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Database: UniProt
Entry: P63048
LinkDB: P63048
Original site: P63048 
ID   RL40_BOVIN              Reviewed;         128 AA.
AC   P63048; O97577; P02248; P02249; P02250; P62990; P80169; Q01235; Q24K23;
AC   Q28169; Q28170; Q29120; Q3T0V5; Q3ZCE3; Q862C1; Q862F4; Q862M4; Q862T5;
AC   Q862X8; Q91887; Q91888;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   10-AUG-2010, sequence version 2.
DT   27-MAR-2024, entry version 134.
DE   RecName: Full=Ubiquitin-ribosomal protein eL40 fusion protein {ECO:0000305};
DE   AltName: Full=Ubiquitin A-52 residue ribosomal protein fusion product 1;
DE   Contains:
DE     RecName: Full=Ubiquitin;
DE   Contains:
DE     RecName: Full=Large ribosomal subunit protein eL40 {ECO:0000305};
DE     AltName: Full=60S ribosomal protein L40;
DE     AltName: Full=CEP52;
DE   Flags: Precursor;
GN   Name=UBA52; Synonyms=UBCEP2;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=12658628; DOI=10.1002/mrd.10292;
RA   Ishiwata H., Katsuma S., Kizaki K., Patel O.V., Nakano H., Takahashi T.,
RA   Imai K., Hirasawa A., Shiojima S., Ikawa H., Suzuki Y., Tsujimoto G.,
RA   Izaike Y., Todoroki J., Hashizume K.;
RT   "Characterization of gene expression profiles in early bovine pregnancy
RT   using a custom cDNA microarray.";
RL   Mol. Reprod. Dev. 65:9-18(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Crossbred X Angus; TISSUE=Ileum, and Liver;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   PROTEIN SEQUENCE OF 1-74.
RX   PubMed=1170880; DOI=10.1021/bi00681a026;
RA   Schlesinger D.H., Goldstein G., Niall H.D.;
RT   "The complete amino acid sequence of ubiquitin, an adenylate cyclase
RT   stimulating polypeptide probably universal in living cells.";
RL   Biochemistry 14:2214-2218(1975).
RN   [4]
RP   PROTEIN SEQUENCE OF 1-50.
RX   PubMed=6254502; DOI=10.1016/0006-291x(80)91188-2;
RA   Hamilton J.W., Rouse J.B.;
RT   "The biosynthesis of ubiquitin by parathyroid gland.";
RL   Biochem. Biophys. Res. Commun. 96:114-120(1980).
RN   [5]
RP   PROTEIN SEQUENCE OF 1-20.
RC   TISSUE=Brain;
RX   PubMed=1333954; DOI=10.1111/j.1432-1033.1992.tb17446.x;
RA   Zdebska E., Antoniewicz J., Nilsson B., Sandhoff K., Fuerst W., Janik P.,
RA   Koscielak J.;
RT   "Ganglioside binding proteins of calf brain with ubiquitin-like N-
RT   terminals.";
RL   Eur. J. Biochem. 210:483-489(1992).
CC   -!- FUNCTION: [Ubiquitin]: Exists either covalently attached to another
CC       protein, or free (unanchored). When covalently bound, it is conjugated
CC       to target proteins via an isopeptide bond either as a monomer
CC       (monoubiquitin), a polymer linked via different Lys residues of the
CC       ubiquitin (polyubiquitin chains) or a linear polymer linked via the
CC       initiator Met of the ubiquitin (linear polyubiquitin chains).
CC       Polyubiquitin chains, when attached to a target protein, have different
CC       functions depending on the Lys residue of the ubiquitin that is linked:
CC       Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved
CC       in ERAD (endoplasmic reticulum-associated degradation) and in cell-
CC       cycle regulation; Lys-29-linked is involved in proteotoxic stress
CC       response and cell cycle; Lys-33-linked is involved in kinase
CC       modification; Lys-48-linked is involved in protein degradation via the
CC       proteasome; Lys-63-linked is involved in endocytosis, DNA-damage
CC       responses as well as in signaling processes leading to activation of
CC       the transcription factor NF-kappa-B. Linear polymer chains formed via
CC       attachment by the initiator Met lead to cell signaling. Ubiquitin is
CC       usually 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 distinct
CC       roles, such as in activation of protein kinases, and in signaling.
CC       {ECO:0000250|UniProtKB:P62987}.
CC   -!- FUNCTION: [Large ribosomal subunit protein eL40]: Component of the 60S
CC       subunit of the ribosome. Ribosomal protein L40 is essential for
CC       translation of a subset of cellular transcripts, and especially for
CC       cap-dependent translation of vesicular stomatitis virus mRNAs.
CC       {ECO:0000250|UniProtKB:P62987}.
CC   -!- SUBUNIT: [Large ribosomal subunit protein eL40]: Part of the 60S
CC       ribosomal subunit. Interacts with UBQLN1 (via UBA domain).
CC       {ECO:0000250|UniProtKB:P62987}.
CC   -!- SUBCELLULAR LOCATION: [Ubiquitin]: Cytoplasm {ECO:0000250}. Nucleus
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: [Large ribosomal subunit protein eL40]: Cytoplasm
CC       {ECO:0000250}.
CC   -!- PTM: [Ubiquitin]: Phosphorylated at Ser-65 by PINK1 during mitophagy.
CC       Phosphorylated ubiquitin specifically binds and activates parkin
CC       (PRKN), triggering mitophagy. Phosphorylation does not affect E1-
CC       mediated E2 charging of ubiquitin but affects discharging of E2 enzymes
CC       to form polyubiquitin chains. It also affects deubiquitination by
CC       deubiquitinase enzymes such as USP30. {ECO:0000250|UniProtKB:P62987}.
CC   -!- PTM: [Ubiquitin]: Mono-ADP-ribosylated at the C-terminus by PARP9, a
CC       component of the PPAR9-DTX3L complex. ADP-ribosylation requires
CC       processing by E1 and E2 enzymes and prevents ubiquitin conjugation to
CC       substrates such as histones. {ECO:0000250|UniProtKB:P62987}.
CC   -!- MISCELLANEOUS: Ubiquitin is encoded by 4 different genes. Uba52 and
CC       Rps27a genes code for a single copy of ubiquitin fused to the ribosomal
CC       proteins eL40 and eS31, respectively. UBB and UBC genes code for a
CC       polyubiquitin precursor with exact head to tail repeats, the number of
CC       repeats differ between species and strains.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the ubiquitin family.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the eukaryotic
CC       ribosomal protein eL40 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC56447.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AB098957; BAC56447.1; ALT_FRAME; mRNA.
DR   EMBL; BC102248; AAI02249.1; -; mRNA.
DR   RefSeq; NP_001069831.1; NM_001076363.2.
DR   PDB; 4LJO; X-ray; 1.56 A; B=1-76.
DR   PDB; 4LJP; X-ray; 2.15 A; B=1-76.
DR   PDB; 4S22; X-ray; 2.30 A; A/B/C/D=1-76.
DR   PDB; 6ZVK; EM; 3.49 A; E2=77-128.
DR   PDB; 7A01; EM; 3.60 A; E2=77-128.
DR   PDB; 7NFX; EM; 3.20 A; m=77-128.
DR   PDB; 7OBR; EM; 2.80 A; m=77-128.
DR   PDBsum; 4LJO; -.
DR   PDBsum; 4LJP; -.
DR   PDBsum; 4S22; -.
DR   PDBsum; 6ZVK; -.
DR   PDBsum; 7A01; -.
DR   PDBsum; 7NFX; -.
DR   PDBsum; 7OBR; -.
DR   AlphaFoldDB; P63048; -.
DR   SASBDB; P63048; -.
DR   SMR; P63048; -.
DR   STRING; 9913.ENSBTAP00000010176; -.
DR   PaxDb; 9913-ENSBTAP00000010176; -.
DR   Ensembl; ENSBTAT00000010176.3; ENSBTAP00000010176.2; ENSBTAG00000007737.3.
DR   GeneID; 615199; -.
DR   KEGG; bta:615199; -.
DR   CTD; 7311; -.
DR   VEuPathDB; HostDB:ENSBTAG00000007737; -.
DR   VGNC; VGNC:49988; UBA52.
DR   eggNOG; KOG0003; Eukaryota.
DR   GeneTree; ENSGT00940000153593; -.
DR   HOGENOM; CLU_010412_3_4_1; -.
DR   InParanoid; P63048; -.
DR   OMA; ARKYKCD; -.
DR   OrthoDB; 312211at2759; -.
DR   TreeFam; TF352129; -.
DR   Reactome; R-BTA-110312; Translesion synthesis by REV1.
DR   Reactome; R-BTA-110314; Recognition of DNA damage by PCNA-containing replication complex.
DR   Reactome; R-BTA-110320; Translesion Synthesis by POLH.
DR   Reactome; R-BTA-1169091; Activation of NF-kappaB in B cells.
DR   Reactome; R-BTA-1234176; Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
DR   Reactome; R-BTA-1253288; Downregulation of ERBB4 signaling.
DR   Reactome; R-BTA-1295596; Spry regulation of FGF signaling.
DR   Reactome; R-BTA-1358803; Downregulation of ERBB2:ERBB3 signaling.
DR   Reactome; R-BTA-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR   Reactome; R-BTA-168638; NOD1/2 Signaling Pathway.
DR   Reactome; R-BTA-174048; APC/C:Cdc20 mediated degradation of Cyclin B.
DR   Reactome; R-BTA-174084; Autodegradation of Cdh1 by Cdh1:APC/C.
DR   Reactome; R-BTA-174113; SCF-beta-TrCP mediated degradation of Emi1.
DR   Reactome; R-BTA-174154; APC/C:Cdc20 mediated degradation of Securin.
DR   Reactome; R-BTA-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
DR   Reactome; R-BTA-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
DR   Reactome; R-BTA-179409; APC-Cdc20 mediated degradation of Nek2A.
DR   Reactome; R-BTA-1799339; SRP-dependent cotranslational protein targeting to membrane.
DR   Reactome; R-BTA-182971; EGFR downregulation.
DR   Reactome; R-BTA-187577; SCF(Skp2)-mediated degradation of p27/p21.
DR   Reactome; R-BTA-195253; Degradation of beta-catenin by the destruction complex.
DR   Reactome; R-BTA-201681; TCF dependent signaling in response to WNT.
DR   Reactome; R-BTA-202424; Downstream TCR signaling.
DR   Reactome; R-BTA-205043; NRIF signals cell death from the nucleus.
DR   Reactome; R-BTA-209543; p75NTR recruits signalling complexes.
DR   Reactome; R-BTA-209560; NF-kB is activated and signals survival.
DR   Reactome; R-BTA-2122948; Activated NOTCH1 Transmits Signal to the Nucleus.
DR   Reactome; R-BTA-2173788; Downregulation of TGF-beta receptor signaling.
DR   Reactome; R-BTA-2173791; TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition).
DR   Reactome; R-BTA-2173795; Downregulation of SMAD2/3:SMAD4 transcriptional activity.
DR   Reactome; R-BTA-2173796; SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.
DR   Reactome; R-BTA-2467813; Separation of Sister Chromatids.
DR   Reactome; R-BTA-2559582; Senescence-Associated Secretory Phenotype (SASP).
DR   Reactome; R-BTA-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR   Reactome; R-BTA-2672351; Stimuli-sensing channels.
DR   Reactome; R-BTA-2871837; FCERI mediated NF-kB activation.
DR   Reactome; R-BTA-3134975; Regulation of innate immune responses to cytosolic DNA.
DR   Reactome; R-BTA-349425; Autodegradation of the E3 ubiquitin ligase COP1.
DR   Reactome; R-BTA-3769402; Deactivation of the beta-catenin transactivating complex.
DR   Reactome; R-BTA-382556; ABC-family proteins mediated transport.
DR   Reactome; R-BTA-450302; activated TAK1 mediates p38 MAPK activation.
DR   Reactome; R-BTA-450321; JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1.
DR   Reactome; R-BTA-450408; AUF1 (hnRNP D0) binds and destabilizes mRNA.
DR   Reactome; R-BTA-4608870; Asymmetric localization of PCP proteins.
DR   Reactome; R-BTA-4641257; Degradation of AXIN.
DR   Reactome; R-BTA-4641258; Degradation of DVL.
DR   Reactome; R-BTA-4641263; Regulation of FZD by ubiquitination.
DR   Reactome; R-BTA-5205685; PINK1-PRKN Mediated Mitophagy.
DR   Reactome; R-BTA-532668; N-glycan trimming in the ER and Calnexin/Calreticulin cycle.
DR   Reactome; R-BTA-5357905; Regulation of TNFR1 signaling.
DR   Reactome; R-BTA-5357956; TNFR1-induced NF-kappa-B signaling pathway.
DR   Reactome; R-BTA-5358346; Hedgehog ligand biogenesis.
DR   Reactome; R-BTA-5607761; Dectin-1 mediated noncanonical NF-kB signaling.
DR   Reactome; R-BTA-5607764; CLEC7A (Dectin-1) signaling.
DR   Reactome; R-BTA-5610780; Degradation of GLI1 by the proteasome.
DR   Reactome; R-BTA-5610785; GLI3 is processed to GLI3R by the proteasome.
DR   Reactome; R-BTA-5632684; Hedgehog 'on' state.
DR   Reactome; R-BTA-5654726; Negative regulation of FGFR1 signaling.
DR   Reactome; R-BTA-5654727; Negative regulation of FGFR2 signaling.
DR   Reactome; R-BTA-5654732; Negative regulation of FGFR3 signaling.
DR   Reactome; R-BTA-5654733; Negative regulation of FGFR4 signaling.
DR   Reactome; R-BTA-5655862; Translesion synthesis by POLK.
DR   Reactome; R-BTA-5656121; Translesion synthesis by POLI.
DR   Reactome; R-BTA-5656169; Termination of translesion DNA synthesis.
DR   Reactome; R-BTA-5668541; TNFR2 non-canonical NF-kB pathway.
DR   Reactome; R-BTA-5675221; Negative regulation of MAPK pathway.
DR   Reactome; R-BTA-5675482; Regulation of necroptotic cell death.
DR   Reactome; R-BTA-5676590; NIK-->noncanonical NF-kB signaling.
DR   Reactome; R-BTA-5684264; MAP3K8 (TPL2)-dependent MAPK1/3 activation.
DR   Reactome; R-BTA-5685942; HDR through Homologous Recombination (HRR).
DR   Reactome; R-BTA-5687128; MAPK6/MAPK4 signaling.
DR   Reactome; R-BTA-5689603; UCH proteinases.
DR   Reactome; R-BTA-5689877; Josephin domain DUBs.
DR   Reactome; R-BTA-5689880; Ub-specific processing proteases.
DR   Reactome; R-BTA-5689896; Ovarian tumor domain proteases.
DR   Reactome; R-BTA-5689901; Metalloprotease DUBs.
DR   Reactome; R-BTA-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
DR   Reactome; R-BTA-5696394; DNA Damage Recognition in GG-NER.
DR   Reactome; R-BTA-5696395; Formation of Incision Complex in GG-NER.
DR   Reactome; R-BTA-5696397; Gap-filling DNA repair synthesis and ligation in GG-NER.
DR   Reactome; R-BTA-5696400; Dual Incision in GG-NER.
DR   Reactome; R-BTA-6781823; Formation of TC-NER Pre-Incision Complex.
DR   Reactome; R-BTA-6782135; Dual incision in TC-NER.
DR   Reactome; R-BTA-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR   Reactome; R-BTA-6783310; Fanconi Anemia Pathway.
DR   Reactome; R-BTA-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR   Reactome; R-BTA-6804756; Regulation of TP53 Activity through Phosphorylation.
DR   Reactome; R-BTA-6804757; Regulation of TP53 Degradation.
DR   Reactome; R-BTA-6804760; Regulation of TP53 Activity through Methylation.
DR   Reactome; R-BTA-6807004; Negative regulation of MET activity.
DR   Reactome; R-BTA-68867; Assembly of the pre-replicative complex.
DR   Reactome; R-BTA-68949; Orc1 removal from chromatin.
DR   Reactome; R-BTA-69017; CDK-mediated phosphorylation and removal of Cdc6.
DR   Reactome; R-BTA-69231; Cyclin D associated events in G1.
DR   Reactome; R-BTA-69481; G2/M Checkpoints.
DR   Reactome; R-BTA-69601; Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
DR   Reactome; R-BTA-72689; Formation of a pool of free 40S subunits.
DR   Reactome; R-BTA-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
DR   Reactome; R-BTA-75815; Ubiquitin-dependent degradation of Cyclin D.
DR   Reactome; R-BTA-8849469; PTK6 Regulates RTKs and Their Effectors AKT1 and DOK1.
DR   Reactome; R-BTA-8852276; The role of GTSE1 in G2/M progression after G2 checkpoint.
DR   Reactome; R-BTA-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
DR   Reactome; R-BTA-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR   Reactome; R-BTA-8856828; Clathrin-mediated endocytosis.
DR   Reactome; R-BTA-8863795; Downregulation of ERBB2 signaling.
DR   Reactome; R-BTA-8866427; VLDLR internalisation and degradation.
DR   Reactome; R-BTA-8866652; Synthesis of active ubiquitin: roles of E1 and E2 enzymes.
DR   Reactome; R-BTA-8866654; E3 ubiquitin ligases ubiquitinate target proteins.
DR   Reactome; R-BTA-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs.
DR   Reactome; R-BTA-8939902; Regulation of RUNX2 expression and activity.
DR   Reactome; R-BTA-8941858; Regulation of RUNX3 expression and activity.
DR   Reactome; R-BTA-8948747; Regulation of PTEN localization.
DR   Reactome; R-BTA-8948751; Regulation of PTEN stability and activity.
DR   Reactome; R-BTA-8951664; Neddylation.
DR   Reactome; R-BTA-901032; ER Quality Control Compartment (ERQC).
DR   Reactome; R-BTA-9010553; Regulation of expression of SLITs and ROBOs.
DR   Reactome; R-BTA-9020702; Interleukin-1 signaling.
DR   Reactome; R-BTA-9033241; Peroxisomal protein import.
DR   Reactome; R-BTA-909733; Interferon alpha/beta signaling.
DR   Reactome; R-BTA-912631; Regulation of signaling by CBL.
DR   Reactome; R-BTA-917729; Endosomal Sorting Complex Required For Transport (ESCRT).
DR   Reactome; R-BTA-917937; Iron uptake and transport.
DR   Reactome; R-BTA-936440; Negative regulators of DDX58/IFIH1 signaling.
DR   Reactome; R-BTA-936964; Activation of IRF3, IRF7 mediated by TBK1, IKBKE.
DR   Reactome; R-BTA-937041; IKK complex recruitment mediated by RIP1.
DR   Reactome; R-BTA-937042; IRAK2 mediated activation of TAK1 complex.
DR   Reactome; R-BTA-937072; TRAF6-mediated induction of TAK1 complex within TLR4 complex.
DR   Reactome; R-BTA-9645460; Alpha-protein kinase 1 signaling pathway.
DR   Reactome; R-BTA-9646399; Aggrephagy.
DR   Reactome; R-BTA-9648002; RAS processing.
DR   Reactome; R-BTA-9664873; Pexophagy.
DR   Reactome; R-BTA-9705462; Inactivation of CSF3 (G-CSF) signaling.
DR   Reactome; R-BTA-9706369; Negative regulation of FLT3.
DR   Reactome; R-BTA-9708530; Regulation of BACH1 activity.
DR   Reactome; R-BTA-975163; IRAK2 mediated activation of TAK1 complex upon TLR7/8 or 9 stimulation.
DR   Reactome; R-BTA-9755511; KEAP1-NFE2L2 pathway.
DR   Reactome; R-BTA-9758274; Regulation of NF-kappa B signaling.
DR   Reactome; R-BTA-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
DR   Reactome; R-BTA-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR   Reactome; R-BTA-9762114; GSK3B and BTRC:CUL1-mediated-degradation of NFE2L2.
DR   Reactome; R-BTA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   Proteomes; UP000009136; Chromosome 7.
DR   Bgee; ENSBTAG00000007737; Expressed in laryngeal cartilage and 107 other cell types or tissues.
DR   GO; GO:0022625; C:cytosolic large ribosomal subunit; IEA:Ensembl.
DR   GO; GO:0022627; C:cytosolic small ribosomal subunit; IBA:GO_Central.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR   GO; GO:0031386; F:protein tag activity; IBA:GO_Central.
DR   GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; IBA:GO_Central.
DR   GO; GO:0019941; P:modification-dependent protein catabolic process; IBA:GO_Central.
DR   GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR   GO; GO:0006412; P:translation; IEA:InterPro.
DR   CDD; cd01803; Ubl_ubiquitin; 1.
DR   Gene3D; 4.10.1060.50; -; 1.
DR   InterPro; IPR001975; Ribosomal_eL40_dom.
DR   InterPro; IPR038587; Ribosomal_eL40_sf.
DR   InterPro; IPR000626; Ubiquitin-like_dom.
DR   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   InterPro; IPR019954; Ubiquitin_CS.
DR   InterPro; IPR019956; Ubiquitin_dom.
DR   PANTHER; PTHR10666; UBIQUITIN; 1.
DR   PANTHER; PTHR10666:SF467; UBIQUITIN-60S RIBOSOMAL PROTEIN L40; 1.
DR   Pfam; PF01020; Ribosomal_L40e; 1.
DR   Pfam; PF00240; ubiquitin; 1.
DR   PRINTS; PR00348; UBIQUITIN.
DR   SMART; SM01377; Ribosomal_L40e; 1.
DR   SMART; SM00213; UBQ; 1.
DR   SUPFAM; SSF54236; Ubiquitin-like; 1.
DR   PROSITE; PS00299; UBIQUITIN_1; 1.
DR   PROSITE; PS50053; UBIQUITIN_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; ADP-ribosylation; Cytoplasm; Direct protein sequencing;
KW   Isopeptide bond; Methylation; Nucleus; Phosphoprotein; Reference proteome;
KW   Ribonucleoprotein; Ribosomal protein; Ubl conjugation.
FT   CHAIN           1..76
FT                   /note="Ubiquitin"
FT                   /id="PRO_0000396432"
FT   CHAIN           77..128
FT                   /note="Large ribosomal subunit protein eL40"
FT                   /id="PRO_0000138748"
FT   DOMAIN          1..76
FT                   /note="Ubiquitin-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT   SITE            54
FT                   /note="Interacts with activating enzyme"
FT   SITE            68
FT                   /note="Essential for function"
FT   SITE            72
FT                   /note="Interacts with activating enzyme"
FT   MOD_RES         65
FT                   /note="Phosphoserine; by PINK1"
FT                   /evidence="ECO:0000250|UniProtKB:P62987"
FT   MOD_RES         76
FT                   /note="ADP-ribosylglycine"
FT                   /evidence="ECO:0000250|UniProtKB:P62987"
FT   MOD_RES         98
FT                   /note="N6,N6,N6-trimethyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P62986"
FT   CROSSLNK        6
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250|UniProtKB:P62987"
FT   CROSSLNK        11
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250|UniProtKB:P62987"
FT   CROSSLNK        27
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250|UniProtKB:P62987"
FT   CROSSLNK        29
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250|UniProtKB:P62987"
FT   CROSSLNK        33
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250|UniProtKB:P62987"
FT   CROSSLNK        48
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250|UniProtKB:P62987"
FT   CROSSLNK        63
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250|UniProtKB:P62987"
FT   CROSSLNK        76
FT                   /note="Glycyl lysine isopeptide (Gly-Lys) (interchain with
FT                   K-? in acceptor proteins)"
FT   STRAND          2..6
FT                   /evidence="ECO:0007829|PDB:4LJO"
FT   STRAND          12..16
FT                   /evidence="ECO:0007829|PDB:4LJO"
FT   HELIX           23..34
FT                   /evidence="ECO:0007829|PDB:4LJO"
FT   HELIX           38..40
FT                   /evidence="ECO:0007829|PDB:4LJO"
FT   STRAND          41..45
FT                   /evidence="ECO:0007829|PDB:4LJO"
FT   HELIX           57..59
FT                   /evidence="ECO:0007829|PDB:4LJO"
FT   STRAND          66..71
FT                   /evidence="ECO:0007829|PDB:4LJO"
SQ   SEQUENCE   128 AA;  14728 MW;  7BCB602ABEFAD02A CRC64;
     MQIFVKTLTG KTITLEVEPS DTIENVKAKI QDKEGIPPDQ QRLIFAGKQL EDGRTLSDYN
     IQKESTLHLV LRLRGGIIEP SLRQLAQKYN CDKMICRKCY ARLHPRAVNC RKKKCGHTNN
     LRPKKKVK
//
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