SSN2_YARLI
ID SSN2_YARLI Reviewed; 1324 AA.
AC Q6C9Q9;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 3.
DT 25-MAY-2022, entry version 72.
DE RecName: Full=Mediator of RNA polymerase II transcription subunit 13;
DE AltName: Full=Mediator complex subunit 13;
GN Name=SSN2; Synonyms=MED13; OrderedLocusNames=YALI0D09086g;
OS Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Dipodascaceae; Yarrowia.
OX NCBI_TaxID=284591;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLIB 122 / E 150;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
CC -!- FUNCTION: Component of the SRB8-11 complex. The SRB8-11 complex is a
CC regulatory module of the Mediator complex which is itself involved in
CC regulation of basal and activated RNA polymerase II-dependent
CC transcription. The SRB8-11 complex may be involved in the
CC transcriptional repression of a subset of genes regulated by Mediator.
CC It may inhibit the association of the Mediator complex with RNA
CC polymerase II to form the holoenzyme complex (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Component of the SRB8-11 complex, which itself associates with
CC the Mediator complex. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the Mediator complex subunit 13 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAG80791.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; CR382130; CAG80791.2; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_502603.2; XM_502603.2.
DR AlphaFoldDB; Q6C9Q9; -.
DR STRING; 4952.CAG80791; -.
DR GeneID; 2910829; -.
DR KEGG; yli:YALI0D09086g; -.
DR InParanoid; Q6C9Q9; -.
DR Proteomes; UP000001300; Chromosome D.
DR GO; GO:0016592; C:mediator complex; IBA:GO_Central.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR InterPro; IPR009401; Med13_C.
DR InterPro; IPR021643; Mediator_Med13_N.
DR Pfam; PF06333; Med13_C; 1.
DR Pfam; PF11597; Med13_N; 1.
PE 3: Inferred from homology;
KW Activator; Nucleus; Reference proteome; Repressor; Transcription;
KW Transcription regulation.
FT CHAIN 1..1324
FT /note="Mediator of RNA polymerase II transcription subunit
FT 13"
FT /id="PRO_0000314252"
FT REGION 296..346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 386..455
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 535..590
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 607..631
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 694..816
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1151..1198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 296..338
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 387..441
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 543..562
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 563..590
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 617..631
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 718..816
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1179..1198
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1324 AA; 143232 MW; 1C0AF1F3FEAF9491 CRC64;
MHRPRSSWPN LVWDHSFPHH VLTQGKYTTI PYRTYICLQG NETSLKEAEW AIRNDNPRAL
VKSYNKELWT FTLQEGVTPP SALDRFQLTE TTTGVFLPST TTPSSLTMTK QLTPPGYVAL
MLAIEAMIQE ALKRDDHYVP FGNNLILPVT GDLLHLDARL TPGGDLLLQM YQQETEWEMF
GKRKRDVANE IVGTKVVVAP TLVEGVVENS TNQIPDNLPV LLEMLDCLCS VRLRAKKQWT
AVRIDTEVLL WPTELLFVDR KSATGKLEDE GKDALLWTED ILDSVFEATQ LIRRGESGVN
TNESTAAQPQ PAQNGTNSMA PAAGTTNATT QRNEENKQIY PTPPEAPKRI LPGILLERAT
APAGGWGELD EELFGGDEVT EADFNFFDDM GGDKNDTDGD NDNGNDNDND KADAMDVDVK
EEAKKEEMIK KETKEEVPVK EEVQEEEPDE SATTAALLTN NPAEEKAVVH GVNDSSTVNG
AVDAAVSATV VSSVPYLPSD FDQLIVNPAE QRTFALVEFN REAEQRLNDK YAAGGRFFVP
DDSSSDNEGS SDNTGDSSDS GDGSESVPRD VKRQKVDEGT LSDQTDEPEI DAKQLHQQWS
AILNYNHDDK PAKKIDSSND TTNSDGNSNN SNYEEAVQRL AEQVVWDNSC YKGLVPQENY
YRPPSARFVK VVEQVFGDTS KRLSLIDFAK MSDKGGQQQP GVGMPINAAA GTAGGGPGTP
VTVSNASGVP SGSSGAQASQ MGALAVGSAL SPSRGATPQP EGSSPETRPS NWTPGITSQV
NSAASSPVPL QQHQQQQQSF SPMSPQTPAQ APVPSANSFA NAANAAPTQR LATPMYSFMR
GGSLIKAQPP ILRFWSTFGL SPRNGPKPLT LTLIYPSGTA IGDAAAAFLI SFKMCYEGCG
FGLVTLGGSN GTGVVSSDYK NLDVSREGVL LVSNPYNDVL GFLNLAKAAA AGSKTATSTS
TILTLPCSIF ASYTALRAPS AMLLAALCRN LYDHLPPTST KRRYGSVIQR QAPACVISKP
VPPFINFKLL ANTPDSVINE DSLLHVAYAA SNRWITCAWS DQWGELAKVK VFCLQSESGP
LRTLEEVCTE IWETTLQLNG STDVRSVAVA KLGGMLDDEL AMWLRVSSVT RGRRITPFFL
VVDNRPSMVV TGSDDGSKGG NVAGGPAPAP PTGAAGAAST GSAPMSTPFR DTDSPDIYNH
VTTPSVGEDK IDYDDMSIVD VHDEIHSVTL NHRQPLTMHS TRLGLATGYL VKTSPLNPNQ
LLVFSLTFVN CPCVVMHVAM KHFLRQYRNL ISLAATTGVC DPEYAIVPWH VEAVDKMMRL
VEEL