RS25_HUMAN
ID RS25_HUMAN Reviewed; 125 AA.
AC P62851; B2R4M7; P25111;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=40S ribosomal protein S25;
DE AltName: Full=Small ribosomal subunit protein eS25 {ECO:0000303|PubMed:24524803};
GN Name=RPS25;
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].
RX PubMed=1748303; DOI=10.1016/0378-1119(91)90335-9;
RA Li M., Latoud C., Center M.S.;
RT "Cloning and sequencing a cDNA encoding human ribosomal protein S25.";
RL Gene 107:329-333(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11875025; DOI=10.1101/gr.214202;
RA Yoshihama M., Uechi T., Asakawa S., Kawasaki K., Kato S., Higa S.,
RA Maeda N., Minoshima S., Tanaka T., Shimizu N., Kenmochi N.;
RT "The human ribosomal protein genes: sequencing and comparative analysis of
RT 73 genes.";
RL Genome Res. 12:379-390(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Tongue;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pancreas, and Skin;
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 [6]
RP PROTEIN SEQUENCE OF 103-114.
RC TISSUE=Placenta;
RX PubMed=8706699; DOI=10.1111/j.1432-1033.1996.0144u.x;
RA Vladimirov S.N., Ivanov A.V., Karpova G.G., Musolyamov A.K., Egorov T.A.,
RA Thiede B., Wittmann-Liebold B., Otto A.;
RT "Characterization of the human small-ribosomal-subunit proteins by N-
RT terminal and internal sequencing, and mass spectrometry.";
RL Eur. J. Biochem. 239:144-149(1996).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Lymphoblast;
RX PubMed=14654843; DOI=10.1038/nature02166;
RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.;
RT "Proteomic characterization of the human centrosome by protein correlation
RT profiling.";
RL Nature 426:570-574(2003).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-52; LYS-60; LYS-66 AND LYS-94,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [9]
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 [10]
RP NOMENCLATURE.
RX PubMed=24524803; DOI=10.1016/j.sbi.2014.01.002;
RA Ban N., Beckmann R., Cate J.H.D., Dinman J.D., Dragon F., Ellis S.R.,
RA Lafontaine D.L.J., Lindahl L., Liljas A., Lipton J.M., McAlear M.A.,
RA Moore P.B., Noller H.F., Ortega J., Panse V.G., Ramakrishnan V.,
RA Spahn C.M.T., Steitz T.A., Tchorzewski M., Tollervey D., Warren A.J.,
RA Williamson J.R., Wilson D., Yonath A., Yusupov M.;
RT "A new system for naming ribosomal proteins.";
RL Curr. Opin. Struct. Biol. 24:165-169(2014).
RN [11]
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 [12]
RP STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS).
RX PubMed=23636399; DOI=10.1038/nature12104;
RA Anger A.M., Armache J.P., Berninghausen O., Habeck M., Subklewe M.,
RA Wilson D.N., Beckmann R.;
RT "Structures of the human and Drosophila 80S ribosome.";
RL Nature 497:80-85(2013).
CC -!- INTERACTION:
CC P62851; Q6NT76: HMBOX1; NbExp=3; IntAct=EBI-353054, EBI-2549423;
CC P62851; Q6ZUT1: NKAPD1; NbExp=3; IntAct=EBI-353054, EBI-3920396;
CC P62851; Q96MF2: STAC3; NbExp=3; IntAct=EBI-353054, EBI-745680;
CC P62851; Q9NVV9: THAP1; NbExp=3; IntAct=EBI-353054, EBI-741515;
CC P62851; Q9H2G4: TSPYL2; NbExp=3; IntAct=EBI-353054, EBI-947459;
CC P62851; O43829: ZBTB14; NbExp=3; IntAct=EBI-353054, EBI-10176632;
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eS25 family.
CC {ECO:0000305}.
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DR EMBL; M64716; AAA16105.1; -; mRNA.
DR EMBL; AB061844; BAB79482.1; -; Genomic_DNA.
DR EMBL; AK311883; BAG34824.1; -; mRNA.
DR EMBL; CH471065; EAW67426.1; -; Genomic_DNA.
DR EMBL; BC003537; AAH03537.1; -; mRNA.
DR EMBL; BC004294; AAH04294.1; -; mRNA.
DR EMBL; BC004986; AAH04986.1; -; mRNA.
DR CCDS; CCDS8406.1; -.
DR PIR; JQ1347; JQ1347.
DR RefSeq; NP_001019.1; NM_001028.2.
DR PDB; 4UG0; EM; -; SZ=1-125.
DR PDB; 4V6X; EM; 5.00 A; AZ=1-125.
DR PDB; 5A2Q; EM; 3.90 A; Z=1-125.
DR PDB; 5AJ0; EM; 3.50 A; BZ=1-125.
DR PDB; 5FLX; EM; 3.90 A; Z=1-125.
DR PDB; 5LKS; EM; 3.60 A; SZ=1-125.
DR PDB; 5OA3; EM; 4.30 A; Z=1-125.
DR PDB; 5T2C; EM; 3.60 A; AR=1-125.
DR PDB; 5VYC; X-ray; 6.00 A; Z1/Z2/Z3/Z4/Z5/Z6=1-125.
DR PDB; 6FEC; EM; 6.30 A; W=41-115.
DR PDB; 6G18; EM; 3.60 A; Z=1-125.
DR PDB; 6G4S; EM; 4.00 A; Z=1-125.
DR PDB; 6G4W; EM; 4.50 A; Z=1-125.
DR PDB; 6G51; EM; 4.10 A; Z=1-125.
DR PDB; 6G53; EM; 4.50 A; Z=1-125.
DR PDB; 6G5H; EM; 3.60 A; Z=1-125.
DR PDB; 6G5I; EM; 3.50 A; Z=1-125.
DR PDB; 6IP5; EM; 3.90 A; 3O=1-125.
DR PDB; 6IP6; EM; 4.50 A; 3O=1-125.
DR PDB; 6IP8; EM; 3.90 A; 3O=1-125.
DR PDB; 6OLE; EM; 3.10 A; SZ=43-115.
DR PDB; 6OLF; EM; 3.90 A; SZ=43-115.
DR PDB; 6OLG; EM; 3.40 A; BZ=28-113.
DR PDB; 6OLI; EM; 3.50 A; SZ=43-115.
DR PDB; 6OLZ; EM; 3.90 A; BZ=28-113.
DR PDB; 6OM0; EM; 3.10 A; SZ=43-115.
DR PDB; 6OM7; EM; 3.70 A; SZ=43-115.
DR PDB; 6QZP; EM; 2.90 A; SZ=41-115.
DR PDB; 6XA1; EM; 2.80 A; SZ=43-112.
DR PDB; 6Y0G; EM; 3.20 A; SZ=1-125.
DR PDB; 6Y2L; EM; 3.00 A; SZ=1-125.
DR PDB; 6Y57; EM; 3.50 A; SZ=1-125.
DR PDB; 6YBS; EM; 3.10 A; e=1-125.
DR PDB; 6Z6L; EM; 3.00 A; SZ=1-125.
DR PDB; 6Z6M; EM; 3.10 A; SZ=1-125.
DR PDB; 6Z6N; EM; 2.90 A; SZ=1-125.
DR PDB; 6ZLW; EM; 2.60 A; a=1-125.
DR PDB; 6ZM7; EM; 2.70 A; SZ=1-125.
DR PDB; 6ZME; EM; 3.00 A; SZ=1-125.
DR PDB; 6ZMI; EM; 2.60 A; SZ=1-125.
DR PDB; 6ZMO; EM; 3.10 A; SZ=1-125.
DR PDB; 6ZMT; EM; 3.00 A; a=1-125.
DR PDB; 6ZMW; EM; 3.70 A; e=1-125.
DR PDB; 6ZN5; EM; 3.20 A; a=42-113.
DR PDB; 6ZOJ; EM; 2.80 A; Z=1-125.
DR PDB; 6ZOL; EM; 2.80 A; Z=1-125.
DR PDB; 6ZON; EM; 3.00 A; P=1-125.
DR PDB; 6ZP4; EM; 2.90 A; P=1-125.
DR PDB; 6ZUO; EM; 3.10 A; Z=1-125.
DR PDB; 6ZV6; EM; 2.90 A; Z=1-125.
DR PDB; 6ZVH; EM; 2.90 A; Z=41-115.
DR PDB; 6ZVJ; EM; 3.80 A; P=44-113.
DR PDB; 6ZXD; EM; 3.20 A; Z=1-125.
DR PDB; 6ZXE; EM; 3.00 A; Z=1-125.
DR PDB; 6ZXF; EM; 3.70 A; Z=1-125.
DR PDB; 6ZXG; EM; 2.60 A; Z=1-125.
DR PDB; 6ZXH; EM; 2.70 A; Z=1-125.
DR PDB; 7A09; EM; 3.50 A; P=1-125.
DR PDB; 7K5I; EM; 2.90 A; Z=1-125.
DR PDBsum; 4UG0; -.
DR PDBsum; 4V6X; -.
DR PDBsum; 5A2Q; -.
DR PDBsum; 5AJ0; -.
DR PDBsum; 5FLX; -.
DR PDBsum; 5LKS; -.
DR PDBsum; 5OA3; -.
DR PDBsum; 5T2C; -.
DR PDBsum; 5VYC; -.
DR PDBsum; 6FEC; -.
DR PDBsum; 6G18; -.
DR PDBsum; 6G4S; -.
DR PDBsum; 6G4W; -.
DR PDBsum; 6G51; -.
DR PDBsum; 6G53; -.
DR PDBsum; 6G5H; -.
DR PDBsum; 6G5I; -.
DR PDBsum; 6IP5; -.
DR PDBsum; 6IP6; -.
DR PDBsum; 6IP8; -.
DR PDBsum; 6OLE; -.
DR PDBsum; 6OLF; -.
DR PDBsum; 6OLG; -.
DR PDBsum; 6OLI; -.
DR PDBsum; 6OLZ; -.
DR PDBsum; 6OM0; -.
DR PDBsum; 6OM7; -.
DR PDBsum; 6QZP; -.
DR PDBsum; 6XA1; -.
DR PDBsum; 6Y0G; -.
DR PDBsum; 6Y2L; -.
DR PDBsum; 6Y57; -.
DR PDBsum; 6YBS; -.
DR PDBsum; 6Z6L; -.
DR PDBsum; 6Z6M; -.
DR PDBsum; 6Z6N; -.
DR PDBsum; 6ZLW; -.
DR PDBsum; 6ZM7; -.
DR PDBsum; 6ZME; -.
DR PDBsum; 6ZMI; -.
DR PDBsum; 6ZMO; -.
DR PDBsum; 6ZMT; -.
DR PDBsum; 6ZMW; -.
DR PDBsum; 6ZN5; -.
DR PDBsum; 6ZOJ; -.
DR PDBsum; 6ZOL; -.
DR PDBsum; 6ZON; -.
DR PDBsum; 6ZP4; -.
DR PDBsum; 6ZUO; -.
DR PDBsum; 6ZV6; -.
DR PDBsum; 6ZVH; -.
DR PDBsum; 6ZVJ; -.
DR PDBsum; 6ZXD; -.
DR PDBsum; 6ZXE; -.
DR PDBsum; 6ZXF; -.
DR PDBsum; 6ZXG; -.
DR PDBsum; 6ZXH; -.
DR PDBsum; 7A09; -.
DR PDBsum; 7K5I; -.
DR AlphaFoldDB; P62851; -.
DR SMR; P62851; -.
DR BioGRID; 112144; 279.
DR ComplexPortal; CPX-5223; 40S cytosolic small ribosomal subunit.
DR CORUM; P62851; -.
DR IntAct; P62851; 78.
DR MINT; P62851; -.
DR STRING; 9606.ENSP00000435096; -.
DR GlyGen; P62851; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P62851; -.
DR PhosphoSitePlus; P62851; -.
DR SwissPalm; P62851; -.
DR BioMuta; RPS25; -.
DR DMDM; 51338648; -.
DR EPD; P62851; -.
DR jPOST; P62851; -.
DR MassIVE; P62851; -.
DR MaxQB; P62851; -.
DR PaxDb; P62851; -.
DR PeptideAtlas; P62851; -.
DR PRIDE; P62851; -.
DR ProteomicsDB; 57437; -.
DR TopDownProteomics; P62851; -.
DR Antibodypedia; 32561; 229 antibodies from 24 providers.
DR DNASU; 6230; -.
DR Ensembl; ENST00000527673.2; ENSP00000435096.1; ENSG00000118181.11.
DR Ensembl; ENST00000628770.2; ENSP00000486392.1; ENSG00000280831.3.
DR GeneID; 6230; -.
DR KEGG; hsa:6230; -.
DR MANE-Select; ENST00000527673.2; ENSP00000435096.1; NM_001028.3; NP_001019.1.
DR UCSC; uc001pun.4; human.
DR CTD; 6230; -.
DR DisGeNET; 6230; -.
DR GeneCards; RPS25; -.
DR HGNC; HGNC:10413; RPS25.
DR HPA; ENSG00000118181; Low tissue specificity.
DR MIM; 180465; gene.
DR neXtProt; NX_P62851; -.
DR OpenTargets; ENSG00000118181; -.
DR PharmGKB; PA34817; -.
DR VEuPathDB; HostDB:ENSG00000118181; -.
DR eggNOG; KOG1767; Eukaryota.
DR GeneTree; ENSGT00390000004856; -.
DR HOGENOM; CLU_129470_0_1_1; -.
DR InParanoid; P62851; -.
DR OMA; RIVHHSG; -.
DR OrthoDB; 1552294at2759; -.
DR PhylomeDB; P62851; -.
DR TreeFam; TF314909; -.
DR PathwayCommons; P62851; -.
DR Reactome; R-HSA-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-HSA-156902; Peptide chain elongation.
DR Reactome; R-HSA-1799339; SRP-dependent cotranslational protein targeting to membrane.
DR Reactome; R-HSA-192823; Viral mRNA Translation.
DR Reactome; R-HSA-2408557; Selenocysteine synthesis.
DR Reactome; R-HSA-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
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 Reactome; R-HSA-72764; Eukaryotic Translation Termination.
DR Reactome; R-HSA-9010553; Regulation of expression of SLITs and ROBOs.
DR Reactome; R-HSA-9633012; Response of EIF2AK4 (GCN2) to amino acid deficiency.
DR Reactome; R-HSA-9754678; SARS-CoV-2 modulates host translation machinery.
DR Reactome; R-HSA-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
DR Reactome; R-HSA-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR SignaLink; P62851; -.
DR SIGNOR; P62851; -.
DR BioGRID-ORCS; 6230; 610 hits in 1019 CRISPR screens.
DR ChiTaRS; RPS25; human.
DR GeneWiki; RPS25; -.
DR GenomeRNAi; 6230; -.
DR Pharos; P62851; Tbio.
DR PRO; PR:P62851; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; P62851; protein.
DR Bgee; ENSG00000118181; Expressed in left ovary and 98 other tissues.
DR ExpressionAtlas; P62851; baseline and differential.
DR Genevisible; P62851; HS.
DR GO; GO:0005737; C:cytoplasm; IC:ComplexPortal.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0022626; C:cytosolic ribosome; IDA:FlyBase.
DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0014069; C:postsynaptic density; IDA:SynGO.
DR GO; GO:0005840; C:ribosome; IDA:UniProtKB.
DR GO; GO:0015935; C:small ribosomal subunit; HDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0003735; F:structural constituent of ribosome; IDA:FlyBase.
DR GO; GO:0002181; P:cytoplasmic translation; IC:FlyBase.
DR GO; GO:0042274; P:ribosomal small subunit biogenesis; IMP:FlyBase.
DR GO; GO:0006364; P:rRNA processing; IMP:FlyBase.
DR GO; GO:0006412; P:translation; NAS:UniProtKB.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR004977; Ribosomal_S25.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR PANTHER; PTHR12850; PTHR12850; 1.
DR Pfam; PF03297; Ribosomal_S25; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Direct protein sequencing; Reference proteome;
KW Ribonucleoprotein; Ribosomal protein.
FT CHAIN 1..125
FT /note="40S ribosomal protein S25"
FT /id="PRO_0000192869"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..28
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 43
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P62852"
FT MOD_RES 52
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 52
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62852"
FT MOD_RES 60
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 66
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 94
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 94
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62852"
FT STRAND 47..49
FT /evidence="ECO:0007829|PDB:6ZLW"
FT HELIX 52..60
FT /evidence="ECO:0007829|PDB:6ZLW"
FT HELIX 62..64
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 65..68
FT /evidence="ECO:0007829|PDB:6ZLW"
FT HELIX 70..77
FT /evidence="ECO:0007829|PDB:6ZLW"
FT HELIX 83..94
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 97..101
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 108..111
FT /evidence="ECO:0007829|PDB:6ZLW"
SQ SEQUENCE 125 AA; 13742 MW; B8E05F04FCF2F1A9 CRC64;
MPPKDDKKKK DAGKSAKKDK DPVNKSGGKA KKKKWSKGKV RDKLNNLVLF DKATYDKLCK
EVPNYKLITP AVVSERLKIR GSLARAALQE LLSKGLIKLV SKHRAQVIYT RNTKGGDAPA
AGEDA
