ID A0A0G2JV86_RAT Unreviewed; 614 AA.
AC A0A0G2JV86;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 2.
DT 27-MAR-2024, entry version 47.
DE SubName: Full=MYB proto-oncogene, transcription factor {ECO:0000313|Ensembl:ENSRNOP00000069389.2};
GN Name=Myb {ECO:0000313|Ensembl:ENSRNOP00000069389.2,
GN ECO:0000313|RGD:1560020};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116 {ECO:0000313|Ensembl:ENSRNOP00000069389.2, ECO:0000313|Proteomes:UP000002494};
RN [1] {ECO:0000313|Ensembl:ENSRNOP00000069389.2, ECO:0000313|Proteomes:UP000002494}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000069389.2,
RC ECO:0000313|Proteomes:UP000002494};
RX PubMed=15057822; DOI=10.1038/nature02426;
RG Rat Genome Sequencing Project Consortium;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2] {ECO:0007829|PubMed:22673903}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [3] {ECO:0000313|Ensembl:ENSRNOP00000069389.2}
RP IDENTIFICATION.
RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000069389.2};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR AlphaFoldDB; A0A0G2JV86; -.
DR Ensembl; ENSRNOT00000081620.2; ENSRNOP00000069389.2; ENSRNOG00000055858.2.
DR AGR; RGD:1560020; -.
DR RGD; 1560020; Myb.
DR VEuPathDB; HostDB:ENSRNOG00000055858; -.
DR eggNOG; KOG0048; Eukaryota.
DR GeneTree; ENSGT00940000156248; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000055858; Expressed in thymus and 14 other cell types or tissues.
DR ExpressionAtlas; A0A0G2JV86; baseline and differential.
DR GO; GO:0005829; C:cytosol; ISO:RGD.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; ISO:RGD.
DR GO; GO:0003677; F:DNA binding; ISO:RGD.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:RGD.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISO:RGD.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:RGD.
DR GO; GO:0071987; F:WD40-repeat domain binding; ISO:RGD.
DR GO; GO:0030183; P:B cell differentiation; ISO:RGD.
DR GO; GO:0006816; P:calcium ion transport; ISO:RGD.
DR GO; GO:0070301; P:cellular response to hydrogen peroxide; IEP:RGD.
DR GO; GO:0071354; P:cellular response to interleukin-6; ISO:RGD.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; ISO:RGD.
DR GO; GO:0071300; P:cellular response to retinoic acid; IEP:RGD.
DR GO; GO:0048566; P:embryonic digestive tract development; ISO:RGD.
DR GO; GO:0030218; P:erythrocyte differentiation; ISO:RGD.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; ISO:RGD.
DR GO; GO:0048872; P:homeostasis of number of cells; ISO:RGD.
DR GO; GO:0001701; P:in utero embryonic development; ISO:RGD.
DR GO; GO:0030099; P:myeloid cell differentiation; ISO:RGD.
DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; ISO:RGD.
DR GO; GO:1901533; P:negative regulation of hematopoietic progenitor cell differentiation; ISO:RGD.
DR GO; GO:0045653; P:negative regulation of megakaryocyte differentiation; ISO:RGD.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0032967; P:positive regulation of collagen biosynthetic process; IMP:RGD.
DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; ISO:RGD.
DR GO; GO:0060252; P:positive regulation of glial cell proliferation; IMP:RGD.
DR GO; GO:2000491; P:positive regulation of hepatic stellate cell activation; IMP:RGD.
DR GO; GO:1904899; P:positive regulation of hepatic stellate cell proliferation; IMP:RGD.
DR GO; GO:1902895; P:positive regulation of miRNA transcription; ISO:RGD.
DR GO; GO:0043525; P:positive regulation of neuron apoptotic process; IMP:RGD.
DR GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; IMP:RGD.
DR GO; GO:2000845; P:positive regulation of testosterone secretion; IMP:RGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0071636; P:positive regulation of transforming growth factor beta production; IMP:RGD.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; ISO:RGD.
DR GO; GO:0010468; P:regulation of gene expression; ISO:RGD.
DR GO; GO:0001666; P:response to hypoxia; IEP:RGD.
DR GO; GO:0002931; P:response to ischemia; IEP:RGD.
DR GO; GO:0014856; P:skeletal muscle cell proliferation; IEP:RGD.
DR GO; GO:0048536; P:spleen development; ISO:RGD.
DR GO; GO:0017145; P:stem cell division; ISO:RGD.
DR GO; GO:0045064; P:T-helper 2 cell differentiation; ISO:RGD.
DR GO; GO:0048538; P:thymus development; ISO:RGD.
DR CDD; cd00167; SANT; 3.
DR Gene3D; 1.10.10.60; Homeodomain-like; 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 PANTHER; PTHR45614:SF25; MYB PROTEIN; 1.
DR PANTHER; PTHR45614; MYB PROTEIN-RELATED; 1.
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; Homeodomain-like; 2.
DR PROSITE; PS51294; HTH_MYB; 3.
DR PROSITE; PS50090; MYB_LIKE; 3.
PE 1: Evidence at protein level;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Reference proteome {ECO:0000313|Proteomes:UP000002494};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
SQ SEQUENCE 614 AA; 69093 MW; FD2C2E09C4B390CC CRC64;
MCDHDYDGLL PKSGKRHLGK TRWTREEDEK LKKLVEQNGT DDWKVIANYL PNRTDVQCQH
RWQKVLNPEL IKGPWTKEED QRVIELVQKY GPKRWSVIAK HLKGRIGKQC RERWHNHLNP
EVKKTSWTED EDRIIYQAHK RLGNRWAEIA KLLPGRTDNA IKNHWNSTMR RKVEQEGYLQ
EPSKASQTPV VSSFQKNNHL MGFAHASPPP TSQSSVNGEY PYYHIAEAQN ISSHVPYPVA
LHVNIVNVPQ PAAAAIQRHY NDEDPEKEKR IKELELLLMS TENELKGQQA LPTQNHTCSY
PGWHSTSIVD QTRPHGDSAP VSCLGENHAT PSLPADPGSL PEESASPARC MIVHQGTILD
NVKNLLEFAE TLQFIDSFLN TSSNHENSGL DTPTLPSTPL IGHKLTPCHR DQTVKTQKEN
SIFRTPAIKR SILESSPRTP TPFKHALAAQ EIKYGPLKML PQTPSHVVED LQDVIKQESD
ESGIVAEFHE NGPPLLKKIK QEVDSPTEKA GNFFCSNHWE ETNLSTQLFA QASPVADAPN
ILTSSVLMTP VSEDEDNVLK AFTVPKNRPL VGPLQPCVGA WEPTPSCGKT EDQMTASGQA
RKYVNTFSAR TLVM
//
