MYBB_MOUSE
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 03-AUG-2022, entry version 186.
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}.
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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; 13.
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; P48972; -.
DR PeptideAtlas; P48972; -.
DR PRIDE; P48972; -.
DR ProteomicsDB; 287647; -.
DR Antibodypedia; 4478; 416 antibodies from 40 providers.
DR DNASU; 17865; -.
DR Ensembl; ENSMUST00000018005; ENSMUSP00000018005; ENSMUSG00000017861.
DR GeneID; 17865; -.
DR KEGG; mmu:17865; -.
DR UCSC; uc008nsl.1; mouse.
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; EFPKQED; -.
DR OrthoDB; 219341at2759; -.
DR PhylomeDB; P48972; -.
DR TreeFam; TF326257; -.
DR BioGRID-ORCS; 17865; 24 hits in 78 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 135 other tissues.
DR ExpressionAtlas; P48972; baseline and differential.
DR Genevisible; P48972; MM.
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 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; 1.
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; 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
