SPT4A_MOUSE
ID SPT4A_MOUSE Reviewed; 117 AA.
AC P63271; B2KGH6; Q16550; Q3TIA2; Q5NCP8; Q5NCP9; Q5NCQ0; Q62387;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Transcription elongation factor SPT4-A;
DE AltName: Full=DRB sensitivity-inducing factor small subunit 1;
DE Short=DSIF small subunit 1;
DE AltName: Full=Transcription elongation factor SPT4 1;
GN Name=Supt4h1a; Synonyms=Spt4h, Supt4a, Supt4h;
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], AND TISSUE SPECIFICITY.
RC STRAIN=Swiss Webster;
RX PubMed=8786137; DOI=10.1006/geno.1996.0299;
RA Chiang P.-W., Wang S.-Q., Smithivas P., Song W.-J., Crombez E., Akhtar A.,
RA Im R., Greenfield J., Ramamoorthy S., van Keuren M.L., Blackburn C.C.,
RA Tsai C.-H., Kurnit D.M.;
RT "Isolation and characterization of the human and mouse homologues (SUPT4H
RT and Supt4h) of the yeast SPT4 gene.";
RL Genomics 34:368-375(1996).
RN [2]
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).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=DBA/2J;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N-3; TISSUE=Brain, Liver, and Mammary tumor;
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).
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: Widely expressed. {ECO:0000269|PubMed:8786137,
CC ECO:0000269|PubMed:9776760}.
CC -!- SIMILARITY: Belongs to the SPT4 family. {ECO:0000305}.
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DR EMBL; U43154; AAB18730.1; -; mRNA.
DR EMBL; U96809; AAC71659.1; -; Genomic_DNA.
DR EMBL; AK167941; BAE39944.1; -; mRNA.
DR EMBL; AL604022; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CU393486; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466556; EDL15830.1; -; Genomic_DNA.
DR EMBL; BC024391; AAH24391.1; -; mRNA.
DR EMBL; BC061174; AAH61174.1; -; mRNA.
DR EMBL; BC087923; AAH87923.1; -; mRNA.
DR EMBL; BC141092; AAI41093.1; -; mRNA.
DR CCDS; CCDS36270.1; -.
DR RefSeq; NP_033322.1; NM_009296.1.
DR AlphaFoldDB; P63271; -.
DR SMR; P63271; -.
DR BioGRID; 203573; 2.
DR IntAct; P63271; 2.
DR STRING; 10090.ENSMUSP00000091487; -.
DR iPTMnet; P63271; -.
DR PhosphoSitePlus; P63271; -.
DR EPD; P63271; -.
DR MaxQB; P63271; -.
DR PaxDb; P63271; -.
DR PeptideAtlas; P63271; -.
DR PRIDE; P63271; -.
DR ProteomicsDB; 261578; -.
DR Antibodypedia; 18387; 173 antibodies from 27 providers.
DR DNASU; 20922; -.
DR Ensembl; ENSMUST00000093955; ENSMUSP00000091487; ENSMUSG00000020485.
DR GeneID; 20922; -.
DR KEGG; mmu:20922; -.
DR UCSC; uc007kuj.1; mouse.
DR CTD; 20922; -.
DR MGI; MGI:107416; Supt4a.
DR VEuPathDB; HostDB:ENSMUSG00000020485; -.
DR eggNOG; KOG3490; Eukaryota.
DR GeneTree; ENSGT00390000018559; -.
DR HOGENOM; CLU_138052_3_0_1; -.
DR InParanoid; P63271; -.
DR OMA; FDGMIAV; -.
DR OrthoDB; 1617752at2759; -.
DR PhylomeDB; P63271; -.
DR TreeFam; TF300105; -.
DR Reactome; R-MMU-112382; Formation of RNA Pol II elongation complex.
DR Reactome; R-MMU-113418; Formation of the Early Elongation Complex.
DR Reactome; R-MMU-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-MMU-6796648; TP53 Regulates Transcription of DNA Repair Genes.
DR Reactome; R-MMU-6807505; RNA polymerase II transcribes snRNA genes.
DR Reactome; R-MMU-75955; RNA Polymerase II Transcription Elongation.
DR BioGRID-ORCS; 20922; 22 hits in 76 CRISPR screens.
DR ChiTaRS; Supt4a; mouse.
DR PRO; PR:P63271; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; P63271; protein.
DR Bgee; ENSMUSG00000020485; Expressed in granulocyte and 77 other tissues.
DR ExpressionAtlas; P63271; baseline and differential.
DR Genevisible; P63271; MM.
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:0034244; P:negative regulation of transcription elongation from RNA polymerase II promoter; IMP: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 Acetylation; Activator; Metal-binding; Nucleus; Reference proteome;
KW Repressor; Transcription; Transcription regulation; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P63272"
FT CHAIN 2..117
FT /note="Transcription elongation factor SPT4-A"
FT /id="PRO_0000210327"
FT ZN_FING 16..36
FT /note="C4-type"
FT /evidence="ECO:0000255"
FT REGION 2..40
FT /note="Interaction with SUPT5H"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P63272"
FT CONFLICT 11
FT /note="R -> L (in Ref. 3; BAE39944)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 117 AA; 13193 MW; 09EDF007501D0F03 CRC64;
MALETVPKDL RHLRACLLCS LVKTIDQFEY DGCDNCDAYL QMKGNREMVY DCTSSSFDGI
IAMMSPEDSW VSKWQRVSNF KPGVYAVSVT GRLPQGIVRE LKSRGVAYKS RDTAIKT
