MYBA_MOUSE
ID MYBA_MOUSE Reviewed; 751 AA.
AC P51960;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Myb-related protein A {ECO:0000303|PubMed:7813437};
DE Short=A-Myb {ECO:0000303|PubMed:7813437};
DE AltName: Full=Myb-like protein 1;
GN Name=Mybl1; Synonyms=Amyb;
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 [MRNA] (ISOFORM LONG), FUNCTION, AND TISSUE
RP SPECIFICITY.
RC STRAIN=BALB/cJ;
RX PubMed=7813437; DOI=10.1002/j.1460-2075.1994.tb06945.x;
RA Trauth K., Mutschler B., Jenkins N.A., Gilbert D.J., Copeland N.G.,
RA Klempnauer K.H.;
RT "Mouse A-myb encodes a trans-activator and is expressed in mitotically
RT active cells of the developing central nervous system, adult testis and B
RT lymphocytes.";
RL EMBO J. 13:5994-6005(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT), AND TISSUE SPECIFICITY.
RC STRAIN=BALB/cJ; TISSUE=Testis;
RX PubMed=8084617;
RA Mettus R.V., Litvin J., Wali A., Toscani A., Latham K., Hatton K.,
RA Reddy E.P.;
RT "Murine A-myb: evidence for differential splicing and tissue-specific
RT expression.";
RL Oncogene 9:3077-3086(1994).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND MUTAGENESIS OF
RP ALA-213.
RX PubMed=21750041; DOI=10.1242/dev.067645;
RA Bolcun-Filas E., Bannister L.A., Barash A., Schimenti K.J., Hartford S.A.,
RA Eppig J.J., Handel M.A., Shen L., Schimenti J.C.;
RT "A-MYB (MYBL1) transcription factor is a master regulator of male
RT meiosis.";
RL Development 138:3319-3330(2011).
RN [5]
RP FUNCTION, AND MUTAGENESIS OF ALA-213.
RX PubMed=23523368; DOI=10.1016/j.molcel.2013.02.016;
RA Li X.Z., Roy C.K., Dong X., Bolcun-Filas E., Wang J., Han B.W., Xu J.,
RA Moore M.J., Schimenti J.C., Weng Z., Zamore P.D.;
RT "An ancient transcription factor initiates the burst of piRNA production
RT during early meiosis in mouse testes.";
RL Mol. Cell 50:67-81(2013).
RN [6]
RP FUNCTION.
RX PubMed=29848638; DOI=10.1242/dev.164723;
RA Zhang D., Xie D., Lin X., Ma L., Chen J., Zhang D., Wang Y., Duo S.,
RA Feng Y., Zheng C., Jiang B., Ning Y., Han C.;
RT "The transcription factor SOX30 is a key regulator of mouse
RT spermiogenesis.";
RL Development 145:0-0(2018).
CC -!- FUNCTION: Transcription factor that specifically recognizes the
CC sequence 5'-YAAC[GT]G-3' (PubMed:7813437, PubMed:23523368). Acts as a
CC master regulator of male meiosis by promoting expression of piRNAs:
CC activates expression of both piRNA precursor RNAs and expression of
CC protein-coding genes involved in piRNA metabolism, such as PIWIL1
CC (PubMed:21750041, PubMed:23523368). The piRNA metabolic process
CC mediates the repression of transposable elements during meiosis by
CC forming complexes composed of piRNAs and Piwi proteins and governs the
CC methylation and subsequent repression of transposons, which is
CC essential for the germline integrity (PubMed:23523368). Transcriptional
CC activator of SOX30 (PubMed:29848638). {ECO:0000269|PubMed:21750041,
CC ECO:0000269|PubMed:23523368, ECO:0000269|PubMed:29848638,
CC ECO:0000269|PubMed:7813437}.
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). {ECO:0000250|UniProtKB:P10243}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21750041}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Long;
CC IsoId=P51960-1; Sequence=Displayed;
CC Name=Short;
CC IsoId=P51960-2; Sequence=VSP_003300;
CC -!- TISSUE SPECIFICITY: Predominantly in the testis. Very low levels in the
CC ovaries, spleen and brain. {ECO:0000269|PubMed:7813437,
CC ECO:0000269|PubMed:8084617}.
CC -!- DEVELOPMENTAL STAGE: During embryogenesis it is predominantly expressed
CC in several regions of the developing central nervous system and the
CC urogenital ridge. Expression in the CNS is confined to the neural tube,
CC the hindbrain, the neural retina and the olfactory epithelium, and
CC coincides with the presence of proliferating immature neuronal
CC precursor cells. In the adult mouse, A-Myb is expressed at high levels
CC in type A spermatogonia (stem cells), and preleptotene and pachytene
CC spermatocytes, with concomitant down-regulation of expression upon
CC terminal differentiation of these cells into mature spermatozoa, and in
CC B lymphocytes located in germinal centers of the spleen
CC (PubMed:7813437, PubMed:8084617). Present in mid-late pachytene and
CC diplotene spermatocytes, but not in late zygotene/early pachytene cells
CC (at protein level) (PubMed:21750041). {ECO:0000269|PubMed:21750041,
CC ECO:0000269|PubMed:7813437, ECO:0000269|PubMed:8084617}.
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DR EMBL; X82327; CAA57771.1; -; mRNA.
DR EMBL; L35261; AAA62182.1; -; mRNA.
DR CCDS; CCDS35510.1; -. [P51960-1]
DR CCDS; CCDS69861.1; -. [P51960-2]
DR PIR; I49497; I49497.
DR RefSeq; NP_032677.2; NM_008651.3.
DR AlphaFoldDB; P51960; -.
DR SMR; P51960; -.
DR STRING; 10090.ENSMUSP00000086034; -.
DR iPTMnet; P51960; -.
DR PhosphoSitePlus; P51960; -.
DR PaxDb; P51960; -.
DR PRIDE; P51960; -.
DR ProteomicsDB; 286091; -. [P51960-1]
DR ProteomicsDB; 286092; -. [P51960-2]
DR DNASU; 17864; -.
DR GeneID; 17864; -.
DR KEGG; mmu:17864; -.
DR CTD; 4603; -.
DR MGI; MGI:99925; Mybl1.
DR eggNOG; KOG0048; Eukaryota.
DR InParanoid; P51960; -.
DR OrthoDB; 219341at2759; -.
DR PhylomeDB; P51960; -.
DR TreeFam; TF326257; -.
DR BioGRID-ORCS; 17864; 4 hits in 75 CRISPR screens.
DR ChiTaRS; Mybl1; mouse.
DR PRO; PR:P51960; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P51960; protein.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IDA:UniProtKB.
DR GO; GO:1990841; F:promoter-specific chromatin binding; IDA:MGI.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0007141; P:male meiosis I; IMP:UniProtKB.
DR GO; GO:0000278; P:mitotic cell cycle; IBA:GO_Central.
DR GO; GO:0010529; P:negative regulation of transposition; IMP:UniProtKB.
DR GO; GO:1990511; P:piRNA biosynthetic process; IDA:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0007283; P:spermatogenesis; IMP:UniProtKB.
DR CDD; cd00167; SANT; 3.
DR InterPro; IPR015395; C-myb_C.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR017930; Myb_dom.
DR InterPro; IPR028317; MYBL1.
DR InterPro; IPR001005; SANT/Myb.
DR InterPro; IPR012642; Tscrpt_reg_Wos2-domain.
DR PANTHER; PTHR45614:SF9; PTHR45614:SF9; 1.
DR Pfam; PF09316; Cmyb_C; 1.
DR Pfam; PF07988; LMSTEN; 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 Acetylation; Activator; Alternative splicing; Differentiation; DNA-binding;
KW Isopeptide bond; Nucleus; Reference proteome; Repeat; Spermatogenesis;
KW Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..751
FT /note="Myb-related protein A"
FT /id="PRO_0000197055"
FT DOMAIN 30..81
FT /note="HTH myb-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT DOMAIN 82..137
FT /note="HTH myb-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT DOMAIN 138..188
FT /note="HTH myb-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT DNA_BIND 58..81
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT DNA_BIND 110..133
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT DNA_BIND 161..184
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 230..294
FT /note="Transcriptional activation domain"
FT /evidence="ECO:0000250"
FT REGION 297..552
FT /note="Negative regulatory domain"
FT /evidence="ECO:0000250"
FT MOD_RES 393
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P10243"
FT CROSSLNK 199
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P10243"
FT CROSSLNK 591
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P10243"
FT CROSSLNK 601
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P10243"
FT VAR_SEQ 649..708
FT /note="Missing (in isoform Short)"
FT /evidence="ECO:0000303|PubMed:8084617"
FT /id="VSP_003300"
FT VARIANT 48
FT /note="K -> R"
FT VARIANT 404
FT /note="M -> V"
FT VARIANT 447
FT /note="R -> G"
FT VARIANT 708
FT /note="L -> P"
FT MUTAGEN 213
FT /note="A->E: In Repro9; male sterility due to defects in
FT spermatogenesis. Impaired piRNA biogenesis."
FT /evidence="ECO:0000269|PubMed:21750041,
FT ECO:0000269|PubMed:23523368"
FT CONFLICT 358..359
FT /note="PR -> AE (in Ref. 2; AAA62182)"
FT /evidence="ECO:0000305"
FT CONFLICT 446
FT /note="S -> L (in Ref. 2; AAA62182)"
FT /evidence="ECO:0000305"
FT CONFLICT 464..465
FT /note="SA -> DG (in Ref. 2; AAA62182)"
FT /evidence="ECO:0000305"
FT CONFLICT 473..475
FT /note="RRI -> AAL (in Ref. 2; AAA62182)"
FT /evidence="ECO:0000305"
FT CONFLICT 751
FT /note="L -> LYCY (in Ref. 1; CAA57771)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 751 AA; 85728 MW; 20A4124BE9B82235 CRC64;
MAKRSRSEDE DDDLQYADHD YEVPQQKGLK KLWNRVKWTR DEDDKLKKLV EQHGTDDWTL
IASHLQNRSD FQCQHRWQKV LNPELIKGPW TKEEDQRVIE LVQKYGPKRW SLIAKHLKGR
IGKQCRERWH NHLNPEVKKS SWTEEEDRII YEAHKRLGNR WAEIAKLLPG RTDNSIKNHW
NSTMRRKVEQ EGYLQDGIKS ERSSSKLQHK PCATMDHLQT QNQFYIPVQI PGYQYVSPDG
NCVEHVQTSA FIQQPFVDED PDKEKKIKEL ELLLMSAENE VRRKRLPPQP GSFSSWSGSF
LMDDSMSNTL NNLEEHTTEF YSMDENQTVS AQQNSPTKFL AVEANAVLSS LQTIPEFPRT
LELIESDPVA WSDVTSFDLS DAAASPVKST PVKLMRIQHN EGAMECQFNV SLVLEGKKNS
RNGGDSEAIP LTSPNVVKFS TPPTISRKKK RIRVGQSAGS ELGSASLSEV GNRRIKHTPV
KTLPFSPSQF FNTCPGNEQL NIENPSFTST PICGQKVLIT TPLQKEATPK DQKENVGFRT
PTIRRSILGT TPRTPTPFKN ALAAQEKKYG PLKIVSQPLA FLEEDIREVL KEETGTDIFL
KEEDEPAYKS CKQEHSASVK KVRKSLALES WDKEEPGTQL LTEDISDMQS ENILTTSLLM
IPLLEIHDNR CNLTPEKQDI NSANKTYTLN KKRPNPNPCK AVKLEKSLQS NCEWETVVYG
KTEDQLIMTE QARRYLSTYT ATSSTSRALI L
