ESF1_MOUSE
ID ESF1_MOUSE Reviewed; 845 AA.
AC Q3V1V3;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=ESF1 homolog;
DE AltName: Full=ABT1-associated protein;
GN Name=Esf1; Synonyms=Abtap;
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 MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [2]
RP PROTEIN SEQUENCE OF 783-791, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-156; SER-651; SER-657;
RP SER-686; SER-688 AND SER-689, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-156, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-305; SER-651; SER-657;
RP SER-686; SER-688 AND SER-689, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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: May constitute a novel regulatory system for basal
CC transcription. Negatively regulates ABT1 (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with ABT1. Forms a complex with ABT1 and suppresses
CC the ABT1-induced activation of polymerase II-directed transcription in
CC mammalian cells (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}. Nucleus,
CC nucleoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ESF1 family. {ECO:0000305}.
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DR EMBL; AK132230; BAE21046.1; -; mRNA.
DR CCDS; CCDS38250.1; -.
DR RefSeq; NP_001074559.1; NM_001081090.1.
DR RefSeq; XP_006500074.1; XM_006500011.3.
DR AlphaFoldDB; Q3V1V3; -.
DR BioGRID; 211568; 33.
DR IntAct; Q3V1V3; 1.
DR MINT; Q3V1V3; -.
DR STRING; 10090.ENSMUSP00000036523; -.
DR iPTMnet; Q3V1V3; -.
DR PhosphoSitePlus; Q3V1V3; -.
DR EPD; Q3V1V3; -.
DR jPOST; Q3V1V3; -.
DR MaxQB; Q3V1V3; -.
DR PaxDb; Q3V1V3; -.
DR PRIDE; Q3V1V3; -.
DR ProteomicsDB; 275782; -.
DR Antibodypedia; 24268; 75 antibodies from 18 providers.
DR Ensembl; ENSMUST00000046030; ENSMUSP00000036523; ENSMUSG00000045624.
DR GeneID; 66580; -.
DR KEGG; mmu:66580; -.
DR UCSC; uc008mpn.1; mouse.
DR CTD; 51575; -.
DR MGI; MGI:1913830; Esf1.
DR VEuPathDB; HostDB:ENSMUSG00000045624; -.
DR eggNOG; KOG2318; Eukaryota.
DR GeneTree; ENSGT00390000004881; -.
DR HOGENOM; CLU_010564_2_1_1; -.
DR InParanoid; Q3V1V3; -.
DR OMA; LTWDETA; -.
DR OrthoDB; 1300279at2759; -.
DR PhylomeDB; Q3V1V3; -.
DR TreeFam; TF105822; -.
DR BioGRID-ORCS; 66580; 24 hits in 73 CRISPR screens.
DR ChiTaRS; Esf1; mouse.
DR PRO; PR:Q3V1V3; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q3V1V3; protein.
DR Bgee; ENSMUSG00000045624; Expressed in embryonic post-anal tail and 258 other tissues.
DR ExpressionAtlas; Q3V1V3; baseline and differential.
DR Genevisible; Q3V1V3; MM.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0006364; P:rRNA processing; IBA:GO_Central.
DR InterPro; IPR039754; Esf1.
DR InterPro; IPR012580; NUC153.
DR PANTHER; PTHR12202; PTHR12202; 2.
DR Pfam; PF08159; NUC153; 1.
PE 1: Evidence at protein level;
KW Acetylation; Coiled coil; Direct protein sequencing; Nucleus;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9H501"
FT CHAIN 2..845
FT /note="ESF1 homolog"
FT /id="PRO_0000233166"
FT REGION 54..321
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 536..570
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 634..660
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 676..696
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 775..803
FT /evidence="ECO:0000255"
FT COMPBIAS 54..91
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 102..193
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 194..211
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 230..254
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 262..292
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 536..553
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 554..570
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H501"
FT MOD_RES 75
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H501"
FT MOD_RES 77
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H501"
FT MOD_RES 79
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H501"
FT MOD_RES 82
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H501"
FT MOD_RES 136
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H501"
FT MOD_RES 156
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19131326,
FT ECO:0007744|PubMed:19144319"
FT MOD_RES 200
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H501"
FT MOD_RES 290
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H501"
FT MOD_RES 292
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H501"
FT MOD_RES 305
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 306
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H501"
FT MOD_RES 307
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H501"
FT MOD_RES 608
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H501"
FT MOD_RES 651
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 657
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 686
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 688
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 689
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 729
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H501"
SQ SEQUENCE 845 AA; 98048 MW; 8EB7F2C2CFB997F5 CRC64;
MSSKQEIMDD QRFRRVSKDP RFWEMPEKER KVKIDKRFRA MFHDKKFKLN YAVDKRGRPI
SHSTTEDLKR FYDLSDSDSD LSDEESKILS QKKAKQKKKQ TKKEAKSIEK PIEEKKKETK
KTDQKDSINK HDLNNSERVQ KMKNSQKPQK IDSEISPKKD NEEFLQNKKK KRGTTDLSVE
ALPKGKLRTK DSSTSEMVKS STMSSSKAKR EKQSVVPVIM AKDNDGKMPD EDALEEDSDS
ASELGSDEES EDEIISDGKT SADEDESEEE DEEEEEDSEE EEEEEEEDES DSGPDLARGK
GNVETSSEDE DDLADLFPEE PGFEHAWREL DKDAPRADEI TRRLAVCNMD WDRLKAKDLL
ALFNSFKPKG GVVFSVKIYP SEFGKERMKE EQVQGPVELL SIPEDAPEKD WASREKLRDY
QFKRLKYYYA VAECDSPETA SKIYEDCDGL EFESSCSFID LRFIPDDITF DDEPKDVALE
VDLTAYKPKY FTSAAMGTST VEITWDETDH ERITTLNRKF KKDELLDMDF QAYLASSSED
EEEVEEAPEG EEGVNIGEDG KTKKSQKDDE EQIAKYRQLL QVIQEKEKKG KENDMEMEIK
WVPGLKESAE EMVKNKLEGK DKLTPWEQFL EKKKEKKRLK KKQKALAEED SEDELPSDVD
FNDPYFAEEV KKIGIKKKSM KSAKDSASSE EETDLEKQKA EMALLVMDEE EDSKKHFNYD
KIVEHQNLSK KKKKQLMKKK ELVEDDFEVN VSDARFQAMY TSHLFNLDPS DPNFKKTKAM
EKILEEKARH RERKEELLIQ AVERAQQDTG KPTQKQPMDP ALSMLIKSVK NKTEQFQARK
KQRVK
