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Information on EC 2.3.2.33 - RCR-type E3 ubiquitin transferase and Organism(s) Mus musculus and UniProt Accession Q7TPH6

for references in articles please use BRENDA:EC2.3.2.33
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EC Tree
     2 Transferases
         2.3 Acyltransferases
             2.3.2 Aminoacyltransferases
                2.3.2.33 RCR-type E3 ubiquitin transferase
IUBMB Comments
RCR-type E3 ubiquitin transferases is a class of RING-type E3 ubiquitin transferase (see EC 2.3.2.27) that mediates ubiquitylation of acceptor proteins via an internal cysteine residue. The RING1 domain binds an EC 2.3.2.23, E2 ubiquitin-conjugating enzyme, and transfers the ubiquitin that is bound to it to an internal cysteine residue on a mediator loop of the RCR-type ligase. The ubiquitin may be transferred to a second internal cysteine before the transfer of the ubiquitin from the RCR-type ligase to the substrate.
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Mus musculus
UNIPROT: Q7TPH6
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Word Map
The taxonomic range for the selected organisms is: Mus musculus
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
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[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine
+
[acceptor protein]-L-threonine
=
[E2 ubiquitin-conjugating enzyme]-L-cysteine
+
[acceptor protein]-3-O-ubiquitinyl-L-threonine
Synonyms
rpm-1, mycbp2, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E3 ubiquitin-protein ligase
-
MYCBP2
-
-
-
-
PHR1
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine:acceptor protein ubiquitin transferase (isopeptide bond-forming; RCR-type)
RCR-type E3 ubiquitin transferases is a class of RING-type E3 ubiquitin transferase (see EC 2.3.2.27) that mediates ubiquitylation of acceptor proteins via an internal cysteine residue. The RING1 domain binds an EC 2.3.2.23, E2 ubiquitin-conjugating enzyme, and transfers the ubiquitin that is bound to it to an internal cysteine residue on a mediator loop of the RCR-type ligase. The ubiquitin may be transferred to a second internal cysteine before the transfer of the ubiquitin from the RCR-type ligase to the substrate.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
Phr1 is associated with the microtubule cytoskeleton within neurons and selectively localizes to axons
Manually annotated by BRENDA team
stimulation of neurons induces a GTPase-activating protein RanGAP1-dependent translocation of MYCBP2 to the nucleus
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
MYCB2_MOUSE
4749
0
521232
Swiss-Prot
Mitochondrion (Reliability: 5)
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
structures of both the first and second PHR domains, displaying a beta sandwich fold composed of 11 anti-parallel beta-strands
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
James, G.; Key, B.; Beverdam, A.
The E3 ubiquitin ligase Mycbp2 genetically interacts with Robo2 to modulate axon guidance in the mouse olfactory system
Brain Struct. Funct.
219
861-874
2014
Mus musculus (Q7TPH6), Mus musculus
Manually annotated by BRENDA team
Babetto, E.; Beirowski, B.; Russler, E.; Milbrandt, J.; DiAntonio, A.
The Phr1 ubiquitin ligase promotes injury-induced axon self-destruction
Cell Rep.
3
1422-1429
2013
Mus musculus (Q7TPH6)
Manually annotated by BRENDA team
Holland, S.; Scholich, K.
Regulation of neuronal functions by the E3-ubiquitinligase protein associated with MYC (MYCBP2)
Commun. Integr. Biol.
4
513-515
2011
Mus musculus (Q7TPH6)
Manually annotated by BRENDA team
Holland, S.; Coste, O.; Zhang, D.D.; Pierre, S.C.; Geisslinger, G.; Scholich, K.
The ubiquitin ligase MYCBP2 regulates transient receptor potential vanilloid receptor 1 (TRPV1) internalization through inhibition of p38 MAPK signaling
J. Biol. Chem.
286
3671-3680
2011
Mus musculus (Q7TPH6)
Manually annotated by BRENDA team
Doerr, A.; Pierre, S.; Zhang, D.D.; Henke, M.; Holland, S.; Scholich, K.
MYCBP2 Is a guanosine exchange factor for Ran rrotein and determines its localization in neurons of dorsal root ganglia
J. Biol. Chem.
290
25620-25635
2015
Mus musculus (Q7TPH6)
Manually annotated by BRENDA team
Sampathkumar, P.; Ozyurt, S.A.; Miller, S.A.; Bain, K.T.; Rutter, M.E.; Gheyi, T.; Abrams, B.; Wang, Y.; Atwell, S.; Luz, J.G.; Thompson, D.A.; Wasserman, S.R.; Emtage, J.S.; Park, E.C.; Rongo, C.; Jin, Y.; Klemke, R.L.; Sauder, J.M.; Burley, S.K.
Structures of PHR domains from Mus musculus Phr1 (Mycbp2) explain the loss-of-function mutation (Gly1092-->Glu) of the C. elegans ortholog RPM-1
J. Mol. Biol.
397
883-892
2010
Caenorhabditis elegans (Q17551), Caenorhabditis elegans, Mus musculus (Q7TPH6), Mus musculus
Manually annotated by BRENDA team
Lewcock, J.; Genoud, N.; Lettieri, K.; Pfaff, S.
The Ubiquitin ligase Phr1 regulates axon outgrowth through modulation of microtubule dynamics
Neuron
56
604-620
2007
Mus musculus (Q7TPH6)
Manually annotated by BRENDA team