SPT5H_CAEEL
ID SPT5H_CAEEL Reviewed; 1208 AA.
AC Q21338; Q22440;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 3.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Transcription elongation factor SPT5;
DE AltName: Full=DRB sensitivity-inducing factor large subunit;
DE Short=DSIF large subunit;
GN Name=spt-5; ORFNames=K08E4.1;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP FUNCTION.
RX PubMed=12183367; DOI=10.1101/gad.999002;
RA Shim E.Y., Walker A.K., Shi Y., Blackwell T.K.;
RT "CDK-9/cyclin T (P-TEFb) is required in two postinitiation pathways for
RT transcription in the C. elegans embryo.";
RL Genes Dev. 16:2135-2146(2002).
CC -!- FUNCTION: May function as a component of the DRB sensitivity-inducing
CC factor complex (DSIF complex), which regulates transcription elongation
CC by RNA polymerase II. DSIF may enhance transcriptional pausing at sites
CC proximal to the promoter, which may in turn facilitate the assembly of
CC an elongation competent RNA polymerase II complex.
CC {ECO:0000269|PubMed:12183367}.
CC -!- SUBUNIT: Interacts with spt-4 to form DSIF. DSIF interacts with RNA
CC polymerase II and with the positive transcription elongation factor b
CC complex (P-TEFb complex), which is composed of cdk-9 and cyclin-T (cit-
CC 1.1 or cit-1.2) (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- PTM: Phosphorylated. Phosphorylation by P-TEFb alleviates
CC transcriptional pausing (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SPT5 family. {ECO:0000305}.
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DR EMBL; Z68316; CAA92685.1; -; Genomic_DNA.
DR EMBL; Z68752; CAA92685.1; JOINED; Genomic_DNA.
DR PIR; T23467; T23467.
DR RefSeq; NP_502283.1; NM_069882.5.
DR AlphaFoldDB; Q21338; -.
DR SMR; Q21338; -.
DR BioGRID; 43237; 9.
DR STRING; 6239.K08E4.1; -.
DR iPTMnet; Q21338; -.
DR EPD; Q21338; -.
DR PaxDb; Q21338; -.
DR PeptideAtlas; Q21338; -.
DR PRIDE; Q21338; -.
DR EnsemblMetazoa; K08E4.1.1; K08E4.1.1; WBGene00005015.
DR GeneID; 178143; -.
DR KEGG; cel:CELE_K08E4.1; -.
DR UCSC; K08E4.1; c. elegans.
DR CTD; 178143; -.
DR WormBase; K08E4.1; CE06145; WBGene00005015; spt-5.
DR eggNOG; KOG1999; Eukaryota.
DR GeneTree; ENSGT00440000037640; -.
DR HOGENOM; CLU_003537_0_0_1; -.
DR InParanoid; Q21338; -.
DR OMA; FLAWDVE; -.
DR OrthoDB; 828863at2759; -.
DR PhylomeDB; Q21338; -.
DR Reactome; R-CEL-112382; Formation of RNA Pol II elongation complex.
DR Reactome; R-CEL-113418; Formation of the Early Elongation Complex.
DR Reactome; R-CEL-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-CEL-6796648; TP53 Regulates Transcription of DNA Repair Genes.
DR Reactome; R-CEL-72086; mRNA Capping.
DR Reactome; R-CEL-75955; RNA Polymerase II Transcription Elongation.
DR Reactome; R-CEL-77075; RNA Pol II CTD phosphorylation and interaction with CE.
DR PRO; PR:Q21338; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00005015; Expressed in embryo and 4 other tissues.
DR GO; GO:0032044; C:DSIF complex; ISS:UniProtKB.
DR GO; GO:0000791; C:euchromatin; IDA:WormBase.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0032784; P:regulation of DNA-templated transcription, elongation; IEA:InterPro.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; IBA:GO_Central.
DR CDD; cd06081; KOW_Spt5_1; 1.
DR CDD; cd06082; KOW_Spt5_2; 1.
DR CDD; cd06083; KOW_Spt5_3; 1.
DR CDD; cd06084; KOW_Spt5_4; 1.
DR CDD; cd06085; KOW_Spt5_5; 1.
DR CDD; cd06086; KOW_Spt5_6; 1.
DR CDD; cd09888; NGN_Euk; 1.
DR Gene3D; 2.30.30.30; -; 3.
DR Gene3D; 3.30.70.940; -; 1.
DR InterPro; IPR005824; KOW.
DR InterPro; IPR041973; KOW_Spt5_1.
DR InterPro; IPR041975; KOW_Spt5_2.
DR InterPro; IPR041976; KOW_Spt5_3.
DR InterPro; IPR041977; KOW_Spt5_4.
DR InterPro; IPR041978; KOW_Spt5_5.
DR InterPro; IPR041980; KOW_Spt5_6.
DR InterPro; IPR005100; NGN-domain.
DR InterPro; IPR006645; NGN_dom.
DR InterPro; IPR036735; NGN_dom_sf.
DR InterPro; IPR039385; NGN_Euk.
DR InterPro; IPR014722; Rib_L2_dom2.
DR InterPro; IPR039659; SPT5.
DR InterPro; IPR024945; Spt5_C_dom.
DR InterPro; IPR022581; Spt5_N.
DR InterPro; IPR017071; TF_Spt5_eukaryote.
DR InterPro; IPR008991; Translation_prot_SH3-like_sf.
DR PANTHER; PTHR11125; PTHR11125; 1.
DR Pfam; PF00467; KOW; 1.
DR Pfam; PF03439; Spt5-NGN; 1.
DR Pfam; PF11942; Spt5_N; 1.
DR PIRSF; PIRSF036945; Spt5; 1.
DR SMART; SM01104; CTD; 2.
DR SMART; SM00739; KOW; 5.
DR SMART; SM00738; NGN; 1.
DR SUPFAM; SSF50104; SSF50104; 1.
PE 3: Inferred from homology;
KW Activator; Nucleus; Phosphoprotein; Reference proteome; Repeat; Repressor;
KW Transcription; Transcription regulation.
FT CHAIN 1..1208
FT /note="Transcription elongation factor SPT5"
FT /id="PRO_0000208474"
FT DOMAIN 420..447
FT /note="KOW 1"
FT DOMAIN 473..506
FT /note="KOW 2"
FT DOMAIN 595..629
FT /note="KOW 3"
FT DOMAIN 730..763
FT /note="KOW 4"
FT REGION 1..116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 151..176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 182..274
FT /note="Interaction with SPT4"
FT /evidence="ECO:0000250"
FT REGION 317..421
FT /note="Interaction with RNA polymerase II"
FT /evidence="ECO:0000250"
FT REGION 658..726
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 792..812
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 836..1004
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..45
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..60
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 86..109
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 151..171
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 658..706
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 865..881
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 900..914
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 922..951
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 815
FT /note="Phosphothreonine; by CDK9"
FT /evidence="ECO:0000250"
FT MOD_RES 822
FT /note="Phosphothreonine; by CDK9"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1208 AA; 133357 MW; 30BA1B988A305660 CRC64;
MSSDESDAAS NKEEDTTLSD DDGSDVEIKN SKKDRKRKLA SESEKSGSDD DDDDDDDEDE
NVTSKKSKKQ KRKNKAPSGR DFLAWDVEVD DEDEDDDNDY DDEDDPSMNA MNEREEAERA
MKEMELSQRN RDRYKFQNMT EDEVQKYFEN KYKGDKNDSQ YDDEDSAMDD ISKNSHLPST
KDPNLWIVKC RMGEEKLVAM HLMRKCLAVE HTNEPFQIKS VVVKEGLKGM IYIEAFKQSH
VMSAIEGFSA LNQFTITMVP IKDMVDVLRV VKDIPQLKLG SYVRLKRTMY KDDLAVVDLV
DIAQNRVNLK LIPRVDYQKR RGAMRTDADK NYKLKRRPMP KLFDQDTIKE VGGEIVTDGD
FLVFEGNHFR RGFLYKYFPI NAIQADGVKP TLGELEKFQE SSDDLKRELE TASLKDTENP
FVPGDIVEVK AGELVNLRGK VMTVDGTKVV MMPDQEDLKE AITLNAHELR KYFKEGDHAK
VISGRYEGHT GLIVRVKDST AIVLSDLGME ELKVRVRDLQ LCADVTTGVD SLGQFQYHDL
VQLDHTGNVG VIVRLEKEHL EVLNMHGVVN RIKPQAIIAK KDVRFAKVLD SQNNSIEAKD
LVKVIGGPNA KERETDEDPV GEVLYAFRGT VFVYSRKVTK NGGVLVCKPK QLILQGAKKT
TSTPMVSRMA SPNPMASPRH SSGGMTPRSP QDGMSSRGSS GGQTPRQGGG GGRGGHFGTA
NQQKVRRDLT LIGKNVRIIK GPMKGHFGIV RDATEDTVRV ELHTQCRTIS VDRARVMVVG
DTGITAGSGG GSSFYSSSKT PMRDSGKTPM YGSKTPMYGA QTPMYGSMTP AYDGGRTPAY
GEGGRTPAYG SKTPAYGDLD EHSSSRTPAY GNDSSRTPAY GSADGARTPA YGSTEGGRTP
AYGSMDNSRT PAYDDSGRTP GYESMPSRTP NYDSSSKTPA YPESEHSART PAYNNDYDIP
LSPAYEPDAP EAYDNAPART PAFVSRTPGY DTYENSSPTY EPDAATKVEE DIGDTSSPTY
DSPPHSYVVP TPGAMLNPAT PGAYHVDTPG FAAPMTPGSG GAYDQYVAPS PFAGYDSNNY
NNADGAIEQI PDHFLAQGVW IVQNLCVQIK DHEGRFNGRE AIIKDVTDGK VDVYMPDHKC
NLEVDFDQLT PMKPQPGDDA RVIFGQDAGH SGQLVSMDGF EAVIRSQEDM SDMRVINIGL
CCKMHSET
