Polyubiquitin-C (UBC)

The protein contains 685 amino acids for an estimated molecular weight of 77039 Da.

 

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. (updated: Dec. 11, 2019)

Protein identification was indicated in the following studies:

  1. Goodman and co-workers. (2013) The proteomics and interactomics of human erythrocytes. Exp Biol Med (Maywood) 238(5), 509-518.
  2. Lange and co-workers. (2014) Annotating N termini for the human proteome project: N termini and Nα-acetylation status differentiate stable cleaved protein species from degradation remnants in the human erythrocyte proteome. J Proteome Res. 13(4), 2028-2044.
  3. Hegedűs and co-workers. (2015) Inconsistencies in the red blood cell membrane proteome analysis: generation of a database for research and diagnostic applications. Database (Oxford) 1-8.

Methods

The following articles were analysed to gather the proteome content of erythrocytes.

The gene or protein list provided in the studies were processed using the ID mapping API of Uniprot in September 2018. The number of proteins identified and mapped without ambiguity in these studies is indicated below.
Only Swiss-Prot entries (reviewed) were considered for protein evidence assignation.

PublicationIdentification 1Uniprot mapping 2Not mapped /
Obsolete
TrEMBLSwiss-Prot
Goodman (2013)2289 (gene list)227853205992269
Lange (2014)123412347281224
Hegedus (2015)2638262202352387
Wilson (2016)165815281702911068
d'Alessandro (2017)18261817201815
Bryk (2017)20902060101081942
Chu (2018)18531804553621387

1 as available in the article and/or in supplementary material
2 uniprot mapping returns all protein isoforms as one entry

The compilation of older studies can be retrieved from the Red Blood Cell Collection database.

The data and differentiation stages presented below come from the proteomic study and analysis performed by our partners of the GReX consortium, more details are available in their published work.

No sequence conservation computed yet.

This protein is annotated as membranous in Gene Ontology.


Interpro domains
Total structural coverage: 24%
Model score: 0
No model available.

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Biological Process

Activation of MAPK activity GO Logo
Aggrephagy GO Logo
Amyloid fibril formation GO Logo
Anaphase-promoting complex-dependent catabolic process GO Logo
Antigen processing and presentation of exogenous peptide antigen via MHC class I GO Logo
Antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent GO Logo
Antigen processing and presentation of peptide antigen via MHC class I GO Logo
Apoptotic process GO Logo
Apoptotic signaling pathway GO Logo
Carbohydrate metabolic process GO Logo
Cellular iron ion homeostasis GO Logo
Cellular protein metabolic process GO Logo
Cellular response to hypoxia GO Logo
Circadian rhythm GO Logo
Cytokine-mediated signaling pathway GO Logo
Cytoplasmic pattern recognition receptor signaling pathway GO Logo
DNA damage response, detection of DNA damage GO Logo
DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest GO Logo
DNA repair GO Logo
Endoplasmic reticulum mannose trimming GO Logo
Endosomal transport GO Logo
Entry of bacterium into host cell GO Logo
Epidermal growth factor receptor signaling pathway GO Logo
ERBB2 signaling pathway GO Logo
Error-free translesion synthesis GO Logo
Error-prone translesion synthesis GO Logo
Fc-epsilon receptor signaling pathway GO Logo
Fibroblast growth factor receptor signaling pathway GO Logo
G1/S transition of mitotic cell cycle GO Logo
G2/M transition of mitotic cell cycle GO Logo
Gene expression GO Logo
Global genome nucleotide-excision repair GO Logo
Glucose metabolic process GO Logo
Glycogen biosynthetic process GO Logo
I-kappaB kinase/NF-kappaB signaling GO Logo
Innate immune response GO Logo
Interleukin-1-mediated signaling pathway GO Logo
Interstrand cross-link repair GO Logo
Intracellular transport of virus GO Logo
Ion transmembrane transport GO Logo
JNK cascade GO Logo
Macroautophagy GO Logo
MAPK cascade GO Logo
Membrane organization GO Logo
Mitotic cell cycle GO Logo
Modification-dependent protein catabolic process GO Logo
Modulation by symbiont of host defense response GO Logo
MyD88-dependent toll-like receptor signaling pathway GO Logo
MyD88-independent toll-like receptor signaling pathway GO Logo
Negative regulation of apoptotic process GO Logo
Negative regulation of canonical Wnt signaling pathway GO Logo
Negative regulation of epidermal growth factor receptor signaling pathway GO Logo
Negative regulation of G2/M transition of mitotic cell cycle GO Logo
Negative regulation of Notch signaling pathway GO Logo
Negative regulation of transcription by RNA polymerase II GO Logo
Negative regulation of transforming growth factor beta receptor signaling pathway GO Logo
Negative regulation of type I interferon production GO Logo
Neurotrophin TRK receptor signaling pathway GO Logo
NIK/NF-kappaB signaling GO Logo
Notch receptor processing GO Logo
Notch signaling pathway GO Logo
Nucleotide-binding domain, leucine rich repeat containing receptor signaling pathway GO Logo
Nucleotide-binding oligomerization domain containing signaling pathway GO Logo
Nucleotide-excision repair, DNA damage recognition GO Logo
Nucleotide-excision repair, DNA duplex unwinding GO Logo
Nucleotide-excision repair, DNA gap filling GO Logo
Nucleotide-excision repair, DNA incision GO Logo
Nucleotide-excision repair, DNA incision, 5'-to lesion GO Logo
Nucleotide-excision repair, preincision complex assembly GO Logo
Obsolete negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle GO Logo
Obsolete positive regulation of ubiquitin-protein ligase activity involved in regulation of mitotic cell cycle transition GO Logo
Obsolete regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle GO Logo
Pathogenesis GO Logo
Positive regulation of apoptotic process GO Logo
Positive regulation of canonical Wnt signaling pathway GO Logo
Positive regulation of epidermal growth factor receptor signaling pathway GO Logo
Positive regulation of I-kappaB kinase/NF-kappaB signaling GO Logo
Positive regulation of NF-kappaB transcription factor activity GO Logo
Positive regulation of transcription by RNA polymerase II GO Logo
Positive regulation of type I interferon production GO Logo
Pre-replicative complex assembly GO Logo
Proteasome-mediated ubiquitin-dependent protein catabolic process GO Logo
Protein deubiquitination GO Logo
Protein folding GO Logo
Protein localization GO Logo
Protein polyubiquitination GO Logo
Protein targeting to peroxisome GO Logo
Protein ubiquitination GO Logo
Protein ubiquitination involved in ubiquitin-dependent protein catabolic process GO Logo
Regulation of apoptotic process GO Logo
Regulation of exit from mitosis GO Logo
Regulation of hematopoietic stem cell differentiation GO Logo
Regulation of mRNA stability GO Logo
Regulation of necroptotic process GO Logo
Regulation of signal transduction by p53 class mediator GO Logo
Regulation of transcription from RNA polymerase II promoter in response to hypoxia GO Logo
Regulation of tumor necrosis factor-mediated signaling pathway GO Logo
Regulation of type I interferon production GO Logo
SCF-dependent proteasomal ubiquitin-dependent protein catabolic process GO Logo
Small molecule metabolic process GO Logo
Stimulatory C-type lectin receptor signaling pathway GO Logo
Stress-activated MAPK cascade GO Logo
T cell receptor signaling pathway GO Logo
Toll-like receptor 10 signaling pathway GO Logo
Toll-like receptor 2 signaling pathway GO Logo
Toll-like receptor 3 signaling pathway GO Logo
Toll-like receptor 4 signaling pathway GO Logo
Toll-like receptor 5 signaling pathway GO Logo
Toll-like receptor 9 signaling pathway GO Logo
Toll-like receptor signaling pathway GO Logo
Toll-like receptor TLR1:TLR2 signaling pathway GO Logo
Toll-like receptor TLR6:TLR2 signaling pathway GO Logo
Transcription initiation from RNA polymerase II promoter GO Logo
Transcription, DNA-templated GO Logo
Transcription-coupled nucleotide-excision repair GO Logo
Transforming growth factor beta receptor signaling pathway GO Logo
Translesion synthesis GO Logo
Transmembrane transport GO Logo
TRIF-dependent toll-like receptor signaling pathway GO Logo
Tumor necrosis factor-mediated signaling pathway GO Logo
Viral life cycle GO Logo
Viral process GO Logo
Viral protein processing GO Logo
Viral translation GO Logo
Virion assembly GO Logo
Wnt signaling pathway GO Logo
Wnt signaling pathway, planar cell polarity pathway GO Logo

The reference OMIM entry for this protein is 191340

Ubiquitin c; ubc
Polyubiquitin

DESCRIPTION

Studies of ubiquitin cDNAs and genes show 2 unusual gene structural arrangements (Schlesinger and Bond, 1987). The first type of arrangement is the polyubiquitin gene, consisting of tandem repeats of a ubiquitin coding unit, with the number of repeats varying considerably even within species. Presumably posttranslational cleavage produces ubiquitin monomers from the primary translation product. The second structural type is the ubiquitin fusion gene, which encodes a single ubiquitin moiety fused to an unrelated tail protein. Three types of ubiquitin have been identified: A, B (191339), and C. The ubiquitin C (UBC) mRNA corresponds to a 9-coding-unit polyubiquitin gene.

MAPPING

During Northern blot analysis of ubiquitin mRNA, Baker and Board (1989) observed a UBC mRNA length polymorphism. They characterized this 'mRLP', showed that it correlated precisely with an HaeIII RFLP, and explained the origin of the polymorphism on the basis of unequal crossover events. Using a 5-prime flanking fragment to probe Southern blots of DNA obtained from somatic cell hybrid cell lines, Board et al. (1992) determined that the UBC gene is located on chromosome 12. In situ hybridization with the same probe refined the assignment to 12q24.3. ... More on the omim web site

Subscribe to this protein entry history

Jan. 22, 2020: Protein entry updated
Automatic update: Entry updated from uniprot information.

Feb. 2, 2018: Protein entry updated
Automatic update: Uniprot description updated

Dec. 19, 2017: Protein entry updated
Automatic update: Uniprot description updated

Nov. 23, 2017: Protein entry updated
Automatic update: Uniprot description updated

March 25, 2017: Additional information
No protein expression data in P. Mayeux work for UBC

Sept. 16, 2016: Protein entry updated
Automatic update: OMIM entry 191340 was added.