ID DENR_HUMAN Reviewed; 198 AA. AC O43583; Q9H3U6; Q9UKZ0; DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot. DT 27-APR-2001, sequence version 2. DT 28-JAN-2026, entry version 180. DE RecName: Full=Density-regulated protein; DE Short=DRP; DE AltName: Full=Protein DRP1; DE AltName: Full=Smooth muscle cell-associated protein 3; DE Short=SMAP-3; GN Name=DENR; Synonyms=DRP1; ORFNames=H14; 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], TISSUE SPECIFICITY, AND INDUCTION. RX PubMed=9628587; DOI=10.1089/dna.1998.17.437; RA Deyo J.E., Chiao P.J., Tainsky M.A.; RT "Drp, a novel protein expressed at high cell density but not during growth RT arrest."; RL DNA Cell Biol. 17:437-447(1998). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Heart; RA Nishimoto S., Toyoda H., Tawara J., Aoki T., Komurasaki T.; RT "Molecular cloning and characterization of human smooth muscle cell RT associated protein-3 (SMAP-3)."; RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16541075; DOI=10.1038/nature04569; RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., RA Gibbs R.A.; RT "The finished DNA sequence of human chromosome 12."; RL Nature 440:346-351(2006). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Uterus; 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 [5] RP NUCLEOTIDE SEQUENCE [MRNA] OF 49-198, AND INDUCTION BY ERBB2. RX PubMed=10497265; DOI=10.1093/nar/27.20.4008; RA Oh J.J., Grosshans D.R., Wong S.G., Slamon D.J.; RT "Identification of differentially expressed genes associated with HER-2/neu RT overexpression in human breast cancer cells."; RL Nucleic Acids Res. 27:4008-4017(1999). RN [6] RP FUNCTION, INTERACTION WITH MCTS1, AND SUBCELLULAR LOCATION. RX PubMed=16982740; DOI=10.1158/0008-5472.can-06-1999; RA Reinert L.S., Shi B., Nandi S., Mazan-Mamczarz K., Vitolo M., Bachman K.E., RA He H., Gartenhaus R.B.; RT "MCT-1 protein interacts with the cap complex and modulates messenger RNA RT translational profiles."; RL Cancer Res. 66:8994-9001(2006). RN [7] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [8] RP INDUCTION BY HNRNPD. RX PubMed=17878526; RA Mazan-Mamczarz K., Gartenhaus R.B.; RT "Post-transcriptional control of the MCT-1-associated protein DENR/DRP by RT RNA-binding protein AUF1."; RL Cancer Genomics Proteomics 4:233-239(2007). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-73, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [10] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-73, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [12] RP FUNCTION. RX PubMed=20713520; DOI=10.1101/gad.1957510; RA Skabkin M.A., Skabkina O.V., Dhote V., Komar A.A., Hellen C.U., RA Pestova T.V.; RT "Activities of ligatin and MCT-1/DENR in eukaryotic translation initiation RT and ribosomal recycling."; RL Genes Dev. 24:1787-1801(2010). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-73, 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 [14] 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 [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-73, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [16] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=22223895; DOI=10.1074/mcp.m111.015131; RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., RA Giglione C.; RT "Comparative large-scale characterisation of plant vs. mammal proteins RT reveals similar and idiosyncratic N-alpha acetylation features."; RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012). RN [17] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [18] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20; SER-73 AND THR-86, 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 [19] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-73, AND IDENTIFICATION BY RP 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 [20] RP INTERACTION WITH MCTS1. RX PubMed=37875108; DOI=10.1016/j.cell.2023.09.024; RA Bohlen J., Zhou Q., Philippot Q., Ogishi M., Rinchai D., Nieminen T., RA Seyedpour S., Parvaneh N., Rezaei N., Yazdanpanah N., Momenilandi M., RA Conil C., Neehus A.L., Schmidt C., Arango-Franco C.A., Voyer T.L., Khan T., RA Yang R., Puchan J., Erazo L., Roiuk M., Vatovec T., Janda Z., Bagaric I., RA Materna M., Gervais A., Li H., Rosain J., Peel J.N., Seeleuthner Y., RA Han J.E., L'Honneur A.S., Moncada-Velez M., Martin-Fernandez M., RA Horesh M.E., Kochetkov T., Schmidt M., AlShehri M.A., Salo E., Saxen H., RA ElGhazali G., Yatim A., Soudee C., Sallusto F., Ensser A., Marr N., RA Zhang P., Bogunovic D., Cobat A., Shahrooei M., Beziat V., Abel L., RA Wang X., Boisson-Dupuis S., Teleman A.A., Bustamante J., Zhang Q., RA Casanova J.L.; RT "Human MCTS1-dependent translation of JAK2 is essential for IFN-gamma RT immunity to mycobacteria."; RL Cell 186:5114.27-5134.e27(2023). CC -!- FUNCTION: Translation regulator forming a complex with MCTS1 to promote CC translation reinitiation. Translation reinitiation is the process where CC the small ribosomal subunit remains attached to the mRNA following CC termination of translation of a regulatory upstream ORF (uORF), and CC resume scanning on the same mRNA molecule to initiate translation of a CC downstream ORF, usually the main ORF (mORF). The MCTS1/DENR complex is CC pivotal to two linked mechanisms essential for translation CC reinitiation. Firstly, the dissociation of deacylated tRNAs from post- CC termination 40S ribosomal complexes during ribosome recycling. CC Secondly, the recruitment in an EIF2-independent manner of CC aminoacylated initiator tRNA to P site of 40S ribosomes for a new round CC of translation. This regulatory mechanism governs the translation of CC more than 150 genes which translation reinitiation is MCTS1/DENR CC complex-dependent. {ECO:0000269|PubMed:16982740, CC ECO:0000269|PubMed:20713520, ECO:0000269|PubMed:37875108}. CC -!- SUBUNIT: Interacts with MCTS1 (via PUA domain); the complex regulates CC translation reinitiation. {ECO:0000269|PubMed:16982740, CC ECO:0000269|PubMed:37875108}. CC -!- INTERACTION: CC O43583; P10636: MAPT; NbExp=2; IntAct=EBI-716083, EBI-366182; CC O43583; Q9NX47: MARCHF5; NbExp=2; IntAct=EBI-716083, EBI-2341610; CC O43583; Q9ULC4: MCTS1; NbExp=11; IntAct=EBI-716083, EBI-716076; CC O43583; Q8WX92: NELFB; NbExp=2; IntAct=EBI-716083, EBI-347721; CC O43583; P0CG48: UBC; NbExp=3; IntAct=EBI-716083, EBI-3390054; CC O43583; P89886: TMA20; Xeno; NbExp=3; IntAct=EBI-716083, EBI-33141; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16982740}. CC -!- TISSUE SPECIFICITY: Highly expressed in heart and skeletal muscle and CC moderately expressed in the brain, placenta, liver and pancreas. Weakly CC expressed in the lung and kidney. {ECO:0000269|PubMed:9628587}. CC -!- INDUCTION: Up-regulated with increasing cell-density by HNRNPD. Up- CC regulated in ovarian and breast cancer cells by ERBB2 overexpression. CC Not induced by TGFB1. {ECO:0000269|PubMed:10497265, CC ECO:0000269|PubMed:17878526, ECO:0000269|PubMed:9628587}. CC -!- SIMILARITY: Belongs to the DENR family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC02985.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and CC Haematology; CC URL="https://atlasgeneticsoncology.org/gene/40295/DENR"; 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; AF038554; AAC02985.2; ALT_INIT; mRNA. DR EMBL; AB014731; BAB20268.1; -; mRNA. DR EMBL; AC026331; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC027290; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC007860; AAH07860.1; -; mRNA. DR EMBL; AF103800; AAF02420.1; -; mRNA. DR CCDS; CCDS45003.1; -. DR RefSeq; NP_003668.2; NM_003677.4. DR PDB; 5ONS; X-ray; 2.14 A; B=24-51. DR PDB; 5VYC; X-ray; 6.00 A; l1/l2/l3/l4/l5/l6=1-198. DR PDB; 6MS4; X-ray; 2.00 A; B=25-70. DR PDB; 6VPQ; X-ray; 1.74 A; A/B/C/D/E/F=1-198. DR PDB; 6VPR; X-ray; 2.20 A; A/B=1-198. DR PDBsum; 5ONS; -. DR PDBsum; 5VYC; -. DR PDBsum; 6MS4; -. DR PDBsum; 6VPQ; -. DR PDBsum; 6VPR; -. DR AlphaFoldDB; O43583; -. DR SMR; O43583; -. DR BioGRID; 114131; 80. DR FunCoup; O43583; 777. DR IntAct; O43583; 45. DR MINT; O43583; -. DR STRING; 9606.ENSP00000280557; -. DR GlyGen; O43583; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; O43583; -. DR PhosphoSitePlus; O43583; -. DR SwissPalm; O43583; -. DR BioMuta; DENR; -. DR jPOST; O43583; -. DR MassIVE; O43583; -. DR PaxDb; 9606-ENSP00000280557; -. DR PeptideAtlas; O43583; -. DR ProteomicsDB; 49063; -. DR Pumba; O43583; -. DR TopDownProteomics; O43583; -. DR Antibodypedia; 31699; 199 antibodies from 30 providers. DR DNASU; 8562; -. DR Ensembl; ENST00000280557.11; ENSP00000280557.6; ENSG00000139726.12. DR GeneID; 8562; -. DR KEGG; hsa:8562; -. DR MANE-Select; ENST00000280557.11; ENSP00000280557.6; NM_003677.5; NP_003668.2. DR UCSC; uc001uda.4; human. DR AGR; HGNC:2769; -. DR ClinPGx; PA27252; -. DR CTD; 8562; -. DR DisGeNET; 8562; -. DR GeneCards; DENR; -. DR HGNC; HGNC:2769; DENR. DR HPA; ENSG00000139726; Low tissue specificity. DR MalaCards; DENR; -. DR MIM; 604550; gene. DR OpenTargets; ENSG00000139726; -. DR VEuPathDB; HostDB:ENSG00000139726; -. DR eggNOG; KOG3239; Eukaryota. DR GeneTree; ENSGT00390000014349; -. DR HOGENOM; CLU_073511_1_0_1; -. DR InParanoid; O43583; -. DR OMA; EVFEIDM; -. DR OrthoDB; 277199at2759; -. DR PAN-GO; O43583; 3 GO annotations based on evolutionary models. DR PhylomeDB; O43583; -. DR PathwayCommons; O43583; -. DR SignaLink; O43583; -. DR SIGNOR; O43583; -. DR Agora; ENSG00000139726; -. DR BioGRID-ORCS; 8562; 640 hits in 1138 CRISPR screens. DR CD-CODE; 91857CE7; Nucleolus. DR CD-CODE; DEE660B4; Stress granule. DR ChiTaRS; DENR; human. DR GenomeRNAi; 8562; -. DR Pharos; O43583; Tbio. DR PRO; PR:O43583; -. DR Proteomes; UP000005640; Chromosome 12. DR RNAct; O43583; protein. DR Bgee; ENSG00000139726; Expressed in germinal epithelium of ovary and 207 other cell types or tissues. DR ExpressionAtlas; O43583; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW. DR GO; GO:0001731; P:formation of translation preinitiation complex; IDA:UniProtKB. DR GO; GO:0075522; P:IRES-dependent viral translational initiation; IDA:UniProtKB. DR GO; GO:0032790; P:ribosome disassembly; IDA:UniProtKB. DR GO; GO:0002188; P:translation reinitiation; IBA:GO_Central. DR CDD; cd11607; DENR_C; 1. DR FunFam; 3.30.780.10:FF:000004; density-regulated protein-like; 1. DR Gene3D; 3.30.780.10; SUI1-like domain; 1. DR InterPro; IPR050318; DENR/SUI1_TIF. DR InterPro; IPR046447; DENR_C. DR InterPro; IPR005873; DENR_eukaryotes. DR InterPro; IPR048517; DENR_N. DR InterPro; IPR001950; SUI1. DR InterPro; IPR036877; SUI1_dom_sf. DR NCBIfam; TIGR01159; DRP1; 1. DR PANTHER; PTHR12789:SF0; DENSITY-REGULATED PROTEIN; 1. DR PANTHER; PTHR12789; DENSITY-REGULATED PROTEIN HOMOLOG; 1. DR Pfam; PF21023; DENR_N; 1. DR Pfam; PF01253; SUI1; 1. DR SUPFAM; SSF55159; eIF1-like; 1. DR PROSITE; PS50296; SUI1; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Cytoplasm; Initiation factor; Phosphoprotein; KW Protein biosynthesis; Proteomics identification; Reference proteome. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0007744|PubMed:19413330, FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378" FT CHAIN 2..198 FT /note="Density-regulated protein" FT /id="PRO_0000130600" FT DOMAIN 115..182 FT /note="SUI1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00200" FT REGION 72..110 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 95..110 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0007744|PubMed:19413330, FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378" FT MOD_RES 20 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 73 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 86 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 189 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9CQJ6" FT CONFLICT 49..50 FT /note="DV -> HE (in Ref. 5; AAF02420)" FT /evidence="ECO:0000305" FT TURN 35..37 FT /evidence="ECO:0007829|PDB:6MS4" FT HELIX 41..43 FT /evidence="ECO:0007829|PDB:6MS4" FT HELIX 44..46 FT /evidence="ECO:0007829|PDB:5ONS" FT HELIX 50..60 FT /evidence="ECO:0007829|PDB:6MS4" FT HELIX 62..69 FT /evidence="ECO:0007829|PDB:6MS4" FT STRAND 115..121 FT /evidence="ECO:0007829|PDB:6VPQ" FT STRAND 125..132 FT /evidence="ECO:0007829|PDB:6VPQ" FT HELIX 134..137 FT /evidence="ECO:0007829|PDB:6VPQ" FT HELIX 141..152 FT /evidence="ECO:0007829|PDB:6VPQ" FT STRAND 156..160 FT /evidence="ECO:0007829|PDB:6VPQ" FT STRAND 163..168 FT /evidence="ECO:0007829|PDB:6VPQ" FT TURN 171..173 FT /evidence="ECO:0007829|PDB:6VPQ" FT HELIX 174..181 FT /evidence="ECO:0007829|PDB:6VPQ" FT HELIX 187..189 FT /evidence="ECO:0007829|PDB:6VPQ" FT STRAND 190..192 FT /evidence="ECO:0007829|PDB:6VPQ" SQ SEQUENCE 198 AA; 22092 MW; 023F70E0C6C0B25D CRC64; MAADISESSG ADCKGDPRNS AKLDADYPLR VLYCGVCSLP TEYCEYMPDV AKCRQWLEKN FPNEFAKLTV ENSPKQEAGI SEGQGTAGEE EEKKKQKRGG RGQIKQKKKT VPQKVTIAKI PRAKKKYVTR VCGLATFEID LKEAQRFFAQ KFSCGASVTG EDEIIIQGDF TDDIIDVIQE KWPEVDDDSI EDLGEVKK //