SPT4B_MOUSE
ID SPT4B_MOUSE Reviewed; 117 AA.
AC Q9Z199;
DT 13-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 25-MAY-2022, entry version 122.
DE RecName: Full=Transcription elongation factor SPT4-B;
DE AltName: Full=DRB sensitivity-inducing factor small subunit 2;
DE Short=DSIF small subunit 2;
DE AltName: Full=Transcription elongation factor SPT4 2;
GN Name=Supt4h1b; Synonyms=Gm3258, Supt4b, Supt4h2;
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 [GENOMIC DNA], AND TISSUE SPECIFICITY.
RX PubMed=9776760; DOI=10.1093/nar/26.21.4960;
RA Chiang P.-W., Zhang R., Stubbs L., Zhang L., Zhu L., Kurnit D.M.;
RT "Comparison of murine Supt4h and a nearly identical expressed, processed
RT gene: evidence of sequence conservation through gene conversion extending
RT into the untranslated regions.";
RL Nucleic Acids Res. 26:4960-4964(1998).
CC -!- FUNCTION: Component of the DRB sensitivity-inducing factor complex
CC (DSIF complex), which regulates mRNA processing and transcription
CC elongation by RNA polymerase II. DSIF positively regulates mRNA capping
CC by stimulating the mRNA guanylyltransferase activity of RNGTT/CAP1A.
CC DSIF also acts cooperatively with the negative elongation factor
CC complex (NELF complex) to enhance transcriptional pausing at sites
CC proximal to the promoter. Transcriptional pausing may facilitate the
CC assembly of an elongation competent RNA polymerase II complex. DSIF and
CC NELF promote pausing by inhibition of the transcription elongation
CC factor TFIIS/S-II. TFIIS/S-II binds to RNA polymerase II at
CC transcription pause sites and stimulates the weak intrinsic nuclease
CC activity of the enzyme. Cleavage of blocked transcripts by RNA
CC polymerase II promotes the resumption of transcription from the new 3'
CC terminus and may allow repeated attempts at transcription through
CC natural pause sites (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with SUPT5H to form DSIF. DSIF interacts with the
CC positive transcription elongation factor b complex (P-TEFb complex),
CC which is composed of CDK9 and cyclin-T (CCNT1 or CCNT2). DSIF interacts
CC with RNA polymerase II, and this interaction is reduced by
CC phosphorylation of the C-terminal domain (CTD) of POLR2A by P-TEFb.
CC DSIF also interacts with the NELF complex, which is composed of
CC WHSC2/NELFA, COBRA1/NELFB, TH1L/NELFD and RDBP/NELFE, and this
CC interaction occurs following prior binding of DSIF to RNA polymerase
CC II. DSIF also interacts with HRMT1L2/PRMT1, HTATSF1/TATSF1,
CC RNGTT/CAP1A, SKB1/PRMT5, SUPT6H, and can interact with PIN1 (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in brain, heart and liver.
CC {ECO:0000269|PubMed:9776760}.
CC -!- SIMILARITY: Belongs to the SPT4 family. {ECO:0000305}.
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DR EMBL; U96810; AAC71660.1; -; Genomic_DNA.
DR RefSeq; NP_035639.1; NM_011509.2.
DR AlphaFoldDB; Q9Z199; -.
DR SMR; Q9Z199; -.
DR IntAct; Q9Z199; 1.
DR EPD; Q9Z199; -.
DR MaxQB; Q9Z199; -.
DR PRIDE; Q9Z199; -.
DR ProteomicsDB; 254548; -.
DR DNASU; 100041294; -.
DR GeneID; 100041294; -.
DR KEGG; mmu:100041294; -.
DR UCSC; uc011xck.1; mouse.
DR CTD; 100041294; -.
DR MGI; MGI:1335090; Supt4b.
DR InParanoid; Q9Z199; -.
DR OrthoDB; 1617752at2759; -.
DR BioGRID-ORCS; 100041294; 4 hits in 10 CRISPR screens.
DR PRO; PR:Q9Z199; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q9Z199; protein.
DR GO; GO:0032044; C:DSIF complex; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0046982; F:protein heterodimerization activity; ISO:MGI.
DR GO; GO:0000993; F:RNA polymerase II complex binding; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006325; P:chromatin organization; IBA:GO_Central.
DR GO; GO:0006397; P:mRNA processing; IBA:GO_Central.
DR GO; GO:0032785; P:negative regulation of DNA-templated transcription, elongation; ISO:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0032786; P:positive regulation of DNA-templated transcription, elongation; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0034243; P:regulation of transcription elongation from RNA polymerase II promoter; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; ISO:MGI.
DR CDD; cd07973; Spt4; 1.
DR Gene3D; 3.30.40.210; -; 1.
DR InterPro; IPR029040; RPABC4/Spt4.
DR InterPro; IPR009287; Spt4.
DR InterPro; IPR022800; Spt4/RpoE2_Znf.
DR InterPro; IPR038510; Spt4_sf.
DR PANTHER; PTHR12882; PTHR12882; 1.
DR Pfam; PF06093; Spt4; 1.
DR PIRSF; PIRSF025023; Spt4; 1.
DR SMART; SM01389; Spt4; 1.
DR SUPFAM; SSF63393; SSF63393; 1.
PE 2: Evidence at transcript level;
KW Activator; Metal-binding; Nucleus; Reference proteome; Repressor;
KW Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..117
FT /note="Transcription elongation factor SPT4-B"
FT /id="PRO_0000210328"
FT ZN_FING 16..36
FT /note="C4-type"
FT /evidence="ECO:0000255"
FT REGION 1..40
FT /note="Interaction with SUPT5H"
FT /evidence="ECO:0000250"
SQ SEQUENCE 117 AA; 13194 MW; 0EEAF000571D0F03 CRC64;
MALETVPKDL RHLRACLLCS LVKTIDQFEY DGCDNCDAYL QMKGNREMVY DCTSSSFDGI
NAMMSPEDSW VSKWQRVSNF KPGVYAVSVT GRLPQGIVRE LKSRGVAYKS RDTAIKT
