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Overview

Uniprot IDP0CG49
Protein NamePolyubiquitin-B
Gene NameUbb
OrganismMus musculus

Kla Sites from experimental identification

Position Flanking peptide
158 GGMQIFVKTLTGKTI
234 GGMQIFVKTLTGKTI
6 **MQIFVKTLTGKTI
82 GGMQIFVKTLTGKTI

Function

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 proteotoxic stress response and cell cycle; 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

Protein Sequence

10 MQIFVKTLTG 20 KTITLEVEPS 30 DTIENVKAKI 40 QDKEGIPPDQ 50 QRLIFAGKQL 60 EDGRTLSDYN 70 IQKESTLHLV 80 LRLRGGMQIF 90 VKTLTGKTIT 100 LEVEPSDTIE 110 NVKAKIQDKE 120 GIPPDQQRLI 130 FAGKQLEDGR 140 TLSDYNIQKE 150 STLHLVLRLR 160 GGMQIFVKTL 170 TGKTITLEVE 180 PSDTIENVKA 190 KIQDKEGIPP 200 DQQRLIFAGK 210 QLEDGRTLSD 220 YNIQKESTLH 230 LVLRLRGGMQ 240 IFVKTLTGKT 250 ITLEVEPSDT 260 IENVKAKIQD 270 KEGIPPDQQR 280 LIFAGKQLED 290 GRTLSDYNIQ 300 KESTLHLVLR LRGGY

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005829 cytosol
Cellular Component GO:0022626 cytosolic ribosome
Cellular Component GO:0005741 mitochondrial outer membrane
Cellular Component GO:0005739 mitochondrion
Cellular Component GO:0043209 myelin sheath
Cellular Component GO:0043005 neuron projection
Cellular Component GO:0043025 neuronal cell body
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Molecular Function GO:0031386 protein tag activity
Molecular Function GO:0003735 structural constituent of ribosome
Biological Process GO:0060612 adipose tissue development
Biological Process GO:0097009 energy homeostasis
Biological Process GO:0060613 fat pad development
Biological Process GO:0008585 female gonad development
Biological Process GO:0007144 female meiosis I
Biological Process GO:0021888 hypothalamus gonadotrophin-releasing hormone neuron development
Biological Process GO:0008584 male gonad development
Biological Process GO:0007141 male meiosis I
Biological Process GO:0047497 mitochondrion transport along microtubule
Biological Process GO:0019941 modification-dependent protein catabolic process
Biological Process GO:0048812 neuron projection morphogenesis
Biological Process GO:1902255 positive regulation of intrinsic apoptotic signaling pathway by p53 class mediator
Biological Process GO:1902527 positive regulation of protein monoubiquitination
Biological Process GO:0031398 positive regulation of protein ubiquitination
Biological Process GO:0016567 protein ubiquitination
Biological Process GO:0051881 regulation of mitochondrial membrane potential
Biological Process GO:0043523 regulation of neuron apoptotic process
Biological Process GO:0061136 regulation of proteasomal protein catabolic process
Biological Process GO:0072520 seminiferous tubule development

Reference

[1] Zhuo W, Zhang M, Tan J, Gao Y, Wang Y et al.. Lysine lactylation analysis of proteins in the heart of the Kawasaki disease mouse model.. Front Cell Dev Biol 13:1550220. 2025. PMID: 40114965.