CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-009674
UniProt Accession
Genbank Protein ID
 U72496 
Genbank Nucleotide ID
Protein Name
 Ubiquitin-60S ribosomal protein L40 
Protein Synonyms/Alias
 CEP52; Ubiquitin A-52 residue ribosomal protein fusion product 1; Ubiquitin; 60S ribosomal protein L40 
Gene Name
 UBA52 
Gene Synonyms/Alias
 UBCEP2 
Created Date
 July 27, 2013 
Organism
 Sus scrofa (Pig) 
NCBI Taxa ID
 9823 
Lysine Modification
Position
Peptide
Type
References
6**MQIFVKTLTGKTIacetylation[1]
11FVKTLTGKTITLEVEacetylation[1]
27SDTIENVKAKIQDKEacetylation[1]
29TIENVKAKIQDKEGIacetylation[1]
33VKAKIQDKEGIPPDQacetylation[1]
48QRLIFAGKQLEDGRTacetylation[1]
63LSDYNIQKESTLHLVacetylation[1]
Reference
 [1] N-epsilon-acetylation of porcine mature erythrocytes ubiquitin.
 Zhu DX, Xu LX, Zhu NZ, Briand G, Han KK.
 Int J Biochem. 1985;17(6):719-21. [PMID: 2993057
Functional Description
 Ubiquitin: exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in lysosomal degradation; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, DNA-damage responses as well as in signaling processes leading to activation of the transcription factor NF-kappa-B. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling (By similarity). 
Sequence Annotation
 DOMAIN 1 76 Ubiquitin-like.
 BINDING 54 54 Activating enzyme.
 BINDING 72 72 Activating enzyme.
 MOD_RES 6 6 N6-acetyllysine; alternate.
 MOD_RES 48 48 N6-acetyllysine; alternate.
 MOD_RES 57 57 Phosphoserine (By similarity).
 MOD_RES 65 65 Phosphoserine.
 MOD_RES 88 88 N6-acetyllysine (By similarity).
 MOD_RES 98 98 N6,N6,N6-trimethyllysine (By similarity).
 CROSSLNK 6 6 Glycyl lysine isopeptide (Lys-Gly)
 CROSSLNK 11 11 Glycyl lysine isopeptide (Lys-Gly)
 CROSSLNK 27 27 Glycyl lysine isopeptide (Lys-Gly)
 CROSSLNK 29 29 Glycyl lysine isopeptide (Lys-Gly)
 CROSSLNK 33 33 Glycyl lysine isopeptide (Lys-Gly)
 CROSSLNK 48 48 Glycyl lysine isopeptide (Lys-Gly)
 CROSSLNK 63 63 Glycyl lysine isopeptide (Lys-Gly)
 CROSSLNK 76 76 Glycyl lysine isopeptide (Gly-Lys)  
Keyword
 Acetylation; Complete proteome; Cytoplasm; Isopeptide bond; Methylation; Nucleus; Phosphoprotein; Reference proteome; Ribonucleoprotein; Ribosomal protein; Ubl conjugation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 128 AA 
Protein Sequence
MQIFVKTLTG KTITLEVEPS DTIENVKAKI QDKEGIPPDQ QRLIFAGKQL EDGRTLSDYN 60
IQKESTLHLV LRLRGGIIEP SLRQLAQKYN CDKMICRKCY ARLHPRAVNC RKKKCGHTNN 120
LRPKKKVK 128 
Gene Ontology
 GO:0022625; C:cytosolic large ribosomal subunit; IEA:Compara.
 GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
 GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
 GO:0006412; P:translation; IEA:InterPro. 
Interpro
 IPR001975; Ribosomal_L40e.
 IPR000626; Ubiquitin.
 IPR019954; Ubiquitin_CS.
 IPR019956; Ubiquitin_subgr.
 IPR019955; Ubiquitin_supergroup. 
Pfam
 PF01020; Ribosomal_L40e
 PF00240; ubiquitin 
SMART
 SM00213; UBQ 
PROSITE
 PS00299; UBIQUITIN_1
 PS50053; UBIQUITIN_2 
PRINTS
 PR00348; UBIQUITIN.