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   27-MAR-2024, entry version 143.
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 (By similarity). Associates with UBR5 and
CC       forms a transcription regulatory complex made of CDK9, Pol II, UBR5 and
CC       TCEA1/TFIIS (By similarity). Part of TBP-based Pol II pre-initiation
CC       complex (PIC), in which Pol II core assembles with general
CC       transcription factors and other specific initiation factors including
CC       GTF2E1, GTF2E2, GTF2F1, GTF2F2, TCEA1, ERCC2, ERCC3, GTF2H2, GTF2H3,
CC       GTF2H4, GTF2H5, GTF2A1, GTF2A2, GTF2B and TBP; this large multi-subunit
CC       PIC complex mediates DNA unwinding and targets Pol II core to the
CC       transcription start site where the first phosphodiester bond forms (By
CC       similarity). {ECO:0000250, ECO:0000250|UniProtKB:P23193}.
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; 10116-ENSRNOP00000010893; -.
DR   Ensembl; ENSRNOT00000007696.5; ENSRNOP00000097722.1; ENSRNOG00000005869.5.
DR   Ensembl; ENSRNOT00000104892.1; ENSRNOP00000084958.1; ENSRNOG00000022323.6.
DR   Ensembl; ENSRNOT00055022514; ENSRNOP00055018281; ENSRNOG00055013145.
DR   Ensembl; ENSRNOT00055029939; ENSRNOP00055024038; ENSRNOG00055017690.
DR   Ensembl; ENSRNOT00060016285; ENSRNOP00060012714; ENSRNOG00060009641.
DR   Ensembl; ENSRNOT00065030820; ENSRNOP00065024531; ENSRNOG00065018368.
DR   GeneID; 362479; -.
DR   KEGG; rno:362479; -.
DR   KEGG; rno:498453; -.
DR   UCSC; RGD:1309880; rat.
DR   AGR; RGD:1309880; -.
DR   AGR; RGD:1591965; -.
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; RFVVMTH; -.
DR   OrthoDB; 1383197at2759; -.
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 cell types or tissues.
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:0006351; P:DNA-templated transcription; IBA:GO_Central.
DR   GO; GO:0030218; P:erythrocyte differentiation; ISO:RGD.
DR   GO; GO:0045893; P:positive regulation of DNA-templated transcription; ISO:RGD.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD.
DR   GO; GO:0006368; P:transcription elongation by RNA polymerase II; IEA:InterPro.
DR   CDD; cd00183; TFIIS_I; 1.
DR   CDD; cd13749; Zn-ribbon_TFIIS; 1.
DR   Gene3D; 2.20.25.10; -; 1.
DR   Gene3D; 1.20.930.10; Conserved domain common to transcription factors TFIIS, elongin A, CRSP70; 1.
DR   Gene3D; 1.10.472.30; Transcription elongation factor S-II, central domain; 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   NCBIfam; TIGR01385; TFSII; 1.
DR   PANTHER; PTHR11477:SF1; TRANSCRIPTION ELONGATION FACTOR A PROTEIN 1; 1.
DR   PANTHER; PTHR11477; TRANSCRIPTION FACTOR S-II ZINC FINGER DOMAIN-CONTAINING PROTEIN; 1.
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; SSF47676; Conserved domain common to transcription factors TFIIS, elongin A, CRSP70; 1.
DR   SUPFAM; SSF46942; Elongation factor TFIIS domain 2; 1.
DR   SUPFAM; SSF57783; Zinc beta-ribbon; 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.
DR   Genevisible; Q4KLL0; RN.
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
//