EAF1_SCHPO
ID EAF1_SCHPO Reviewed; 251 AA.
AC A0ZWU1;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Ell1-associated factor 1;
GN Name=eaf1; ORFNames=SPCC1223.10c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1] {ECO:0000305, ECO:0000312|EMBL:ABM68355.1}
RP NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION
RP IN TRANSCRIPTION, INTERACTION WITH ELL1, AND SUBUNIT.
RX PubMed=17150956; DOI=10.1074/jbc.m610393200;
RA Banks C.A., Kong S.E., Spahr H., Florens L., Martin-Brown S.,
RA Washburn M.P., Conaway J.W., Mushegian A., Conaway R.C.;
RT "Identification and characterization of a Schizosaccharomyces pombe RNA
RT polymerase II elongation factor with similarity to the metazoan
RT transcription factor ELL.";
RL J. Biol. Chem. 282:5761-5769(2007).
RN [2] {ECO:0000312|EMBL:CAL92194.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-247, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
CC -!- FUNCTION: Activates transcription elongation by RNA polymerase II and
CC pyrophosphorolysis as a complex with ell1. Acts as a transcriptional
CC transactivator of ell1 elongation activities.
CC {ECO:0000269|PubMed:17150956}.
CC -!- SUBUNIT: Forms a stable heterodimer with ell1. Ell1-eaf1 complex
CC interacts with RNA polymerase II. {ECO:0000269|PubMed:17150956}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q96JC9}.
CC -!- SIMILARITY: Belongs to the EAF family. {ECO:0000255}.
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DR EMBL; EF192607; ABM68355.1; -; mRNA.
DR EMBL; CU329672; CAL92194.1; -; Genomic_DNA.
DR RefSeq; XP_001713171.1; XM_001713119.2.
DR AlphaFoldDB; A0ZWU1; -.
DR SMR; A0ZWU1; -.
DR BioGRID; 275676; 26.
DR STRING; 4896.SPCC1223.10c.1; -.
DR iPTMnet; A0ZWU1; -.
DR MaxQB; A0ZWU1; -.
DR PaxDb; A0ZWU1; -.
DR PRIDE; A0ZWU1; -.
DR EnsemblFungi; SPCC1223.10c.1; SPCC1223.10c.1:pep; SPCC1223.10c.
DR PomBase; SPCC1223.10c; eaf1.
DR VEuPathDB; FungiDB:SPCC1223.10c; -.
DR eggNOG; ENOG502SEGQ; Eukaryota.
DR HOGENOM; CLU_947163_0_0_1; -.
DR InParanoid; A0ZWU1; -.
DR OMA; RNVDCVL; -.
DR Reactome; R-SPO-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-SPO-75955; RNA Polymerase II Transcription Elongation.
DR PRO; PR:A0ZWU1; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0032783; C:super elongation complex; IDA:PomBase.
DR GO; GO:0008023; C:transcription elongation factor complex; IBA:GO_Central.
DR GO; GO:0003711; F:transcription elongation regulator activity; EXP:PomBase.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:PomBase.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0034243; P:regulation of transcription elongation from RNA polymerase II promoter; IBA:GO_Central.
DR GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; IDA:PomBase.
DR DisProt; DP01791; -.
DR InterPro; IPR027093; EAF_fam.
DR InterPro; IPR019194; Tscrpt_elong_fac_Eaf_N.
DR PANTHER; PTHR15970; PTHR15970; 1.
DR Pfam; PF09816; EAF; 1.
PE 1: Evidence at protein level;
KW Activator; Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..251
FT /note="Ell1-associated factor 1"
FT /id="PRO_0000307925"
FT REGION 110..187
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 201..251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 110..140
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 141..155
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 156..178
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 206..244
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 247
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 251 AA; 27657 MW; C194E0A3459E5245 CRC64;
MNSLQKGSYK VIPGSSFSKN SNGLLSIKYN FIPESVDPSR RGVLEKAQEA YRLRLPSTFD
DDRPHIFEGS CQRARNVDCV LIFNAKTKTF TLEHIDEIAR LNALRNPKVS KTVPSNAITQ
SDNSQISESK STSQSAVTTN STRRKEKELE ASKDGKIKPS SSNTRYPAIS SKGPITTDTN
DEPDMEVMEL DDFAKELELG FDQEFNSIDD PSTVSQTASK PISLRGLSSQ ERDYASSAQA
EGISSASEDE D
