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Transcription factor jun-B (MyD21)

 JUNB_MOUSE              Reviewed;         344 AA.
P09450; Q8C2G9;
01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
01-JUL-1989, sequence version 1.
12-SEP-2018, entry version 173.
RecName: Full=Transcription factor jun-B;
AltName: Full=MyD21;
Name=Junb; Synonyms=Jun-b;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3422745; DOI=10.1073/pnas.85.5.1487;
Ryder K., Lau L.F., Nathans D.;
"A gene activated by growth factors is related to the oncogene v-
jun.";
Proc. Natl. Acad. Sci. U.S.A. 85:1487-1491(1988).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=BALB/cJ;
PubMed=8530030; DOI=10.1006/geno.1995.1135;
Phinney D.G., Tseng S.W., Ryder K.;
"Complex genetic organization of junB: multiple blocks of flanking
evolutionarily conserved sequence at the murine and human junB loci.";
Genomics 28:228-234(1995).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=NOD; TISSUE=Thymus;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N; TISSUE=Mammary gland;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-30.
PubMed=1690380;
Lord K.A., Hoffman-Liebermann B., Liebermann D.A.;
"Complexity of the immediate early response of myeloid cells to
terminal differentiation and growth arrest includes ICAM-1, Jun-B and
histone variants.";
Oncogene 5:387-396(1990).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-256, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-248; THR-252 AND
SER-256, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Brain, Heart, Kidney, Lung, and Spleen;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[8]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-237, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z.,
Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
"SIRT5-mediated lysine desuccinylation impacts diverse metabolic
pathways.";
Mol. Cell 50:919-930(2013).
-!- FUNCTION: Transcription factor involved in regulating gene
activity following the primary growth factor response. Binds to
the DNA sequence 5'-TGA[CG]TCA-3'.
-!- SUBUNIT: Binds DNA as a homodimer or as a heterodimer with another
member of the Jun/Fos family. Interacts with NFE2 (via its WW
domains). {ECO:0000250}.
-!- INTERACTION:
Q9DGW5:MDV005 (xeno); NbExp=2; IntAct=EBI-5347760, EBI-10889526;
-!- SUBCELLULAR LOCATION: Nucleus.
-!- INDUCTION: By growth factors.
-!- PTM: Ubiquitinated by ITCH, leading to its degradation.
{ECO:0000250}.
-!- SIMILARITY: Belongs to the bZIP family. Jun subfamily.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; J03236; AAA39343.1; -; mRNA.
EMBL; U20735; AAA74916.1; -; Genomic_DNA.
EMBL; AK088643; BAC40473.1; -; mRNA.
EMBL; BC003790; AAH03790.1; -; mRNA.
EMBL; X54332; -; NOT_ANNOTATED_CDS; mRNA.
CCDS; CCDS22488.1; -.
PIR; A28963; TVMSJB.
RefSeq; NP_032442.1; NM_008416.3.
UniGene; Mm.1167; -.
ProteinModelPortal; P09450; -.
SMR; P09450; -.
BioGrid; 200872; 104.
CORUM; P09450; -.
DIP; DIP-1069N; -.
ELM; P09450; -.
IntAct; P09450; 103.
STRING; 10090.ENSMUSP00000064680; -.
iPTMnet; P09450; -.
PhosphoSitePlus; P09450; -.
EPD; P09450; -.
PaxDb; P09450; -.
PeptideAtlas; P09450; -.
PRIDE; P09450; -.
Ensembl; ENSMUST00000064922; ENSMUSP00000064680; ENSMUSG00000052837.
GeneID; 16477; -.
KEGG; mmu:16477; -.
UCSC; uc009mop.1; mouse.
CTD; 3726; -.
MGI; MGI:96647; Junb.
eggNOG; KOG0837; Eukaryota.
eggNOG; ENOG410XRWH; LUCA.
GeneTree; ENSGT00390000009929; -.
HOGENOM; HOG000006648; -.
HOVERGEN; HBG001722; -.
InParanoid; P09450; -.
KO; K09028; -.
OMA; PTPAHYL; -.
OrthoDB; EOG091G0N0L; -.
PhylomeDB; P09450; -.
PRO; PR:P09450; -.
Proteomes; UP000000589; Chromosome 8.
Bgee; ENSMUSG00000052837; Expressed in 169 organ(s), highest expression level in subcutaneous adipose tissue.
CleanEx; MM_JUNB; -.
ExpressionAtlas; P09450; baseline and differential.
Genevisible; P09450; MM.
GO; GO:0000790; C:nuclear chromatin; IBA:GO_Central.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; ISO:MGI.
GO; GO:0035976; C:transcription factor AP-1 complex; ISO:MGI.
GO; GO:0005667; C:transcription factor complex; IBA:GO_Central.
GO; GO:0003677; F:DNA binding; IDA:MGI.
GO; GO:0003700; F:DNA-binding transcription factor activity; ISO:MGI.
GO; GO:0003690; F:double-stranded DNA binding; ISO:MGI.
GO; GO:0000978; F:RNA polymerase II proximal promoter sequence-specific DNA binding; IMP:NTNU_SB.
GO; GO:0000977; F:RNA polymerase II regulatory region sequence-specific DNA binding; IDA:MGI.
GO; GO:0043565; F:sequence-specific DNA binding; ISO:MGI.
GO; GO:0003713; F:transcription coactivator activity; IBA:GO_Central.
GO; GO:0008134; F:transcription factor binding; IBA:GO_Central.
GO; GO:0001077; F:transcriptional activator activity, RNA polymerase II proximal promoter sequence-specific DNA binding; IMP:NTNU_SB.
GO; GO:0009987; P:cellular process; IDA:MGI.
GO; GO:0071277; P:cellular response to calcium ion; IDA:MGI.
GO; GO:0032870; P:cellular response to hormone stimulus; IBA:GO_Central.
GO; GO:0046697; P:decidualization; IMP:MGI.
GO; GO:0060136; P:embryonic process involved in female pregnancy; IMP:MGI.
GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
GO; GO:0060716; P:labyrinthine layer blood vessel development; IMP:MGI.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
GO; GO:0001649; P:osteoblast differentiation; IMP:MGI.
GO; GO:0033687; P:osteoblast proliferation; IMP:MGI.
GO; GO:0030316; P:osteoclast differentiation; IMP:MGI.
GO; GO:0045597; P:positive regulation of cell differentiation; IDA:MGI.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:NTNU_SB.
GO; GO:0051726; P:regulation of cell cycle; IDA:MGI.
GO; GO:0010941; P:regulation of cell death; IBA:GO_Central.
GO; GO:0042127; P:regulation of cell proliferation; IBA:GO_Central.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:MGI.
GO; GO:0051591; P:response to cAMP; IBA:GO_Central.
GO; GO:0034097; P:response to cytokine; IBA:GO_Central.
GO; GO:0042493; P:response to drug; IBA:GO_Central.
GO; GO:0032496; P:response to lipopolysaccharide; IBA:GO_Central.
GO; GO:0009612; P:response to mechanical stimulus; IBA:GO_Central.
GO; GO:0009314; P:response to radiation; IBA:GO_Central.
GO; GO:0006366; P:transcription by RNA polymerase II; ISO:MGI.
GO; GO:0001829; P:trophectodermal cell differentiation; IDA:MGI.
GO; GO:0001570; P:vasculogenesis; IMP:MGI.
InterPro; IPR004827; bZIP.
InterPro; IPR005643; JNK.
InterPro; IPR029822; JunB.
InterPro; IPR002112; Leuzip_Jun.
InterPro; IPR008917; TF_DNA-bd_sf.
PANTHER; PTHR11462:SF37; PTHR11462:SF37; 1.
Pfam; PF00170; bZIP_1; 1.
Pfam; PF03957; Jun; 1.
PRINTS; PR00043; LEUZIPPRJUN.
SMART; SM00338; BRLZ; 1.
SUPFAM; SSF47454; SSF47454; 1.
PROSITE; PS50217; BZIP; 1.
PROSITE; PS00036; BZIP_BASIC; 1.
1: Evidence at protein level;
Acetylation; Complete proteome; DNA-binding; Isopeptide bond; Nucleus;
Phosphoprotein; Reference proteome; Transcription;
Transcription regulation; Ubl conjugation.
CHAIN 1 344 Transcription factor jun-B.
/FTId=PRO_0000076439.
DOMAIN 265 328 bZIP. {ECO:0000255|PROSITE-
ProRule:PRU00978}.
REGION 265 292 Basic motif. {ECO:0000255|PROSITE-
ProRule:PRU00978}.
REGION 293 321 Leucine-zipper. {ECO:0000255|PROSITE-
ProRule:PRU00978}.
MOD_RES 102 102 Phosphothreonine.
{ECO:0000250|UniProtKB:P17275}.
MOD_RES 104 104 Phosphothreonine.
{ECO:0000250|UniProtKB:P17275}.
MOD_RES 117 117 Phosphoserine.
{ECO:0000250|UniProtKB:P17275}.
MOD_RES 237 237 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:23806337}.
MOD_RES 248 248 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 252 252 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 256 256 Phosphoserine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:21183079}.
CROSSLNK 4 4 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P17275}.
CROSSLNK 33 33 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P17275}.
CROSSLNK 36 36 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P17275}.
CROSSLNK 81 81 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P17275}.
CROSSLNK 138 138 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P17275}.
CROSSLNK 237 237 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1);
alternate.
{ECO:0000250|UniProtKB:P17275}.
CROSSLNK 237 237 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:P17275}.
CROSSLNK 340 340 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P17275}.
CONFLICT 53 53 P -> S (in Ref. 3; BAC40473).
{ECO:0000305}.
CONFLICT 200 200 G -> R (in Ref. 2; AAA74916).
{ECO:0000305}.
SEQUENCE 344 AA; 35765 MW; 6F52D4FECC32E234 CRC64;
MCTKMEQPFY HDDSYAAAGY GRSPGSLSLH DYKLLKPTLA LNLADPYRGL KGPGARGPGP
EGSGAGSYFS GQGSDTGASL KLASTELERL IVPNSNGVIT TTPTPPGQYF YPRGGGSGGG
TGGGVTEEQE GFADGFVKAL DDLHKMNHVT PPNVSLGASG GPQAGPGGVY AGPEPPPVYT
NLSSYSPASA PSGGSGTAVG TGSSYPTATI SYLPHAPPFA GGHPAQLGLS RGASAFKEEP
QTVPEARSRD ATPPVSPINM EDQERIKVER KRLRNRLAAT KCRKRKLERI ARLEDKVKTL
KAENAGLSSA AGLLREQVAQ LKQKVMTHVS NGCQLLLGVK GHAF


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