Tag | Content |
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CPLM ID | CPLM-003708 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Polyubiquitin |
Protein Synonyms/Alias | Ubiquitin |
Gene Name | UBI4 |
Gene Synonyms/Alias | SCD2; YLL039C |
Created Date | July 27, 2013 |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
NCBI Taxa ID | 559292 |
Lysine Modification | Position | Peptide | Type | References |
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82 | GGMQIFVKTLTGKTI | ubiquitination | [1] |
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Reference | [1] Sites of ubiquitin attachment in Saccharomyces cerevisiae. Starita LM, Lo RS, Eng JK, von Haller PD, Fields S. Proteomics. 2012 Jan;12(2):236-40. [ PMID: 22106047] |
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, and DNA-damage responses. 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 1. DOMAIN 77 152 Ubiquitin-like 2. DOMAIN 153 228 Ubiquitin-like 3. DOMAIN 229 304 Ubiquitin-like 4. DOMAIN 305 380 Ubiquitin-like 5. MOD_RES 57 57 Phosphoserine. 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 | 3D-structure; Complete proteome; Cytoplasm; DNA damage; DNA repair; Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome; Repeat; Ubl conjugation. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 381 AA |
Protein Sequence | MQIFVKTLTG KTITLEVESS DTIDNVKSKI QDKEGIPPDQ QRLIFAGKQL EDGRTLSDYN 60 IQKESTLHLV LRLRGGMQIF VKTLTGKTIT LEVESSDTID NVKSKIQDKE GIPPDQQRLI 120 FAGKQLEDGR TLSDYNIQKE STLHLVLRLR GGMQIFVKTL TGKTITLEVE SSDTIDNVKS 180 KIQDKEGIPP DQQRLIFAGK QLEDGRTLSD YNIQKESTLH LVLRLRGGMQ IFVKTLTGKT 240 ITLEVESSDT IDNVKSKIQD KEGIPPDQQR LIFAGKQLED GRTLSDYNIQ KESTLHLVLR 300 LRGGMQIFVK TLTGKTITLE VESSDTIDNV KSKIQDKEGI PPDQQRLIFA GKQLEDGRTL 360 SDYNIQKEST LHLVLRLRGG N 381 |
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