| Tag | Content |
|---|
| CPLM ID | CPLM-003706 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Polyubiquitin-B |
Protein Synonyms/Alias | Ubiquitin |
Gene Name | Ubb |
Gene Synonyms/Alias | |
Created Date | July 27, 2013 |
Organism | Mus musculus (Mouse) |
NCBI Taxa ID | 10090 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 29 | TIENVKAKIQDKEGI | ubiquitination | [1] | | 33 | VKAKIQDKEGIPPDQ | ubiquitination | [1] | | 48 | QRLIFAGKQLEDGRT | ubiquitination | [1] | | 63 | LSDYNIQKESTLHLV | ubiquitination | [1] |
|
Reference | [1] BTB-ZF factors recruit the E3 ligase cullin 3 to regulate lymphoid effector programs. Mathew R, Seiler MP, Scanlon ST, Mao AP, Constantinides MG, Bertozzi-Villa C, Singer JD, Bendelac A. Nature. 2012 Nov 22;491(7425):618-21. [ PMID: 23086144] |
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. |
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.
BINDING 54 54 Activating enzyme.
BINDING 72 72 Activating enzyme.
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 | Complete proteome; Cytoplasm; Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome; Repeat; Ubl conjugation. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 305 AA |
Protein Sequence | MQIFVKTLTG KTITLEVEPS DTIENVKAKI QDKEGIPPDQ QRLIFAGKQL EDGRTLSDYN 60
IQKESTLHLV LRLRGGMQIF VKTLTGKTIT LEVEPSDTIE NVKAKIQDKE GIPPDQQRLI 120
FAGKQLEDGR TLSDYNIQKE STLHLVLRLR GGMQIFVKTL TGKTITLEVE PSDTIENVKA 180
KIQDKEGIPP DQQRLIFAGK QLEDGRTLSD YNIQKESTLH LVLRLRGGMQ IFVKTLTGKT 240
ITLEVEPSDT IENVKAKIQD KEGIPPDQQR LIFAGKQLED GRTLSDYNIQ KESTLHLVLR 300
LRGGY 305 |
Gene Ontology | |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |