ID MYBB_MOUSE Reviewed; 704 AA. AC P48972; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 27-MAR-2024, entry version 195. DE RecName: Full=Myb-related protein B; DE Short=B-Myb; DE AltName: Full=Myb-like protein 2; GN Name=Mybl2; Synonyms=Bmyb; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE. RX PubMed=1501895; RA Lam E.W., Robinson C., Watson R.J.; RT "Characterization and cell cycle-regulated expression of mouse B-myb."; RL Oncogene 7:1885-1890(1992). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Skin; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Limb; 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 [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-6. RX PubMed=8334989; DOI=10.1002/j.1460-2075.1993.tb05932.x; RA Lam E.W., Watson R.J.; RT "An E2F-binding site mediates cell-cycle regulated repression of mouse B- RT myb transcription."; RL EMBO J. 12:2705-2713(1993). RN [5] RP STRUCTURE BY NMR OF 31-78. RG RIKEN structural genomics initiative (RSGI); RT "Solution structure of RSGI RUH-050, a myb DNA-binding domain in mouse."; RL Submitted (JUN-2006) to the PDB data bank. CC -!- FUNCTION: Transcription factor involved in the regulation of cell CC survival, proliferation, and differentiation. Transactivates the CC expression of the CLU gene (By similarity). {ECO:0000250}. 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 MYBL2 (By similarity). Interacts with CCNF (via the Cyclin N- CC terminal domain) (By similarity). {ECO:0000250|UniProtKB:P10244}. CC -!- SUBCELLULAR LOCATION: Nucleus. CC -!- PTM: Phosphorylated by cyclin A/CDK2 during S-phase. Phosphorylation at CC Thr-524 is probably involved in transcriptional activity (By CC similarity). {ECO:0000250}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X70472; CAA49898.1; -; mRNA. DR EMBL; AK028497; BAC25979.1; -; mRNA. DR EMBL; BC050842; AAH50842.1; -; mRNA. DR EMBL; X73028; CAA51511.1; -; Genomic_DNA. DR CCDS; CCDS17006.1; -. DR PIR; S33704; S33704. DR RefSeq; NP_032678.1; NM_008652.2. DR PDB; 2D9A; NMR; -; A=31-77. DR PDBsum; 2D9A; -. DR AlphaFoldDB; P48972; -. DR BMRB; P48972; -. DR SMR; P48972; -. DR BioGRID; 201633; 14. DR IntAct; P48972; 3. DR STRING; 10090.ENSMUSP00000018005; -. DR iPTMnet; P48972; -. DR PhosphoSitePlus; P48972; -. DR EPD; P48972; -. DR jPOST; P48972; -. DR MaxQB; P48972; -. DR PaxDb; 10090-ENSMUSP00000018005; -. DR PeptideAtlas; P48972; -. DR ProteomicsDB; 287647; -. DR Antibodypedia; 4478; 485 antibodies from 40 providers. DR DNASU; 17865; -. DR Ensembl; ENSMUST00000018005.10; ENSMUSP00000018005.4; ENSMUSG00000017861.12. DR GeneID; 17865; -. DR KEGG; mmu:17865; -. DR UCSC; uc008nsl.1; mouse. DR AGR; MGI:101785; -. DR CTD; 4605; -. DR MGI; MGI:101785; Mybl2. DR VEuPathDB; HostDB:ENSMUSG00000017861; -. DR eggNOG; KOG0048; Eukaryota. DR GeneTree; ENSGT00940000156091; -. DR HOGENOM; CLU_015440_1_0_1; -. DR InParanoid; P48972; -. DR OMA; EWETVVC; -. DR OrthoDB; 20023at2759; -. DR PhylomeDB; P48972; -. DR TreeFam; TF326257; -. DR BioGRID-ORCS; 17865; 25 hits in 83 CRISPR screens. DR ChiTaRS; Mybl2; mouse. DR EvolutionaryTrace; P48972; -. DR PRO; PR:P48972; -. DR Proteomes; UP000000589; Chromosome 2. DR RNAct; P48972; Protein. DR Bgee; ENSMUSG00000017861; Expressed in animal zygote and 138 other cell types or tissues. DR ExpressionAtlas; P48972; baseline and differential. DR Genevisible; P48972; MM. DR GO; GO:0005829; C:cytosol; ISO:MGI. DR GO; GO:0031523; C:Myb complex; IDA:MGI. DR GO; GO:0005654; C:nucleoplasm; ISO:MGI. DR GO; GO:0005634; C:nucleus; IDA:MGI. DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:MGI. 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; ISO:MGI. DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI. DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEP:MGI. DR GO; GO:0000278; P:mitotic cell cycle; IBA:GO_Central. DR GO; GO:0090307; P:mitotic spindle assembly; IDA:MGI. DR GO; GO:0043525; P:positive regulation of neuron apoptotic process; ISO:MGI. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI. DR CDD; cd00167; SANT; 3. DR Gene3D; 1.10.10.60; Homeodomain-like; 3. DR InterPro; IPR015395; C-myb_C. DR InterPro; IPR009057; Homeobox-like_sf. DR InterPro; IPR017930; Myb_dom. DR InterPro; IPR001005; SANT/Myb. DR PANTHER; PTHR45614; MYB PROTEIN-RELATED; 1. DR PANTHER; PTHR45614:SF30; MYB-RELATED PROTEIN B; 1. DR Pfam; PF09316; Cmyb_C; 1. DR Pfam; PF13921; Myb_DNA-bind_6; 1. DR Pfam; PF00249; Myb_DNA-binding; 1. DR SMART; SM00717; SANT; 3. DR SUPFAM; SSF46689; Homeodomain-like; 2. DR PROSITE; PS51294; HTH_MYB; 3. PE 1: Evidence at protein level; KW 3D-structure; DNA-binding; Isopeptide bond; Nucleus; Phosphoprotein; KW Reference proteome; Repeat; Transcription; Transcription regulation; KW Ubl conjugation. FT CHAIN 1..704 FT /note="Myb-related protein B" FT /id="PRO_0000197059" 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 325..412 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 603..626 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 336..369 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 607..626 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 267 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P10244" FT MOD_RES 282 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P10244" FT MOD_RES 396 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P10244" FT MOD_RES 443 FT /note="Phosphothreonine; by CDK2" FT /evidence="ECO:0000250|UniProtKB:P10244" FT MOD_RES 447 FT /note="Phosphothreonine; by CDK2" FT /evidence="ECO:0000250|UniProtKB:P10244" FT MOD_RES 490 FT /note="Phosphothreonine; by CDK2" FT /evidence="ECO:0000250|UniProtKB:P10244" FT MOD_RES 497 FT /note="Phosphothreonine; by CDK2" FT /evidence="ECO:0000250|UniProtKB:P10244" FT MOD_RES 524 FT /note="Phosphothreonine; by CDK2" FT /evidence="ECO:0000250|UniProtKB:P10244" FT MOD_RES 581 FT /note="Phosphoserine; by CDK2" FT /evidence="ECO:0000250|UniProtKB:P10244" FT CROSSLNK 104 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P10244" FT CROSSLNK 197 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P10244" FT CROSSLNK 275 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P10244" FT CROSSLNK 414 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P10244" FT CROSSLNK 450 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P10244" FT CROSSLNK 485 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P10244" FT CROSSLNK 502 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P10244" FT CROSSLNK 513 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P10244" FT CROSSLNK 527 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P10244" FT CROSSLNK 537 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P10244" FT CROSSLNK 550 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P10244" FT CROSSLNK 588 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P10244" FT CROSSLNK 600 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P10244" FT CROSSLNK 629 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P10244" FT CROSSLNK 643 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P10244" FT CROSSLNK 652 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P10244" FT HELIX 36..48 FT /evidence="ECO:0007829|PDB:2D9A" FT HELIX 54..60 FT /evidence="ECO:0007829|PDB:2D9A" FT STRAND 62..64 FT /evidence="ECO:0007829|PDB:2D9A" FT HELIX 66..75 FT /evidence="ECO:0007829|PDB:2D9A" SQ SEQUENCE 704 AA; 79103 MW; 0EF09C1EE2184E47 CRC64; MSRRTRCEDL DELHYQDVDS DLLEQRDNRC KVKWTHEEDE QLRALVRQFG QQDWKFLASH FPNRTDQQCQ YRWLRVLNPD LVKGPWTKEE DQKVIELVKK YGTKQWTLIA KHLKGRLGKQ CRERWHNHLN PEVKKSCWTE EEDRIICEAH KVLGNRWAEI AKMLPGRTDN AVKNHWNSTI KRKVDTGGFP AESRDCKPVY LLLELEDKEQ HQGVQPVDGQ GSLVSSWPLV PSIVKEESSE EEIAIAATSA KELGHEPVPA DLGEVRTPEP PESLKREYQE FSSPETSLPY KWVVEAANLL IPAVGSSLSE ALDLIESDPD AWCDLSKFDL PEEPSTEGSV VSSPVQPQTS QQQQEEALQS SQQAATPGPS VTEYRLDGHT ISDLSRSSRG ELIPISPSTE FGGSGIGTPP SVLKRQKKRR VALSPVTENS ASLSFLDSCN SLTPKSTPVK TLPFSPSQFL NFWNKQDTLE LESPSLTSTP VCSQKVVVTT PLHRDKTPLH QKYPSSEVLP DQKYSMDNTP HTPTPFKNAL EKYGPLKPLP QTPHLEEDLK EVLRSEAGME LIIEDDMRPE KQKRKPGLRR SPIKKVRKSL ALDIMDEDGK LMSSTMPKPL SLPTSVTPSS CGFTSPGSKE GNSLLNQGFL QAKPEKVVAA QKTRSHIPTP APMTHAWKTV ACGGTKDQLF MQEKARQLLS RLKSSHTSRT LILS //