MYBA_HUMAN
ID MYBA_HUMAN Reviewed; 752 AA.
AC P10243; E7EW29; Q495F9;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 2.
DT 03-AUG-2022, entry version 196.
DE RecName: Full=Myb-related protein A {ECO:0000303|PubMed:7987850, ECO:0000303|PubMed:8058310};
DE Short=A-Myb {ECO:0000303|PubMed:7987850, ECO:0000303|PubMed:8058310};
DE AltName: Full=Myb-like protein 1;
GN Name=MYBL1; Synonyms=AMYB;
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 [LARGE SCALE GENOMIC DNA].
RX PubMed=16421571; DOI=10.1038/nature04406;
RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M.,
RA Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
RA Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
RA Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
RA Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
RA Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
RA Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B.,
RA O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K.,
RA Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
RA Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
RA Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
RA Platzer M., Shimizu N., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 8.";
RL Nature 439:331-335(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [MRNA] OF 1-745 (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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 398-752 (ISOFORM 1), AND FUNCTION.
RX PubMed=8058310;
RA Golay J., Loffarelli L., Luppi M., Castellano M., Introna M.;
RT "The human A-myb protein is a strong activator of transcription.";
RL Oncogene 9:2469-2479(1994).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 727-752 (ISOFORM 1/2), AND FUNCTION.
RX PubMed=7987850;
RA Ma X.P., Calabretta B.;
RT "DNA binding and transactivation activity of A-myb, a C-myb-related gene.";
RL Cancer Res. 54:6512-6516(1994).
RN [7]
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 [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-394, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
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 [10]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-602, AND IDENTIFICATION BY MASS
RP 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 [11]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-199; LYS-592 AND LYS-602, AND
RP IDENTIFICATION BY MASS 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 that specifically recognizes the
CC sequence 5'-YAAC[GT]G-3' (PubMed:8058310, PubMed:7987850). 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 (By similarity). The
CC piRNA metabolic process mediates the repression of transposable
CC elements during meiosis by forming complexes composed of piRNAs and
CC Piwi proteins and governs the methylation and subsequent repression of
CC transposons, which is essential for the germline integrity (By
CC similarity). Transcriptional activator of SOX30 (By similarity).
CC {ECO:0000250|UniProtKB:P51960, ECO:0000269|PubMed:7987850,
CC ECO:0000269|PubMed:8058310}.
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. {ECO:0000269|PubMed:17531812}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P51960}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P10243-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P10243-2; Sequence=VSP_042912;
CC -!- TISSUE SPECIFICITY: Expressed in a variety of lymphoid and solid tumor
CC lines cultured in vitro.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/MYBL1ID41468ch8q13.html";
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DR EMBL; AC083928; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471068; EAW86912.1; -; Genomic_DNA.
DR EMBL; BC101188; AAI01189.1; -; mRNA.
DR EMBL; X13294; CAA31656.1; -; mRNA.
DR EMBL; X66087; CAA46886.1; -; mRNA.
DR CCDS; CCDS47867.1; -. [P10243-1]
DR CCDS; CCDS55241.1; -. [P10243-2]
DR PIR; S03423; S03423.
DR RefSeq; NP_001073885.1; NM_001080416.3. [P10243-1]
DR RefSeq; NP_001138227.1; NM_001144755.2. [P10243-2]
DR AlphaFoldDB; P10243; -.
DR SMR; P10243; -.
DR BioGRID; 110688; 12.
DR DIP; DIP-624N; -.
DR IntAct; P10243; 7.
DR STRING; 9606.ENSP00000429633; -.
DR GlyGen; P10243; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P10243; -.
DR PhosphoSitePlus; P10243; -.
DR BioMuta; MYBL1; -.
DR DMDM; 1171089; -.
DR jPOST; P10243; -.
DR MassIVE; P10243; -.
DR MaxQB; P10243; -.
DR PaxDb; P10243; -.
DR PeptideAtlas; P10243; -.
DR PRIDE; P10243; -.
DR ProteomicsDB; 52584; -. [P10243-1]
DR ProteomicsDB; 52585; -. [P10243-2]
DR Antibodypedia; 1831; 218 antibodies from 26 providers.
DR DNASU; 4603; -.
DR Ensembl; ENST00000522677.8; ENSP00000429633.2; ENSG00000185697.17. [P10243-1]
DR Ensembl; ENST00000524176.2; ENSP00000428011.2; ENSG00000185697.17. [P10243-2]
DR GeneID; 4603; -.
DR KEGG; hsa:4603; -.
DR MANE-Select; ENST00000522677.8; ENSP00000429633.2; NM_001080416.4; NP_001073885.1.
DR UCSC; uc003xwj.4; human. [P10243-1]
DR CTD; 4603; -.
DR DisGeNET; 4603; -.
DR GeneCards; MYBL1; -.
DR HGNC; HGNC:7547; MYBL1.
DR HPA; ENSG00000185697; Tissue enhanced (lymphoid tissue, testis).
DR MalaCards; MYBL1; -.
DR MIM; 159405; gene.
DR neXtProt; NX_P10243; -.
DR OpenTargets; ENSG00000185697; -.
DR PharmGKB; PA31347; -.
DR VEuPathDB; HostDB:ENSG00000185697; -.
DR eggNOG; KOG0048; Eukaryota.
DR GeneTree; ENSGT00940000157709; -.
DR HOGENOM; CLU_015440_2_2_1; -.
DR InParanoid; P10243; -.
DR OMA; CTSKNVK; -.
DR OrthoDB; 219341at2759; -.
DR PhylomeDB; P10243; -.
DR TreeFam; TF326257; -.
DR PathwayCommons; P10243; -.
DR Reactome; R-HSA-5601884; PIWI-interacting RNA (piRNA) biogenesis.
DR SignaLink; P10243; -.
DR SIGNOR; P10243; -.
DR BioGRID-ORCS; 4603; 35 hits in 1103 CRISPR screens.
DR ChiTaRS; MYBL1; human.
DR GenomeRNAi; 4603; -.
DR Pharos; P10243; Tbio.
DR PRO; PR:P10243; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; P10243; protein.
DR Bgee; ENSG00000185697; Expressed in calcaneal tendon and 189 other tissues.
DR ExpressionAtlas; P10243; baseline and differential.
DR Genevisible; P10243; HS.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
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:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0007141; P:male meiosis I; ISS:UniProtKB.
DR GO; GO:0000278; P:mitotic cell cycle; IBA:GO_Central.
DR GO; GO:0010529; P:negative regulation of transposition; ISS:UniProtKB.
DR GO; GO:1990511; P:piRNA biosynthetic process; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; NAS:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0007283; P:spermatogenesis; ISS: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..752
FT /note="Myb-related protein A"
FT /id="PRO_0000197054"
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..295
FT /note="Transcriptional activation domain"
FT /evidence="ECO:0000250"
FT REGION 298..553
FT /note="Negative regulatory domain"
FT /evidence="ECO:0000250"
FT REGION 451..480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 394
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT CROSSLNK 199
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 592
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 602
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 VAR_SEQ 650..709
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_042912"
SQ SEQUENCE 752 AA; 85887 MW; 4C6D1823A7CAFCDA CRC64;
MAKRSRSEDE DDDLQYADHD YEVPQQKGLK KLWNRVKWTR DEDDKLKKLV EQHGTDDWTL
IASHLQNRSD FQCQHRWQKV LNPELIKGPW TKEEDQRVIE LVQKYGPKRW SLIAKHLKGR
IGKQCRERWH NHLNPEVKKS SWTEEEDRII YEAHKRLGNR WAEIAKLLPG RTDNSIKNHW
NSTMRRKVEQ EGYLQDGIKS ERSSSKLQHK PCAAMDHMQT QNQFYIPVQI PGYQYVSPEG
NCIEHVQPTS AFIQQPFIDE DPDKEKKIKE LEMLLMSAEN EVRRKRIPSQ PGSFSSWSGS
FLMDDNMSNT LNSLDEHTSE FYSMDENQPV SAQQNSPTKF LAVEANAVLS SLQTIPEFAE
TLELIESDPV AWSDVTSFDI SDAAASPIKS TPVKLMRIQH NEGAMECQFN VSLVLEGKKN
TCNGGNSEAV PLTSPNIAKF STPPAILRKK RKMRVGHSPG SELRDGSLND GGNMALKHTP
LKTLPFSPSQ FFNTCPGNEQ LNIENPSFTS TPICGQKALI TTPLHKETTP KDQKENVGFR
TPTIRRSILG TTPRTPTPFK NALAAQEKKY GPLKIVSQPL AFLEEDIREV LKEETGTDLF
LKEEDEPAYK SCKQENTASG KKVRKSLVLD NWEKEESGTQ LLTEDISDMQ SENRFTTSLL
MIPLLEIHDN RCNLIPEKQD INSTNKTYTL TKKKPNPNTS KVVKLEKNLQ SNCEWETVVY
GKTEDQLIMT EQARRYLSTY TATSSTSRAL IL
