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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_HUMAN             Reviewed;        4678 AA.
O75592; A6NJC6; Q5JSX8; Q5VZN6; Q6PIB6; Q9UQ11; Q9Y6E4;
21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
20-JUN-2018, sequence version 4.
10-OCT-2018, entry version 176.
RecName: Full=E3 ubiquitin-protein ligase MYCBP2 {ECO:0000305};
EC=2.3.2.- {ECO:0000269|PubMed:29643511};
AltName: Full=Myc-binding protein 2 {ECO:0000305};
AltName: Full=Protein associated with Myc {ECO:0000303|PubMed:9689053};
Name=MYCBP2 {ECO:0000312|HGNC:HGNC:23386};
Synonyms=KIAA0916 {ECO:0000303|PubMed:12168954},
PAM {ECO:0000303|PubMed:9689053};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH
MYC, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=9689053; DOI=10.1073/pnas.95.16.9172;
Guo Q., Xie J., Dang C.V., Liu E.T., Bishop J.M.;
"Identification of a large Myc-binding protein that contains RCC1-like
repeats.";
Proc. Natl. Acad. Sci. U.S.A. 95:9172-9177(1998).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ISOFORM 2).
PubMed=15057823; DOI=10.1038/nature02379;
Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E.,
Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E.,
Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.,
Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R.,
Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S.,
Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M.,
Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J.,
Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E.,
Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L.,
Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J.,
Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S.,
Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J.,
Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M.,
King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A.,
Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S.,
Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I.,
Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S.,
Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A.,
Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L.,
Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M.,
Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.;
"The DNA sequence and analysis of human chromosome 13.";
Nature 428:522-528(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3469-4678 (ISOFORM 1).
TISSUE=Brain {ECO:0000269|PubMed:10048485};
PubMed=10048485; DOI=10.1093/dnares/5.6.355;
Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M.,
Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. XII.
The complete sequences of 100 new cDNA clones from brain which code
for large proteins in vitro.";
DNA Res. 5:355-364(1998).
[5]
SEQUENCE REVISION.
PubMed=12168954; DOI=10.1093/dnares/9.3.99;
Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
"Construction of expression-ready cDNA clones for KIAA genes: manual
curation of 330 KIAA cDNA clones.";
DNA Res. 9:99-106(2002).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3827-4678 (ISOFORM 1).
TISSUE=Brain {ECO:0000312|EMBL:AAH37971.1};
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).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 4405-4678.
TISSUE=Umbilical cord blood {ECO:0000269|PubMed:11042152};
PubMed=11042152; DOI=10.1101/gr.140200;
Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
"Cloning and functional analysis of cDNAs with open reading frames for
300 previously undefined genes expressed in CD34+ hematopoietic
stem/progenitor cells.";
Genome Res. 10:1546-1560(2000).
[8]
INTERACTION WITH TSC2.
PubMed=14559897; DOI=10.1074/jbc.M310208200;
Murthy V., Han S., Beauchamp R.L., Smith N., Haddad L.A., Ito N.,
Ramesh V.;
"Pam and its ortholog highwire interact with and may negatively
regulate the TSC1.TSC2 complex.";
J. Biol. Chem. 279:1351-1358(2004).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3090, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[10]
FUNCTION, AND AUTOUBIQUITINATION.
PubMed=18308511; DOI=10.1016/j.cellsig.2008.01.020;
Han S., Witt R.M., Santos T.M., Polizzano C., Sabatini B.L.,
Ramesh V.;
"Pam (Protein associated with Myc) functions as an E3 ubiquitin ligase
and regulates TSC/mTOR signaling.";
Cell. Signal. 20:1084-1091(2008).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3505, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-178; SER-181; SER-183;
THR-2683; SER-2789; SER-3478 AND SER-3505, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[14]
IDENTIFICATION BY MASS SPECTROMETRY, AND 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).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3505, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-2683; SER-2920 AND
SER-3505, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-2683 AND SER-3505, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[18]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[19]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[20]
INTERACTION WITH RAE1.
PubMed=22357847; DOI=10.1523/JNEUROSCI.2901-11.2012;
Grill B., Chen L., Tulgren E.D., Baker S.T., Bienvenut W.,
Anderson M., Quadroni M., Jin Y., Garner C.C.;
"RAE-1, a novel PHR binding protein, is required for axon termination
and synapse formation in Caenorhabditis elegans.";
J. Neurosci. 32:2628-2636(2012).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-127; SER-1624; THR-2683;
SER-2769; SER-2787; SER-2789; SER-2833; SER-2839; SER-2871; SER-2985;
SER-3505; SER-3931 AND SER-3932, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3478, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[23]
FUNCTION, INTERACTION WITH RAN AND RANGAP1, AND SUBCELLULAR LOCATION.
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).
[24]
X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 4416-4678 IN COMPLEX WITH
ZINC, FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITES, ZINC-BINDING, AND
MUTAGENESIS OF CYS-4558; GLU-4572; CYS-4610; PHE-4611; PHE-4616;
HIS-4621 AND PHE-4624.
PubMed=29643511; DOI=10.1038/s41586-018-0026-1;
Pao K.C., Wood N.T., Knebel A., Rafie K., Stanley M., Mabbitt P.D.,
Sundaramoorthy R., Hofmann K., van Aalten D.M.F., Virdee S.;
"Activity-based E3 ligase profiling uncovers an E3 ligase with
esterification activity.";
Nature 556:381-385(2018).
-!- FUNCTION: Atypical E3 ubiquitin-protein ligase which specifically
mediates ubiquitination of threonine and serine residues on target
proteins, instead of ubiquitinating lysine residues
(PubMed:29643511). 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 (PubMed:29643511).
Interacts with the E2 enzymes UBE2D1, UBE2D3, UBE2E1 and UBE2L3
(PubMed:18308511, PubMed:29643511). Plays a key role in neural
development, probably by mediating ubiquitination of threonine
residues on target proteins (Probable). Involved in different
processes such as regulation of neurite outgrowth, synaptic
growth, synaptogenesis and axon degeneration (By similarity).
Required for the formation of major central nervous system axon
tracts (By similarity). Required for proper axon growth by
regulating axon navigation and axon branching: acts by regulating
the subcellular location and stability of MAP3K12/DLK (By
similarity). Required for proper localization of retinogeniculate
projections but not for eye-specific segregation (By similarity).
Regulates axon guidance in the olfactory system (By similarity).
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 (By similarity). Catalyzes ubiquitination of threonine
and/or serine residues on NMNAT2, consequences of threonine and/or
serine ubiquitination are however unknown (PubMed:29643511).
Regulates the internalization of TRPV1 in peripheral sensory
neurons (By similarity). May mediate ubiquitination and subsequent
proteasomal degradation of TSC2/tuberin (PubMed:18308511).
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
(PubMed:9689053). {ECO:0000250|UniProtKB:Q7TPH6,
ECO:0000269|PubMed:18308511, ECO:0000269|PubMed:26304119,
ECO:0000269|PubMed:29643511, ECO:0000269|PubMed:9689053}.
-!- CATALYTIC ACTIVITY: S-ubiquitinyl-[E2 ubiquitin-conjugating
enzyme]-L-cysteine + [acceptor protein]-L-threonine = [E2
ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-
[acceptor protein]-L-threonine. {ECO:0000269|PubMed:29643511}.
-!- CATALYTIC ACTIVITY: S-ubiquitinyl-[E2 ubiquitin-conjugating
enzyme]-L-cysteine + [acceptor protein]-L-serine = [E2 ubiquitin-
conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor
protein]-L-serine. {ECO:0000269|PubMed:29643511}.
-!- PATHWAY: Protein modification; protein ubiquitination.
{ECO:0000269|PubMed:18308511, ECO:0000269|PubMed:29643511}.
-!- SUBUNIT: Interacts with MYC (PubMed:9689053). Interacts with TSC2
(tuberin) when TSC2 is in complex with TSC1 (hamartin)
(PubMed:14559897). Interacts with FBXO45 (PubMed:19398581).
Interacts with RAE1 (PubMed:22357847). Interacts with CPNE1 (via
VWFA domain) and CPNE4 (via VWFA domain) (By similarity).
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). Interacts with RAN (PubMed:26304119).
{ECO:0000250|UniProtKB:Q7TPH6, ECO:0000269|PubMed:14559897,
ECO:0000269|PubMed:19398581, ECO:0000269|PubMed:22357847,
ECO:0000269|PubMed:26304119, ECO:0000269|PubMed:9689053}.
-!- INTERACTION:
Q99IB8:- (xeno); NbExp=3; IntAct=EBI-1043774, EBI-6927928;
Q3SWS8:Rae1 (xeno); NbExp=2; IntAct=EBI-1043774, EBI-6920222;
P63104:YWHAZ; NbExp=2; IntAct=EBI-1043774, EBI-347088;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:26304119,
ECO:0000269|PubMed:9689053}. Cell projection, axon
{ECO:0000250|UniProtKB:Q7TPH6}. Cytoplasm, cytoskeleton
{ECO:0000250|UniProtKB:Q7TPH6}. Note=Localizes to axon shafts and
associates with microtubule cytoskeleton (By similarity).
Translocates to the nucleus following interaction with sumoylated
RANGAP1 (PubMed:26304119). {ECO:0000250|UniProtKB:Q7TPH6,
ECO:0000269|PubMed:26304119}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1 {ECO:0000269|PubMed:9689053};
IsoId=O75592-1; Sequence=Displayed;
Name=2 {ECO:0000305};
IsoId=O75592-2; Sequence=VSP_014183;
Note=Derived from EST data. {ECO:0000305};
-!- TISSUE SPECIFICITY: Expressed in all tissues examined, expression
is exceptionally abundant in brain and thymus. Colocalizes with
TSC1 and TSC2 along the neurites and in the growth cones. Highly
expressed in peripheral and central neurons. Colocalized with TSC1
in one of the filopodial extensions at the tip of a growth cone.
{ECO:0000269|PubMed:9689053}.
-!- 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 (By similarity).
{ECO:0000250|UniProtKB:Q7TPH6}.
-!- 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:0000269|PubMed:29643511}.
-!- PTM: Autoubiquitinated. {ECO:0000269|PubMed:18308511}.
-!- SIMILARITY: Belongs to the RING-Cys relay (RCR) family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAD39842.1; Type=Frameshift; Positions=4674; Evidence={ECO:0000305};
Sequence=AAH37971.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=CAI39758.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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EMBL; AF075587; AAC39928.1; -; mRNA.
EMBL; AL159154; CAH73736.1; -; Genomic_DNA.
EMBL; AL159158; CAH73736.1; JOINED; Genomic_DNA.
EMBL; AL359257; CAH73736.1; JOINED; Genomic_DNA.
EMBL; AC001226; CAH73736.1; JOINED; Genomic_DNA.
EMBL; AL159158; CAI16842.1; -; Genomic_DNA.
EMBL; AL159154; CAI16842.1; JOINED; Genomic_DNA.
EMBL; AL359257; CAI16842.1; JOINED; Genomic_DNA.
EMBL; AC001226; CAI16842.1; JOINED; Genomic_DNA.
EMBL; AL359257; CAI39759.1; -; Genomic_DNA.
EMBL; AL159158; CAI39759.1; JOINED; Genomic_DNA.
EMBL; AL159154; CAI39759.1; JOINED; Genomic_DNA.
EMBL; AC001226; CAI39759.1; JOINED; Genomic_DNA.
EMBL; AL359257; CAI39758.1; ALT_SEQ; Genomic_DNA.
EMBL; AC001226; CAI39758.1; JOINED; Genomic_DNA.
EMBL; CH471093; EAW80565.1; -; Genomic_DNA.
EMBL; AB020723; BAA74939.1; -; mRNA.
EMBL; BC037971; AAH37971.1; ALT_INIT; mRNA.
EMBL; AF083244; AAD39842.1; ALT_FRAME; mRNA.
RefSeq; NP_055872.4; NM_015057.4. [O75592-1]
UniGene; Hs.591221; -.
PDB; 5O6C; X-ray; 1.75 A; A=4416-4678.
PDBsum; 5O6C; -.
ProteinModelPortal; O75592; -.
SMR; O75592; -.
BioGrid; 116709; 86.
DIP; DIP-28142N; -.
IntAct; O75592; 51.
MINT; O75592; -.
STRING; 9606.ENSP00000384288; -.
iPTMnet; O75592; -.
PhosphoSitePlus; O75592; -.
BioMuta; MYCBP2; -.
EPD; O75592; -.
MaxQB; O75592; -.
PaxDb; O75592; -.
PeptideAtlas; O75592; -.
PRIDE; O75592; -.
ProteomicsDB; 50101; -.
ProteomicsDB; 50102; -. [O75592-2]
Ensembl; ENST00000357337; ENSP00000349892; ENSG00000005810.
Ensembl; ENST00000544440; ENSP00000444596; ENSG00000005810.
GeneID; 23077; -.
KEGG; hsa:23077; -.
UCSC; uc058xok.1; human. [O75592-1]
CTD; 23077; -.
DisGeNET; 23077; -.
EuPathDB; HostDB:ENSG00000005810.17; -.
GeneCards; MYCBP2; -.
HGNC; HGNC:23386; MYCBP2.
HPA; HPA058807; -.
MIM; 610392; gene.
neXtProt; NX_O75592; -.
PharmGKB; PA134871126; -.
eggNOG; KOG1428; Eukaryota.
eggNOG; ENOG410XP1T; LUCA.
HOVERGEN; HBG053153; -.
InParanoid; O75592; -.
KO; K10693; -.
OMA; TVSVECF; -.
OrthoDB; EOG091G0018; -.
PhylomeDB; O75592; -.
TreeFam; TF313151; -.
UniPathway; UPA00143; -.
ChiTaRS; MYCBP2; human.
GeneWiki; MYCBP2; -.
GenomeRNAi; 23077; -.
PRO; PR:O75592; -.
Proteomes; UP000005640; Chromosome 13.
Bgee; ENSG00000005810; Expressed in 244 organ(s), highest expression level in primary visual cortex.
CleanEx; HS_MYCBP2; -.
CleanEx; HS_PAM; -.
ExpressionAtlas; O75592; baseline and differential.
Genevisible; O75592; HS.
GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IDA:UniProtKB.
GO; GO:0008536; F:Ran GTPase binding; IDA:UniProtKB.
GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:UniProtKB.
GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
GO; GO:0021952; P:central nervous system projection neuron axonogenesis; ISS:UniProtKB.
GO; GO:0050905; P:neuromuscular process; ISS:UniProtKB.
GO; GO:0016567; P:protein ubiquitination; IDA:UniProtKB.
GO; GO:1902667; P:regulation of axon guidance; ISS:UniProtKB.
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; 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; 2.
SUPFAM; SSF81296; SSF81296; 2.
PROSITE; PS51284; DOC; 1.
PROSITE; PS50194; FILAMIN_REPEAT; 1.
PROSITE; PS00626; RCC1_2; 2.
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; Disulfide bond;
Guanine-nucleotide releasing factor; Metal-binding; Nucleus;
Phosphoprotein; Polymorphism; Reference proteome; Repeat; Transferase;
Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger.
CHAIN 1 4678 E3 ubiquitin-protein ligase MYCBP2.
/FTId=PRO_0000055963.
REPEAT 600 655 RCC1 1. {ECO:0000255}.
REPEAT 699 755 RCC1 2. {ECO:0000255}.
REPEAT 907 957 RCC1 3. {ECO:0000255}.
REPEAT 958 1008 RCC1 4. {ECO:0000255}.
REPEAT 1010 1066 RCC1 5. {ECO:0000255}.
REPEAT 2341 2443 Filamin. {ECO:0000255}.
DOMAIN 3719 3897 DOC. {ECO:0000255|PROSITE-
ProRule:PRU00614}.
ZN_FING 4428 4479 RING-type; atypical.
{ECO:0000255|PROSITE-ProRule:PRU00175}.
ZN_FING 4582 4632 B box-type.
REGION 1235 1386 PHR domain 1. {ECO:0000250}.
REGION 1726 1884 PHR domain 2. {ECO:0000250}.
REGION 2022 2550 RAE1 binding.
{ECO:0000269|PubMed:22357847}.
REGION 4539 4676 Tandem cysteine domain.
{ECO:0000305|PubMed:29643511}.
COMPBIAS 103 126 Lys-rich. {ECO:0000255}.
COMPBIAS 766 814 Cys-rich. {ECO:0000255}.
COMPBIAS 2720 2844 Ser-rich. {ECO:0000255}.
COMPBIAS 3194 3215 Lys-rich. {ECO:0000255}.
COMPBIAS 3262 3293 Gly-rich.
ACT_SITE 4558 4558 {ECO:0000269|PubMed:29643511}.
ACT_SITE 4610 4610 {ECO:0000269|PubMed:29643511}.
METAL 4428 4428 Zinc 1. {ECO:0000244|PDB:5O6C,
ECO:0000269|PubMed:29643511}.
METAL 4431 4431 Zinc 1. {ECO:0000244|PDB:5O6C,
ECO:0000269|PubMed:29643511}.
METAL 4446 4446 Zinc 2. {ECO:0000244|PDB:5O6C,
ECO:0000269|PubMed:29643511}.
METAL 4448 4448 Zinc 2. {ECO:0000244|PDB:5O6C,
ECO:0000269|PubMed:29643511}.
METAL 4451 4451 Zinc 1. {ECO:0000244|PDB:5O6C,
ECO:0000269|PubMed:29643511}.
METAL 4454 4454 Zinc 1. {ECO:0000244|PDB:5O6C,
ECO:0000269|PubMed:29643511}.
METAL 4475 4475 Zinc 2. {ECO:0000244|PDB:5O6C,
ECO:0000269|PubMed:29643511}.
METAL 4478 4478 Zinc 2. {ECO:0000244|PDB:5O6C,
ECO:0000269|PubMed:29643511}.
METAL 4544 4544 Zinc 3. {ECO:0000244|PDB:5O6C,
ECO:0000269|PubMed:29643511}.
METAL 4547 4547 Zinc 3. {ECO:0000244|PDB:5O6C,
ECO:0000269|PubMed:29643511}.
METAL 4575 4575 Zinc 3. {ECO:0000244|PDB:5O6C,
ECO:0000269|PubMed:29643511}.
METAL 4578 4578 Zinc 3. {ECO:0000244|PDB:5O6C,
ECO:0000269|PubMed:29643511}.
METAL 4587 4587 Zinc 4. {ECO:0000244|PDB:5O6C,
ECO:0000269|PubMed:29643511}.
METAL 4590 4590 Zinc 4. {ECO:0000244|PDB:5O6C,
ECO:0000269|PubMed:29643511}.
METAL 4599 4599 Zinc 5. {ECO:0000244|PDB:5O6C,
ECO:0000269|PubMed:29643511}.
METAL 4602 4602 Zinc 5. {ECO:0000244|PDB:5O6C,
ECO:0000269|PubMed:29643511}.
METAL 4603 4603 Zinc 6. {ECO:0000244|PDB:5O6C,
ECO:0000269|PubMed:29643511}.
METAL 4617 4617 Zinc 5. {ECO:0000244|PDB:5O6C,
ECO:0000269|PubMed:29643511}.
METAL 4620 4620 Zinc 5. {ECO:0000244|PDB:5O6C,
ECO:0000269|PubMed:29643511}.
METAL 4638 4638 Zinc 6. {ECO:0000244|PDB:5O6C,
ECO:0000269|PubMed:29643511}.
METAL 4652 4652 Zinc 6. {ECO:0000244|PDB:5O6C,
ECO:0000269|PubMed:29643511}.
METAL 4658 4658 Zinc 6. {ECO:0000244|PDB:5O6C,
ECO:0000269|PubMed:29643511}.
METAL 4669 4669 Zinc 4. {ECO:0000244|PDB:5O6C,
ECO:0000269|PubMed:29643511}.
METAL 4672 4672 Zinc 4. {ECO:0000244|PDB:5O6C,
ECO:0000269|PubMed:29643511}.
SITE 4611 4611 Important for catalysis.
{ECO:0000269|PubMed:29643511}.
SITE 4616 4616 Important for catalysis.
{ECO:0000269|PubMed:29643511}.
SITE 4624 4624 Important for catalysis.
{ECO:0000269|PubMed:29643511}.
MOD_RES 127 127 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 178 178 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 181 181 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 183 183 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 1624 1624 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 2683 2683 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 2769 2769 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 2787 2787 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 2789 2789 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 2833 2833 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 2839 2839 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 2869 2869 Phosphoserine.
{ECO:0000250|UniProtKB:Q7TPH6}.
MOD_RES 2871 2871 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 2920 2920 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 2985 2985 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 3090 3090 Phosphoserine.
{ECO:0000244|PubMed:17081983}.
MOD_RES 3478 3478 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:24275569}.
MOD_RES 3505 3505 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 3921 3921 Phosphothreonine.
{ECO:0000250|UniProtKB:Q7TPH6}.
MOD_RES 3931 3931 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 3932 3932 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
DISULFID 1748 1863 {ECO:0000250|UniProtKB:Q7TPH6}.
VAR_SEQ 3939 3941 Missing (in isoform 2). {ECO:0000305}.
/FTId=VSP_014183.
VARIANT 1919 1919 A -> S (in dbSNP:rs35887505).
/FTId=VAR_052086.
VARIANT 2626 2626 V -> M (in dbSNP:rs9574002).
/FTId=VAR_030070.
MUTAGEN 4558 4558 C->S: Abolished E3 ubiquitin-protein
ligase activity.
{ECO:0000269|PubMed:29643511}.
MUTAGEN 4572 4572 E->A,Q: Does not affect E3 ubiquitin-
protein ligase activity.
{ECO:0000269|PubMed:29643511}.
MUTAGEN 4610 4610 C->A: Increased thiol-sensitive adduct
formation. {ECO:0000269|PubMed:29643511}.
MUTAGEN 4610 4610 C->S: Retains activity while also forming
a discrete monoubiquitin adduct that is
resistant to thiolysis but is reversible
after base treatment.
{ECO:0000269|PubMed:29643511}.
MUTAGEN 4611 4611 F->A: Reduced E3 ubiquitin-protein ligase
activity in threonine discharge assay.
{ECO:0000269|PubMed:29643511}.
MUTAGEN 4616 4616 F->A: Reduced E3 ubiquitin-protein ligase
activity in threonine discharge assay.
{ECO:0000269|PubMed:29643511}.
MUTAGEN 4621 4621 H->N: Abolished E3 ubiquitin-protein
ligase activity in threonine discharge
assay, associated with enhanced thiol-
sensitive ubiquitin adduct formation.
{ECO:0000269|PubMed:29643511}.
MUTAGEN 4624 4624 F->A: Reduced E3 ubiquitin-protein ligase
activity in threonine discharge assay.
{ECO:0000269|PubMed:29643511}.
CONFLICT 61 61 R -> P (in Ref. 1; AAC39928).
{ECO:0000305}.
CONFLICT 240 240 G -> V (in Ref. 1; AAC39928).
{ECO:0000305}.
CONFLICT 510 510 G -> R (in Ref. 1; AAC39928).
{ECO:0000305}.
CONFLICT 618 618 T -> I (in Ref. 1; AAC39928).
{ECO:0000305}.
CONFLICT 903 904 QL -> HV (in Ref. 1; AAC39928).
{ECO:0000305}.
CONFLICT 1512 1513 GV -> PL (in Ref. 1; AAC39928).
{ECO:0000305}.
CONFLICT 2139 2139 K -> M (in Ref. 1; AAC39928).
{ECO:0000305}.
CONFLICT 3201 3201 E -> GR (in Ref. 1; AAC39928).
{ECO:0000305}.
CONFLICT 3645 3645 A -> R (in Ref. 1; AAC39928).
{ECO:0000305}.
TURN 4429 4431 {ECO:0000244|PDB:5O6C}.
STRAND 4432 4435 {ECO:0000244|PDB:5O6C}.
HELIX 4436 4438 {ECO:0000244|PDB:5O6C}.
STRAND 4441 4443 {ECO:0000244|PDB:5O6C}.
STRAND 4449 4451 {ECO:0000244|PDB:5O6C}.
HELIX 4452 4461 {ECO:0000244|PDB:5O6C}.
STRAND 4464 4467 {ECO:0000244|PDB:5O6C}.
HELIX 4471 4473 {ECO:0000244|PDB:5O6C}.
TURN 4476 4478 {ECO:0000244|PDB:5O6C}.
HELIX 4485 4487 {ECO:0000244|PDB:5O6C}.
HELIX 4488 4511 {ECO:0000244|PDB:5O6C}.
HELIX 4518 4521 {ECO:0000244|PDB:5O6C}.
TURN 4526 4529 {ECO:0000244|PDB:5O6C}.
HELIX 4531 4538 {ECO:0000244|PDB:5O6C}.
STRAND 4539 4543 {ECO:0000244|PDB:5O6C}.
TURN 4545 4547 {ECO:0000244|PDB:5O6C}.
STRAND 4550 4555 {ECO:0000244|PDB:5O6C}.
HELIX 4570 4572 {ECO:0000244|PDB:5O6C}.
HELIX 4577 4579 {ECO:0000244|PDB:5O6C}.
TURN 4588 4590 {ECO:0000244|PDB:5O6C}.
TURN 4592 4594 {ECO:0000244|PDB:5O6C}.
STRAND 4595 4598 {ECO:0000244|PDB:5O6C}.
STRAND 4602 4605 {ECO:0000244|PDB:5O6C}.
STRAND 4608 4610 {ECO:0000244|PDB:5O6C}.
TURN 4611 4613 {ECO:0000244|PDB:5O6C}.
STRAND 4614 4616 {ECO:0000244|PDB:5O6C}.
HELIX 4618 4622 {ECO:0000244|PDB:5O6C}.
HELIX 4624 4629 {ECO:0000244|PDB:5O6C}.
HELIX 4632 4634 {ECO:0000244|PDB:5O6C}.
STRAND 4638 4641 {ECO:0000244|PDB:5O6C}.
HELIX 4642 4644 {ECO:0000244|PDB:5O6C}.
STRAND 4648 4650 {ECO:0000244|PDB:5O6C}.
STRAND 4666 4669 {ECO:0000244|PDB:5O6C}.
HELIX 4672 4674 {ECO:0000244|PDB:5O6C}.
SEQUENCE 4678 AA; 513636 MW; F76B95A12613E74B CRC64;
MMMCAATASP AAASSGLGGD GFYPAATFSS SPAPGALFMP VPDGSVAAAG LGLGLPAADS
RGHYQLLLSG RALADRYRRI YTAALNDRDQ GGGSAGHPAS RNKKILNKKK LKRKQKSKSK
VKTRSKSENL ENTVIIPDIK LHSNPSAFNI YCNVRHCVLE WQKKEISLAA ASKNSVQSGE
SDSDEEEESK EPPIKLPKII EVGLCEVFEL IKETRFSHPS LCLRSLQALL NVLQGQQPEG
LQSEPPEVLE SLFQLLLEIT VRSTGMNDST GQSLTALSCA CLFSLVASWG ETGRTLQAIS
AILTNNGSHA CQTIQVPTIL NSLQRSVQAV LVGKIQIQDW FSNGIKKAAL MHKWPLKEIS
VDEDDQCLLQ NDGFFLYLLC KDGLYKIGSG YSGTVRGHIY NSTSRIRNRK EKKSWLGYAQ
GYLLYRDVNN HSMTAIRISP ETLEQDGTVM LPDCHTEGQN ILFTDGEYIN QIAASRDDGF
VVRIFATSTE PVLQQELQLK LARKCLHACG ISLFDLEKDL HIISTGFDEE SAILGAGREF
ALMKTANGKI YYTGKYQSLG IKQGGPSAGK WVELPITKSP KIVHFSVGHD GSHALLVAED
GSIFFTGSAS KGEDGESTKS RRQSKPYKPK KIIKMEGKIV VYTACNNGSS SVISKDGELY
MFGKDAIYSD SSSLVTDLKG HFVTQVAMGK AHTCVLMKNG EVWTFGVNNK GQCGRDTGAM
NQGGKGFGVE NMATAMDEDL EEELDEKDEK SMMCPPGMHK WKLEQCMVCT VCGDCTGYGA
SCVSSGRPDR VPGGICGCGS GESGCAVCGC CKACARELDG QEARQRGILD AVKEMIPLDL
LLAVPVPGVN IEEHLQLRQE EKRQRVIRRH RLEEGRGPLV FAGPIFMNHR EQALARLRSH
PAQLKHKRDK HKDGSGERGE KDASKITTYP PGSVRFDCEL RAVQVSCGFH HSVVLMENGD
VYTFGYGQHG QLGHGDVNSR GCPTLVQALP GPSTQVTAGS NHTAVLLMDG QVFTFGSFSK
GQLGRPILDV PYWNAKPAPM PNIGSKYGRK ATWIGASGDQ TFLRIDEALI NSHVLATSEI
FASKHIIGLV PASISEPPPF KCLLINKVDG SCKTFNDSEQ EDLQGFGVCL DPVYDVIWRF
RPNTRELWCY NAVVADARLP SAADMQSRCS ILSPELALPT GSRALTTRSH AALHILGCLD
TLAAMQDLKM GVASTEEETQ AVMKVYSKED YSVVNRFESH GGGWGYSAHS VEAIRFSADT
DILLGGLGLF GGRGEYTAKI KLFELGPDGG DHETDGDLLA ETDVLAYDCA AREKYAMMFD
EPVLLQAGWW YVAWARVSGP SSDCGSHGQA SITTDDGVVF QFKSSKKSNN GTDVNAGQIP
QLLYRLPTSD GSASKGKQQT SEPVHILKRS FARTVSVECF ESLLSILHWS WTTLVLGVEE
LRGLKGFQFT ATLLDLERLR FVGTCCLRLL RVYTCEIYPV SATGKAVVEE TSKLAECIGK
TRTLLRKILS EGVDHCMVKL DNDPQGYLSQ PLSLLEAVLQ ECHNTFTACF HSFYPTPALQ
WACLCDLLNC LDQDIQEANF KTSSSRLLAA VMSALCHTSV KLTSIFPIAY DGEVLLRSIV
KQVSTENDST LVHRFPLLVA HMEKLSQSEE NISGMTSFRE VLEKMLVIVV LPVRNSLRRE
NELFSSHLVS NTCGLLASIV SELTASALGS EVDGLNSLHS VKASANRFTK TSQGRSWNTG
NGSPDAICFS VDKPGIVVVG FSVYGGGGIH EYELEVLVDD SEHAGDSTHS HRWTSLELVK
GTYTTDDSPS DIAEIRLDKV VPLKENVKYA VRLRNYGSRT ANGDGGMTTV QCPDGVTFTF
STCSLSSNGT NQTRGQIPQI LYYRSEFDGD LQSQLLSKAN EEDKNCSRAL SVVSTVVRAS
KDLLHRALAV DADDIPELLS SSSLFSMLLP LIIAYIGPVA AAIPKVAVEV FGLVQQLLPS
VAILNQKYAP PAFNPNQSTD STTGNQPEQG LSACTTSSHY AVIESEHPYK PACVMHYKVT
FPECVRWMTI EFDPQCGTAQ SEDVLRLLIP VRTVQNSGYG PKLTSVHENL NSWIELKKFS
GSSGWPTMVL VLPGNEALFS LETASDYVKD DKASFYGFKC FAIGYEFSPG PDEGVIQLEK
ELANLGGVCA AALMKKDLAL PIGNELEEDL EILEEAALQV CKTHSGILGK GLALSHSPTI
LEALEGNLPL QIQSNEQSFL DDFIACVPGS SGGRLARWLQ PDSYADPQKT SLILNKDDIR
CGWPTTITVQ TKDQYGDVVH VPNMKVEVKA VPVSQKKMSL QQDQAKKPQR IPGSPAVTAA
SSNTDMTYGG LASPKLDVSY EPMIVKEARY IAITMMKVYE NYSFEELRFA SPTPKRPSEN
MLIRVNNDGT YCANWTPGAI GLYTLHVTID GIEIDAGLEV KVKDPPKGMI PPGTQLVKPK
SEPQPNKVRK FVAKDSAGLR IRSHPSLQSE QIGIVKVNGT ITFIDEIHND DGVWLRLNDE
TIKKYVPNMN GYTEAWCLSF NQHLGKSLLV PVDESKTNTD DFFKDINSCC PQEATMQEQD
MPFLRGGPGM YKVVKTGPSG HNIRSCPNLR GIPIGMLVLG NKVKAVGEVT NSEGTWVQLD
QNSMVEFCES DEGEAWSLAR DRGGNQYLRH EDEQALLDQN SQTPPPSPFS VQAFNKGASC
SAQGFDYGLG NSKGDRGNIS TSSKPASTSG KSELSSKHSR SLKPDGRMSR TTADQKKPRG
TESLSASESL ILKSDAAKLR SDSHSRSLSP NHNTLQTLKS DGRMPSSSRA ESPGPGSRLS
SPKPKTLPAN RSSPSGASSP RSSSPHDKNL PQKSTAPVKT KLDPPRERSK SDSYTLDPDT
LRKKKMPLTE PLRGRSTSPK PKSVPKDSTD SPGSENRAPS PHVVQENLHS EVVEVCTSST
LKTNSLTDST CDDSSEFKSV DEGSNKVHFS IGKAPLKDEQ EMRASPKISR KCANRHTRPK
KEKSSFLFKG DGSKPLEPAK QAMSPSVAEC ARAVFASFLW HEGIVHDAMA CSSFLKFHPE
LSKEHAPIRS SLNSQQPTEE KETKLKNRHS LEISSALNMF NIAPHGPDIS KMGSINKNKV
LSMLKEPPLH EKCEDGKTET TFEMSMHNTM KSKSPLPLTL QHLVAFWEDI SLATIKAASQ
NMIFPSPGSC AVLKKKECEK ENKKSKKEKK KKEKAEVRPR GNLFGEMAQL AVGGPEKDTI
CELCGESHPY PVTYHMRQAH PGCGRYAGGQ GYNSIGHFCG GWAGNCGDGG IGGSTWYLVC
DRCREKYLRE KQAAAREKVK QSRRKPMQVK TPRALPTMEA HQVIKANALF LLSLSSAAEP
SILCYHPAKP FQSQLPSVKE GISEDLPVKM PCLYLQTLAR HHHENFVGYQ DDNLFQDEMR
YLRSTSVPAP YISVTPDASP NVFEEPESNM KSMPPSLETS PITDTDLAKR TVFQRSYSVV
ASEYDKQHSI LPARVKAIPR RRVNSGDTEV GSSLLRHPSP ELSRLISAHS SLSKGERNFQ
WPVLAFVIQH HDLEGLEIAM KQALRKSACR VFAMEAFNWL LCNVIQTTSL HDILWHFVAS
LTPAPVEPEE EEDEENKTSK ENSEQEKDTR VCEHPLSDIV IAGEAAHPLP HTFHRLLQTI
SDLMMSLPSG SSLQQMALRC WSLKFKQSDH QFLHQSNVFH HINNILSKSD DGDSEESFSI
SIQSGFEAMS QELCIVMCLK DLTSIVDIKT SSRPAMIGSL TDGSTETFWE SGDEDKNKTK
NITINCVKGI NARYVSVHVD NSRDLGNKVT SMTFLTGKAV EDLCRIKQVD LDSRHIGWVT
SELPGGDNHI IKIELKGPEN TLRVRQVKVL GWKDGESTKI AGQISASVAQ QRNCEAETLR
VFRLITSQVF GKLISGDAEP TPEQEEKALL SSPEGEEKVY NATSDADLKE HMVGIIFSRS
KLTNLQKQVC AHIVQAIRME ATRVREEWEH AISSKENANS QPNDEDASSD AYCFELLSMV
LALSGSNVGR QYLAQQLTLL QDLFSLLHTA SPRVQRQVTS LLRRVLPEVT PSRLASIIGV
KSLPPADISD IIHSTEKGDW NKLGILDMFL GCIAKALTVQ LKAKGTTITG TAGTTVGKGV
TTVTLPMIFN SSYLRRGESH WWMKGSTPTQ ISEIIIKLIK DMAAGHLSEA WSRVTKNAIA
ETIIALTKME EEFRSPVRCI ATTRLWLALA SLCVLDQDHV DRLSSGRWMG KDGQQKQMPM
CDNHDDGETA AIILCNVCGN LCTDCDRFLH LHRRTKTHQR QVFKEEEEAI KVDLHEGCGR
TKLFWLMALA DSKTMKAMVE FREHTGKPTT SSSEACRFCG SRSGTELSAV GSVCSDADCQ
EYAKIACSKT HPCGHPCGGV KNEEHCLPCL HGCDKSATSL KQDADDMCMI CFTEALSAAP
AIQLDCSHIF HLQCCRRVLE NRWLGPRITF GFISCPICKN KINHIVLKDL LDPIKELYED
VRRKALMRLE YEGLHKSEAI TTPGVRFYND PAGYAMNRYA YYVCYKCRKA YFGGEARCDA
EAGRGDDYDP RELICGACSD VSRAQMCPKH GTDFLEYKCR YCCSVAVFFC FGTTHFCNAC
HDDFQRMTSI PKEELPHCPA GPKGKQLEGT ECPLHVVHPP TGEEFALGCG VCRNAHTF


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EIAAB25919 Homo sapiens,Human,KIAA0916,Myc-binding protein 2,MYCBP2,PAM,Pam_highwire_rpm-1 protein,Probable E3 ubiquitin-protein ligase MYCBP2,Protein associated with Myc
EIAAB25920 Mouse,Mus musculus,Myc-binding protein 2,Mycbp2,Pam,Pam_highwire_rpm-1 protein,Phr1,Probable E3 ubiquitin-protein ligase MYCBP2,Protein associated with Myc
CSB-EL015272MO Mouse Probable E3 ubiquitin-protein ligase MYCBP2(MYCBP2) ELISA kit 96T
CSB-EL015272HU Human Probable E3 ubiquitin-protein ligase MYCBP2(MYCBP2) ELISA kit 96T
G1083 Probable E3 ubiquitin-protein ligase MYCBP2 (MYCBP2), Human, ELISA Kit 96T
G1084 Probable E3 ubiquitin-protein ligase MYCBP2 (MYCBP2), Mouse, ELISA Kit 96T
CSB-EL015272MO Mouse Probable E3 ubiquitin-protein ligase MYCBP2(MYCBP2) ELISA kit SpeciesMouse 96T
CSB-EL015272HU Human Probable E3 ubiquitin-protein ligase MYCBP2(MYCBP2) ELISA kit SpeciesHuman 96T
MYCB2_MOUSE ELISA Kit FOR Probable E3 ubiquitin-protein ligase MYCBP2; organism: Mouse; gene name: Mycbp2 96T
EIAAB45296 Ac2-121,E3 ubiquitin-protein ligase UHRF1,Liver regeneration-related protein LRRG126,Rat,Rattus norvegicus,Ubiquitin-like PHD and RING finger domain-containing protein 1,Ubiquitin-like-containing PHD
EIAAB35402 E3 ubiquitin-protein ligase RNF128,Gene related to anergy in lymphocytes protein,Goliath-related E3 ubiquitin-protein ligase 1,Grail,Greul1,MNCb-3816,Mouse,Mus musculus,RING finger protein 128,Rnf128
EIAAB38246 Heart protein phosphatase 1-binding protein,HEPP1,Homo sapiens,Human,Putative E3 ubiquitin-protein ligase SH3RF2,RING finger protein 158,RNF158,SH3 domain-containing RING finger protein 2,SH3RF2
EIAAB35404 E3 ubiquitin-protein ligase RNF133,Goliath-related E3 ubiquitin-protein ligase 2,Greul2,Mouse,Mus musculus,RING finger protein 133,Rnf133
EIAAB35429 E3 ubiquitin-protein ligase RNF149,Goliath-related E3 ubiquitin-protein ligase 4,Greul4,Mouse,Mus musculus,RING finger protein 149,Rnf149
EIAAB35497 E3 ubiquitin-protein ligase RNF216,Mouse,Mus musculus,RING finger protein 216,Rnf216,Triad domain-containing protein 3,Triad3,Ubce7ip1,UbcM4-interacting protein 83,Ubiquitin-conjugating enzyme 7-inter
EIAAB35496 E3 ubiquitin-protein ligase RNF216,Homo sapiens,Human,RING finger protein 216,RNF216,Triad domain-containing protein 3,TRIAD3,UBCE7IP1,Ubiquitin-conjugating enzyme 7-interacting protein 1,ZIN,Zinc fin
EIAAB43448 E3 ubiquitin-protein ligase Topors,Mouse,Mus musculus,p53-binding protein 3,p53BP3,SUMO1-protein E3 ligase Topors,Topoisomerase I-binding arginine_serine-rich protein,Topoisomerase I-binding RING fing
EIAAB43449 E3 ubiquitin-protein ligase Topors,Homo sapiens,Human,LUN,p53-binding protein 3,p53BP3,SUMO1-protein E3 ligase Topors,Topoisomerase I-binding arginine_serine-rich protein,Topoisomerase I-binding RING
EIAAB05540 Casitas B-lineage lymphoma proto-oncogene b,CBLB,E3 ubiquitin-protein ligase CBL-B,Homo sapiens,Human,Nbla00127,RING finger protein 56,RNF56,SH3-binding protein CBL-B,Signal transduction protein CBL-B
EIAAB45297 E3 ubiquitin-protein ligase UHRF1,Mouse,Mus musculus,Np95,Nuclear protein 95,Nuclear zinc finger protein Np95,Ubiquitin-like PHD and RING finger domain-containing protein 1,Ubiquitin-like-containing P
EIAAB33372 Kiaa0161,Mouse,Mus musculus,Probable E3 ubiquitin-protein ligase RNF144A,RING finger protein 144A,Rnf144,Rnf144a,Ubce7ip4,UbcM4-interacting protein 4,Ubiquitin-conjugating enzyme 7-interacting protein
EIAAB45116 E3 ubiquitin-protein ligase UBR3,Homo sapiens,Human,KIAA2024,N-recognin-3,Ubiquitin-protein ligase E3-alpha-3,Ubiquitin-protein ligase E3-alpha-III,UBR3,Zinc finger protein 650,ZNF650
EIAAB45117 E3 ubiquitin-protein ligase UBR3,Kiaa2024,Mouse,Mus musculus,N-recognin-3,Ubiquitin-protein ligase E3-alpha-3,Ubiquitin-protein ligase E3-alpha-III,Ubr3,Zfp650,Zinc finger protein 650,Znf650
EIAAB33371 Homo sapiens,Human,KIAA0161,Probable E3 ubiquitin-protein ligase RNF144A,RING finger protein 144A,RNF144,RNF144A,UBCE7IP4,UbcM4-interacting protein 4,Ubiquitin-conjugating enzyme 7-interacting protein
EIAAB35409 E3 ubiquitin-protein ligase RNF135,Homo sapiens,Human,L13,REUL,RIG-I E3 ubiquitin ligase,RING finger protein 135,Riplet,RNF135


 

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