ID MYBA_HUMAN Reviewed; 752 AA. AC P10243; DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 2. DT 13-OCT-2009, entry version 93. DE RecName: Full=Myb-related protein A; DE AltName: Full=A-Myb; GN Name=MYBL1; Synonyms=AMYB; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-745. RX MEDLINE=89083548; 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- RT myb."; RL Nucleic Acids Res. 16:11075-11089(1988). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] OF 398-752, AND CHARACTERIZATION. RX MEDLINE=94336200; 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 [3] RP NUCLEOTIDE SEQUENCE [MRNA] OF 727-752. RX MEDLINE=95079434; PubMed=7987850; RA Ma X.P., Calabretta B.; RT "DNA binding and transactivation activity of A-myb, a C-myb-related RT gene."; RL Cancer Res. 54:6512-6516(1994). RN [4] 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 RT complex represses human cell cycle-dependent genes in quiescence."; RL Mol. Cell 26:539-551(2007). RN [5] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-394, AND MASS SPECTROMETRY. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., 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). CC -!- FUNCTION: Strong transcriptional activator; DNA-binding protein CC that specifically recognize the sequence 5'-YAAC[GT]G-3'. Could CC have a role in the proliferation and/or differentiation of CC neurogenic, spermatogenic and B-lymphoid cells. CC -!- SUBUNIT: Component of the DREAM complex (also named LINC complex) CC at least composed of E2F4, E2F5, LIN9, LIN37, LIN52, LIN54, MYBL1, CC MYBL2, RBL1, RBL2, RBBP4, TFDP1 and TFDP2. The complex exists in CC quiescent cells where it represses cell cycle-dependent genes. It CC dissociates in S phase when LIN9, LIN37, LIN52 and LIN54 form a CC subcomplex that binds to MYBL2. CC -!- SUBCELLULAR LOCATION: Nucleus. CC -!- TISSUE SPECIFICITY: Expressed in a variety of lymphoid and solid CC tumor lines cultured in vitro. CC -!- SIMILARITY: Contains 3 HTH myb-type DNA-binding domains. CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology CC and Haematology; CC URL="http://atlasgeneticsoncology.org/Genes/MYBL1ID41468ch8q13.html"; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X13294; CAA31656.1; -; mRNA. DR EMBL; X66087; CAA46886.1; -; mRNA. DR IPI; IPI00941501; -. DR PIR; S03423; S03423. DR RefSeq; NP_001073885.1; -. DR UniGene; Hs.445898; -. DR HSSP; P06876; 1MBG. DR SMR; P10243; 35-185. DR DIP; DIP:624N; -. DR STRING; P10243; -. DR PhosphoSite; P10243; -. DR PRIDE; P10243; -. DR Ensembl; ENST00000331406; ENSP00000332150; ENSG00000185697; Homo sapiens. DR Ensembl; ENST00000399555; ENSP00000382469; ENSG00000185697; Homo sapiens. DR Ensembl; ENST00000402282; ENSP00000385360; ENSG00000185697; Homo sapiens. DR GeneID; 4603; -. DR KEGG; hsa:4603; -. DR UCSC; uc003xwj.1; human. DR CTD; 4603; -. DR GeneCards; GC08M067636; -. DR H-InvDB; HIX0034339; -. DR HGNC; HGNC:7547; MYBL1. DR HPA; CAB017780; -. DR HPA; HPA008791; -. DR MIM; 159405; gene. DR PharmGKB; PA31347; -. DR HOGENOM; P10243; -. DR HOVERGEN; P10243; -. DR Pathway_Interaction_DB; il4_2pathway; IL4-mediated signaling events. DR NextBio; 17704; -. DR ArrayExpress; P10243; -. DR Bgee; P10243; -. DR CleanEx; HS_MYBL1; -. DR Genevestigator; P10243; -. DR GO; GO:0005634; C:nucleus; NAS:UniProtKB. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0016563; F:transcription activator activity; NAS:UniProtKB. DR GO; GO:0006355; P:regulation of transcription, DNA-dependent; NAS:UniProtKB. DR GO; GO:0006350; P:transcription; IEA:UniProtKB-KW. DR InterPro; IPR015395; C-myb_C. DR InterPro; IPR012287; Homeodomain-rel. DR InterPro; IPR017930; Myb-type_HTH. DR InterPro; IPR014778; Myb_DNA-bd. DR InterPro; IPR015495; Myb_trans_fac. DR InterPro; IPR001005; SANT_DNA-bd. DR InterPro; IPR012642; Trans_reg_Wos2-domain. DR Gene3D; G3DSA:1.10.10.60; Homeodomain-rel; 3. DR PANTHER; PTHR10641; Myb_transfac; 1. DR Pfam; PF09316; Cmyb_C; 1. DR Pfam; PF00249; Myb_DNA-binding; 3. DR Pfam; PF07988; Wos2; 1. DR SMART; SM00717; SANT; 3. DR PROSITE; PS51294; HTH_MYB; 3. PE 1: Evidence at protein level; KW Acetylation; Activator; Complete proteome; DNA-binding; Nucleus; KW Repeat; Transcription; Transcription regulation. FT CHAIN 1 752 Myb-related protein A. FT /FTId=PRO_0000197054. FT DOMAIN 30 81 HTH myb-type 1. FT DOMAIN 82 137 HTH myb-type 2. FT DOMAIN 138 188 HTH myb-type 3. FT DNA_BIND 58 81 H-T-H motif (By similarity). FT DNA_BIND 110 133 H-T-H motif (By similarity). FT DNA_BIND 161 184 H-T-H motif (By similarity). FT REGION 230 295 Transcriptional activation domain (By FT similarity). FT REGION 298 553 Negative regulatory domain (By FT similarity). FT MOD_RES 394 394 N6-acetyllysine. 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 //