ID   TCEA1_RAT               Reviewed;         301 AA.
AC   Q4KLL0;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   03-AUG-2022, entry version 134.
DE   RecName: Full=Transcription elongation factor A protein 1;
DE   AltName: Full=Transcription elongation factor S-II protein 1;
GN   Name=Tcea1;
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 [LARGE SCALE MRNA].
RC   TISSUE=Placenta;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-100, AND IDENTIFICATION BY
RP   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: Necessary for efficient RNA polymerase II transcription
CC       elongation past template-encoded arresting sites. The arresting sites
CC       in DNA have the property of trapping a certain fraction of elongating
CC       RNA polymerases that pass through, resulting in locked ternary
CC       complexes. Cleavage of the nascent transcript by S-II allows the
CC       resumption of elongation from the new 3'-terminus (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with EAF2. Associates with UBR5 and forms a
CC       transcription regulatory complex made of CDK9, RNAP II, UBR5 and
CC       TFIIS/TCEA1 that can stimulate target gene transcription by recruiting
CC       their promoters. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00649,
CC       ECO:0000255|PROSITE-ProRule:PRU00651}.
CC   -!- MISCELLANEOUS: S-II binds to RNA-polymerase II in the absence of
CC       transcription.
CC   -!- SIMILARITY: Belongs to the TFS-II family. {ECO:0000305}.
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DR   EMBL; BC099141; AAH99141.1; -; mRNA.
DR   RefSeq; NP_001020906.1; NM_001025735.1.
DR   RefSeq; XP_003752832.1; XM_003752784.4.
DR   RefSeq; XP_006237878.1; XM_006237816.3.
DR   RefSeq; XP_006251782.1; XM_006251720.3.
DR   AlphaFoldDB; Q4KLL0; -.
DR   SMR; Q4KLL0; -.
DR   BioGRID; 263480; 1.
DR   STRING; 10116.ENSRNOP00000010893; -.
DR   iPTMnet; Q4KLL0; -.
DR   PhosphoSitePlus; Q4KLL0; -.
DR   jPOST; Q4KLL0; -.
DR   PaxDb; Q4KLL0; -.
DR   PRIDE; Q4KLL0; -.
DR   Ensembl; ENSRNOT00000007696; ENSRNOP00000097722; ENSRNOG00000005869.
DR   Ensembl; ENSRNOT00000104892; ENSRNOP00000084958; ENSRNOG00000022323.
DR   GeneID; 362479; -.
DR   GeneID; 498453; -.
DR   KEGG; rno:362479; -.
DR   KEGG; rno:498453; -.
DR   UCSC; RGD:1309880; rat.
DR   CTD; 498453; -.
DR   CTD; 6917; -.
DR   RGD; 1309880; Tcea1.
DR   eggNOG; KOG1105; Eukaryota.
DR   GeneTree; ENSGT00940000155121; -.
DR   HOGENOM; CLU_037637_2_0_1; -.
DR   InParanoid; Q4KLL0; -.
DR   OMA; TTFCECT; -.
DR   OrthoDB; 1579101at2759; -.
DR   PhylomeDB; Q4KLL0; -.
DR   TreeFam; TF314970; -.
DR   Reactome; R-RNO-112382; Formation of RNA Pol II elongation complex.
DR   Reactome; R-RNO-674695; RNA Polymerase II Pre-transcription Events.
DR   Reactome; R-RNO-6781823; Formation of TC-NER Pre-Incision Complex.
DR   Reactome; R-RNO-6782135; Dual incision in TC-NER.
DR   Reactome; R-RNO-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR   Reactome; R-RNO-6796648; TP53 Regulates Transcription of DNA Repair Genes.
DR   Reactome; R-RNO-75955; RNA Polymerase II Transcription Elongation.
DR   PRO; PR:Q4KLL0; -.
DR   Proteomes; UP000002494; Chromosome 15.
DR   Proteomes; UP000002494; Chromosome 5.
DR   Bgee; ENSRNOG00000022323; Expressed in thymus and 19 other tissues.
DR   Genevisible; Q4KLL0; RN.
DR   GO; GO:0005654; C:nucleoplasm; ISO:RGD.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0005669; C:transcription factor TFIID complex; ISO:RGD.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0030218; P:erythrocyte differentiation; ISO:RGD.
DR   GO; GO:1901919; P:positive regulation of exoribonuclease activity; IDA:RGD.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:RGD.
DR   GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; IEA:InterPro.
DR   GO; GO:0006351; P:transcription, DNA-templated; IBA:GO_Central.
DR   Gene3D; 1.10.472.30; -; 1.
DR   Gene3D; 1.20.930.10; -; 1.
DR   InterPro; IPR035100; TF_IIS-typ.
DR   InterPro; IPR003617; TFIIS/CRSP70_N_sub.
DR   InterPro; IPR035441; TFIIS/LEDGF_dom_sf.
DR   InterPro; IPR003618; TFIIS_cen_dom.
DR   InterPro; IPR036575; TFIIS_cen_dom_sf.
DR   InterPro; IPR017923; TFIIS_N.
DR   InterPro; IPR006289; TFSII.
DR   InterPro; IPR001222; Znf_TFIIS.
DR   Pfam; PF08711; Med26; 1.
DR   Pfam; PF01096; TFIIS_C; 1.
DR   Pfam; PF07500; TFIIS_M; 1.
DR   PIRSF; PIRSF006704; TF_IIS; 1.
DR   SMART; SM00510; TFS2M; 1.
DR   SMART; SM00509; TFS2N; 1.
DR   SMART; SM00440; ZnF_C2C2; 1.
DR   SUPFAM; SSF46942; SSF46942; 1.
DR   SUPFAM; SSF47676; SSF47676; 1.
DR   TIGRFAMs; TIGR01385; TFSII; 1.
DR   PROSITE; PS51321; TFIIS_CENTRAL; 1.
DR   PROSITE; PS51319; TFIIS_N; 1.
DR   PROSITE; PS00466; ZF_TFIIS_1; 1.
DR   PROSITE; PS51133; ZF_TFIIS_2; 1.
PE   1: Evidence at protein level;
KW   Acetylation; DNA-binding; Isopeptide bond; Metal-binding; Nucleus;
KW   Phosphoprotein; Reference proteome; Transcription;
KW   Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT   CHAIN           1..301
FT                   /note="Transcription elongation factor A protein 1"
FT                   /id="PRO_0000121448"
FT   DOMAIN          3..80
FT                   /note="TFIIS N-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00649"
FT   DOMAIN          140..256
FT                   /note="TFIIS central"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00651"
FT   ZN_FING         259..299
FT                   /note="TFIIS-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00472"
FT   REGION          76..139
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        77..95
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        109..123
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         263
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00472"
FT   BINDING         266
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00472"
FT   BINDING         291
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00472"
FT   BINDING         294
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00472"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:P23193"
FT   MOD_RES         57
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P23193"
FT   MOD_RES         81
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P23193"
FT   MOD_RES         97
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P23193"
FT   MOD_RES         100
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   CROSSLNK        55
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250|UniProtKB:Q15560"
SQ   SEQUENCE   301 AA;  33893 MW;  AD85071FBB589CB5 CRC64;
     MEDEVVRIAK KMDKMVQKKN AAGALDLLKE LKNIPMTLEL LQSTRIGMSV NAIRKQSTDE
     EVTSLAKSLI KSWKKLLDGP STDKDSEEKK KEPAISSQNS PEAREESSSS SHVSSRKDET
     NARDTYVSSF PRAPSTSDSV RLKCREMLAA ALRTGDDYVA IGADEEELGS QIEEAIYQEI
     RNTDMKYKNR VRSRISNLKD AKNPNLRKNV LCGNIPPDLF ARMTAEEMAS DELKEMRKNL
     TKEAIREHQM AKTGGTQTDL FTCGKCKKKN CTYTQVQTRS ADEPMTTFVV CNECGNRWKF
     C