Tag | Content |
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CPLM ID | CPLM-009643 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Ubiquitin-40S ribosomal protein S27a |
Protein Synonyms/Alias | Ubiquitin carboxyl extension protein 80; Ubiquitin; 40S ribosomal protein S27a |
Gene Name | RPS27A |
Gene Synonyms/Alias | UBA80; UBCEP1 |
Created Date | July 27, 2013 |
Organism | Bos taurus (Bovine) |
NCBI Taxa ID | 9913 |
Lysine Modification | Position | Peptide | Type | References |
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6 | **MQIFVKTLTGKTI | acetylation | [1] | 11 | FVKTLTGKTITLEVE | acetylation | [1] | 27 | SDTIENVKAKIQDKE | acetylation | [1] | 29 | TIENVKAKIQDKEGI | acetylation | [1] | 33 | VKAKIQDKEGIPPDQ | acetylation | [1] | 48 | QRLIFAGKQLEDGRT | acetylation | [1] | 63 | LSDYNIQKESTLHLV | acetylation | [1] |
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Reference | [1] Localization of lysines acetylated in ubiquitin reacted with p-nitrophenyl acetate. Jabusch JR, Deutsch HF. Arch Biochem Biophys. 1985 Apr;238(1):170-7. [ PMID: 2984995] |
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. ZN_FING 121 144 C4-type. BINDING 54 54 Activating enzyme. BINDING 72 72 Activating enzyme. MOD_RES 57 57 Phosphoserine (By similarity). MOD_RES 104 104 N6-acetyllysine (By similarity). MOD_RES 113 113 N6-acetyllysine (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; Direct protein sequencing; Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat; Ribonucleoprotein; Ribosomal protein; Ubl conjugation; Zinc; Zinc-finger. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 156 AA |
Protein Sequence | MQIFVKTLTG KTITLEVEPS DTIENVKAKI QDKEGIPPDQ QRLIFAGKQL EDGRTLSDYN 60 IQKESTLHLV LRLRGGAKKR KKKSYTTPKK NKHKRKKVKL AVLKYYKVDE NGKISRLRRE 120 CPSDECGAGV FMASHFDRHY CGKCCLTYCF NKPEDK 156 |
Gene Ontology | GO:0022627; C:cytosolic small ribosomal subunit; IEA:Compara. GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. GO:0003735; F:structural constituent of ribosome; IEA:Compara. GO:0006412; P:translation; IEA:InterPro. |
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SMART | |
PROSITE | |
PRINTS | |