MYBB_HUMAN
ID MYBB_HUMAN Reviewed; 700 AA.
AC P10244; B2RBS5; B7Z8D9; F8W6N6; Q53F07;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 222.
DE RecName: Full=Myb-related protein B;
DE Short=B-Myb;
DE AltName: Full=Myb-like protein 2;
GN Name=MYBL2; Synonyms=BMYB;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=3060855; DOI=10.1093/nar/16.23.11075;
RA Nomura N., Takahashi M., Matsui M., Ishii S., Date T., Sasamoto S.,
RA Ishizaki R.;
RT "Isolation of human cDNA clones of myb-related genes, A-myb and B-myb.";
RL Nucleic Acids Res. 16:11075-11089(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP GLY-427.
RC TISSUE=Brain, and Thymus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, and Eye;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP PHOSPHORYLATION AT THR-444; THR-487; THR-494 AND SER-577.
RX PubMed=9840932; DOI=10.1038/sj.onc.1202503;
RA Saville M.K., Watson R.J.;
RT "The cell-cycle regulated transcription factor B-Myb is phosphorylated by
RT cyclin A/Cdk2 at sites that enhance its transactivation properties.";
RL Oncogene 17:2679-2689(1998).
RN [8]
RP PHOSPHORYLATION AT THR-440; THR-444; THR-494; THR-520 AND SER-577.
RX PubMed=10095772; DOI=10.1046/j.1432-1327.1999.00191.x;
RA Bartsch O., Horstmann S., Toprak K., Klempnauer K.H., Ferrari S.;
RT "Identification of cyclin A/Cdk2 phosphorylation sites in B-Myb.";
RL Eur. J. Biochem. 260:384-391(1999).
RN [9]
RP FUNCTION.
RX PubMed=10770937; DOI=10.1074/jbc.m002055200;
RA Cervellera M., Raschella G., Santilli G., Tanno B., Ventura A., Mancini C.,
RA Sevignani C., Calabretta B., Sala A.;
RT "Direct transactivation of the anti-apoptotic gene apolipoprotein J
RT (clusterin) by B-MYB.";
RL J. Biol. Chem. 275:21055-21060(2000).
RN [10]
RP NUCLEAR LOCALIZATION SIGNALS.
RX PubMed=8062924; DOI=10.1016/0014-5793(94)00733-0;
RA Takemoto Y., Tashiro S., Handa H., Ishii S.;
RT "Multiple nuclear localization signals of the B-myb gene product.";
RL FEBS Lett. 350:55-60(1994).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-266, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [12]
RP IDENTIFICATION IN THE DREAM COMPLEX.
RX PubMed=17671431; DOI=10.4161/cc.6.15.4512;
RA Schmit F., Korenjak M., Mannefeld M., Schmitt K., Franke C., von Eyss B.,
RA Gagrica S., Haenel F., Brehm A., Gaubatz S.;
RT "LINC, a human complex that is related to pRB-containing complexes in
RT invertebrates regulates the expression of G2/M genes.";
RL Cell Cycle 6:1903-1913(2007).
RN [13]
RP IDENTIFICATION IN THE DREAM COMPLEX.
RX PubMed=17531812; DOI=10.1016/j.molcel.2007.04.015;
RA Litovchick L., Sadasivam S., Florens L., Zhu X., Swanson S.K.,
RA Velmurugan S., Chen R., Washburn M.P., Liu X.S., DeCaprio J.A.;
RT "Evolutionarily conserved multisubunit RBL2/p130 and E2F4 protein complex
RT represses human cell cycle-dependent genes in quiescence.";
RL Mol. Cell 26:539-551(2007).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-241, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-241, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-241, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-241; SER-282; SER-393 AND
RP THR-505, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [19]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-197; LYS-509; LYS-546 AND
RP LYS-639, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [20]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-197; LYS-509; LYS-596 AND
RP LYS-639, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
RA Vertegaal A.C.;
RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
RL Cell Rep. 10:1778-1791(2015).
RN [21]
RP INTERACTION WITH CCNF.
RX PubMed=25557911; DOI=10.1038/ncomms6800;
RA Klein D.K., Hoffmann S., Ahlskog J.K., O'Hanlon K., Quaas M., Larsen B.D.,
RA Rolland B., Roesner H.I., Walter D., Kousholt A.N., Menzel T., Lees M.,
RA Johansen J.V., Rappsilber J., Engeland K., Soerensen C.S.;
RT "Cyclin F suppresses B-Myb activity to promote cell cycle checkpoint
RT control.";
RL Nat. Commun. 6:5800-5800(2015).
RN [22]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-104; LYS-194; LYS-197; LYS-275;
RP LYS-411; LYS-447; LYS-482; LYS-499; LYS-509; LYS-523; LYS-533; LYS-546;
RP LYS-584; LYS-596; LYS-625; LYS-639 AND LYS-648, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
CC -!- FUNCTION: Transcription factor involved in the regulation of cell
CC survival, proliferation, and differentiation. Transactivates the
CC expression of the CLU gene. {ECO:0000269|PubMed:10770937}.
CC -!- SUBUNIT: Component of the DREAM complex (also named LINC complex) at
CC least composed of E2F4, E2F5, LIN9, LIN37, LIN52, LIN54, MYBL1, MYBL2,
CC RBL1, RBL2, RBBP4, TFDP1 and TFDP2. The complex exists in quiescent
CC cells where it represses cell cycle-dependent genes. It dissociates in
CC S phase when LIN9, LIN37, LIN52 and LIN54 form a subcomplex that binds
CC to MYBL22. Interacts with CCNF (via the Cyclin N-terminal domain)
CC (PubMed:25557911). {ECO:0000269|PubMed:17531812,
CC ECO:0000269|PubMed:17671431, ECO:0000269|PubMed:25557911}.
CC -!- INTERACTION:
CC P10244; Q6MZP7: LIN54; NbExp=4; IntAct=EBI-1389468, EBI-1389411;
CC P10244; Q5TKA1: LIN9; NbExp=7; IntAct=EBI-1389468, EBI-1389424;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P10244-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P10244-2; Sequence=VSP_053987;
CC -!- PTM: Phosphorylated by cyclin A/CDK2 during S-phase. Phosphorylation at
CC Thr-520 is probably involved in transcriptional activity.
CC {ECO:0000269|PubMed:10095772, ECO:0000269|PubMed:9840932}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/MYBL2ID41469ch20q13.html";
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DR EMBL; X13293; CAA31655.1; -; mRNA.
DR EMBL; AK303249; BAH13925.1; -; mRNA.
DR EMBL; AK314791; BAG37322.1; -; mRNA.
DR EMBL; AK223482; BAD97202.1; -; mRNA.
DR EMBL; AL121886; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471077; EAW75951.1; -; Genomic_DNA.
DR EMBL; BC007585; AAH07585.1; -; mRNA.
DR EMBL; BC053555; AAH53555.1; -; mRNA.
DR CCDS; CCDS13322.1; -. [P10244-1]
DR CCDS; CCDS63276.1; -. [P10244-2]
DR PIR; S01991; S01991.
DR RefSeq; NP_001265539.1; NM_001278610.1. [P10244-2]
DR RefSeq; NP_002457.1; NM_002466.3. [P10244-1]
DR PDB; 6C48; X-ray; 2.32 A; C/F=657-688.
DR PDBsum; 6C48; -.
DR AlphaFoldDB; P10244; -.
DR BMRB; P10244; -.
DR SMR; P10244; -.
DR BioGRID; 110690; 128.
DR CORUM; P10244; -.
DR IntAct; P10244; 41.
DR MINT; P10244; -.
DR STRING; 9606.ENSP00000217026; -.
DR GlyGen; P10244; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P10244; -.
DR PhosphoSitePlus; P10244; -.
DR BioMuta; MYBL2; -.
DR DMDM; 127584; -.
DR EPD; P10244; -.
DR jPOST; P10244; -.
DR MassIVE; P10244; -.
DR MaxQB; P10244; -.
DR PaxDb; P10244; -.
DR PeptideAtlas; P10244; -.
DR PRIDE; P10244; -.
DR ProteomicsDB; 29817; -.
DR ProteomicsDB; 52586; -. [P10244-1]
DR Antibodypedia; 4478; 416 antibodies from 40 providers.
DR DNASU; 4605; -.
DR Ensembl; ENST00000217026.5; ENSP00000217026.4; ENSG00000101057.16. [P10244-1]
DR Ensembl; ENST00000396863.8; ENSP00000380072.4; ENSG00000101057.16. [P10244-2]
DR GeneID; 4605; -.
DR KEGG; hsa:4605; -.
DR MANE-Select; ENST00000217026.5; ENSP00000217026.4; NM_002466.4; NP_002457.1.
DR UCSC; uc002xlb.3; human. [P10244-1]
DR CTD; 4605; -.
DR DisGeNET; 4605; -.
DR GeneCards; MYBL2; -.
DR HGNC; HGNC:7548; MYBL2.
DR HPA; ENSG00000101057; Group enriched (bone marrow, lymphoid tissue).
DR MIM; 601415; gene.
DR neXtProt; NX_P10244; -.
DR OpenTargets; ENSG00000101057; -.
DR PharmGKB; PA31348; -.
DR VEuPathDB; HostDB:ENSG00000101057; -.
DR eggNOG; KOG0048; Eukaryota.
DR GeneTree; ENSGT00940000156091; -.
DR HOGENOM; CLU_015440_1_0_1; -.
DR InParanoid; P10244; -.
DR OMA; EFPKQED; -.
DR OrthoDB; 219341at2759; -.
DR PhylomeDB; P10244; -.
DR TreeFam; TF326257; -.
DR PathwayCommons; P10244; -.
DR Reactome; R-HSA-1362300; Transcription of E2F targets under negative control by p107 (RBL1) and p130 (RBL2) in complex with HDAC1.
DR Reactome; R-HSA-156711; Polo-like kinase mediated events.
DR Reactome; R-HSA-8869496; TFAP2A acts as a transcriptional repressor during retinoic acid induced cell differentiation.
DR SignaLink; P10244; -.
DR SIGNOR; P10244; -.
DR BioGRID-ORCS; 4605; 399 hits in 1121 CRISPR screens.
DR ChiTaRS; MYBL2; human.
DR GeneWiki; MYBL2; -.
DR GenomeRNAi; 4605; -.
DR Pharos; P10244; Tbio.
DR PRO; PR:P10244; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; P10244; protein.
DR Bgee; ENSG00000101057; Expressed in endometrium epithelium and 134 other tissues.
DR Genevisible; P10244; HS.
DR GO; GO:0031523; C:Myb complex; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:NTNU_SB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEA:Ensembl.
DR GO; GO:0000278; P:mitotic cell cycle; IBA:GO_Central.
DR GO; GO:0090307; P:mitotic spindle assembly; IEA:Ensembl.
DR GO; GO:0043525; P:positive regulation of neuron apoptotic process; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR CDD; cd00167; SANT; 3.
DR InterPro; IPR015395; C-myb_C.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR017930; Myb_dom.
DR InterPro; IPR028311; MYBL2.
DR InterPro; IPR001005; SANT/Myb.
DR PANTHER; PTHR45614:SF30; PTHR45614:SF30; 2.
DR Pfam; PF09316; Cmyb_C; 1.
DR Pfam; PF00249; Myb_DNA-binding; 1.
DR SMART; SM00717; SANT; 3.
DR SUPFAM; SSF46689; SSF46689; 2.
DR PROSITE; PS51294; HTH_MYB; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; DNA-binding; Isopeptide bond; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..700
FT /note="Myb-related protein B"
FT /id="PRO_0000197058"
FT DOMAIN 26..77
FT /note="HTH myb-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT DOMAIN 78..133
FT /note="HTH myb-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT DOMAIN 134..184
FT /note="HTH myb-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT DNA_BIND 54..77
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT DNA_BIND 106..129
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT DNA_BIND 157..180
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT REGION 212..287
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 391..412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 411..417
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000269|PubMed:8062924"
FT MOTIF 564..584
FT /note="Bipartite nuclear localization signal"
FT COMPBIAS 214..234
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 265..282
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 241
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 266
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17081983"
FT MOD_RES 282
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 393
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 440
FT /note="Phosphothreonine; by CDK2"
FT /evidence="ECO:0000269|PubMed:10095772"
FT MOD_RES 444
FT /note="Phosphothreonine; by CDK2"
FT /evidence="ECO:0000269|PubMed:10095772,
FT ECO:0000269|PubMed:9840932"
FT MOD_RES 487
FT /note="Phosphothreonine; by CDK2"
FT /evidence="ECO:0000269|PubMed:9840932"
FT MOD_RES 494
FT /note="Phosphothreonine; by CDK2"
FT /evidence="ECO:0000269|PubMed:10095772,
FT ECO:0000269|PubMed:9840932"
FT MOD_RES 505
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 520
FT /note="Phosphothreonine; by CDK2"
FT /evidence="ECO:0000269|PubMed:10095772"
FT MOD_RES 577
FT /note="Phosphoserine; by CDK2"
FT /evidence="ECO:0000269|PubMed:10095772,
FT ECO:0000269|PubMed:9840932"
FT CROSSLNK 104
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 194
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 197
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733"
FT CROSSLNK 275
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 411
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 447
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 482
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 499
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 509
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733"
FT CROSSLNK 523
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 533
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 546
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 584
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 596
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25772364,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 625
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 639
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733"
FT CROSSLNK 648
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 39..62
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_053987"
FT VARIANT 341
FT /note="N -> S (in dbSNP:rs6017146)"
FT /id="VAR_050190"
FT VARIANT 427
FT /note="S -> G (in dbSNP:rs2070235)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_020422"
FT VARIANT 595
FT /note="V -> M (in dbSNP:rs7660)"
FT /id="VAR_050191"
FT VARIANT 624
FT /note="I -> M (in dbSNP:rs11556379)"
FT /id="VAR_050192"
FT CONFLICT 184
FT /note="V -> A (in Ref. 3; BAD97202)"
FT /evidence="ECO:0000305"
FT HELIX 663..667
FT /evidence="ECO:0007829|PDB:6C48"
FT HELIX 672..685
FT /evidence="ECO:0007829|PDB:6C48"
SQ SEQUENCE 700 AA; 78764 MW; D91B28B3DAB94061 CRC64;
MSRRTRCEDL DELHYQDTDS DVPEQRDSKC KVKWTHEEDE QLRALVRQFG QQDWKFLASH
FPNRTDQQCQ YRWLRVLNPD LVKGPWTKEE DQKVIELVKK YGTKQWTLIA KHLKGRLGKQ
CRERWHNHLN PEVKKSCWTE EEDRIICEAH KVLGNRWAEI AKMLPGRTDN AVKNHWNSTI
KRKVDTGGFL SESKDCKPPV YLLLELEDKD GLQSAQPTEG QGSLLTNWPS VPPTIKEEEN
SEEELAAATT SKEQEPIGTD LDAVRTPEPL EEFPKREDQE GSPPETSLPY KWVVEAANLL
IPAVGSSLSE ALDLIESDPD AWCDLSKFDL PEEPSAEDSI NNSLVQLQAS HQQQVLPPRQ
PSALVPSVTE YRLDGHTISD LSRSSRGELI PISPSTEVGG SGIGTPPSVL KRQRKRRVAL
SPVTENSTSL SFLDSCNSLT PKSTPVKTLP FSPSQFLNFW NKQDTLELES PSLTSTPVCS
QKVVVTTPLH RDKTPLHQKH AAFVTPDQKY SMDNTPHTPT PFKNALEKYG PLKPLPQTPH
LEEDLKEVLR SEAGIELIIE DDIRPEKQKR KPGLRRSPIK KVRKSLALDI VDEDVKLMMS
TLPKSLSLPT TAPSNSSSLT LSGIKEDNSL LNQGFLQAKP EKAAVAQKPR SHFTTPAPMS
SAWKTVACGG TRDQLFMQEK ARQLLGRLKP SHTSRTLILS
