ID RS27A_HUMAN Reviewed; 156 AA. AC P62979; P02248; P02249; P02250; P14798; P62988; Q29120; Q6LBL4; AC Q6LDU5; Q8WYN8; Q91887; Q91888; Q9BQ77; Q9BWD6; Q9BX98; Q9UEF2; AC Q9UEG1; Q9UEK8; Q9UPK7; DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot. DT 10-AUG-2010, sequence version 2. DT 25-JAN-2012, entry version 78. DE RecName: Full=Ubiquitin-40S ribosomal protein S27a; DE AltName: Full=Ubiquitin carboxyl extension protein 80; DE Contains: DE RecName: Full=Ubiquitin; DE Contains: DE RecName: Full=40S ribosomal protein S27a; DE Flags: Precursor; GN Name=RPS27A; Synonyms=UBA80, UBCEP1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=92037818; PubMed=1657614; DOI=10.1002/eji.1830211113; RA Pancre V., Pierce R.J., Fournier F., Mehtali M., Delanoye A., RA Capron A., Auriault C.; RT "Effect of ubiquitin on platelet functions: possible identity with RT platelet activity suppressive lymphokine (PASL)."; RL Eur. J. Immunol. 21:2735-2741(1991). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=92126503; PubMed=1370760; RA Adams S.M., Sharp M.G., Walker R.A., Brammar W.J., Varley J.M.; RT "Differential expression of translation-associated genes in benign and RT malignant human breast tumours."; RL Br. J. Cancer 65:65-71(1992). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15815621; DOI=10.1038/nature03466; RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J., RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., RA Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., RA McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., RA Waterston R.H., Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 RT and 4."; RL Nature 434:724-731(2005). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Placenta, 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP PROTEIN SEQUENCE OF 1-98. RC TISSUE=Placenta; RX MEDLINE=96305378; PubMed=8706699; RX DOI=10.1111/j.1432-1033.1996.0144u.x; RA Vladimirov S.N., Ivanov A.V., Karpova G.G., Musolyamov A.K., RA Egorov T.A., 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 [6] RP PROTEIN SEQUENCE OF 1-74. RX MEDLINE=75156547; PubMed=124018; DOI=10.1038/255423a0; RA Schlesinger D.H., Goldstein G.; RT "Hybrid troponin reconstituted from vertebrate and arthropod RT subunits."; RL Nature 255:423-424(1975). RN [7] RP PROTEIN SEQUENCE OF 1-27; 30-42 AND 55-72, AND MASS SPECTROMETRY. RC TISSUE=Fetal brain cortex; RA Lubec G., Chen W.-Q., Sun Y.; RL Submitted (DEC-2008) to UniProtKB. RN [8] RP PROTEIN SEQUENCE OF 1-27 AND 43-54, UBIQUITINATION AT LYS-6; LYS-11 RP AND LYS-48, AND MASS SPECTROMETRY. RX PubMed=16443603; DOI=10.1074/jbc.M512786200; RA Cripps D., Thomas S.N., Jeng Y., Yang F., Davies P., Yang A.J.; RT "Alzheimer disease-specific conformation of hyperphosphorylated paired RT helical filament-tau is polyubiquitinated through Lys-48, Lys-11, and RT Lys-6 ubiquitin conjugation."; RL J. Biol. Chem. 281:10825-10838(2006). RN [9] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-34. RX MEDLINE=21864036; 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 RT analysis of 73 genes."; RL Genome Res. 12:379-390(2002). RN [10] RP NUCLEOTIDE SEQUENCE [MRNA] OF 5-156. RX MEDLINE=85207809; PubMed=2581967; RA Lund P.K., Moats-Staats B.M., Simmons J.G., Hoyt E., D'Ercole A.J., RA Martin F., van Wyk J.J.; RT "Nucleotide sequence analysis of a cDNA encoding human ubiquitin RT reveals that ubiquitin is synthesized as a precursor."; RL J. Biol. Chem. 260:7609-7613(1985). RN [11] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 98-148. RX MEDLINE=98248690; PubMed=9582194; RA Kenmochi N., Kawaguchi T., Rozen S., Davis E., Goodman N., RA Hudson T.J., Tanaka T., Page D.C.; RT "A map of 75 human ribosomal protein genes."; RL Genome Res. 8:509-523(1998). RN [12] RP FUNCTION, UBIQUITINATION AT LYS-11; LYS-29; LYS-48 AND LYS-63, AND RP MASS SPECTROMETRY. RX PubMed=16543144; DOI=10.1016/j.molcel.2006.02.018; RA Huang F., Kirkpatrick D., Jiang X., Gygi S.P., Sorkin A.; RT "Differential regulation of EGF receptor internalization and RT degradation by multiubiquitination within the kinase domain."; RL Mol. Cell 21:737-748(2006). RN [13] RP UBIQUITINATION AT LYS-27. RX PubMed=15466860; DOI=10.1074/jbc.M402916200; RA Okumura F., Hatakeyama S., Matsumoto M., Kamura T., Nakayama K.; RT "Functional regulation of FEZ1 by the U-box-type ubiquitin ligase E4B RT contributes to neuritogenesis."; RL J. Biol. Chem. 279:53533-53543(2004). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65, AND MASS RP SPECTROMETRY. RC TISSUE=Epithelium; 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., RA Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in RT signaling networks."; RL Cell 127:635-648(2006). RN [15] RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-48, AND MASS RP SPECTROMETRY. RX PubMed=17323924; DOI=10.1021/bi061994u; RA Wang X., Chen C.-F., Baker P.R., Chen P.-L., Kaiser P., Huang L.; RT "Mass spectrometric characterization of the affinity-purified human RT 26S proteasome complex."; RL Biochemistry 46:3553-3565(2007). RN [16] RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-48, AND MASS RP SPECTROMETRY. RC TISSUE=Lung adenocarcinoma; RX PubMed=17203973; DOI=10.1021/pr060438j; RA Vasilescu J., Zweitzig D.R., Denis N.J., Smith J.C., Ethier M., RA Haines D.S., Figeys D.; RT "The proteomic reactor facilitates the analysis of affinity-purified RT proteins by mass spectrometry: application for identifying RT ubiquitinated proteins in human cells."; RL J. Proteome Res. 6:298-305(2007). RN [17] RP UBIQUITINATION AT LYS-63, AND MUTAGENESIS OF LYS-48 AND LYS-63. RX PubMed=18719106; DOI=10.1073/pnas.0805685105; RA Motegi A., Liaw H.-J., Lee K.-Y., Roest H.P., Maas A., Wu X., RA Moinova H., Markowitz S.D., Ding H., Hoeijmakers J.H.J., Myung K.; RT "Polyubiquitination of proliferating cell nuclear antigen by HLTF and RT SHPRH prevents genomic instability from stalled replication forks."; RL Proc. Natl. Acad. Sci. U.S.A. 105:12411-12416(2008). RN [18] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-6; LYS-48; LYS-104; LYS-107 RP AND LYS-113, AND MASS SPECTROMETRY. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., 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 [19] RP REVIEW, AND FUNCTION. RX PubMed=19754430; DOI=10.1042/BST0370937; RA Komander D.; RT "The emerging complexity of protein ubiquitination."; RL Biochem. Soc. Trans. 37:937-953(2009). RN [20] 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., RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). CC -!- FUNCTION: Ubiquitin exists either covalently attached to another CC protein, or free (unanchored). When covalently bound, it is CC conjugated to target proteins via an isopeptide bond either as a CC monomer (monoubiquitin), a polymer linked via different Lys CC residues of the ubiquitin (polyubiquitin chains) or a linear CC polymer linked via the initiator Met of the ubiquitin (linear CC polyubiquitin chains). Polyubiquitin chains, when attached to a CC target protein, have different functions depending on the Lys CC residue of the ubiquitin that is linked: Lys-6-linked may be CC involved in DNA repair; Lys-11-linked is involved in ERAD CC (endoplasmic reticulum-associated degradation) and in cell-cycle CC regulation; Lys-29-linked is involved in lysosomal degradation; CC Lys-33-linked is involved in kinase modification; Lys-48-linked is CC involved in protein degradation via the proteasome; Lys-63-linked CC is involved in endocytosis, DNA-damage responses as well as in CC signaling processes leading to activation of the transcription CC factor NF-kappa-B. Linear polymer chains formed via attachment by CC the initiator Met lead to cell signaling. Ubiquitin is usually CC conjugated to Lys residues of target proteins, however, in rare CC cases, conjugation to Cys or Ser residues has been observed. When CC polyubiquitin is free (unanchored-polyubiquitin), it also has CC distinct roles, such as in activation of protein kinases, and in CC signaling. CC -!- FUNCTION: Ribosomal protein S27a is a component of the 40S subunit CC of the ribosome. CC -!- SUBUNIT: Ribosomal protein S27a is part of the 40S ribosomal CC subunit (By similarity). CC -!- SUBCELLULAR LOCATION: Ubiquitin: Cytoplasm (By similarity). CC Nucleus (By similarity). CC -!- MISCELLANEOUS: Ubiquitin is encoded by 4 different genes. UBA52 CC and RPS27A genes code for a single copy of ubiquitin fused to the CC ribosomal proteins L40 and S27a, respectively. UBB and UBC genes CC code for a polyubiquitin precursor with exact head to tail CC repeats, the number of repeats differ between species and strains. CC -!- MISCELLANEOUS: For a better understanding, features related to CC ubiquitin are only indicated for the first chain. CC -!- SIMILARITY: In the N-terminal section; belongs to the ubiquitin CC family. CC -!- SIMILARITY: In the C-terminal section; belongs to the ribosomal CC protein S27Ae family. CC -!- SIMILARITY: Contains 1 ubiquitin-like domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X63237; CAA44911.1; -; mRNA. DR EMBL; S79522; AAB21188.1; -; mRNA. DR EMBL; AC012358; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC001392; AAH01392.1; -; mRNA. DR EMBL; BC066293; AAH66293.1; -; mRNA. DR EMBL; AB062071; BAB79490.1; -; Genomic_DNA. DR EMBL; M10939; AAA36788.1; -; mRNA. DR EMBL; AB007163; BAA25826.1; -; Genomic_DNA. DR IPI; IPI00179330; -. DR RefSeq; NP_001129064.1; NM_001135592.2. DR RefSeq; NP_001170884.1; NM_001177413.1. DR RefSeq; NP_002945.1; NM_002954.5. DR UniGene; Hs.311640; -. DR UniGene; Hs.546292; -. DR PDB; 2KHW; NMR; -; B=1-76. DR PDB; 2KOX; NMR; -; A=1-76. DR PDB; 2KTF; NMR; -; A=1-76. DR PDB; 2KWU; NMR; -; B=1-76. DR PDB; 2KWV; NMR; -; B=1-76. DR PDB; 2L0F; NMR; -; A=1-76. DR PDB; 2L0T; NMR; -; A=1-76. DR PDB; 2XEW; X-ray; 2.20 A; A/B/C/D/E/F/G/H/I/J/K/L=1-76. DR PDB; 2XK5; X-ray; 3.00 A; A/B=1-76. DR PDB; 3K9P; X-ray; 2.80 A; B=1-76. DR PDB; 3N30; X-ray; 3.00 A; A/B=1-76. DR PDB; 3N32; X-ray; 1.80 A; A=1-76. DR PDB; 3NHE; X-ray; 1.26 A; B=1-76. DR PDB; 3NOB; X-ray; 2.19 A; A/B/C/D/E/F/G/H=1-76. DR PDB; 3NS8; X-ray; 1.71 A; A/B=1-76. DR PDB; 3PHD; X-ray; 3.00 A; E/F/G/H=1-76. DR PDB; 3PHW; X-ray; 2.00 A; B/D/F/H=1-75. DR PDBsum; 2KHW; -. DR PDBsum; 2KOX; -. DR PDBsum; 2KTF; -. DR PDBsum; 2KWU; -. DR PDBsum; 2KWV; -. DR PDBsum; 2L0F; -. DR PDBsum; 2L0T; -. DR PDBsum; 2XEW; -. DR PDBsum; 2XK5; -. DR PDBsum; 3K9P; -. DR PDBsum; 3N30; -. DR PDBsum; 3N32; -. DR PDBsum; 3NHE; -. DR PDBsum; 3NOB; -. DR PDBsum; 3NS8; -. DR PDBsum; 3PHD; -. DR PDBsum; 3PHW; -. DR ProteinModelPortal; P62979; -. DR SMR; P62979; 1-76, 100-156. DR IntAct; P62979; 12. DR MINT; MINT-1138719; -. DR STRING; P62979; -. DR PhosphoSite; P62979; -. DR DMDM; 302393745; -. DR UCD-2DPAGE; P02248; -. DR PRIDE; P62979; -. DR Ensembl; ENST00000272317; ENSP00000272317; ENSG00000143947. DR Ensembl; ENST00000402285; ENSP00000383981; ENSG00000143947. DR Ensembl; ENST00000404735; ENSP00000385659; ENSG00000143947. DR Ensembl; ENST00000449323; ENSP00000408482; ENSG00000143947. DR GeneID; 6233; -. DR KEGG; hsa:6233; -. DR UCSC; uc002ryk.1; human. DR CTD; 6233; -. DR GeneCards; GC02P055459; -. DR H-InvDB; HIX0002061; -. DR HGNC; HGNC:10417; RPS27A. DR HPA; CAB033319; -. DR MIM; 191343; gene. DR neXtProt; NX_P62979; -. DR eggNOG; prNOG20257; -. DR GeneTree; ENSGT00550000074763; -. DR HOVERGEN; HBG079148; -. DR InParanoid; P62979; -. DR OMA; QYCGRCH; -. DR OrthoDB; EOG4PZJ82; -. DR PhylomeDB; P62979; -. DR Reactome; REACT_111045; Developmental Biology. DR Reactome; REACT_111102; Signal Transduction. DR Reactome; REACT_111217; Metabolism. DR Reactome; REACT_11123; Membrane Trafficking. DR Reactome; REACT_13505; Proteasome mediated degradation of PAK-2p34. DR Reactome; REACT_152; Cell Cycle, Mitotic. DR Reactome; REACT_1538; Cell Cycle Checkpoints. DR Reactome; REACT_15380; Diabetes pathways. DR Reactome; REACT_17015; Metabolism of proteins. DR Reactome; REACT_1762; 3' -UTR-mediated translational regulation. DR Reactome; REACT_216; DNA Repair. DR Reactome; REACT_24941; Circadian Clock. DR Reactome; REACT_25177; RNF125 mediated ubiquitination of RIG-I, MDA5 and IPS-1. DR Reactome; REACT_383; DNA Replication. DR Reactome; REACT_578; Apoptosis. DR Reactome; REACT_6167; Influenza Infection. DR Reactome; REACT_6185; HIV Infection. DR Reactome; REACT_6850; Cdc20:Phospho-APC/C mediated degradation of Cyclin A. DR Reactome; REACT_6900; Immune System. DR Reactome; REACT_71; Gene Expression. DR Reactome; REACT_8017; APC-Cdc20 mediated degradation of Nek2A. DR ArrayExpress; P62979; -. DR Bgee; P62979; -. DR CleanEx; HS_RPS27A; -. DR Genevestigator; P62979; -. DR GermOnline; ENSG00000143947; Homo sapiens. DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IDA:UniProtKB. DR GO; GO:0030666; C:endocytic vesicle membrane; TAS:Reactome. DR GO; GO:0010008; C:endosome membrane; TAS:Reactome. DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0003735; F:structural constituent of ribosome; IDA:UniProtKB. DR GO; GO:0004842; F:ubiquitin-protein ligase activity; TAS:Reactome. DR GO; GO:0000187; P:activation of MAPK activity; TAS:Reactome. DR GO; GO:0031145; P:anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process; TAS:Reactome. DR GO; GO:0006916; P:anti-apoptosis; TAS:Reactome. DR GO; GO:0002474; P:antigen processing and presentation of peptide antigen via MHC class I; TAS:Reactome. DR GO; GO:0006915; P:apoptotic process; TAS:Reactome. DR GO; GO:0016044; P:cellular membrane organization; TAS:Reactome. DR GO; GO:0006977; P:DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest; TAS:Reactome. DR GO; GO:0006281; P:DNA repair; TAS:Reactome. DR GO; GO:0031018; P:endocrine pancreas development; TAS:Reactome. DR GO; GO:0016197; P:endosome transport; TAS:Reactome. DR GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; TAS:Reactome. DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; TAS:Reactome. DR GO; GO:0007249; P:I-kappaB kinase/NF-kappaB cascade; TAS:Reactome. DR GO; GO:0008624; P:induction of apoptosis by extracellular signals; TAS:Reactome. DR GO; GO:0045087; P:innate immune response; TAS:Reactome. DR GO; GO:0007254; P:JNK cascade; TAS:Reactome. DR GO; GO:0000216; P:M/G1 transition of mitotic cell cycle; TAS:Reactome. DR GO; GO:0016071; P:mRNA metabolic process; TAS:Reactome. DR GO; GO:0002755; P:MyD88-dependent toll-like receptor signaling pathway; TAS:Reactome. DR GO; GO:0002756; P:MyD88-independent toll-like receptor signaling pathway; TAS:Reactome. DR GO; GO:0042059; P:negative regulation of epidermal growth factor receptor signaling pathway; TAS:Reactome. DR GO; GO:0032480; P:negative regulation of type I interferon production; TAS:Reactome. DR GO; GO:0051436; P:negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle; TAS:Reactome. DR GO; GO:0048011; P:nerve growth factor receptor signaling pathway; TAS:Reactome. DR GO; GO:0070423; P:nucleotide-binding oligomerization domain containing signaling pathway; TAS:Reactome. DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB cascade; TAS:Reactome. DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; TAS:Reactome. DR GO; GO:0051437; P:positive regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle; TAS:Reactome. DR GO; GO:0000209; P:protein polyubiquitination; TAS:Reactome. DR GO; GO:0000084; P:S phase of mitotic cell cycle; TAS:Reactome. DR GO; GO:0051403; P:stress-activated MAPK cascade; TAS:Reactome. DR GO; GO:0050852; P:T cell receptor signaling pathway; TAS:Reactome. DR GO; GO:0008063; P:Toll signaling pathway; TAS:Reactome. DR GO; GO:0034130; P:toll-like receptor 1 signaling pathway; TAS:Reactome. DR GO; GO:0034134; P:toll-like receptor 2 signaling pathway; TAS:Reactome. DR GO; GO:0034138; P:toll-like receptor 3 signaling pathway; TAS:Reactome. DR GO; GO:0034142; P:toll-like receptor 4 signaling pathway; TAS:Reactome. DR GO; GO:0006414; P:translational elongation; TAS:Reactome. DR GO; GO:0006415; P:translational termination; TAS:Reactome. DR GO; GO:0019083; P:viral transcription; TAS:Reactome. DR InterPro; IPR002906; Ribosomal_S27a. DR InterPro; IPR000626; Ubiquitin. DR InterPro; IPR019954; Ubiquitin_CS. DR InterPro; IPR019956; Ubiquitin_subgr. DR InterPro; IPR019955; Ubiquitin_supergroup. DR KO; K02977; -. DR Pfam; PF01599; Ribosomal_S27; 1. DR Pfam; PF00240; ubiquitin; 1. DR PRINTS; PR00348; UBIQUITIN. DR SMART; SM00213; UBQ; 1. DR PROSITE; PS00299; UBIQUITIN_1; 1. DR PROSITE; PS50053; UBIQUITIN_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Complete proteome; Cytoplasm; KW Direct protein sequencing; Isopeptide bond; Metal-binding; Nucleus; KW Phosphoprotein; Reference proteome; Ribonucleoprotein; KW Ribosomal protein; Ubl conjugation; Zinc; Zinc-finger. FT CHAIN 1 76 Ubiquitin. FT /FTId=PRO_0000396477. FT CHAIN 77 156 40S ribosomal protein S27a. FT /FTId=PRO_0000396478. FT DOMAIN 1 76 Ubiquitin-like. FT ZN_FING 121 144 C4-type. FT COMPBIAS 77 99 Lys-rich (highly basic). FT BINDING 54 54 Activating enzyme. FT BINDING 72 72 Activating enzyme. FT SITE 68 68 Essential for function. FT MOD_RES 6 6 N6-acetyllysine. FT MOD_RES 48 48 N6-acetyllysine. FT MOD_RES 57 57 Phosphoserine (By similarity). FT MOD_RES 65 65 Phosphoserine. FT MOD_RES 104 104 N6-acetyllysine. FT MOD_RES 107 107 N6-acetyllysine. FT MOD_RES 113 113 N6-acetyllysine. FT CROSSLNK 6 6 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in ubiquitin). FT CROSSLNK 11 11 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in ubiquitin). FT CROSSLNK 27 27 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in ubiquitin) FT (Probable). FT CROSSLNK 29 29 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in ubiquitin). FT CROSSLNK 33 33 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in ubiquitin) (By FT similarity). FT CROSSLNK 48 48 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in ubiquitin). FT CROSSLNK 63 63 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in ubiquitin). FT CROSSLNK 76 76 Glycyl lysine isopeptide (Gly-Lys) FT (interchain with K-? in acceptor FT proteins). FT MUTAGEN 48 48 K->R: No effect on HLTF-mediated FT polyubiquitination of PCNA. FT MUTAGEN 63 63 K->R: Abolishes HLTF-mediated FT polyubiquitination of PCNA. FT STRAND 2 6 FT STRAND 12 16 FT HELIX 23 33 FT HELIX 38 40 FT STRAND 42 44 FT HELIX 57 59 FT STRAND 66 70 SQ SEQUENCE 156 AA; 17965 MW; 617BC63DF3A904F7 CRC64; MQIFVKTLTG KTITLEVEPS DTIENVKAKI QDKEGIPPDQ QRLIFAGKQL EDGRTLSDYN IQKESTLHLV LRLRGGAKKR KKKSYTTPKK NKHKRKKVKL AVLKYYKVDE NGKISRLRRE CPSDECGAGV FMASHFDRHY CGKCCLTYCF NKPEDK //