TCEA1_MOUSE
ID TCEA1_MOUSE Reviewed; 301 AA.
AC P10711; P10712; P23713;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 12-FEB-2003, sequence version 2.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Transcription elongation factor A protein 1;
DE AltName: Full=Transcription elongation factor S-II protein 1;
DE AltName: Full=Transcription elongation factor TFIIS.o;
GN Name=Tcea1; Synonyms=Tceat;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND PARTIAL PROTEIN
RP SEQUENCE.
RX PubMed=3346229; DOI=10.1016/s0021-9258(18)69004-0;
RA Hirashima S., Hirai H., Nakanishi Y., Natori S.;
RT "Molecular cloning and characterization of cDNA for eukaryotic
RT transcription factor S-II.";
RL J. Biol. Chem. 263:3858-3863(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver, and Mammary gland;
RX PubMed=1917889; DOI=10.1093/oxfordjournals.jbchem.a123439;
RA Kanai A., Kuzuhara T., Sekimizu K., Natori S.;
RT "Heterogeneity and tissue-specific expression of eukaryotic transcription
RT factor S-II-related protein mRNA.";
RL J. Biochem. 109:674-677(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=Czech II, and FVB/N; TISSUE=Mammary gland, and Olfactory epithelium;
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 [4]
RP INTERACTION WITH EAF2.
RX PubMed=12761297; DOI=10.1093/jb/mvg065;
RA Saso K., Ito T., Natori S., Sekimizu K.;
RT "Identification of a novel tissue-specific transcriptional activator FESTA
RT as a protein that interacts with the transcription elongation factor S-
RT II.";
RL J. Biochem. 133:493-500(2003).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-100, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-100, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18630941; DOI=10.1021/pr800223m;
RA Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT "Specific phosphopeptide enrichment with immobilized titanium ion affinity
RT chromatography adsorbent for phosphoproteome analysis.";
RL J. Proteome Res. 7:3957-3967(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-97 AND SER-100, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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.
CC -!- SUBUNIT: Associates with UBR5 and forms a transcription regulatory
CC complex made of CDK9, RNAP II, UBR5 and TFIIS/TCEA1 that can stimulates
CC target gene transcription by recruiting their promoters (By
CC similarity). Interacts with EAF2. {ECO:0000250,
CC ECO:0000269|PubMed:12761297}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=2; Synonyms=PSII-3;
CC IsoId=P10711-1; Sequence=Displayed;
CC Name=1; Synonyms=PSII-2;
CC IsoId=P10711-2; Sequence=VSP_006410;
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA00768.1; Type=Miscellaneous discrepancy; Note=Chimeric cDNA.; Evidence={ECO:0000305};
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DR EMBL; M18209; AAA40418.1; -; mRNA.
DR EMBL; M18210; AAA40419.1; -; mRNA.
DR EMBL; D00925; BAA00768.1; ALT_SEQ; mRNA.
DR EMBL; BC006022; AAH06022.1; -; mRNA.
DR EMBL; BC061490; AAH61490.1; -; mRNA.
DR EMBL; BC083127; AAH83127.1; -; mRNA.
DR CCDS; CCDS35505.1; -. [P10711-1]
DR PIR; A29950; A29950.
DR RefSeq; NP_001153222.1; NM_001159750.1.
DR RefSeq; NP_001153223.1; NM_001159751.1.
DR RefSeq; NP_035671.1; NM_011541.4. [P10711-1]
DR AlphaFoldDB; P10711; -.
DR SMR; P10711; -.
DR BioGRID; 203995; 13.
DR IntAct; P10711; 2.
DR MINT; P10711; -.
DR STRING; 10090.ENSMUSP00000129157; -.
DR iPTMnet; P10711; -.
DR PhosphoSitePlus; P10711; -.
DR EPD; P10711; -.
DR MaxQB; P10711; -.
DR PaxDb; P10711; -.
DR PeptideAtlas; P10711; -.
DR PRIDE; P10711; -.
DR ProteomicsDB; 263021; -. [P10711-1]
DR ProteomicsDB; 263022; -. [P10711-2]
DR Antibodypedia; 6001; 215 antibodies from 27 providers.
DR DNASU; 21399; -.
DR Ensembl; ENSMUST00000081551; ENSMUSP00000080266; ENSMUSG00000033813. [P10711-1]
DR GeneID; 21399; -.
DR KEGG; mmu:21399; -.
DR UCSC; uc007afi.2; mouse. [P10711-1]
DR CTD; 6917; -.
DR MGI; MGI:1196624; Tcea1.
DR VEuPathDB; HostDB:ENSMUSG00000033813; -.
DR eggNOG; KOG1105; Eukaryota.
DR GeneTree; ENSGT00940000155121; -.
DR HOGENOM; CLU_037637_2_0_1; -.
DR InParanoid; P10711; -.
DR OMA; TTFCECT; -.
DR OrthoDB; 1579101at2759; -.
DR PhylomeDB; P10711; -.
DR Reactome; R-MMU-112382; Formation of RNA Pol II elongation complex.
DR Reactome; R-MMU-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-MMU-6781823; Formation of TC-NER Pre-Incision Complex.
DR Reactome; R-MMU-6782135; Dual incision in TC-NER.
DR Reactome; R-MMU-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR Reactome; R-MMU-6796648; TP53 Regulates Transcription of DNA Repair Genes.
DR Reactome; R-MMU-75955; RNA Polymerase II Transcription Elongation.
DR BioGRID-ORCS; 21399; 10 hits in 77 CRISPR screens.
DR ChiTaRS; Tcea1; mouse.
DR PRO; PR:P10711; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; P10711; protein.
DR Bgee; ENSMUSG00000033813; Expressed in animal zygote and 264 other tissues.
DR ExpressionAtlas; P10711; baseline and differential.
DR Genevisible; P10711; MM.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; IDA:MGI.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005669; C:transcription factor TFIID complex; ISO:MGI.
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; IMP:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:MGI.
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; Alternative splicing; Direct protein sequencing; DNA-binding;
KW Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation;
KW Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..301
FT /note="Transcription elongation factor A protein 1"
FT /id="PRO_0000121447"
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 96..116
FT /note="Polar 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:0007744|PubMed:21183079"
FT MOD_RES 100
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:18630941, ECO:0007744|PubMed:21183079"
FT CROSSLNK 55
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q15560"
FT VAR_SEQ 1..35
FT /note="Missing (in isoform 1)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:3346229"
FT /id="VSP_006410"
SQ SEQUENCE 301 AA; 33880 MW; 14B5105F8D77DA87 CRC64;
MEDEVVRIAK KMDKMVQKKN AAGALDLLKE LKNIPMTLEL LQSTRIGMSV NALRKQSTDE
EVTSLAKSLI KSWKKLLDGP STDKDPEEKK KEPAISSQNS PEAREESSSS SNVSSRKDET
NARDTYVSSF PRAPSTSDSV RLKCREMLAA ALRTGDDYVA IGADEEELGS QIEEAIYQEI
RNTDMKYKNR VRSRISNLKD AKNPNLRKNV LCGNIPPDLF ARMTAEEMAS DELKEMRKNL
TKEAIREHQM AKTGGTQTDL FTCGKCKKKN CTYTQVQTRS ADEPMTTFVV CNECGNRWKF
C
