10.1016/j.cell.2005.10.024;
RA Holz M.K., Ballif B.A., Gygi S.P., Blenis J.;
RT "mTOR and S6K1 mediate assembly of the translation preinitiation complex
RT through dynamic protein interchange and ordered phosphorylation events.";
RL Cell 123:569-580(2005).
RN [5]
RP CHARACTERIZATION OF THE EIF-3 COMPLEX.
RX PubMed=15703437; DOI=10.1261/rna.7215305;
RA Kolupaeva V.G., Unbehaun A., Lomakin I.B., Hellen C.U.T., Pestova T.V.;
RT "Binding of eukaryotic initiation factor 3 to ribosomal 40S subunits and
RT its role in ribosomal dissociation and anti-association.";
RL RNA 11:470-486(2005).
RN [6]
RP INTERACTION WITH RNF139.
RX PubMed=20068067; DOI=10.1158/1541-7786.mcr-08-0491;
RA Lee J.P., Brauweiler A., Rudolph M., Hooper J.E., Drabkin H.A.,
RA Gemmill R.M.;
RT "The TRC8 ubiquitin ligase is sterol regulated and interacts with lipid and
RT protein biosynthetic pathways.";
RL Mol. Cancer Res. 8:93-106(2010).
RN [7]
RP IDENTIFICATION IN THE EIF-3 COMPLEX, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=16766523; DOI=10.1074/jbc.m605418200;
RA LeFebvre A.K., Korneeva N.L., Trutschl M., Cvek U., Duzan R.D.,
RA Bradley C.A., Hershey J.W.B., Rhoads R.E.;
RT "Translation initiation factor eIF4G-1 binds to eIF3 through the eIF3e
RT subunit.";
RL J. Biol. Chem. 281:22917-22932(2006).
RN [8]
RP FUNCTION, AND CHARACTERIZATION OF THE EIF-3 COMPLEX.
RX PubMed=17581632; DOI=10.1038/sj.emboj.7601765;
RA Masutani M., Sonenberg N., Yokoyama S., Imataka H.;
RT "Reconstitution reveals the functional core of mammalian eIF3.";
RL EMBO J. 26:3373-3383(2007).
RN [9]
RP IDENTIFICATION IN THE EIF-3 COMPLEX, CHARACTERIZATION OF THE EIF-3 COMPLEX,
RP PHOSPHORYLATION AT SER-183, AND MASS SPECTROMETRY.
RX PubMed=17322308; DOI=10.1074/mcp.m600399-mcp200;
RA Damoc E., Fraser C.S., Zhou M., Videler H., Mayeur G.L., Hershey J.W.B.,
RA Doudna J.A., Robinson C.V., Leary J.A.;
RT "Structural characterization of the human eukaryotic initiation factor 3
RT protein complex by mass spectrometry.";
RL Mol. Cell. Proteomics 6:1135-1146(2007).
RN [10]
RP IDENTIFICATION IN THE EIF-3 COMPLEX, CHARACTERIZATION OF THE EIF-3 COMPLEX,
RP MASS SPECTROMETRY, AND INTERACTION WITH EIF3B; EIF3F AND EIF3M.
RX PubMed=18599441; DOI=10.1073/pnas.0801313105;
RA Zhou M., Sandercock A.M., Fraser C.S., Ridlova G., Stephens E.,
RA Schenauer M.R., Yokoi-Fong T., Barsky D., Leary J.A., Hershey J.W.B.,
RA Doudna J.A., Robinson C.V.;
RT "Mass spectrometry reveals modularity and a complete subunit interaction
RT map of the eukaryotic translation factor eIF3.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:18139-18144(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-183, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3 AND SER-183, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [15]
RP INTERACTION WITH DHX33.
RX PubMed=26100019; DOI=10.1128/mcb.00315-15;
RA Zhang Y., You J., Wang X., Weber J.;
RT "The DHX33 RNA Helicase Promotes mRNA Translation Initiation.";
RL Mol. Cell. Biol. 35:2918-2931(2015).
RN [16]
RP FUNCTION, AND IDENTIFICATION IN THE EIF-3 COMPLEX.
RX PubMed=25849773; DOI=10.1038/nature14267;
RA Lee A.S., Kranzusch P.J., Cate J.H.;
RT "eIF3 targets cell-proliferation messenger RNAs for translational
RT activation or repression.";
RL Nature 522:111-114(2015).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [18]
RP FUNCTION.
RX PubMed=27462815; DOI=10.1038/nature18954;
RA Lee A.S., Kranzusch P.J., Doudna J.A., Cate J.H.;
RT "eIF3d is an mRNA cap-binding protein that is required for specialized
RT translation initiation.";
RL Nature 536:96-99(2016).
RN [19]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-303, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [20]
RP 3D-STRUCTURE MODELING, AND ELECTRON MICROSCOPY.
RX PubMed=16322461; DOI=10.1126/science.1118977;
RA Siridechadilok B., Fraser C.S., Hall R.J., Doudna J.A., Nogales E.;
RT "Structural roles for human translation factor eIF3 in initiation of
RT protein synthesis.";
RL Science 310:1513-1515(2005).
CC -!- FUNCTION: Component of the eukaryotic translation initiation factor 3
CC (eIF-3) complex, which is required for several steps in the initiation
CC of protein synthesis (PubMed:17581632, PubMed:25849773,
CC PubMed:27462815). The eIF-3 complex associates with the 40S ribosome
CC and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-
CC tRNAi and eIF-5 to form the 43S pre-initiation complex (43S PIC). The
CC eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning
CC of the mRNA for AUG recognition. The eIF-3 complex is also required for
CC disassembly and recycling of post-termination ribosomal complexes and
CC subsequently prevents premature joining of the 40S and 60S ribosomal
CC subunits prior to initiation (PubMed:17581632). The eIF-3 complex
CC specifically targets and initiates translation of a subset of mRNAs
CC involved in cell proliferation, including cell cycling, differentiation
CC and apoptosis, and uses different modes of RNA stem-loop binding to
CC exert either translational activation or repression (PubMed:25849773).
CC {ECO:0000255|HAMAP-Rule:MF_03007, ECO:0000269|PubMed:17581632,
CC ECO:0000269|PubMed:25849773, ECO:0000269|PubMed:27462815}.
CC -!- SUBUNIT: Component of the eukaryotic translation initiation factor 3
CC (eIF-3) complex, which is composed of 13 subunits: EIF3A, EIF3B, EIF3C,
CC EIF3D, EIF3E, EIF3F, EIF3G, EIF3H, EIF3I, EIF3J, EIF3K, EIF3L and
CC EIF3M. The eIF-3 complex appears to include 3 stable modules: module A
CC is composed of EIF3A, EIF3B, EIF3G and EIF3I; module B is composed of
CC EIF3F, EIF3H, and EIF3M; and module C is composed of EIF3C, EIF3D,
CC EIF3E, EIF3K and EIF3L. EIF3C of module C binds EIF3B of module A and
CC EIF3H of module B, thereby linking the three modules. EIF3J is a labile
CC subunit that binds to the eIF-3 complex via EIF3B. The eIF-3 complex
CC interacts with RPS6KB1 under conditions of nutrient depletion.
CC Mitogenic stimulation leads to binding and activation of a complex
CC composed of MTOR and RPTOR, leading to phosphorylation and release of
CC RPS6KB1 and binding of EIF4B to eIF-3. Interacts with RNF139; the
CC interaction leads to protein translation inhibitions in a
CC ubiquitination-dependent manner. Interacts with DHX33; the interaction
CC is independent of RNA (PubMed:26100019). {ECO:0000255|HAMAP-
CC Rule:MF_03007, ECO:0000269|PubMed:16286006,
CC ECO:0000269|PubMed:16766523, ECO:0000269|PubMed:17322308,
CC ECO:0000269|PubMed:18599441, ECO:0000269|PubMed:20068067,
CC ECO:0000269|PubMed:25849773, ECO:0000269|PubMed:26100019}.
CC -!- INTERACTION:
CC O15372; Q8IZP0-5: ABI1; NbExp=3; IntAct=EBI-709735, EBI-11743294;
CC O15372; Q9P2A4: ABI3; NbExp=6; IntAct=EBI-709735, EBI-742038;
CC O15372; Q9NRI5: DISC1; NbExp=6; IntAct=EBI-709735, EBI-529989;
CC O15372; Q9NRI5-1: DISC1; NbExp=3; IntAct=EBI-709735, EBI-15881455;
CC O15372; P55884: EIF3B; NbExp=6; IntAct=EBI-709735, EBI-366696;
CC O15372; B5ME19: EIF3CL; NbExp=2; IntAct=EBI-709735, EBI-8456517;
CC O15372; O00303: EIF3F; NbExp=7; IntAct=EBI-709735, EBI-711990;
CC O15372; Q7L2H7: EIF3M; NbExp=6; IntAct=EBI-709735, EBI-353901;
CC O15372; O43639: NCK2; NbExp=6; IntAct=EBI-709735, EBI-713635;
CC O15372; O94875-10: SORBS2; NbExp=3; IntAct=EBI-709735, EBI-12037893;
CC O15372; O60504: SORBS3; NbExp=3; IntAct=EBI-709735, EBI-741237;
CC O15372; Q9Q2G4: ORF; Xeno; NbExp=3; IntAct=EBI-709735, EBI-6248094;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03007}.
CC -!- MASS SPECTROMETRY: Mass=40010.4; Method=Unknown;
CC Evidence={ECO:0000269|PubMed:17322308};
CC -!- MASS SPECTROMETRY: Mass=39842.6; Mass_error=0.4; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:18599441};
CC -!- SIMILARITY: Belongs to the eIF-3 subunit H family. {ECO:0000255|HAMAP-
CC Rule:MF_03007}.
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DR EMBL; U54559; AAD03465.1; -; mRNA.
DR EMBL; AF092576; AAC84044.1; -; Genomic_DNA.
DR EMBL; AF092569; AAC84044.1; JOINED; Genomic_DNA.
DR EMBL; AF092570; AAC84044.1; JOINED; Genomic_DNA.
DR EMBL; AF092571; AAC84044.1; JOINED; Genomic_DNA.
DR EMBL; AF092572; AAC84044.1; JOINED; Genomic_DNA.
DR EMBL; AF092573; AAC84044.1; JOINED; Genomic_DNA.
DR EMBL; AF092574; AAC84044.1; JOINED; Genomic_DNA.
DR EMBL; AF092575; AAC84044.1; JOINED; Genomic_DNA.
DR EMBL; BC000386; AAH00386.1; -; mRNA.
DR CCDS; CCDS6319.1; -.
DR RefSeq; NP_003747.1; NM_003756.2.
DR PDB; 3J8B; EM; -; H=1-221.
DR PDB; 3J8C; EM; -; H=1-221.
DR PDB; 6YBD; EM; 3.30 A; 8=1-352.
DR PDB; 6ZMW; EM; 3.70 A; 8=1-352.
DR PDB; 6ZON; EM; 3.00 A; H=1-352.
DR PDB; 6ZP4; EM; 2.90 A; H=1-352.
DR PDB; 6ZVJ; EM; 3.80 A; H=35-352.
DR PDB; 7A09; EM; 3.50 A; H=1-352.
DR PDBsum; 3J8B; -.
DR PDBsum; 3J8C; -.
DR PDBsum; 6YBD; -.
DR PDBsum; 6ZMW; -.
DR PDBsum; 6ZON; -.
DR PDBsum; 6ZP4; -.
DR PDBsum; 6ZVJ; -.
DR PDBsum; 7A09; -.
DR AlphaFoldDB; O15372; -.
DR SMR; O15372; -.
DR BioGRID; 114216; 217.
DR ComplexPortal; CPX-6036; Eukaryotic translation initiation factor 3 complex.
DR CORUM; O15372; -.
DR DIP; DIP-33689N; -.
DR IntAct; O15372; 88.
DR MINT; O15372; -.
DR STRING; 9606.ENSP00000429931; -.
DR MEROPS; M67.971; -.
DR GlyGen; O15372; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; O15372; -.
DR MetOSite; O15372; -.
DR PhosphoSitePlus; O15372; -.
DR SwissPalm; O15372; -.
DR BioMuta; EIF3H; -.
DR EPD; O15372; -.
DR jPOST; O15372; -.
DR MassIVE; O15372; -.
DR PaxDb; O15372; -.
DR PeptideAtlas; O15372; -.
DR PRIDE; O15372; -.
DR ProteomicsDB; 48615; -.
DR Antibodypedia; 13577; 303 antibodies from 32 providers.
DR DNASU; 8667; -.
DR Ensembl; ENST00000521861.6; ENSP00000429931.1; ENSG00000147677.12.
DR GeneID; 8667; -.
DR KEGG; hsa:8667; -.
DR MANE-Select; ENST00000521861.6; ENSP00000429931.1; NM_003756.3; NP_003747.1.
DR CTD; 8667; -.
DR DisGeNET; 8667; -.
DR GeneCards; EIF3H; -.
DR HGNC; HGNC:3273; EIF3H.
DR HPA; ENSG00000147677; Low tissue specificity.
DR MIM; 603912; gene.
DR neXtProt; NX_O15372; -.
DR OpenTargets; ENSG00000147677; -.
DR PharmGKB; PA162384854; -.
DR VEuPathDB; HostDB:ENSG00000147677; -.
DR eggNOG; KOG1560; Eukaryota.
DR GeneTree; ENSGT00730000111042; -.
DR HOGENOM; CLU_044094_0_0_1; -.
DR InParanoid; O15372; -.
DR OrthoDB; 976469at2759; -.
DR PhylomeDB; O15372; -.
DR TreeFam; TF101504; -.
DR PathwayCommons; O15372; -.
DR Reactome; R-HSA-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-HSA-72649; Translation initiation complex formation.
DR Reactome; R-HSA-72689; Formation of a pool of free 40S subunits.
DR Reactome; R-HSA-72695; Formation of the ternary complex, and subsequently, the 43S complex.
DR Reactome; R-HSA-72702; Ribosomal scanning and start codon recognition.
DR Reactome; R-HSA-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
DR SignaLink; O15372; -.
DR SIGNOR; O15372; -.
DR BioGRID-ORCS; 8667; 523 hits in 1110 CRISPR screens.
DR ChiTaRS; EIF3H; human.
DR GeneWiki; EIF3H; -.
DR GenomeRNAi; 8667; -.
DR Pharos; O15372; Tbio.
DR PRO; PR:O15372; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; O15372; protein.
DR Bgee; ENSG00000147677; Expressed in cortical plate and 209 other tissues.
DR ExpressionAtlas; O15372; baseline and differential.
DR Genevisible; O15372; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0016282; C:eukaryotic 43S preinitiation complex; IBA:GO_Central.
DR GO; GO:0033290; C:eukaryotic 48S preinitiation complex; IEA:UniProtKB-UniRule.
DR GO; GO:0005852; C:eukaryotic translation initiation factor 3 complex; IDA:UniProtKB.
DR GO; GO:0071541; C:eukaryotic translation initiation factor 3 complex, eIF3m; IEA:Ensembl.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0042788; C:polysomal ribosome; IBA:GO_Central.
DR GO; GO:0070122; F:isopeptidase activity; IEA:InterPro.
DR GO; GO:0140492; F:metal-dependent deubiquitinase activity; IDA:FlyBase.
DR GO; GO:0008237; F:metallopeptidase activity; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-UniRule.
DR GO; GO:0001732; P:formation of cytoplasmic translation initiation complex; IC:ComplexPortal.
DR GO; GO:0032435; P:negative regulation of proteasomal ubiquitin-dependent protein catabolic process; IDA:FlyBase.
DR GO; GO:0006446; P:regulation of translational initiation; TAS:UniProtKB.
DR GO; GO:0006413; P:translational initiation; IDA:UniProtKB.
DR CDD; cd08065; MPN_eIF3h; 1.
DR HAMAP; MF_03007; eIF3h; 1.
DR InterPro; IPR027524; eIF3h.
DR InterPro; IPR045810; eIF3h_C.
DR InterPro; IPR000555; JAMM/MPN+_dom.
DR InterPro; IPR037518; MPN.
DR PANTHER; PTHR10410:SF3; PTHR10410:SF3; 1.
DR Pfam; PF19445; eIF3h_C; 1.
DR Pfam; PF01398; JAB; 1.
DR SMART; SM00232; JAB_MPN; 1.
DR PROSITE; PS50249; MPN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Initiation factor; Isopeptide bond;
KW Phosphoprotein; Protein biosynthesis; Reference proteome; Ubl conjugation.
FT CHAIN 1..352
FT /note="Eukaryotic translation initiation factor 3 subunit
FT H"
FT /id="PRO_0000213961"
FT DOMAIN 39..173
FT /note="MPN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 265..310
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..21
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 265..290
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 3
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 183
FT /note="Phosphoserine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03007,
FT ECO:0000269|PubMed:17322308, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT CROSSLNK 303
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CONFLICT 73
FT /note="E -> K (in Ref. 2; AAC84044)"
FT /evidence="ECO:0000305"
FT HELIX 33..35
FT /evidence="ECO:0007829|PDB:6YBD"
FT HELIX 43..50
FT /evidence="ECO:0007829|PDB:6YBD"
FT TURN 51..53
FT /evidence="ECO:0007829|PDB:6YBD"
FT STRAND 65..71
FT /evidence="ECO:0007829|PDB:6YBD"
FT STRAND 73..80
FT /evidence="ECO:0007829|PDB:6YBD"
FT STRAND 89..91
FT /evidence="ECO:0007829|PDB:6YBD"
FT HELIX 98..104
FT /evidence="ECO:0007829|PDB:6YBD"
FT TURN 105..110
FT /evidence="ECO:0007829|PDB:6YBD"
FT STRAND 116..122
FT /evidence="ECO:0007829|PDB:6YBD"
FT HELIX 132..143
FT /evidence="ECO:0007829|PDB:6YBD"
FT STRAND 148..152
FT /evidence="ECO:0007829|PDB:6YBD"
FT TURN 154..159
FT /evidence="ECO:0007829|PDB:6YBD"
FT STRAND 164..169
FT /evidence="ECO:0007829|PDB:6YBD"
FT HELIX 171..175
FT /evidence="ECO:0007829|PDB:6YBD"
FT TURN 187..192
FT /evidence="ECO:0007829|PDB:6YBD"
FT STRAND 198..200
FT /evidence="ECO:0007829|PDB:6YBD"
FT HELIX 212..223
FT /evidence="ECO:0007829|PDB:6YBD"
FT TURN 224..228
FT /evidence="ECO:0007829|PDB:6YBD"
FT HELIX 229..237
FT /evidence="ECO:0007829|PDB:6YBD"
FT TURN 238..242
FT /evidence="ECO:0007829|PDB:6YBD"
FT HELIX 248..275
FT /evidence="ECO:0007829|PDB:6YBD"
FT TURN 276..280
FT /evidence="ECO:0007829|PDB:6YBD"
FT HELIX 281..284
FT /evidence="ECO:0007829|PDB:6YBD"
FT TURN 285..289
FT /evidence="ECO:0007829|PDB:6YBD"
FT TURN 299..301
FT /evidence="ECO:0007829|PDB:6YBD"
FT HELIX 316..350
FT /evidence="ECO:0007829|PDB:6YBD"
SQ SEQUENCE 352 AA; 39930 MW; F3A6EFA0CEF587D0 CRC64;
MASRKEGTGS TATSSSSTAG AAGKGKGKGG SGDSAVKQVQ IDGLVVLKII KHYQEEGQGT
EVVQGVLLGL VVEDRLEITN CFPFPQHTED DADFDEVQYQ MEMMRSLRHV NIDHLHVGWY
QSTYYGSFVT RALLDSQFSY QHAIEESVVL IYDPIKTAQG SLSLKAYRLT PKLMEVCKEK
DFSPEALKKA NITFEYMFEE VPIVIKNSHL INVLMWELEK KSAVADKHEL LSLASSNHLG
KNLQLLMDRV DEMSQDIVKY NTYMRNTSKQ QQQKHQYQQR RQQENMQRQS RGEPPLPEED
LSKLFKPPQP PARMDSLLIA GQINTYCQNI KEFTAQNLGK LFMAQALQEY NN
