TMF1_MOUSE
ID TMF1_MOUSE Reviewed; 1091 AA.
AC B9EKI3; E9QPJ3; Q3UMH8; Q3UMR3;
DT 26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=TATA element modulatory factor;
DE Short=TMF;
DE AltName: Full=Androgen receptor coactivator 160 kDa protein;
DE AltName: Full=Androgen receptor-associated protein of 160 kDa;
GN Name=Tmf1; Synonyms=Ara160, Gm153;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-619.
RC TISSUE=Lung;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP PHOSPHORYLATION BY FER.
RX PubMed=9742951; DOI=10.1016/s0014-5793(98)01003-5;
RA Schwartz Y., Ben-Dor I., Navon A., Motro B., Nir U.;
RT "Tyrosine phosphorylation of the TATA element modulatory factor by the FER
RT nuclear tyrosine kinases.";
RL FEBS Lett. 434:339-345(1998).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH FER AND STAT3.
RX PubMed=15467733; DOI=10.1038/sj.onc.1208149;
RA Perry E., Tsruya R., Levitsky P., Pomp O., Taller M., Weisberg S.,
RA Parris W., Kulkarni S., Malovani H., Pawson T., Shpungin S., Nir U.;
RT "TMF/ARA160 is a BC-box-containing protein that mediates the degradation of
RT Stat3.";
RL Oncogene 23:8908-8919(2004).
RN [6]
RP INTERACTION WITH TRNP1.
RX PubMed=16792503; DOI=10.1089/dna.2006.25.331;
RA Volpe M., Shpungin S., Barbi C., Abrham G., Malovani H., Wides R., Nir U.;
RT "TRNP: a conserved mammalian gene encoding a nuclear protein that
RT accelerates cell-cycle progression.";
RL DNA Cell Biol. 25:331-339(2006).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-324; SER-326; SER-329;
RP SER-340; SER-357; SER-411; SER-926; THR-927 AND SER-931, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Potential coactivator of the androgen receptor. May play
CC critical roles in two RAB6-dependent retrograde transport processes:
CC one from endosomes to the Golgi and the other from the Golgi to the ER
CC (By similarity). Mediates STAT3 degradation. {ECO:0000250,
CC ECO:0000269|PubMed:15467733}.
CC -!- SUBUNIT: Component of the SNF/SWI transcription factor complexes (By
CC similarity). Interacts with RAB6A. Interacts with TCEB1 (By
CC similarity). Interacts with STAT3 and FER. Interacts with TRNP1; may
CC regulate TRNP1 proteasomal degradation. {ECO:0000250,
CC ECO:0000269|PubMed:15467733, ECO:0000269|PubMed:16792503}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC Golgi apparatus membrane {ECO:0000250}. Note=Concentrated at the
CC budding structures localized at the tips of cisternae. {ECO:0000250}.
CC -!- DOMAIN: The Elongin BC complex binding domain is also known as BC-box
CC with the consensus [APST]-L-x(3)-C-x(3)-[AILV].
CC -!- PTM: Phosphorylated by FER. {ECO:0000269|PubMed:9742951}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE26035.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AC155724; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC150931; AAI50932.1; -; mRNA.
DR EMBL; AK144898; BAE26120.1; -; mRNA.
DR EMBL; AK144729; BAE26035.1; ALT_FRAME; mRNA.
DR CCDS; CCDS39575.1; -.
DR RefSeq; NP_001074580.1; NM_001081111.2.
DR AlphaFoldDB; B9EKI3; -.
DR SMR; B9EKI3; -.
DR BioGRID; 231235; 8.
DR IntAct; B9EKI3; 1.
DR STRING; 10090.ENSMUSP00000093325; -.
DR iPTMnet; B9EKI3; -.
DR PhosphoSitePlus; B9EKI3; -.
DR EPD; B9EKI3; -.
DR jPOST; B9EKI3; -.
DR MaxQB; B9EKI3; -.
DR PaxDb; B9EKI3; -.
DR PeptideAtlas; B9EKI3; -.
DR PRIDE; B9EKI3; -.
DR ProteomicsDB; 259127; -.
DR Antibodypedia; 1796; 106 antibodies from 23 providers.
DR Ensembl; ENSMUST00000095664; ENSMUSP00000093325; ENSMUSG00000030059.
DR GeneID; 232286; -.
DR KEGG; mmu:232286; -.
DR UCSC; uc009dak.2; mouse.
DR CTD; 7110; -.
DR MGI; MGI:2684999; Tmf1.
DR VEuPathDB; HostDB:ENSMUSG00000030059; -.
DR eggNOG; KOG4673; Eukaryota.
DR GeneTree; ENSGT00390000010697; -.
DR HOGENOM; CLU_009915_0_0_1; -.
DR InParanoid; B9EKI3; -.
DR OMA; LQVDMNE; -.
DR OrthoDB; 145696at2759; -.
DR PhylomeDB; B9EKI3; -.
DR TreeFam; TF329420; -.
DR Reactome; R-MMU-6811440; Retrograde transport at the Trans-Golgi-Network.
DR BioGRID-ORCS; 232286; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Tmf1; mouse.
DR PRO; PR:B9EKI3; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; B9EKI3; protein.
DR Bgee; ENSMUSG00000030059; Expressed in spermatid and 227 other tissues.
DR ExpressionAtlas; B9EKI3; baseline and differential.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
DR GO; GO:0005794; C:Golgi apparatus; IDA:MGI.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0050681; F:nuclear androgen receptor binding; ISO:MGI.
DR GO; GO:0030374; F:nuclear receptor coactivator activity; ISO:MGI.
DR GO; GO:0001675; P:acrosome assembly; IMP:MGI.
DR GO; GO:0030521; P:androgen receptor signaling pathway; ISO:MGI.
DR GO; GO:0006915; P:apoptotic process; IMP:MGI.
DR GO; GO:0071407; P:cellular response to organic cyclic compound; IMP:MGI.
DR GO; GO:0042742; P:defense response to bacterium; IMP:MGI.
DR GO; GO:1904019; P:epithelial cell apoptotic process; IMP:MGI.
DR GO; GO:0030317; P:flagellated sperm motility; IMP:MGI.
DR GO; GO:0033327; P:Leydig cell differentiation; IMP:MGI.
DR GO; GO:0032275; P:luteinizing hormone secretion; IMP:MGI.
DR GO; GO:0008584; P:male gonad development; IMP:MGI.
DR GO; GO:1904036; P:negative regulation of epithelial cell apoptotic process; IMP:MGI.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:MGI.
DR GO; GO:0001819; P:positive regulation of cytokine production; IMP:MGI.
DR GO; GO:2000845; P:positive regulation of testosterone secretion; IMP:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0061136; P:regulation of proteasomal protein catabolic process; IDA:UniProtKB.
DR GO; GO:0007286; P:spermatid development; IMP:MGI.
DR GO; GO:0007289; P:spermatid nucleus differentiation; IMP:MGI.
DR InterPro; IPR022092; TMF_DNA-bd.
DR InterPro; IPR022091; TMF_TATA-bd.
DR Pfam; PF12329; TMF_DNA_bd; 1.
DR Pfam; PF12325; TMF_TATA_bd; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Cytoplasm; DNA-binding; Golgi apparatus; Membrane; Nucleus;
KW Phosphoprotein; Reference proteome; Repressor; Transcription;
KW Transcription regulation.
FT CHAIN 1..1091
FT /note="TATA element modulatory factor"
FT /id="PRO_0000376797"
FT REGION 42..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 100..280
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 329..338
FT /note="Interaction with Elongin BC complex"
FT /evidence="ECO:0000250"
FT REGION 360..443
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 443..767
FT /evidence="ECO:0000255"
FT COILED 824..894
FT /evidence="ECO:0000255"
FT COILED 984..1090
FT /evidence="ECO:0000255"
FT COMPBIAS 54..83
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 100..119
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 132..148
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 169..188
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 194..218
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 220..234
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 235..280
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 370..387
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 415..429
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 73
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P82094"
FT MOD_RES 78
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P82094"
FT MOD_RES 112
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P82094"
FT MOD_RES 136
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P82094"
FT MOD_RES 213
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P82094"
FT MOD_RES 324
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 326
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 329
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 334
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P82094"
FT MOD_RES 340
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 357
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 411
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 540
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P82094"
FT MOD_RES 923
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P82094"
FT MOD_RES 926
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 927
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 931
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 106
FT /note="A -> V (in Ref. 2; AAI50932)"
FT /evidence="ECO:0000305"
FT CONFLICT 144
FT /note="V -> A (in Ref. 2; AAI50932)"
FT /evidence="ECO:0000305"
FT CONFLICT 161
FT /note="S -> P (in Ref. 2; AAI50932)"
FT /evidence="ECO:0000305"
FT CONFLICT 203
FT /note="T -> S (in Ref. 2; AAI50932)"
FT /evidence="ECO:0000305"
FT CONFLICT 439
FT /note="P -> L (in Ref. 2; AAI50932)"
FT /evidence="ECO:0000305"
FT CONFLICT 871
FT /note="L -> I (in Ref. 2; AAI50932)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1091 AA; 121803 MW; D208A815FF740CF1 CRC64;
MSWFNASQLS SFAKQALSQA QKSIDRVLDI QEEEPSAWAE AIPYGEPGIS PPVSGGWDTS
TWGLNSTSSE PQSPPTASQA ITKPVRRTVV DESENFFSAF LSPSDAHTIQ KSPVVSKPPS
KSQRPEEEVK SSLQESSSPG QSRVSETAEV RDSVCVSGET SAVGTPSPVP EDKHEETAGE
ESEVKVPTVR LKASENVVNV NTTEDVSTTS TQSLTAETKD MALEPKEQKH EDRQSNTPSP
PVSSFSSGTS TTSDIEVLDH ESVISESSAS SRQETSDAKS SLHLMQTSFQ LLSASACPEY
SRLDDFQKLN ESCCSSDAFE RIDSFSVQSL DSRSVSEINS DDELPGKGYA LVPIIVSPST
PKTKVVESTE ENAEEEEGNE TLVAPSEEAE LEESGRSATP VNCDQPDILA SPTAGSGGHS
ASGPATEQCE AVENQPKAPP EKEDVCKTVE FLNEKLEKRE TQLLSLSKEK ALLEEAYDNL
KDEMFRVKEE SSSISSLKDE FTQRIAEAEK KVQLACKERD AAKKEMKTIK EELATRLNSS
QTADLLKEKD EQIQGLMEEG EKLSKQQLHN SNIIKKLRAK DKDNENVIAK LNRKAKELEE
ELQHLRQVLD GKEEVEKQHR ENIKKLNSVV ERQEKDLGRL QVDMDELEEK SRSTQAALDS
AYRELTDLHK ANAAKDSEVQ EAALRREMKA KEELSGALEK AQEEARQQQE ALVLQVGDLR
LALQRAEQAA ARKEDYLRHE ISELQQRLQE AENRNQELSQ SVSSTARPLL RQIENLQATL
GSQTSSWETL EKSLSDRLGE SQTLLAAAVE RERAATEELL ANKIQMSSVE SQNTLLRQEN
SRLQAQLESE KNKLRKLEDE NSRYQVELEN LKDEYVRTLE ESRKEKTLLS SQLEMERMKV
EQERKKTIFT QEALKEKDHK LFSVCSTPTM SRSSSISGVD AAGLQASFLS QDESHDHSFG
PMSTSASGSN LYEAVRMGAG SSIIENLQSQ LKLREGEISH LQLEISNLEK TRSIMSEELV
KLTNQNDELE EKVKEIPKLR VQLRDLDQRY NTILQMYGEK AEEAEELRLD LEDVKNMYKT
QIDELLRQRL S
