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  • 11.0 [archived version]
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KCMF1 KCMF1 UBR4 UBR4 TRIM36 TRIM36 HECTD1 HECTD1 UBE2A UBE2A UBR2 UBR2 PJA2 PJA2 HERC2 HERC2 UBE3A UBE3A UBR1 UBR1 HUWE1 HUWE1
"UBR4" - E3 ubiquitin-protein ligase UBR4 in Homo sapiens
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Predicted Interactions
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textmining
co-expression
protein homology
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UBR4E3 ubiquitin-protein ligase UBR4; E3 ubiquitin-protein ligase which is a component of the N-end rule pathway. Recognizes and binds to proteins bearing specific N-terminal residues that are destabilizing according to the N-end rule, leading to their ubiquitination and subsequent degradation. Together with clathrin, forms meshwork structures involved in membrane morphogenesis and cytoskeletal organization. Regulates integrin-mediated signaling. May play a role in activation of FAK in response to cell-matrix interactions. Mediates ubiquitination of ACLY, leading to its subsequent degradat [...] (5183 aa)    
Predicted Functional Partners:
HECTD1
E3 ubiquitin-protein ligase HECTD1; E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Mediates ’Lys-63’-linked polyubiquitination of HSP90AA1 which leads to its intracellular localization and reduced secretion. Negatively regulating HSP90AA1 secretion in cranial mesenchyme cells may impair their emigration and may be essential for the correct development of the cranial neural folds and neural tube closure; Belongs to the UPL family. K-HECT subfamily (2610 aa)
     
 
  0.984
UBR2
E3 ubiquitin-protein ligase UBR2; E3 ubiquitin-protein ligase which is a component of the N-end rule pathway. Recognizes and binds to proteins bearing specific N-terminal residues that are destabilizing according to the N-end rule, leading to their ubiquitination and subsequent degradation. Plays a critical role in chromatin inactivation and chromosome-wide transcriptional silencing during meiosis via ubiquitination of histone H2A. Binds leucine and is a negative regulator of the leucine-mTOR signaling pathway, thereby controlling cell growth. Required for spermatogenesis, promotes, wi [...] (1755 aa)
     
 
  0.984
UBR1
E3 ubiquitin-protein ligase UBR1; E3 ubiquitin-protein ligase which is a component of the N-end rule pathway. Recognizes and binds to proteins bearing specific N-terminal residues that are destabilizing according to the N-end rule, leading to their ubiquitination and subsequent degradation. May be involved in pancreatic homeostasis. Binds leucine and is a negative regulator of the leucine-mTOR signaling pathway, thereby controlling cell growth; Belongs to the UBR1 family (1749 aa)
     
 
  0.981
KCMF1
E3 ubiquitin-protein ligase KCMF1; Has intrinsic E3 ubiquitin ligase activity and promotes ubiquitination; Belongs to the KCMF1 family (381 aa)
     
 
  0.952
HUWE1
E3 ubiquitin-protein ligase HUWE1; E3 ubiquitin-protein ligase which mediates ubiquitination and subsequent proteasomal degradation of target proteins. Regulates apoptosis by catalyzing the polyubiquitination and degradation of MCL1. Mediates monoubiquitination of DNA polymerase beta (POLB) at ’Lys-41’, ’Lys-61’ and ’Lys-81’, thereby playing a role in base-excision repair. Also ubiquitinates the p53/TP53 tumor suppressor and core histones including H1, H2A, H2B, H3 and H4. Binds to an upstream initiator-like sequence in the preprodynorphin gene. Regulates neural differentiation and pro [...] (4374 aa)
     
 
  0.951
HERC2
E3 ubiquitin-protein ligase HERC2; E3 ubiquitin-protein ligase that regulates ubiquitin- dependent retention of repair proteins on damaged chromosomes. Recruited to sites of DNA damage in response to ionizing radiation (IR) and facilitates the assembly of UBE2N and RNF8 promoting DNA damage-induced formation of ’Lys-63’-linked ubiquitin chains. Acts as a mediator of binding specificity between UBE2N and RNF8. Involved in the maintenance of RNF168 levels. E3 ubiquitin-protein ligase that promotes the ubiquitination and proteasomal degradation of XPA which influences the circadian oscill [...] (4834 aa)
     
  0.949
PJA2
E3 ubiquitin-protein ligase Praja-2; Has E2-dependent E3 ubiquitin-protein ligase activity. Responsible for ubiquitination of cAMP-dependent protein kinase type I and type II-alpha/beta regulatory subunits and for targeting them for proteasomal degradation. Essential for PKA- mediated long-term memory processes; Ring finger proteins (708 aa)
     
 
  0.947
UBE2A
Ubiquitin-conjugating enzyme E2 A; Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In association with the E3 enzyme BRE1 (RNF20 and/or RNF40), it plays a role in transcription regulation by catalyzing the monoubiquitination of histone H2B at ’Lys-120’ to form H2BK120ub1. H2BK120ub1 gives a specific tag for epigenetic transcriptional activation, elongation by RNA polymerase II, telomeric silencing, and is also a prerequisite for H3K4me and H3K79me formation. In vitro catalyzes ’Lys-11’, as well as ’Lys-48’-linked polyubiquitination. Requir [...] (152 aa)
     
  0.945
TRIM36
E3 ubiquitin-protein ligase TRIM36; E3 ubiquitin-protein ligase which mediates ubiquitination and subsequent proteasomal degradation of target proteins. Involved in chromosome segregation and cell cycle regulation. May play a role in the acrosome reaction and fertilization; Belongs to the TRIM/RBCC family (728 aa)
     
 
  0.944
UBE3A
Ubiquitin-protein ligase E3A; E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and transfers it to its substrates. Several substrates have been identified including the RAD23A and RAD23B, MCM7 (which is involved in DNA replication), annexin A1, the PML tumor suppressor, and the cell cycle regulator CDKN1B. Catalyzes the high-risk human papilloma virus E6-mediated ubiquitination of p53/TP53, contributing to the neoplastic progression of cells infected by these viruses. Additionally, may function as a cellular quality [...] (875 aa)
     
 
  0.944
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo sapiens, human, man
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