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Overview

Uniprot IDP0CG50
Protein NamePolyubiquitin-C
Gene NameUbc
OrganismMus musculus

Kla Sites from experimental identification

Position Flanking peptide
158 GGMQIFVKTLTGKTI
234 GGMQIFVKTLTGKTI
310 GGMQIFVKTLTGKTI
386 GGMQIFVKTLTGKTI
462 GGMQIFVKTLTGKTI
538 GGMQIFVKTLTGKTI
6 **MQIFVKTLTGKTI
614 GGMQIFVKTLTGKTI
690 GGMQIFVKTLTGKTI
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. During ubiquitination, the acceptor ubiquitin is positioned in the active site via direct interaction with the E2 ubiquitin-conjugating enzymes such as UBE2R2 (By similarity). As a monoubiquitin, its C-terminal glycine is recognized as a C-degron by Cul2-RING (CRL2) E3 ubiquitin-protein ligase complexes (By similarity)

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 310 LRGGMQIFVK 320 TLTGKTITLE 330 VEPSDTIENV 340 KAKIQDKEGI 350 PPDQQRLIFA 360 GKQLEDGRTL 370 SDYNIQKEST 380 LHLVLRLRGG 390 MQIFVKTLTG 400 KTITLEVEPS 410 DTIENVKAKI 420 QDKEGIPPDQ 430 QRLIFAGKQL 440 EDGRTLSDYN 450 IQKESTLHLV 460 LRLRGGMQIF 470 VKTLTGKTIT 480 LEVEPSDTIE 490 NVKAKIQDKE 500 GIPPDQQRLI 510 FAGKQLEDGR 520 TLSDYNIQKE 530 STLHLVLRLR 540 GGMQIFVKTL 550 TGKTITLEVE 560 PSDTIENVKA 570 KIQDKEGIPP 580 DQQRLIFAGK 590 QLEDGRTLSD 600 YNIQKESTLH 610 LVLRLRGGMQ 620 IFVKTLTGKT 630 ITLEVEPSDT 640 IENVKAKIQD 650 KEGIPPDQQR 660 LIFAGKQLED 670 GRTLSDYNIQ 680 KESTLHLVLR 690 LRGGMQIFVK 700 TLTGKTITLD 710 VEPSVTTKKV 720 KQEDRRTFLT 730 TVSKKSPPCA CSWV

Gene Ontology

Classification GO ID Description
Cellular Component GO:0043209 myelin sheath
Cellular Component GO:0005829 cytosol
Cellular Component GO:0022626 cytosolic ribosome
Cellular Component GO:0005741 mitochondrial outer membrane
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:0019941 modification-dependent protein catabolic process
Biological Process GO:0016567 protein ubiquitination

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.