TCEA2_MOUSE
ID TCEA2_MOUSE Reviewed; 299 AA.
AC Q9QVN7; O08667;
DT 12-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 12-FEB-2003, sequence version 2.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Transcription elongation factor A protein 2;
DE AltName: Full=Protein S-II-T1;
DE AltName: Full=Testis-specific S-II;
DE AltName: Full=Transcription elongation factor S-II protein 2;
DE AltName: Full=Transcription elongation factor TFIIS.l;
GN Name=Tcea2;
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].
RX PubMed=9133631; DOI=10.1093/oxfordjournals.jbchem.a021627;
RA Umehara T., Kida S., Hasegawa S., Fujimoto H., Horikoshi M.;
RT "Restricted expression of a member of the transcription elongation factor
RT S-II family in testicular germ cells during and after meiosis.";
RL J. Biochem. 121:598-603(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=ddY; TISSUE=Testis;
RX PubMed=9799847; DOI=10.1007/s003359900897;
RA Ito T., Seldin M.F., Taketo M.M., Kubo T., Natori S.;
RT "Gene organization and chromosome mapping of the testis-specific S-II.";
RL Mamm. Genome 9:915-917(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 80-190.
RX PubMed=8641458; DOI=10.1016/0014-5793(96)00340-7;
RA Ito T., Xu Q., Takeuchi H., Kubo T., Natori S.;
RT "Spermatocyte-specific expression of the gene for mouse testis-specific
RT transcription elongation factor S-II.";
RL FEBS Lett. 385:21-24(1996).
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: Interacts with the basal transcription factor GTF2B. Interacts
CC with REXO1 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- TISSUE SPECIFICITY: Testis and ovary specific. Specific to testicular
CC germ cells.
CC -!- DEVELOPMENTAL STAGE: Expressed in testicular germ cells during and
CC after meiosis in the course of spermatogenesis, while it is not
CC expressed in premeiotic or early meiotic testicular germ cells.
CC -!- SIMILARITY: Belongs to the TFS-II family. {ECO:0000305}.
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DR EMBL; D86081; BAA19752.1; -; mRNA.
DR EMBL; AB010271; BAA82313.1; -; mRNA.
DR CCDS; CCDS17219.1; -.
DR PIR; JC5430; JC5430.
DR RefSeq; NP_033352.1; NM_009326.2.
DR AlphaFoldDB; Q9QVN7; -.
DR SMR; Q9QVN7; -.
DR STRING; 10090.ENSMUSP00000099331; -.
DR PhosphoSitePlus; Q9QVN7; -.
DR MaxQB; Q9QVN7; -.
DR PaxDb; Q9QVN7; -.
DR PRIDE; Q9QVN7; -.
DR ProteomicsDB; 254677; -.
DR Antibodypedia; 15504; 132 antibodies from 18 providers.
DR DNASU; 21400; -.
DR Ensembl; ENSMUST00000103042; ENSMUSP00000099331; ENSMUSG00000059540.
DR GeneID; 21400; -.
DR KEGG; mmu:21400; -.
DR UCSC; uc012cmu.2; mouse.
DR CTD; 6919; -.
DR MGI; MGI:107368; Tcea2.
DR VEuPathDB; HostDB:ENSMUSG00000059540; -.
DR eggNOG; KOG1105; Eukaryota.
DR GeneTree; ENSGT00940000159974; -.
DR HOGENOM; CLU_037637_2_0_1; -.
DR InParanoid; Q9QVN7; -.
DR OMA; KMVTRKS; -.
DR OrthoDB; 1579101at2759; -.
DR PhylomeDB; Q9QVN7; -.
DR TreeFam; TF314970; -.
DR BioGRID-ORCS; 21400; 2 hits in 73 CRISPR screens.
DR PRO; PR:Q9QVN7; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q9QVN7; protein.
DR Bgee; ENSMUSG00000059540; Expressed in spermatocyte and 170 other tissues.
DR ExpressionAtlas; Q9QVN7; baseline and differential.
DR Genevisible; Q9QVN7; MM.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO: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 2: Evidence at transcript level;
KW DNA-binding; Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation;
KW Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..299
FT /note="Transcription elongation factor A protein 2"
FT /id="PRO_0000121450"
FT DOMAIN 5..82
FT /note="TFIIS N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00649"
FT DOMAIN 138..254
FT /note="TFIIS central"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00651"
FT ZN_FING 257..297
FT /note="TFIIS-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00472"
FT REGION 82..127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 86..105
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 261
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00472"
FT BINDING 264
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00472"
FT BINDING 289
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00472"
FT BINDING 292
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00472"
FT MOD_RES 59
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P23193"
FT MOD_RES 100
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P23193"
FT CROSSLNK 57
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q15560"
SQ SEQUENCE 299 AA; 33663 MW; F89A30B7984EEDDB CRC64;
MGKEEEIARI ARRLDKMVTR KNAEGAMDLL RELKNMPITL HLLQSTRVGM SVNALRKQSS
DEELIALAKS LIKSWKKLLD VSDGKSRNQG RGTPLPTSSS KDASRTTDLS CKKPDPPRTP
STPRITTFPQ VPITCDAVRN KCREMLTLAL QTDHDHVAVG VNCEHLSSQI EECIFLDVGN
TDMKYKNRVR SRISNLKDAK NPGLRRNVLC GAITPQQIAV MTSEEMASDE LKEIRKAMTK
EAIREHQMAR TGGTQTDLFT CNKCRKKNCT YTQVQTRSSD EPMTTYVVCN ECGNRWKFC
