MYB_BOVIN
ID MYB_BOVIN Reviewed; 640 AA.
AC P46200;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 25-MAY-2022, entry version 123.
DE RecName: Full=Transcriptional activator Myb;
DE AltName: Full=Proto-oncogene c-Myb;
GN Name=MYB;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Holstein; TISSUE=Lymphoma;
RX PubMed=7929419; DOI=10.1016/s0021-9258(18)47093-7;
RA Ishiguro N., Ohzono T., Shinagawa T., Horiuchi M., Shinagawa M.;
RT "A spontaneous internal deletion of the c-myb protooncogene enhances
RT transcriptional activation in bovine T lymphoma cells.";
RL J. Biol. Chem. 269:26822-26829(1994).
CC -!- FUNCTION: Transcriptional activator; DNA-binding protein that
CC specifically recognize the sequence 5'-YAAC[GT]G-3'. Plays an important
CC role in the control of proliferation and differentiation of
CC hematopoietic progenitor cells.
CC -!- SUBUNIT: Interacts with HIPK1, HIPK2, MAF and NLK. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- DOMAIN: Comprised of 3 domains; an N-terminal DNA-binding domain, a
CC centrally located transcriptional activation domain and a C-terminal
CC domain involved in transcriptional repression.
CC -!- PTM: Phosphorylated by NLK on multiple sites, which induces proteasomal
CC degradation. {ECO:0000250}.
CC -!- PTM: Phosphorylated by HIPK1. This phosphorylation reduces MYB
CC transcription factor activity but not MYB protein levels (By
CC similarity). {ECO:0000250}.
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DR EMBL; D26147; BAA05135.1; -; mRNA.
DR PIR; A55073; A55073.
DR AlphaFoldDB; P46200; -.
DR BMRB; P46200; -.
DR SMR; P46200; -.
DR STRING; 9913.ENSBTAP00000043305; -.
DR PaxDb; P46200; -.
DR eggNOG; KOG0048; Eukaryota.
DR InParanoid; P46200; -.
DR OrthoDB; 219341at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0000278; P:mitotic cell cycle; IBA:GO_Central.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
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; IPR001005; SANT/Myb.
DR InterPro; IPR012642; Tscrpt_reg_Wos2-domain.
DR Pfam; PF09316; Cmyb_C; 1.
DR Pfam; PF07988; LMSTEN; 1.
DR Pfam; PF00249; Myb_DNA-binding; 3.
DR SMART; SM00717; SANT; 3.
DR SUPFAM; SSF46689; SSF46689; 2.
DR PROSITE; PS51294; HTH_MYB; 3.
PE 2: Evidence at transcript level;
KW Acetylation; Activator; DNA-binding; Isopeptide bond; Nucleus;
KW Phosphoprotein; Proto-oncogene; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..640
FT /note="Transcriptional activator Myb"
FT /id="PRO_0000197047"
FT DOMAIN 35..86
FT /note="HTH myb-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT DOMAIN 87..142
FT /note="HTH myb-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT DOMAIN 143..193
FT /note="HTH myb-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT DNA_BIND 63..86
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT DNA_BIND 115..138
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT DNA_BIND 166..189
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT REGION 90..193
FT /note="Interaction with HIPK2 and NLK"
FT /evidence="ECO:0000250"
FT REGION 275..327
FT /note="Transcriptional activation domain"
FT /evidence="ECO:0000250"
FT REGION 328..464
FT /note="Negative regulatory domain"
FT /evidence="ECO:0000250"
FT REGION 338..368
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 375..396
FT /note="Leucine-zipper"
FT MOD_RES 471
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P10242"
FT MOD_RES 480
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P10242"
FT MOD_RES 532
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10242"
FT MOD_RES 534
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P10242"
FT CROSSLNK 480
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P10242"
SQ SEQUENCE 640 AA; 72511 MW; E6DA275B3BEAB55D CRC64;
MARRPRHSIY SSDEDDEDIE MCDHDYDGLL PKSGKRHLGK TRWTREEDEK LKKLVEQNGT
DDWKVIANYL PNRTDVQCQH RWQKVLNPEL IKGPWTKEED QRVIELVQKY GPKRWSVIAK
HLKGRIGKQC RERWHNHLNP EVKKTSWTEE EDRIIYQAHK RLGNRWAEIA KLLPGRTDNA
IKNHWNSTMR RKVEQEGYLQ ESSKASQPAV TTSFQKNSHL MGFTHAPPSA QLPPAGQPSV
NSDYPYYHIS EAQNVSSHVP YPVALHVNIV NVPQPAAAAI QRHYNDEDPE KEKRIKELEL
LLMSTENELK GQQALPTQNH TCSYPGWHST TIADHTRPHG DSAPVSCLEE HHSTPSLPAD
PGSLPEESAS PARCMIFHQS TILDNVKNLL EFAETLQFID SFLNTSNNHE NLDLEMPSLT
STPLNGHKLT VTTPFHRDQT VKIQKENTIF RTPAIKRSIL EGSPRTPTPF KHALTAQEIK
YGPLKMLPQT PSHLVEDLQD EIKQESDESG IVAEFQENGQ PLLKKIKQEV ESPTDKAGNF
FCSNHWEGDS LNTQLFTQAS PVADMPNILT SSVLMTPVSE DEDNVLKAFT VPKSRSLASP
LQPCNGAWES ASCGKTDDQM TASGQSRKYV NAFSTRTLVM
