ELL1_SCHPO
ID ELL1_SCHPO Reviewed; 533 AA.
AC Q9P7X2;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=RNA polymerase II elongation factor ell1;
GN Name=ell1 {ECO:0000312|EMBL:CAB66442.1}; ORFNames=SPBP23A10.14c;
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}
RP NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION
RP IN TRANSCRIPTION, INTERACTION WITH EAF1, 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:CAB66442.1}
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] {ECO:0000305}
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
CC -!- FUNCTION: Activates transcription elongation by RNA polymerase II and
CC pyrophosphorolysis as a complex with eaf1. Elongation factor that can
CC increase the catalytic rate of RNA polymerase II transcription by
CC suppressing transient pausing by the polymerase at multiple sites along
CC the DNA. {ECO:0000269|PubMed:17150956}.
CC -!- SUBUNIT: Forms a stable heterodimer with eaf1. Ell1-eaf1 complex
CC interacts with RNA polymerase II. {ECO:0000269|PubMed:17150956}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16823372}.
CC -!- MISCELLANEOUS: Deletion of ell1 renders cells sensitive to the drug 6-
CC azauracil. {ECO:0000250|UniProtKB:P55199, ECO:0000269|PubMed:17150956}.
CC -!- SIMILARITY: Belongs to the ELL/occludin family. {ECO:0000255}.
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DR EMBL; CU329671; CAB66442.1; -; Genomic_DNA.
DR PIR; T50401; T50401.
DR RefSeq; NP_595826.1; NM_001021730.2.
DR AlphaFoldDB; Q9P7X2; -.
DR SMR; Q9P7X2; -.
DR BioGRID; 277771; 21.
DR STRING; 4896.SPBP23A10.14c.1; -.
DR iPTMnet; Q9P7X2; -.
DR MaxQB; Q9P7X2; -.
DR PaxDb; Q9P7X2; -.
DR PRIDE; Q9P7X2; -.
DR EnsemblFungi; SPBP23A10.14c.1; SPBP23A10.14c.1:pep; SPBP23A10.14c.
DR GeneID; 2541257; -.
DR KEGG; spo:SPBP23A10.14c; -.
DR PomBase; SPBP23A10.14c; ell1.
DR VEuPathDB; FungiDB:SPBP23A10.14c; -.
DR HOGENOM; CLU_500734_0_0_1; -.
DR InParanoid; Q9P7X2; -.
DR OMA; APHEVYR; -.
DR PRO; PR:Q9P7X2; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0032783; C:super elongation complex; IDA:PomBase.
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:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; IC:PomBase.
DR GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; IDA:PomBase.
DR Gene3D; 1.10.10.2670; -; 1.
DR InterPro; IPR042065; E3_ELL-like.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR SUPFAM; SSF46785; SSF46785; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Nucleus; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..533
FT /note="RNA polymerase II elongation factor ell1"
FT /id="PRO_0000307924"
FT REGION 112..193
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 303..460
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 104..132
FT /evidence="ECO:0000255"
FT COMPBIAS 112..129
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 149..172
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 303..448
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 533 AA; 59358 MW; BE757B69FC2657E0 CRC64;
MIRNSSISDA LPVALGGNEE ESPLLMLVQL PKEFLEGYLS GTITDVSLEC SDVGTSILAN
DRSYKCTSVP ETAPHEIYRL VDSNSLQLVG RVSQKLQLRR ELDSLTAERV KNRTQEAQKE
KEEKRIVTLQ NDGGSKNTTA RKQKQLKKNG LRPLNTSASR IGLSSSPTNT PSPNLPVSQP
SASPHYSGDK NSAKGIDLRT RVIQLLAIAP ETEDFLRLRT KASLSKLQAL LPEVAWKNNM
NQWELLNPVY KDVRVFDWRP YSIADRNAVL SRMSNAFDNM QLPPDAPERS LLVSKQKNIT
KLNNEKRIPP QLAQPTSHVP SFIDTNSPSM PSISSVSSYQ QQHRIPKLNA SNYSPLLSPS
SHRKTSGNLS RTGSESSAVS LSDTTNLNTP ISDIPSPGSS TTCSNLSSPH IKRKSRSPPQ
SLPSTPFPTS SSSTNGTLEP NANSPKKNEQ DAWIAKKRRQ QRYTTEEMRA LAKRFRETYP
RYKNLYLKVS SYYDNNDTNN PNLNKLQDEL ISLHSQLKSW KNTLYDASSE LAL
