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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;        4640 AA.
O75592; A6NJC6; Q5JSX8; Q5VZN6; Q6PIB6; Q9UQ11; Q9Y6E4;
21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
23-MAY-2018, entry version 172.
RecName: Full=E3 ubiquitin-protein ligase MYCBP2;
EC=2.3.2.27;
AltName: Full=Myc-binding protein 2;
AltName: Full=Pam/highwire/rpm-1 protein;
AltName: Full=Protein associated with Myc;
AltName: Full=RING-type E3 ubiquitin transferase MYCBP2 {ECO:0000305};
Name=MYCBP2 {ECO:0000312|HGNC:HGNC:23386};
Synonyms=KIAA0916 {ECO:0000312|EMBL:BAA74939.1},
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] {ECO:0000305, ECO:0000312|EMBL:AAC39928.1}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), 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] {ECO:0000305, ECO:0000312|EMBL:CAI39758.1}
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] {ECO:0000305, ECO:0000312|EMBL:CAH73736.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3431-4640 (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] {ECO:0000305, ECO:0000312|EMBL:CAH73736.1}
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] {ECO:0000305, ECO:0000312|EMBL:AAH37971.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3789-4640 (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] {ECO:0000305, ECO:0000312|EMBL:AAD39842.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 4367-4640.
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] {ECO:0000305}
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-3052, 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-3467, 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-140; SER-143; SER-145;
THR-2645; SER-2751; SER-3440 AND SER-3467, 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-3467, 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-2645; SER-2882 AND
SER-3467, 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-2645 AND SER-3467, 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-89; SER-1586; THR-2645;
SER-2731; SER-2749; SER-2751; SER-2795; SER-2801; SER-2833; SER-2947;
SER-3467; SER-3893 AND SER-3894, 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-3440, 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).
-!- FUNCTION: E3 ubiquitin-protein ligase which mediates
ubiquitination and subsequent proteasomal degradation of
TSC2/tuberin. Interacts with the E2 enzymes UBE2D1, UBE2D3 and
UBE2L3 (in vitro). May function as a facilitator or regulator of
transcriptional activation by MYC. May have a role during
synaptogenesis. {ECO:0000269|PubMed:18308511}.
-!- CATALYTIC ACTIVITY: S-ubiquitinyl-[E2 ubiquitin-conjugating
enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-
conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor
protein]-L-lysine.
-!- PATHWAY: Protein modification; protein ubiquitination.
-!- 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).
{ECO:0000250|UniProtKB:Q7TPH6, ECO:0000269|PubMed:14559897,
ECO:0000269|PubMed:19398581, ECO:0000269|PubMed:22357847,
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:9689053}.
-!- 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.
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}.
-!- PTM: Autoubiquitinated. {ECO:0000269|PubMed:18308511}.
-!- SIMILARITY: Belongs to the highwire family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAD39842.1; Type=Frameshift; Positions=4636; 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_SEQ; mRNA.
RefSeq; NP_055872.4; NM_015057.4.
UniGene; Hs.591221; -.
ProteinModelPortal; O75592; -.
BioGrid; 116709; 84.
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; -.
Ensembl; ENST00000357337; ENSP00000349892; ENSG00000005810. [O75592-1]
Ensembl; ENST00000544440; ENSP00000444596; ENSG00000005810. [O75592-1]
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; HPA039945; -.
MIM; 610392; gene.
neXtProt; NX_O75592; -.
OpenTargets; ENSG00000005810; -.
PharmGKB; PA134871126; -.
eggNOG; KOG1428; Eukaryota.
eggNOG; ENOG410XP1T; LUCA.
GeneTree; ENSGT00910000144248; -.
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; -.
CleanEx; HS_MYCBP2; -.
CleanEx; HS_PAM; -.
ExpressionAtlas; O75592; baseline and differential.
Genevisible; O75592; HS.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:HPA.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
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;
Alternative splicing; Complete proteome; Disulfide bond;
Metal-binding; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome; Repeat; Transcription; Transcription regulation;
Transferase; Ubl conjugation; Ubl conjugation pathway; Zinc;
Zinc-finger.
CHAIN 1 4640 E3 ubiquitin-protein ligase MYCBP2.
/FTId=PRO_0000055963.
REPEAT 562 617 RCC1 1. {ECO:0000255}.
REPEAT 661 717 RCC1 2. {ECO:0000255}.
REPEAT 869 919 RCC1 3. {ECO:0000255}.
REPEAT 920 970 RCC1 4. {ECO:0000255}.
REPEAT 972 1028 RCC1 5. {ECO:0000255}.
REPEAT 2303 2405 Filamin. {ECO:0000255}.
DOMAIN 3681 3859 DOC. {ECO:0000255|PROSITE-
ProRule:PRU00614}.
ZN_FING 4390 4441 RING-type; atypical.
{ECO:0000255|PROSITE-ProRule:PRU00175}.
ZN_FING 4544 4594 B box-type.
REGION 1197 1348 PHR domain 1. {ECO:0000250}.
REGION 1688 1846 PHR domain 2. {ECO:0000250}.
REGION 1984 2512 RAE1 binding.
{ECO:0000269|PubMed:22357847}.
COMPBIAS 65 88 Lys-rich. {ECO:0000255}.
COMPBIAS 728 776 Cys-rich. {ECO:0000255}.
COMPBIAS 2682 2806 Ser-rich. {ECO:0000255}.
COMPBIAS 3156 3177 Lys-rich. {ECO:0000255}.
COMPBIAS 3224 3255 Gly-rich.
MOD_RES 89 89 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 140 140 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 143 143 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 145 145 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 1586 1586 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 2645 2645 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 2731 2731 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 2749 2749 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 2751 2751 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 2795 2795 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 2801 2801 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 2831 2831 Phosphoserine.
{ECO:0000250|UniProtKB:Q7TPH6}.
MOD_RES 2833 2833 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 2882 2882 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 2947 2947 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 3052 3052 Phosphoserine.
{ECO:0000244|PubMed:17081983}.
MOD_RES 3440 3440 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:24275569}.
MOD_RES 3467 3467 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 3883 3883 Phosphothreonine.
{ECO:0000250|UniProtKB:Q7TPH6}.
MOD_RES 3893 3893 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 3894 3894 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
DISULFID 1710 1825 {ECO:0000250}.
VAR_SEQ 3901 3903 Missing (in isoform 2). {ECO:0000305}.
/FTId=VSP_014183.
VARIANT 1881 1881 A -> S (in dbSNP:rs35887505).
/FTId=VAR_052086.
VARIANT 2588 2588 V -> M (in dbSNP:rs9574002).
/FTId=VAR_030070.
CONFLICT 23 23 R -> P (in Ref. 1; AAC39928).
{ECO:0000305}.
CONFLICT 202 202 G -> V (in Ref. 1; AAC39928).
{ECO:0000305}.
CONFLICT 472 472 G -> R (in Ref. 1; AAC39928).
{ECO:0000305}.
CONFLICT 580 580 T -> I (in Ref. 1; AAC39928).
{ECO:0000305}.
CONFLICT 865 866 QL -> HV (in Ref. 1; AAC39928).
{ECO:0000305}.
CONFLICT 1474 1475 GV -> PL (in Ref. 1; AAC39928).
{ECO:0000305}.
CONFLICT 2101 2101 K -> M (in Ref. 1; AAC39928).
{ECO:0000305}.
CONFLICT 3163 3163 E -> GR (in Ref. 1; AAC39928).
{ECO:0000305}.
CONFLICT 3607 3607 A -> R (in Ref. 1; AAC39928).
{ECO:0000305}.
SEQUENCE 4640 AA; 510084 MW; 0557ADF6D26472D6 CRC64;
MPVPDGSVAA AGLGLGLPAA DSRGHYQLLL SGRALADRYR RIYTAALNDR DQGGGSAGHP
ASRNKKILNK KKLKRKQKSK SKVKTRSKSE NLENTVIIPD IKLHSNPSAF NIYCNVRHCV
LEWQKKEISL AAASKNSVQS GESDSDEEEE SKEPPIKLPK IIEVGLCEVF ELIKETRFSH
PSLCLRSLQA LLNVLQGQQP EGLQSEPPEV LESLFQLLLE ITVRSTGMND STGQSLTALS
CACLFSLVAS WGETGRTLQA ISAILTNNGS HACQTIQVPT ILNSLQRSVQ AVLVGKIQIQ
DWFSNGIKKA ALMHKWPLKE ISVDEDDQCL LQNDGFFLYL LCKDGLYKIG SGYSGTVRGH
IYNSTSRIRN RKEKKSWLGY AQGYLLYRDV NNHSMTAIRI SPETLEQDGT VMLPDCHTEG
QNILFTDGEY INQIAASRDD GFVVRIFATS TEPVLQQELQ LKLARKCLHA CGISLFDLEK
DLHIISTGFD EESAILGAGR EFALMKTANG KIYYTGKYQS LGIKQGGPSA GKWVELPITK
SPKIVHFSVG HDGSHALLVA EDGSIFFTGS ASKGEDGEST KSRRQSKPYK PKKIIKMEGK
IVVYTACNNG SSSVISKDGE LYMFGKDAIY SDSSSLVTDL KGHFVTQVAM GKAHTCVLMK
NGEVWTFGVN NKGQCGRDTG AMNQGGKGFG VENMATAMDE DLEEELDEKD EKSMMCPPGM
HKWKLEQCMV CTVCGDCTGY GASCVSSGRP DRVPGGICGC GSGESGCAVC GCCKACAREL
DGQEARQRGI LDAVKEMIPL DLLLAVPVPG VNIEEHLQLR QEEKRQRVIR RHRLEEGRGP
LVFAGPIFMN HREQALARLR SHPAQLKHKR DKHKDGSGER GEKDASKITT YPPGSVRFDC
ELRAVQVSCG FHHSVVLMEN GDVYTFGYGQ HGQLGHGDVN SRGCPTLVQA LPGPSTQVTA
GSNHTAVLLM DGQVFTFGSF SKGQLGRPIL DVPYWNAKPA PMPNIGSKYG RKATWIGASG
DQTFLRIDEA LINSHVLATS EIFASKHIIG LVPASISEPP PFKCLLINKV DGSCKTFNDS
EQEDLQGFGV CLDPVYDVIW RFRPNTRELW CYNAVVADAR LPSAADMQSR CSILSPELAL
PTGSRALTTR SHAALHILGC LDTLAAMQDL KMGVASTEEE TQAVMKVYSK EDYSVVNRFE
SHGGGWGYSA HSVEAIRFSA DTDILLGGLG LFGGRGEYTA KIKLFELGPD GGDHETDGDL
LAETDVLAYD CAAREKYAMM FDEPVLLQAG WWYVAWARVS GPSSDCGSHG QASITTDDGV
VFQFKSSKKS NNGTDVNAGQ IPQLLYRLPT SDGSASKGKQ QTSEPVHILK RSFARTVSVE
CFESLLSILH WSWTTLVLGV EELRGLKGFQ FTATLLDLER LRFVGTCCLR LLRVYTCEIY
PVSATGKAVV EETSKLAECI GKTRTLLRKI LSEGVDHCMV KLDNDPQGYL SQPLSLLEAV
LQECHNTFTA CFHSFYPTPA LQWACLCDLL NCLDQDIQEA NFKTSSSRLL AAVMSALCHT
SVKLTSIFPI AYDGEVLLRS IVKQVSTEND STLVHRFPLL VAHMEKLSQS EENISGMTSF
REVLEKMLVI VVLPVRNSLR RENELFSSHL VSNTCGLLAS IVSELTASAL GSEVDGLNSL
HSVKASANRF TKTSQGRSWN TGNGSPDAIC FSVDKPGIVV VGFSVYGGGG IHEYELEVLV
DDSEHAGDST HSHRWTSLEL VKGTYTTDDS PSDIAEIRLD KVVPLKENVK YAVRLRNYGS
RTANGDGGMT TVQCPDGVTF TFSTCSLSSN GTNQTRGQIP QILYYRSEFD GDLQSQLLSK
ANEEDKNCSR ALSVVSTVVR ASKDLLHRAL AVDADDIPEL LSSSSLFSML LPLIIAYIGP
VAAAIPKVAV EVFGLVQQLL PSVAILNQKY APPAFNPNQS TDSTTGNQPE QGLSACTTSS
HYAVIESEHP YKPACVMHYK VTFPECVRWM TIEFDPQCGT AQSEDVLRLL IPVRTVQNSG
YGPKLTSVHE NLNSWIELKK FSGSSGWPTM VLVLPGNEAL FSLETASDYV KDDKASFYGF
KCFAIGYEFS PGPDEGVIQL EKELANLGGV CAAALMKKDL ALPIGNELEE DLEILEEAAL
QVCKTHSGIL GKGLALSHSP TILEALEGNL PLQIQSNEQS FLDDFIACVP GSSGGRLARW
LQPDSYADPQ KTSLILNKDD IRCGWPTTIT VQTKDQYGDV VHVPNMKVEV KAVPVSQKKM
SLQQDQAKKP QRIPGSPAVT AASSNTDMTY GGLASPKLDV SYEPMIVKEA RYIAITMMKV
YENYSFEELR FASPTPKRPS ENMLIRVNND GTYCANWTPG AIGLYTLHVT IDGIEIDAGL
EVKVKDPPKG MIPPGTQLVK PKSEPQPNKV RKFVAKDSAG LRIRSHPSLQ SEQIGIVKVN
GTITFIDEIH NDDGVWLRLN DETIKKYVPN MNGYTEAWCL SFNQHLGKSL LVPVDESKTN
TDDFFKDINS CCPQEATMQE QDMPFLRGGP GMYKVVKTGP SGHNIRSCPN LRGIPIGMLV
LGNKVKAVGE VTNSEGTWVQ LDQNSMVEFC ESDEGEAWSL ARDRGGNQYL RHEDEQALLD
QNSQTPPPSP FSVQAFNKGA SCSAQGFDYG LGNSKGDRGN ISTSSKPAST SGKSELSSKH
SRSLKPDGRM SRTTADQKKP RGTESLSASE SLILKSDAAK LRSDSHSRSL SPNHNTLQTL
KSDGRMPSSS RAESPGPGSR LSSPKPKTLP ANRSSPSGAS SPRSSSPHDK NLPQKSTAPV
KTKLDPPRER SKSDSYTLDP DTLRKKKMPL TEPLRGRSTS PKPKSVPKDS TDSPGSENRA
PSPHVVQENL HSEVVEVCTS STLKTNSLTD STCDDSSEFK SVDEGSNKVH FSIGKAPLKD
EQEMRASPKI SRKCANRHTR PKKEKSSFLF KGDGSKPLEP AKQAMSPSVA ECARAVFASF
LWHEGIVHDA MACSSFLKFH PELSKEHAPI RSSLNSQQPT EEKETKLKNR HSLEISSALN
MFNIAPHGPD ISKMGSINKN KVLSMLKEPP LHEKCEDGKT ETTFEMSMHN TMKSKSPLPL
TLQHLVAFWE DISLATIKAA SQNMIFPSPG SCAVLKKKEC EKENKKSKKE KKKKEKAEVR
PRGNLFGEMA QLAVGGPEKD TICELCGESH PYPVTYHMRQ AHPGCGRYAG GQGYNSIGHF
CGGWAGNCGD GGIGGSTWYL VCDRCREKYL REKQAAAREK VKQSRRKPMQ VKTPRALPTM
EAHQVIKANA LFLLSLSSAA EPSILCYHPA KPFQSQLPSV KEGISEDLPV KMPCLYLQTL
ARHHHENFVG YQDDNLFQDE MRYLRSTSVP APYISVTPDA SPNVFEEPES NMKSMPPSLE
TSPITDTDLA KRTVFQRSYS VVASEYDKQH SILPARVKAI PRRRVNSGDT EVGSSLLRHP
SPELSRLISA HSSLSKGERN FQWPVLAFVI QHHDLEGLEI AMKQALRKSA CRVFAMEAFN
WLLCNVIQTT SLHDILWHFV ASLTPAPVEP EEEEDEENKT SKENSEQEKD TRVCEHPLSD
IVIAGEAAHP LPHTFHRLLQ TISDLMMSLP SGSSLQQMAL RCWSLKFKQS DHQFLHQSNV
FHHINNILSK SDDGDSEESF SISIQSGFEA MSQELCIVMC LKDLTSIVDI KTSSRPAMIG
SLTDGSTETF WESGDEDKNK TKNITINCVK GINARYVSVH VDNSRDLGNK VTSMTFLTGK
AVEDLCRIKQ VDLDSRHIGW VTSELPGGDN HIIKIELKGP ENTLRVRQVK VLGWKDGEST
KIAGQISASV AQQRNCEAET LRVFRLITSQ VFGKLISGDA EPTPEQEEKA LLSSPEGEEK
VYNATSDADL KEHMVGIIFS RSKLTNLQKQ VCAHIVQAIR MEATRVREEW EHAISSKENA
NSQPNDEDAS SDAYCFELLS MVLALSGSNV GRQYLAQQLT LLQDLFSLLH TASPRVQRQV
TSLLRRVLPE VTPSRLASII GVKSLPPADI SDIIHSTEKG DWNKLGILDM FLGCIAKALT
VQLKAKGTTI TGTAGTTVGK GVTTVTLPMI FNSSYLRRGE SHWWMKGSTP TQISEIIIKL
IKDMAAGHLS EAWSRVTKNA IAETIIALTK MEEEFRSPVR CIATTRLWLA LASLCVLDQD
HVDRLSSGRW MGKDGQQKQM PMCDNHDDGE TAAIILCNVC GNLCTDCDRF LHLHRRTKTH
QRQVFKEEEE AIKVDLHEGC GRTKLFWLMA LADSKTMKAM VEFREHTGKP TTSSSEACRF
CGSRSGTELS AVGSVCSDAD CQEYAKIACS KTHPCGHPCG GVKNEEHCLP CLHGCDKSAT
SLKQDADDMC MICFTEALSA APAIQLDCSH IFHLQCCRRV LENRWLGPRI TFGFISCPIC
KNKINHIVLK DLLDPIKELY EDVRRKALMR LEYEGLHKSE AITTPGVRFY NDPAGYAMNR
YAYYVCYKCR KAYFGGEARC DAEAGRGDDY DPRELICGAC SDVSRAQMCP KHGTDFLEYK
CRYCCSVAVF FCFGTTHFCN ACHDDFQRMT SIPKEELPHC PAGPKGKQLE GTECPLHVVH
PPTGEEFALG CGVCRNAHTF


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