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E3 ubiquitin-protein ligase MYCBP2 (EC 2.3.2.27) (Myc-binding protein 2) (Pam/highwire/rpm-1 protein) (Protein associated with Myc) (RING-type E3 ubiquitin transferase MYCBP2)

 MYCB2_MOUSE             Reviewed;        4749 AA.
Q7TPH6; E9PUJ6; Q6PCM8;
21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
20-JUN-2018, sequence version 3.
05-DEC-2018, entry version 146.
RecName: Full=E3 ubiquitin-protein ligase MYCBP2 {ECO:0000305};
EC=2.3.2.- {ECO:0000250|UniProtKB:O75592};
AltName: Full=Myc-binding protein 2 {ECO:0000305};
AltName: Full=Pam/highwire/rpm-1 protein {ECO:0000303|PubMed:14729956};
AltName: Full=Protein Magellan {ECO:0000303|PubMed:18031680};
AltName: Full=Protein associated with Myc {ECO:0000303|PubMed:14729956};
Name=Mycbp2 {ECO:0000312|MGI:MGI:2179432};
Synonyms=Pam {ECO:0000303|PubMed:14729956},
Phr1 {ECO:0000303|PubMed:14729956};
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 24-4749 (ISOFORM 1), FUNCTION, TISSUE
SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
STRAIN=C57BL/6J {ECO:0000312|EMBL:AAP88591.1};
TISSUE=Embryo {ECO:0000269|PubMed:14729956};
PubMed=14729956; DOI=10.1128/MCB.24.3.1096-1105.2004;
Burgess R.W., Peterson K.A., Johnson M.J., Roix J.J., Welsh I.C.,
O'Brien T.P.;
"Evidence for a conserved function in synapse formation reveals Phr1
as a candidate gene for respiratory failure in newborn mice.";
Mol. Cell. Biol. 24:1096-1105(2004).
[3]
PROTEIN SEQUENCE OF 2365-2390 AND 2904-2913, AND IDENTIFICATION BY
MASS SPECTROMETRY.
STRAIN=C57BL/6J; TISSUE=Brain;
Lubec G., Kang S.U.;
Submitted (APR-2007) to UniProtKB.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3288-4749 (ISOFORM 2).
STRAIN=C57BL/6J {ECO:0000312|EMBL:AAH59257.1};
TISSUE=Brain {ECO:0000312|EMBL:AAH59257.1};
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
INTERACTION WITH CPNE1 AND CPNE4.
PubMed=12522145; DOI=10.1074/jbc.M212632200;
Tomsig J.L., Snyder S.L., Creutz C.E.;
"Identification of targets for calcium signaling through the copine
family of proteins. Characterization of a coiled-coil copine-binding
motif.";
J. Biol. Chem. 278:10048-10054(2003).
[6]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=17901218; DOI=10.1101/gad.1592107;
Bloom A.J., Miller B.R., Sanes J.R., DiAntonio A.;
"The requirement for Phr1 in CNS axon tract formation reveals the
corticostriatal boundary as a choice point for cortical axons.";
Genes Dev. 21:2593-2606(2007).
[7]
FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL
STAGE, AND DISRUPTION PHENOTYPE.
PubMed=18031680; DOI=10.1016/j.neuron.2007.09.009;
Lewcock J.W., Genoud N., Lettieri K., Pfaff S.L.;
"The ubiquitin ligase Phr1 regulates axon outgrowth through modulation
of microtubule dynamics.";
Neuron 56:604-620(2007).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain cortex;
PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
"Qualitative and quantitative analyses of protein phosphorylation in
naive and stimulated mouse synaptosomal preparations.";
Mol. Cell. Proteomics 6:283-293(2007).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3550, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[10]
INTERACTION WITH FBXO45.
PubMed=19398581; DOI=10.1128/MCB.00364-09;
Saiga T., Fukuda T., Matsumoto M., Tada H., Okano H.J., Okano H.,
Nakayama K.I.;
"Fbxo45 forms a novel ubiquitin ligase complex and is required for
neuronal development.";
Mol. Cell. Biol. 29:3529-3543(2009).
[11]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=19371781; DOI=10.1016/j.mcn.2009.04.001;
Culican S.M., Bloom A.J., Weiner J.A., DiAntonio A.;
"Phr1 regulates retinogeniculate targeting independent of activity and
ephrin-A signalling.";
Mol. Cell. Neurosci. 41:304-312(2009).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-178; SER-181; SER-183;
SER-2941; SER-2992 AND THR-3992, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[13]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=21098484; DOI=10.1074/jbc.M110.154765;
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).
[14]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=21324225; DOI=10.1017/S0952523810000386;
Vo B.Q., Bloom A.J., Culican S.M.;
"Phr1 is required for proper retinocollicular targeting of nasal-
dorsal retinal ganglion cells.";
Vis. Neurosci. 28:175-181(2011).
[15]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=23665224; DOI=10.1016/j.celrep.2013.04.013;
Babetto E., Beirowski B., Russler E.V., Milbrandt J., DiAntonio A.;
"The Phr1 ubiquitin ligase promotes injury-induced axon self-
destruction.";
Cell Rep. 3:1422-1429(2013).
[16]
FUNCTION.
PubMed=23525682; DOI=10.1007/s00429-013-0540-8;
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).
[17]
FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH RAN AND RANGAP1, AND
MUTAGENESIS OF 950-HIS-HIS-951.
PubMed=26304119; DOI=10.1074/jbc.M115.646901;
Doerr A., Pierre S., Zhang D.D., Henke M., Holland S., Scholich K.;
"MYCBP2 is a guanosine exchange factor for Ran protein and determines
its localization in neurons of dorsal root ganglia.";
J. Biol. Chem. 290:25620-25635(2015).
[18]
X-RAY CRYSTALLOGRAPHY (1.32 ANGSTROMS) OF 1229-1390, X-RAY
CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 1723-1883, DOMAIN PHR, AND
DISULFIDE BOND.
PubMed=20156452; DOI=10.1016/j.jmb.2010.02.017;
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).
-!- 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 (PubMed:14729956, PubMed:17901218,
PubMed:18031680). Required for the formation of major central
nervous system axon tracts (PubMed:17901218, PubMed:18031680).
Required for proper axon growth by regulating axon navigation and
axon branching: acts by regulating the subcellular location and
stability of MAP3K12/DLK (PubMed:18031680). Required for proper
localization of retinogeniculate projections but not for eye-
specific segregation (PubMed:19371781, PubMed:21324225). Regulates
axon guidance in the olfactory system (PubMed:23525682). Involved
in Wallerian axon degeneration, an evolutionarily conserved
process that drives the loss of damaged axons: acts by promoting
destabilization of NMNAT2, probably via ubiquitination of NMNAT2
(PubMed:23665224). Catalyzes ubiquitination of threonine and/or
serine residues on NMNAT2, consequences of threonine and/or serine
ubiquitination are however unknown (By similarity). Regulates the
internalization of TRPV1 in peripheral sensory neurons
(PubMed:21098484). May mediate ubiquitination and subsequent
proteasomal degradation of TSC2/tuberin (By similarity).
Independently of the E3 ubiquitin-protein ligase activity, also
acts as a guanosine exchange factor (GEF) for RAN in neurons of
dorsal root ganglia (PubMed:26304119). May function as a
facilitator or regulator of transcriptional activation by MYC (By
similarity). {ECO:0000250|UniProtKB:O75592,
ECO:0000269|PubMed:14729956, ECO:0000269|PubMed:17901218,
ECO:0000269|PubMed:18031680, ECO:0000269|PubMed:19371781,
ECO:0000269|PubMed:21098484, ECO:0000269|PubMed:21324225,
ECO:0000269|PubMed:23525682, ECO:0000269|PubMed:23665224,
ECO:0000269|PubMed:26304119}.
-!- PATHWAY: Protein modification; protein ubiquitination.
{ECO:0000250|UniProtKB:O75592}.
-!- SUBUNIT: Interacts with MYC (By similarity). Interacts with TSC2
(tuberin) when TSC2 is in complex with TSC1 (hamartin) (By
similarity). Interacts with FBXO45 (PubMed:19398581). Interacts
with RAE1 (By similarity). Interacts with CPNE1 (via VWFA domain)
and CPNE4 (via VWFA domain) (PubMed:12522145). Interacts with
(sumoylated) RANGAP1; interaction with sumoylated RANGAP1 inhibits
E3 ubiquitin-protein ligase activity and promotes MYCBP2
translocation to the nucleus (PubMed:26304119). Interacts with RAN
(PubMed:26304119). {ECO:0000250|UniProtKB:O75592,
ECO:0000269|PubMed:12522145, ECO:0000269|PubMed:19398581,
ECO:0000269|PubMed:26304119}.
-!- INTERACTION:
Q63633:Slc12a5 (xeno); NbExp=4; IntAct=EBI-1811542, EBI-1811510;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:26304119}. Cell
projection, axon {ECO:0000269|PubMed:18031680}. Cytoplasm,
cytoskeleton {ECO:0000269|PubMed:18031680}. Note=Localizes to axon
shafts and associates with microtubule cytoskeleton
(PubMed:18031680). Translocates to the nucleus following
interaction with sumoylated RANGAP1 (PubMed:26304119).
{ECO:0000269|PubMed:18031680, ECO:0000269|PubMed:26304119}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1 {ECO:0000303|PubMed:14729956};
IsoId=Q7TPH6-1; Sequence=Displayed;
Name=2 {ECO:0000305};
IsoId=Q7TPH6-2; Sequence=VSP_014184;
-!- TISSUE SPECIFICITY: Expression is mostly restricted to the nervous
system, including expression in motor and sensory axons
(PubMed:18031680). During postnatal development, expression is
particularly strong in the cerebellum, hippocampus and retina
(PubMed:14729956). Lower levels of expression are observed
throughout the cerebral cortex (PubMed:14729956).
{ECO:0000269|PubMed:14729956, ECO:0000269|PubMed:18031680}.
-!- DEVELOPMENTAL STAGE: Dynamically expressed in embryonic nervous
system from E8.5 through E18.5 (PubMed:14729956, PubMed:18031680).
At E10.5, shortly after the birth of the first motor neurons,
highly expressed in the developing motor columns, dorsal root
ganglion and newly formed neurons within the dorsal neural tube
(PubMed:18031680). As embryos develop to E11.5, expression levels
increase in the dorsal root ganglion and expression in the spinal
cord expandes as the number of postmitotic neurons increase
(PubMed:18031680). By E12.5 expression is widespread within the
spinal cord (PubMed:18031680). {ECO:0000269|PubMed:14729956,
ECO:0000269|PubMed:18031680}.
-!- DOMAIN: The PHR domains are compact beta-sandwich folds composed
of 11 antiparallel strands and decorated with conserved apical
loops. They are likely to play a structural role and mediate
interactions with substrates or partners.
{ECO:0000269|PubMed:20156452}.
-!- DOMAIN: The tandem cysteine domain region confers threonine
specificity and contains the two essential catalytic cysteine
residues that relay ubiquitin. It binds four zinc ions in a
C5HC7HC2 configuration. {ECO:0000250|UniProtKB:O75592}.
-!- PTM: Autoubiquitinated. {ECO:0000250|UniProtKB:O75592}.
-!- DISRUPTION PHENOTYPE: Lethality caused by defects in neuromuscular
development (PubMed:17901218). Mice die at birth without taking a
breath: phrenic nerves are markedly narrower and contain fewer
axons than controls (PubMed:17901218). Mice display incomplete
innervation of the diaphragm by the phrenic nerve
(PubMed:14729956, PubMed:17901218). Intercostal muscles are
completely innervated, but show dysmorphic nerve terminals
(PubMed:14729956, PubMed:17901218). Sensory neuron terminals in
the diaphragm are abnormal and neuromuscular junctions show
excessive sprouting of nerve terminals, consistent with inadequate
presynaptic stimulation of the muscle (PubMed:14729956). Embryos
display motor axon misprojections and stalling: motor axons are
error-prone and wander inefficiently at choice points within
embryos (PubMed:18031680). Conditional knockout mice lacking
Mycbp2 in the retina, exhibit no gross retinal developmental
defects; mutants retain normal retinal lamination, monocular
segregation and spontaneous retinal wave activity, but mutant
retinal ganglion cells exhibit ipsilateral projection to an
improper region of the dorsal lateral geniculate nucleus (dLGN)
(PubMed:19371781, PubMed:21324225). Conditional knockout mice
lacking Mycbp2 in peripheral sensory neurons display prolonged
thermal hyperalgesia: defects are caused by constitutive
activation of MAP kinase p38 (Mapk11, Mapk12, Mapk13 and/or
Mapk14), leading to inhibit internalization of Trpv1
(PubMed:21098484). {ECO:0000269|PubMed:14729956,
ECO:0000269|PubMed:17901218, ECO:0000269|PubMed:18031680,
ECO:0000269|PubMed:19371781, ECO:0000269|PubMed:21098484,
ECO:0000269|PubMed:21324225}.
-!- SIMILARITY: Belongs to the RING-Cys relay (RCR) family.
{ECO:0000305}.
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EMBL; AC114410; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC114585; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CT025554; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AY325887; AAP88591.1; -; mRNA.
EMBL; BC059257; AAH59257.1; -; mRNA.
CCDS; CCDS49559.1; -. [Q7TPH6-2]
RefSeq; NP_997098.2; NM_207215.2. [Q7TPH6-2]
UniGene; Mm.6478; -.
PDB; 3GBW; X-ray; 1.32 A; A=1229-1390.
PDB; 3HWJ; X-ray; 2.25 A; A/B=1723-1883.
PDBsum; 3GBW; -.
PDBsum; 3HWJ; -.
ProteinModelPortal; Q7TPH6; -.
SMR; Q7TPH6; -.
BioGrid; 222897; 146.
IntAct; Q7TPH6; 141.
STRING; 10090.ENSMUSP00000124710; -.
iPTMnet; Q7TPH6; -.
PhosphoSitePlus; Q7TPH6; -.
EPD; Q7TPH6; -.
PaxDb; Q7TPH6; -.
PRIDE; Q7TPH6; -.
DNASU; 105689; -.
Ensembl; ENSMUST00000159855; ENSMUSP00000124710; ENSMUSG00000033004. [Q7TPH6-2]
GeneID; 105689; -.
KEGG; mmu:105689; -.
CTD; 23077; -.
MGI; MGI:2179432; Mycbp2.
eggNOG; KOG1428; Eukaryota.
eggNOG; ENOG410XP1T; LUCA.
GeneTree; ENSGT00940000155756; -.
HOGENOM; HOG000112908; -.
HOVERGEN; HBG053153; -.
InParanoid; Q7TPH6; -.
KO; K10693; -.
PhylomeDB; Q7TPH6; -.
TreeFam; TF313151; -.
UniPathway; UPA00143; -.
ChiTaRS; Mycbp2; mouse.
EvolutionaryTrace; Q7TPH6; -.
PRO; PR:Q7TPH6; -.
Proteomes; UP000000589; Chromosome 14.
Bgee; ENSMUSG00000033004; Expressed in 306 organ(s), highest expression level in secondary oocyte.
CleanEx; MM_MYCBP2; -.
CleanEx; MM_PAM; -.
GO; GO:0030424; C:axon; IDA:MGI.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
GO; GO:0015630; C:microtubule cytoskeleton; IDA:MGI.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; ISS:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IPI:MGI.
GO; GO:0008536; F:Ran GTPase binding; ISS:UniProtKB.
GO; GO:0061630; F:ubiquitin protein ligase activity; ISS:UniProtKB.
GO; GO:0008270; F:zinc ion binding; ISO:MGI.
GO; GO:0021785; P:branchiomotor neuron axon guidance; IMP:MGI.
GO; GO:0048667; P:cell morphogenesis involved in neuron differentiation; IMP:MGI.
GO; GO:0021952; P:central nervous system projection neuron axonogenesis; IMP:UniProtKB.
GO; GO:0008045; P:motor neuron axon guidance; IMP:MGI.
GO; GO:0042177; P:negative regulation of protein catabolic process; IDA:MGI.
GO; GO:0050905; P:neuromuscular process; IMP:UniProtKB.
GO; GO:0016567; P:protein ubiquitination; ISS:UniProtKB.
GO; GO:1902667; P:regulation of axon guidance; IMP:UniProtKB.
GO; GO:0051493; P:regulation of cytoskeleton organization; IMP:MGI.
GO; GO:0032880; P:regulation of protein localization; IMP:MGI.
Gene3D; 2.130.10.30; -; 2.
Gene3D; 2.60.120.260; -; 1.
Gene3D; 2.60.120.820; -; 2.
Gene3D; 3.30.40.10; -; 1.
InterPro; IPR004939; APC_su10/DOC_dom.
InterPro; IPR017868; Filamin/ABP280_repeat-like.
InterPro; IPR008979; Galactose-bd-like_sf.
InterPro; IPR014756; Ig_E-set.
InterPro; IPR012983; PHR.
InterPro; IPR038648; PHR_sf.
InterPro; IPR009091; RCC1/BLIP-II.
InterPro; IPR000408; Reg_chr_condens.
InterPro; IPR003646; SH3-like_bac-type.
InterPro; IPR001841; Znf_RING.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
Pfam; PF03256; ANAPC10; 1.
Pfam; PF00630; Filamin; 1.
Pfam; PF08005; PHR; 2.
Pfam; PF00415; RCC1; 1.
Pfam; PF08239; SH3_3; 1.
Pfam; PF13639; zf-RING_2; 1.
PRINTS; PR00633; RCCNDNSATION.
SMART; SM01337; APC10; 1.
SMART; SM00184; RING; 1.
SUPFAM; SSF49785; SSF49785; 1.
SUPFAM; SSF50985; SSF50985; 1.
SUPFAM; SSF81296; SSF81296; 1.
PROSITE; PS51284; DOC; 1.
PROSITE; PS50194; FILAMIN_REPEAT; 1.
PROSITE; PS00626; RCC1_2; 1.
PROSITE; PS50012; RCC1_3; 3.
PROSITE; PS50089; ZF_RING_2; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell projection;
Complete proteome; Cytoplasm; Cytoskeleton; Direct protein sequencing;
Disulfide bond; Guanine-nucleotide releasing factor; Metal-binding;
Nucleus; Phosphoprotein; Reference proteome; Repeat; Transferase;
Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger.
CHAIN 1 4749 E3 ubiquitin-protein ligase MYCBP2.
/FTId=PRO_0000055964.
REPEAT 600 655 RCC1 1. {ECO:0000255}.
REPEAT 699 755 RCC1 2. {ECO:0000255}.
REPEAT 907 957 RCC1 3. {ECO:0000255}.
REPEAT 958 1009 RCC1 4. {ECO:0000255}.
REPEAT 1011 1066 RCC1 5. {ECO:0000255}.
REPEAT 2331 2438 Filamin. {ECO:0000255}.
DOMAIN 3789 3967 DOC. {ECO:0000255|PROSITE-
ProRule:PRU00614}.
ZN_FING 4499 4550 RING-type; atypical.
{ECO:0000255|PROSITE-ProRule:PRU00175}.
ZN_FING 4653 4703 B box-type.
REGION 1235 1386 PHR domain 1.
REGION 1723 1881 PHR domain 2.
REGION 2018 2544 RAE1 binding.
{ECO:0000250|UniProtKB:O75592}.
REGION 4610 4747 Tandem cysteine domain.
{ECO:0000250|UniProtKB:O75592}.
COMPBIAS 103 126 Lys-rich. {ECO:0000255}.
COMPBIAS 766 814 Cys-rich. {ECO:0000255}.
COMPBIAS 2792 2916 Ser-rich. {ECO:0000255}.
COMPBIAS 2885 2993 Pro-rich. {ECO:0000255}.
COMPBIAS 3266 3286 Lys-rich. {ECO:0000255}.
COMPBIAS 3334 3365 Gly-rich. {ECO:0000255}.
ACT_SITE 4629 4629 {ECO:0000250|UniProtKB:O75592}.
ACT_SITE 4681 4681 {ECO:0000250|UniProtKB:O75592}.
METAL 4499 4499 Zinc 1. {ECO:0000250|UniProtKB:O75592}.
METAL 4502 4502 Zinc 1. {ECO:0000250|UniProtKB:O75592}.
METAL 4517 4517 Zinc 2. {ECO:0000250|UniProtKB:O75592}.
METAL 4519 4519 Zinc 2. {ECO:0000250|UniProtKB:O75592}.
METAL 4522 4522 Zinc 1. {ECO:0000250|UniProtKB:O75592}.
METAL 4525 4525 Zinc 1. {ECO:0000250|UniProtKB:O75592}.
METAL 4546 4546 Zinc 2. {ECO:0000250|UniProtKB:O75592}.
METAL 4549 4549 Zinc 2. {ECO:0000250|UniProtKB:O75592}.
METAL 4615 4615 Zinc 3. {ECO:0000250|UniProtKB:O75592}.
METAL 4618 4618 Zinc 3. {ECO:0000250|UniProtKB:O75592}.
METAL 4646 4646 Zinc 3. {ECO:0000250|UniProtKB:O75592}.
METAL 4649 4649 Zinc 3. {ECO:0000250|UniProtKB:O75592}.
METAL 4658 4658 Zinc 4. {ECO:0000250|UniProtKB:O75592}.
METAL 4661 4661 Zinc 4. {ECO:0000250|UniProtKB:O75592}.
METAL 4670 4670 Zinc 5. {ECO:0000250|UniProtKB:O75592}.
METAL 4673 4673 Zinc 5. {ECO:0000250|UniProtKB:O75592}.
METAL 4674 4674 Zinc 6. {ECO:0000250|UniProtKB:O75592}.
METAL 4688 4688 Zinc 5. {ECO:0000250|UniProtKB:O75592}.
METAL 4691 4691 Zinc 5. {ECO:0000250|UniProtKB:O75592}.
METAL 4709 4709 Zinc 6. {ECO:0000250|UniProtKB:O75592}.
METAL 4723 4723 Zinc 6. {ECO:0000250|UniProtKB:O75592}.
METAL 4729 4729 Zinc 6. {ECO:0000250|UniProtKB:O75592}.
METAL 4740 4740 Zinc 4. {ECO:0000250|UniProtKB:O75592}.
METAL 4743 4743 Zinc 4. {ECO:0000250|UniProtKB:O75592}.
SITE 4682 4682 Important for catalysis.
{ECO:0000250|UniProtKB:O75592}.
SITE 4687 4687 Important for catalysis.
{ECO:0000250|UniProtKB:O75592}.
SITE 4695 4695 Important for catalysis.
{ECO:0000250|UniProtKB:O75592}.
MOD_RES 127 127 Phosphoserine.
{ECO:0000250|UniProtKB:O75592}.
MOD_RES 178 178 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 181 181 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 183 183 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1621 1621 Phosphoserine.
{ECO:0000250|UniProtKB:O75592}.
MOD_RES 2841 2841 Phosphoserine.
{ECO:0000250|UniProtKB:O75592}.
MOD_RES 2859 2859 Phosphoserine.
{ECO:0000250|UniProtKB:O75592}.
MOD_RES 2861 2861 Phosphoserine.
{ECO:0000250|UniProtKB:O75592}.
MOD_RES 2905 2905 Phosphoserine.
{ECO:0000250|UniProtKB:O75592}.
MOD_RES 2911 2911 Phosphoserine.
{ECO:0000250|UniProtKB:O75592}.
MOD_RES 2941 2941 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 2943 2943 Phosphoserine.
{ECO:0000250|UniProtKB:O75592}.
MOD_RES 2992 2992 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 3057 3057 Phosphoserine.
{ECO:0000250|UniProtKB:O75592}.
MOD_RES 3162 3162 Phosphoserine.
{ECO:0000250|UniProtKB:O75592}.
MOD_RES 3550 3550 Phosphoserine.
{ECO:0000244|PubMed:17242355}.
MOD_RES 3577 3577 Phosphoserine.
{ECO:0000250|UniProtKB:O75592}.
MOD_RES 3992 3992 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 4002 4002 Phosphoserine.
{ECO:0000250|UniProtKB:O75592}.
MOD_RES 4003 4003 Phosphoserine.
{ECO:0000250|UniProtKB:O75592}.
DISULFID 1745 1860 {ECO:0000305|PubMed:20156452}.
VAR_SEQ 4010 4012 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_014184.
MUTAGEN 950 951 HH->AA: Abolished guanosine exchange
factor (GEF) activity for Ran.
{ECO:0000269|PubMed:26304119}.
CONFLICT 860 860 E -> K (in Ref. 2; AAP88591).
CONFLICT 999 999 G -> C (in Ref. 2; AAP88591).
CONFLICT 1831 1831 R -> S (in Ref. 2; AAP88591).
CONFLICT 1987 1987 P -> S (in Ref. 2; AAP88591).
CONFLICT 3685 3685 E -> G (in Ref. 2; AAP88591).
CONFLICT 4636 4636 G -> E (in Ref. 2; AAP88591).
STRAND 1232 1235 {ECO:0000244|PDB:3GBW}.
STRAND 1237 1240 {ECO:0000244|PDB:3GBW}.
STRAND 1252 1260 {ECO:0000244|PDB:3GBW}.
STRAND 1262 1270 {ECO:0000244|PDB:3GBW}.
STRAND 1276 1286 {ECO:0000244|PDB:3GBW}.
TURN 1287 1291 {ECO:0000244|PDB:3GBW}.
STRAND 1297 1301 {ECO:0000244|PDB:3GBW}.
STRAND 1305 1307 {ECO:0000244|PDB:3GBW}.
STRAND 1314 1325 {ECO:0000244|PDB:3GBW}.
STRAND 1330 1340 {ECO:0000244|PDB:3GBW}.
STRAND 1345 1348 {ECO:0000244|PDB:3GBW}.
STRAND 1350 1353 {ECO:0000244|PDB:3GBW}.
STRAND 1359 1364 {ECO:0000244|PDB:3GBW}.
STRAND 1373 1378 {ECO:0000244|PDB:3GBW}.
STRAND 1381 1385 {ECO:0000244|PDB:3GBW}.
STRAND 1724 1728 {ECO:0000244|PDB:3HWJ}.
STRAND 1730 1732 {ECO:0000244|PDB:3HWJ}.
HELIX 1737 1739 {ECO:0000244|PDB:3HWJ}.
STRAND 1742 1751 {ECO:0000244|PDB:3HWJ}.
STRAND 1753 1761 {ECO:0000244|PDB:3HWJ}.
STRAND 1767 1775 {ECO:0000244|PDB:3HWJ}.
STRAND 1791 1800 {ECO:0000244|PDB:3HWJ}.
STRAND 1808 1819 {ECO:0000244|PDB:3HWJ}.
STRAND 1826 1835 {ECO:0000244|PDB:3HWJ}.
STRAND 1840 1843 {ECO:0000244|PDB:3HWJ}.
STRAND 1845 1848 {ECO:0000244|PDB:3HWJ}.
STRAND 1854 1858 {ECO:0000244|PDB:3HWJ}.
STRAND 1869 1873 {ECO:0000244|PDB:3HWJ}.
STRAND 1876 1881 {ECO:0000244|PDB:3HWJ}.
SEQUENCE 4749 AA; 521232 MW; D225D8DCA55961E7 CRC64;
MMMCAATASP AAASSGPGGD GFFAAATISS SPAPGALFMP VPDGSVAAAG LGLGLPTTDS
RGHYQLLLSG RALADRYRRI YTTALSDRDQ AGSSTGHPAS RNKKILNKKK LKRKQKSKSK
VKTRSKSENV ENTVIIPDIK LHSNPSAFNI YCNVRHCVLE WQKKETSLAA ASKNSVQSGE
SDSDEEEESR EPPIKLPKII EVGLCEVFEL IKETRFSHPS LCLRSLQALL NVLQGQQPEG
LQSEPPEVLE SLFQLLLEIT VRSTGMNDST GQSLTALSCA CLFSLVASWG ETGRTLQAIS
AILTNNGSHA CQTIQVPTIL NSLQRSVQAV LVGKIQVQDW FSNGIKKAAL MHKWPLKEVS
VDEDDQCLLQ NDGFFLYLLC KDGLYKIGSG YSGTVRGHIY NSTSRIRNRK EKKSWLGYAQ
GYLLYRDLNN HSMTAIRISP ETLEQDGTVL LPDCHTEGQN ILFTDGEYIN QIAASRDDGF
VVRIFATSTE PVLQQELQLK LARKCLHACG ISLFDLEKDL HIISTGFDEE SAILGAGREF
ALMKTANGKI YYTGKYQSLG IKQGGPSAGK WVELPITKSP KIVHFSVGHD GSHALLVAED
GSVFFTGSAS KGEDGESTKS RRQSKPYKPK KIIKMEGKIV VYTACNNGSS SVISKDGELY
MFGKDAIYSD SSSLVSDLKG HFVTQVAMGK AHTCVLMKNG EVWTFGVNNK GQCGRDTGAM
NQGGKGFGVE NMATAMDEDL EEELDEKDEK SMMCPPGMHK WKLEQCMVCT VCGDCTGYGA
SCVSSGRPDR VPGGICGCGS GESGCAVCGC CKACARELDG QEARQRGILD AVKEMIPLDL
LLAVPVPGVN IEEHLQLRQE EKRQRVIRRH RLEDGRGPLV FAGPIFMNHR EQALARLRSH
PAQLKHKRDK HKDGSGDRGE KDASKITTYP PGSVRFDCEL RAVQVSCGFH HSVVLMENGD
VYTFGYGQHG QLGHGDVNSR GCPTLVQALP GPSTQVTAGS NHTAVLLMDG QVFTFGSFSK
GQLGRPILDI PYWNAKPAPM PNIGSKYGRK ATWIGASGDQ TFLRIDEALI NSHVLATSEI
FASKHIIGLV PASISEPPPF KCLLINKVDG SCKTFNDSEQ EDLQGFGVCL DPVYDVLWRF
RPSTRELWCY NAVVADARLP SATDMQSRCS ILSPELALPT GSRALTTRSH AALHILGCLD
TLAAMQDLKM GIASTEEETQ AVMKVYSKED YSVVNRFESH GGGWGYSAHS VEAIRFSADT
DILLGGLGLF GGRGEYTAKI KLFELGPDGG DHETDGDLLA ETDVLAYDCA AREKYAMMFD
EPVLLQAGWW YVAWARVSGP SSDCGSHGQA SITTDDGVIF QFKSSKKSNN GTDVNAGQIP
QLLYRLPTSD GSTSKGKQQT SEPVHILKRS FARTVSVECF ESLLSILHWS WTTLVLGVEE
LRGLKGFQFT ATLLDLERLR FVGTCCLRLL RVYTCEIYPV SATGKAVVEE TSKLAECIGK
TRTLLRKILS EGVDHCMVKL DNDPQGYLSQ PLRLLEAVLQ ECHNTFTACF HSFYPTPALQ
WACLCDLLNC LDQEANFKTS SSRLLAAVMS ALCHTSVKLT SLFPIAYDGE VLLRSIVKQV
STENDSTLVH RFPLLVGHME KLSQSEENIS GMTSFREVLE KMLVIVVLPV RNSLRRESEL
FSSHLVSNTC GLLASIVSEL TASALGSEVD GLNSLHSVKA SANRFTKTSQ GRSWNTGNGS
PDAICFAVDK PGIVVVGFAV YGGGGIHEYE LEVLVDDSEH AGDSTHSHRW TSLELVKGTY
TTDDSPSDIA EIRLDKVVPL KENVKYAVRL RNYGSRTANG DGGMTTVQCP DGVTFTFSTC
SLSSNGTNQT RGQIPQILYY RSEFDGDLQS QLLSKANEED KNCSRALSVV STVVRAAKDL
LHRALAVDAD DIPELLSSSS LFSMLLPLII AYIGPVAAAI PKVAVEVFGL VQQLLPSVAI
LNQKYAPPAF NPNQSTDSTT GNQPEQGLSA CTTSNHYAVI ESEHPYKPAC VMHYKVTFPE
CVRWMTIEFD PQCGTAQSED VIRLLIPVRT IQNSGYGAKL TSVHENLNSW VELKKYSGSS
GWPTMVLVLP GNEALFSLET ASDYVKDDKA SFYGFKCFAI GYEFSPGPDE GVIQLEKELA
NLGGVCAAAL MKKDLALPVG NELEEDLEIL EEAALQVCKT HSGILGKGLA LSHSPTILEA
LEGNLPLQIQ SNEQSFLDDF IACVPGSSGG RLARWLQPDS YADPQKTSLI LNKDDIRCGW
PTTITVQTKD QYGDVVHVPN MKVEVKAVPV SQKKTSLQQD QGKKCQRIPG SPSAAASSAD
MTFGGLASPK LDVSYEPMIV KEARYIAITM MKVYENYSFE ELRFASPTPK RPSENMLIRV
NNDGTYCANW TPGAIGLYTV HVTIDGIEID AGLEVKVKDP PKGMIPPGTQ LVKPKADPQP
NKIRKFVAKD SAGLRIRSHP SLQSEQIGIV RVNGTITFID EIHNDDGVWL RLNEETIKKY
VPNMNGYTEA WCLSFNQHLG KSLLVPVDNI FNASQGVRDL DVFSWTSKAF FPQEPKTNTD
DFFKDMNSCG PQEATMQERD HPFLRGGPGM YKVVKTGPSG HNIRSCPNLR GIPIGMLVLG
NKVKAVGEVT NSEGAWVQLD KNSMVEFCES DEGEAWSLAR DRGGNQYLRH EDEQVLLDQN
SQPPPPSPFS VQAFNKGASC SAQGFDYGLG NNKGDQLSAI LNSIQSRPNL PAPSIFDQAA
KPPSSLVHSP FVFGQPLSFQ QRQLQSDRGT ISTSSRPVST SGKSELPSKH SRSVKPDGHV
SRTPADQKKP RGTEGLSASE SLMLKSDAAK LRSDSHSRSL SPNHNTLQTL KSDGRTSSGF
RAESPGPGSR SSSPKPKPLP TPRSSPSGAS SPRSSSPQDK NLPQKSTAPA KTKLDPPRER
SKSDSYTLDP DTLRKKKMPL TEPLRGRSTS PKPKPVPKDP KDSPGSENRA PSPHVVQENL
HSEVVEVCTS STLKTNGVTD STCDDSGDLK SVDEGSNKVH FSIGKAPLKD EQEMRASPKI
SRKCANRHTR PKKEKSNFLF KGDGTKSLEP AKQAMSPSVA ECARAVFASF LWHEGIVHDA
MACSSFLKFN PDLSKEHAPI RSSLNSQPPT EEKEIKLKNR HSLEISSALN MFNIAPHGPD
ISKMGSINKN KVLSMLKEPP LHEKCEDGKS EATFEMSMHH TMKSKSPLPL TLQHLVAFWE
DISLATIKAA SQNMIFPSPG SCAVLKKKEC EKENKKTKKE KKKKEKTEIR PRGNLFGEMA
QLAVGGPEKD TICELCGESH PYPVTYHMRQ AHPGCGRYAG GQGYNSIGHF CGGWAGNCGD
GGMGGSTWYL VCDRCREKYL REKQAAAREK VKQSRRKPMQ VKTPRALPTM EAHQVIKANA
LFLLSLSSAA EPSILCYHPA KPFQSQLPIV KEGVSEDLPV KMPCLYLQTL ARHHHENFVG
YQDDNLFQDE MRYLRSTSVP APYISVTPDA SPNVFEEPES NMKSMPPSLE TSPITDTDLA
KRTVFQRSYS VVASEYDKQH SILPARVKAI PRRRVNSGDT VGSSLLRHPS PELSRLISAH
SSLSKGERNF QWPVLAFVIQ HHDLEGLEIA MKQALRKSAC RVFAMEAFNW LLCNVIQTTS
LHDILWHFVA ALTPSPVEAE EDEDEDNKSN KENAEQEKDT RVCEHPLSDI VIAGEAAHPL
PHTFHRLLQT ISDLMMSLPS GSSLQQMALR CWSLKFKQSD HQFLHQSNVF HHINNILSKS
DDGDSEESFS ISVQSGFEAM SQELCIVMCL KDLTSIVDIK TSSRPAMIGS LTDGSTETFW
ESGDEDKNKT KNITINCVKG INARYVSVHV DNSRDLGNKV TSMTFLTGKA VEELCRIKQV
DLDSRHIGWV TSELPGGDNQ IIKIELKGPE NTLRVRQVKV LGWKDGESTK IAGQISASVA
QQRSCEAETL RVFRLITSQV FGKLISGDAE PTPEQEEKAL LSSPEGEEKV YNATSDADLK
EHMVGIIFSR SKLTNLQKQV CAHIVQAIRM EATRVREEWE HAISSKENAN SQPSDEDASS
DAYCFELLSM VLALSGSNVG RQYLAQQLTL LQDLFSLLHT ASPRVQRQVT SLLRRVLPEV
TPNRLASIIG VKSLPPADIS DIIHSTEKGD WNKLGILDMF LGCIAKALTV QLKAKGTTIT
GTAGTTVGKG VTTVTLPMIF NSSYLRRGES HWWMKGSTPT QISEIIIRLI KDMAAGHLSE
AWSRVTKNAI AETIIALTKM EEEFRSPVRC IATTRLWLAL ASLCVLDQDH VDRLSSGRWM
GKDGQQKQMP MCDNHDDGET AAIILCNICG NLCTDCDRFL HLHRRTKTHQ RQVFKEEEEA
IKVDLHEGCG RTKLFWLMAL ADSKTMKAMV EFREHTGKPT TSSSEACRFC GSRSGTELSA
VGSVCSDADC QEYAKIACSK THPCGHPCGG VRNEEHCLPC LHGCDKSATT LKQDADDMCM
ICFTEALSAA PAIQLDCSHV FHLQCCRRVL ENRWLGPRIT FGFISCPICK NKINHIVLKD
LLDPIKELYE DVRRKALMRL EYEGLHKSEA ITTPGVRFYN DAAGYAMNRY AYYVCYKCRK
AYFGGEARCD AEAGQGDDYD PRELICGACS DVSRAQMCPK HGTDFLEYKC RYCCSVAVFF
CFGTTHFCNA CHDDFQRMTS IPKEELPHCP AGPKGKQLEG TECPLHVVHP PTGEEFALGC
GVCRNAHTF


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