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Showing Protein E3 ubiquitin-protein ligase MYCBP2 (HMDBP14139)

IdentificationBiological propertiesGene propertiesProtein propertiesExternal linksReferencesXMLShow 1 metabolite
Identification
HMDB Protein ID HMDBP14139
Secondary Accession Numbers None
Name E3 ubiquitin-protein ligase MYCBP2
Synonyms
  1. Myc-binding protein 2
  2. Protein Esrom
Gene Name MYCBP2
Protein Type Unknown
Biological Properties
General Function Not Available
Specific Function Atypical E3 ubiquitin-protein ligase which specifically mediates ubiquitination of threonine and serine residues on target proteins, instead of ubiquitinating lysine residues (By similarity). Shows esterification activity towards both threonine and serine, with a preference for threonine, and acts via two essential catalytic cysteine residues that relay ubiquitin to its substrate via thioester intermediates (By similarity). Interacts with the E2 enzymes UBE2D1, UBE2D3, UBE2E1 and UBE2L3 (By similarity). Plays a key role in neural development, probably by mediating ubiquitination of threonine residues on target proteins (By similarity). Involved in different processes such as regulation of neurite outgrowth, synaptic growth, synaptogenesis and axon degeneration (By similarity). Required in the visual system for correct fasciculation, targeting and mapping of retinal axons (PubMed:15590740). Acts as a regulator of pteridine synthesis (PubMed:15617681). May play a role in the regulation of the circadian clock gene expression (By similarity).
Pathways
  • protein ubiquitination
Reactions Not Available
GO Classification
Biological Process
axon choice point recognition
axon extension involved in regeneration
central nervous system projection neuron axonogenesis
regulation of axon guidance
regulation of pteridine metabolic process
developmental pigmentation
habenula development
neuromuscular process
axon guidance
retinal ganglion cell axon guidance
circadian regulation of gene expression
Cellular Component
cytoskeleton
cytoplasm
nucleus
axon
Molecular Function
ubiquitin-protein ligase activity
metal ion binding
ubiquitin protein ligase activity
guanyl-nucleotide exchange factor activity
small GTPase binding
Cellular Location Not Available
Gene Properties
Chromosome Location Not Available
Locus Not Available
SNPs Not Available
Gene Sequence Not Available
Protein Properties
Number of Residues 4574
Molecular Weight 501843.035
Theoretical pI 6.928
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence Not Available
GenBank ID Protein Not Available
UniProtKB/Swiss-Prot ID F1RD40
UniProtKB/Swiss-Prot Entry Name MYCB2_DANRE
PDB IDs Not Available
GenBank Gene ID Not Available
GeneCard ID Not Available
GenAtlas ID Not Available
HGNC ID Not Available
References
General References
  1. Howe K, Clark MD, Torroja CF, Torrance J, Berthelot C, Muffato M, Collins JE, Humphray S, McLaren K, Matthews L, McLaren S, Sealy I, Caccamo M, Churcher C, Scott C, Barrett JC, Koch R, Rauch GJ, White S, Chow W, Kilian B, Quintais LT, Guerra-Assuncao JA, Zhou Y, Gu Y, Yen J, Vogel JH, Eyre T, Redmond S, Banerjee R, Chi J, Fu B, Langley E, Maguire SF, Laird GK, Lloyd D, Kenyon E, Donaldson S, Sehra H, Almeida-King J, Loveland J, Trevanion S, Jones M, Quail M, Willey D, Hunt A, Burton J, Sims S, McLay K, Plumb B, Davis J, Clee C, Oliver K, Clark R, Riddle C, Elliot D, Threadgold G, Harden G, Ware D, Begum S, Mortimore B, Kerry G, Heath P, Phillimore B, Tracey A, Corby N, Dunn M, Johnson C, Wood J, Clark S, Pelan S, Griffiths G, Smith M, Glithero R, Howden P, Barker N, Lloyd C, Stevens C, Harley J, Holt K, Panagiotidis G, Lovell J, Beasley H, Henderson C, Gordon D, Auger K, Wright D, Collins J, Raisen C, Dyer L, Leung K, Robertson L, Ambridge K, Leongamornlert D, McGuire S, Gilderthorp R, Griffiths C, Manthravadi D, Nichol S, Barker G, Whitehead S, Kay M, Brown J, Murnane C, Gray E, Humphries M, Sycamore N, Barker D, Saunders D, Wallis J, Babbage A, Hammond S, Mashreghi-Mohammadi M, Barr L, Martin S, Wray P, Ellington A, Matthews N, Ellwood M, Woodmansey R, Clark G, Cooper J, Tromans A, Grafham D, Skuce C, Pandian R, Andrews R, Harrison E, Kimberley A, Garnett J, Fosker N, Hall R, Garner P, Kelly D, Bird C, Palmer S, Gehring I, Berger A, Dooley CM, Ersan-Urun Z, Eser C, Geiger H, Geisler M, Karotki L, Kirn A, Konantz J, Konantz M, Oberlander M, Rudolph-Geiger S, Teucke M, Lanz C, Raddatz G, Osoegawa K, Zhu B, Rapp A, Widaa S, Langford C, Yang F, Schuster SC, Carter NP, Harrow J, Ning Z, Herrero J, Searle SM, Enright A, Geisler R, Plasterk RH, Lee C, Westerfield M, de Jong PJ, Zon LI, Postlethwait JH, Nusslein-Volhard C, Hubbard TJ, Roest Crollius H, Rogers J, Stemple DL: The zebrafish reference genome sequence and its relationship to the human genome. Nature. 2013 Apr 25;496(7446):498-503. doi: 10.1038/nature12111. Epub 2013 Apr 17. [PubMed:23594743 ]
  2. D'Souza J, Hendricks M, Le Guyader S, Subburaju S, Grunewald B, Scholich K, Jesuthasan S: Formation of the retinotectal projection requires Esrom, an ortholog of PAM (protein associated with Myc). Development. 2005 Jan;132(2):247-56. doi: 10.1242/dev.01578. Epub 2004 Dec 8. [PubMed:15590740 ]
  3. Wang H: Characterization of zebrafish Esrom (Myc-binding protein 2) RCC1-like domain splice variants. Mol Cell Biochem. 2010 Jun;339(1-2):191-9. doi: 10.1007/s11010-010-0385-x. Epub 2010 Feb 9. [PubMed:20143133 ]
  4. Le Guyader S, Maier J, Jesuthasan S: Esrom, an ortholog of PAM (protein associated with c-myc), regulates pteridine synthesis in the zebrafish. Dev Biol. 2005 Jan 15;277(2):378-86. doi: 10.1016/j.ydbio.2004.09.029. [PubMed:15617681 ]