ESF1_RAT
ID ESF1_RAT Reviewed; 842 AA.
AC Q76MT4;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=ESF1 homolog;
DE AltName: Full=ABT1-associated protein;
GN Name=Esf1; Synonyms=Abtap;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH ABT1, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, AND POSSIBLE FUNCTION.
RX PubMed=15660422; DOI=10.1002/jcb.20114;
RA Oda T., Fukuda A., Hagiwara H., Masuho Y., Muramatsu M.-A., Hisatake K.,
RA Yamashita T.;
RT "ABT1-associated protein (ABTAP), a novel nuclear protein conserved from
RT yeast to mammals, represses transcriptional activation by ABT1.";
RL J. Cell. Biochem. 93:788-806(2004).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75; SER-77; SER-79; SER-82;
RP SER-180; THR-303; SER-304; SER-305; SER-648; SER-654 AND SER-686, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
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).
CC -!- FUNCTION: May constitute a novel regulatory system for basal
CC transcription. Negatively regulates ABT1.
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. Disrupts the interaction between ABT1 and TATA-binding
CC protein (TBP), and suppresses the ABT1-induced activation of polymerase
CC II-directed basal transcription in vitro.
CC {ECO:0000269|PubMed:15660422}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:15660422}.
CC Nucleus, nucleoplasm {ECO:0000269|PubMed:15660422}. Note=Is
CC concomitantly relocalized into discrete nuclear bodies at higher
CC expression.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC {ECO:0000269|PubMed:15660422}.
CC -!- SIMILARITY: Belongs to the ESF1 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB038233; BAD10946.1; -; mRNA.
DR RefSeq; NP_001094241.1; NM_001100771.1.
DR RefSeq; XP_006235167.1; XM_006235105.3.
DR RefSeq; XP_006235168.1; XM_006235106.2.
DR RefSeq; XP_017447439.1; XM_017591950.1.
DR AlphaFoldDB; Q76MT4; -.
DR STRING; 10116.ENSRNOP00000037915; -.
DR iPTMnet; Q76MT4; -.
DR PhosphoSitePlus; Q76MT4; -.
DR jPOST; Q76MT4; -.
DR PaxDb; Q76MT4; -.
DR PRIDE; Q76MT4; -.
DR Ensembl; ENSRNOT00000034487; ENSRNOP00000037915; ENSRNOG00000004777.
DR GeneID; 366203; -.
DR KEGG; rno:366203; -.
DR UCSC; RGD:1306067; rat.
DR CTD; 51575; -.
DR RGD; 1306067; Esf1.
DR eggNOG; KOG2318; Eukaryota.
DR GeneTree; ENSGT00390000004881; -.
DR HOGENOM; CLU_010564_2_1_1; -.
DR InParanoid; Q76MT4; -.
DR OMA; LTWDETA; -.
DR OrthoDB; 1300279at2759; -.
DR PhylomeDB; Q76MT4; -.
DR PRO; PR:Q76MT4; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Bgee; ENSRNOG00000004777; Expressed in lung and 19 other tissues.
DR Genevisible; Q76MT4; RN.
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; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9H501"
FT CHAIN 2..842
FT /note="ESF1 homolog"
FT /id="PRO_0000233167"
FT REGION 54..317
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 534..568
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 631..657
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 674..693
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 785..816
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 772..804
FT /evidence="ECO:0000255"
FT COMPBIAS 54..185
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 191..206
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 210..230
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 253..289
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 534..550
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 551..568
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 785..799
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:0007744|PubMed:22673903"
FT MOD_RES 77
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 79
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 82
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 135
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H501"
FT MOD_RES 155
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H501"
FT MOD_RES 180
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 198
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H501"
FT MOD_RES 288
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 303
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 304
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 305
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 605
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H501"
FT MOD_RES 648
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 654
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 686
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 726
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H501"
SQ SEQUENCE 842 AA; 97534 MW; 590CF5618ABF1C10 CRC64;
MSSKQEIMDD QRFRRVSKDP RFWEMPEKDR KVKIDKRFRA MFHDKKFKLN YAVDKRGRPI
SHSTTEDLKR FYDLSDSDSD LSDEESKVLD EKRVKEKKKQ TKKETKSKTP IEEKKKETKK
TDQKDSINKN DLNNSERIQK MKNSHKSPKI DSEVSPKDSE ESLQSRKKKR DTTDLSVEAS
PKGKLRTKDP STSAMVKSST VSGSKAKREK QAVIMAKDNA GRMLHEEAPE EDSDSASELG
RDEESEGEIT SDDRASADDD ENEDEEEEED GEEEEEEEEE EDESDDESDS GPDLARGKGN
VETSSEDEDD LADLFPEEPG FEHAWRELDK DAPRADEITR RLAVCNMDWD RLKAKDLLAL
FNSFKPKGGV VFSVKIYPSE FGKQRMKEEQ IQGPVELLSI PEDAPEKDWA SREKLRDYQF
KRLKYYYAVV ECDSPETASK IYEDCDGLEF ESSCSFIDLR FIPDDITFDD EPKDAASEVD
LTAYKPKYFT SAAMGTSTVE ITWDETDHER ITTLNRKFKK DELLDMDFEA YLASSSEDEE
EVEEAPEGED GVSIEDGKTK KSQKDDEEQI AKYRQLLQVI QEKEKKGKEN DMEMEIKWVP
GLKESAEEMV KNKLEGKDKL TPWEQFLEKK KEKKRLKKKQ KALAEEASED EIPSDVDLND
PYFAEEVKKI GIKKKSMKSA KDGATSEEET ELEKQKAEMA LLVMDEEEDS KKHFNYDKIV
EHQNLSKKKK KQLMKKKELL EDDFEVNVSD ARFQAMYTSH LFNLDPSDPN FKKTKAMEKI
LEEKARHREQ KEERLIQAVE RAQQDTGKPA QKQPMDPALS MLIKSVKNKT EQFQARKKQR
IK
