SPT5H_DANRE
ID SPT5H_DANRE Reviewed; 1084 AA.
AC Q9DDT5; Q6PFJ3;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Transcription elongation factor SPT5;
DE AltName: Full=DRB sensitivity-inducing factor large subunit;
DE Short=DSIF large subunit;
DE AltName: Full=Protein foggy;
GN Name=supt5h; Synonyms=fog, spt5;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION,
RP DEVELOPMENTAL STAGE, AND MUTAGENESIS OF VAL-1012.
RX PubMed=11099044; DOI=10.1038/35042590;
RA Guo S., Yamaguchi Y., Schilbach S., Wada T., Lee J., Goddard A., French D.,
RA Handa H., Rosenthal A.;
RT "A regulator of transcriptional elongation controls vertebrate neuronal
RT development.";
RL Nature 408:366-369(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=11923199; DOI=10.1242/dev.129.7.1623;
RA Keegan B.R., Feldman J.L., Lee D.H., Koos D.S., Ho R.K., Stainier D.Y.R.,
RA Yelon D.;
RT "The elongation factors Pandora/Spt6 and Foggy/Spt5 promote transcription
RT in the zebrafish embryo.";
RL Development 129:1623-1632(2002).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-665, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18307296; DOI=10.1021/pr700667w;
RA Lemeer S., Pinkse M.W.H., Mohammed S., van Breukelen B., den Hertog J.,
RA Slijper M., Heck A.J.R.;
RT "Online automated in vivo zebrafish phosphoproteomics: from large-scale
RT analysis down to a single embryo.";
RL J. Proteome Res. 7:1555-1564(2008).
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. Probably enhances transcriptional pausing at
CC sites proximal to the promoter, which may facilitate the assembly of an
CC elongation competent RNA polymerase II complex. Also acts to stimulate
CC transcriptional elongation at low nucleotide concentrations. Regulation
CC of transcriptional elongation by this protein is required for the
CC expression of genes which control neuronal development.
CC {ECO:0000269|PubMed:11099044, ECO:0000269|PubMed:11923199}.
CC -!- SUBUNIT: Interacts with SUPT4H1 to form the DSIF complex. DSIF
CC interacts with RNA polymerase II and with the positive transcription
CC elongation factor b complex (P-TEFb complex), which is composed of CDK9
CC and cyclin-T (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11099044}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9DDT5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9DDT5-2; Sequence=VSP_016284;
CC -!- DEVELOPMENTAL STAGE: Maternally expressed throughout the early
CC blastoderm. Expressed in the neural plate of the tailbud stage embryo,
CC at 10 hours post-fertilization (hpf). Highly expressed in the
CC developing brain at 28 hpf, and at lower levels in the rest of the
CC embryo. {ECO:0000269|PubMed:11099044, ECO:0000269|PubMed:11923199}.
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; AF288409; AAG37030.1; -; mRNA.
DR EMBL; BC057529; AAH57529.1; -; mRNA.
DR AlphaFoldDB; Q9DDT5; -.
DR SMR; Q9DDT5; -.
DR STRING; 7955.ENSDARP00000062675; -.
DR iPTMnet; Q9DDT5; -.
DR PaxDb; Q9DDT5; -.
DR ZFIN; ZDB-GENE-001207-1; supt5h.
DR eggNOG; KOG1999; Eukaryota.
DR InParanoid; Q9DDT5; -.
DR PhylomeDB; Q9DDT5; -.
DR Reactome; R-DRE-113418; Formation of the Early Elongation Complex.
DR Reactome; R-DRE-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-DRE-6796648; TP53 Regulates Transcription of DNA Repair Genes.
DR Reactome; R-DRE-6807505; RNA polymerase II transcribes snRNA genes.
DR Reactome; R-DRE-72086; mRNA Capping.
DR Reactome; R-DRE-75955; RNA Polymerase II Transcription Elongation.
DR Reactome; R-DRE-77075; RNA Pol II CTD phosphorylation and interaction with CE.
DR PRO; PR:Q9DDT5; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0032044; C:DSIF complex; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:ZFIN.
DR GO; GO:0003677; F:DNA binding; IDA:ZFIN.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0021954; P:central nervous system neuron development; IMP:ZFIN.
DR GO; GO:0030097; P:hemopoiesis; IMP:ZFIN.
DR GO; GO:0040037; P:negative regulation of fibroblast growth factor receptor signaling pathway; IMP:ZFIN.
DR GO; GO:0034244; P:negative regulation of transcription elongation from RNA polymerase II promoter; IMP:ZFIN.
DR GO; GO:0001764; P:neuron migration; IMP:ZFIN.
DR GO; GO:1901534; P:positive regulation of hematopoietic progenitor cell differentiation; IMP:ZFIN.
DR GO; GO:1902038; P:positive regulation of hematopoietic stem cell differentiation; IMP:ZFIN.
DR GO; GO:0060335; P:positive regulation of interferon-gamma-mediated signaling pathway; IMP:ZFIN.
DR GO; GO:0046427; P:positive regulation of receptor signaling pathway via JAK-STAT; IMP:ZFIN.
DR GO; GO:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; IMP:ZFIN.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP:ZFIN.
DR GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; IMP:ZFIN.
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; 1.
DR SMART; SM00739; KOW; 6.
DR SMART; SM00738; NGN; 1.
DR SUPFAM; SSF50104; SSF50104; 1.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation.
FT CHAIN 1..1084
FT /note="Transcription elongation factor SPT5"
FT /id="PRO_0000208472"
FT DOMAIN 272..305
FT /note="KOW 1"
FT DOMAIN 419..450
FT /note="KOW 2"
FT DOMAIN 471..502
FT /note="KOW 3"
FT DOMAIN 593..626
FT /note="KOW 4"
FT DOMAIN 702..735
FT /note="KOW 5"
FT REPEAT 758..763
FT /note="CTR1-1; approximate"
FT REPEAT 764..769
FT /note="CTR1-2; approximate"
FT REPEAT 770..776
FT /note="CTR1-3"
FT REPEAT 779..785
FT /note="CTR1-4"
FT REPEAT 786..792
FT /note="CTR1-5"
FT REPEAT 794..800
FT /note="CTR1-6"
FT REPEAT 801..807
FT /note="CTR1-7"
FT REPEAT 809..815
FT /note="CTR1-8"
FT REPEAT 842..849
FT /note="CTR2-1"
FT REPEAT 852..860
FT /note="CTR2-2; approximate"
FT REPEAT 861..867
FT /note="CTR2-3; approximate"
FT REPEAT 879..883
FT /note="CTR2-4; half-length"
FT REPEAT 894..900
FT /note="CTR2-5; approximate"
FT REPEAT 902..909
FT /note="CTR2-6"
FT REPEAT 914..919
FT /note="CTR2-7; approximate"
FT REPEAT 922..928
FT /note="CTR2-8"
FT REPEAT 930..937
FT /note="CTR2-9"
FT REPEAT 941..948
FT /note="CTR2-10"
FT REGION 1..91
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 175..269
FT /note="Interaction with SUPT4H1"
FT /evidence="ECO:0000250"
FT REGION 312..419
FT /note="Interaction with RNA polymerase II"
FT /evidence="ECO:0000250"
FT REGION 667..700
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 748..973
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 758..815
FT /note="8 X 7 AA approximate tandem repeats of G-S-[QR]-T-P-
FT X-[YQ], motif CTR1"
FT REGION 842..948
FT /note="10 X 8 AA approximate tandem repeats of P-[TS]-P-S-
FT P-[QA]-[SG]-Y, motif CTR2"
FT COMPBIAS 42..60
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 61..78
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 748..829
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 857..873
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 874..945
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 946..960
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 665
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18307296"
FT MOD_RES 773
FT /note="Phosphothreonine; by CDK9"
FT /evidence="ECO:0000250"
FT MOD_RES 782
FT /note="Phosphothreonine; by CDK9"
FT /evidence="ECO:0000250"
FT VAR_SEQ 603..830
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_016284"
FT MUTAGEN 1012
FT /note="V->D: In fog(m806); reduced development of dopamine
FT containing neurons in the hypothalamus. Specifically
FT abrogates inhibition of transcriptional elongation. No
FT effect on the stimulation of transcriptional elongation at
FT low nucleotide concentrations."
FT /evidence="ECO:0000269|PubMed:11099044"
SQ SEQUENCE 1084 AA; 120379 MW; 467C60789E1A57AB CRC64;
MSDSEDSDFS DNQSERSSEA EEVEENEEEE EQGSVAGSDK AEEEGEDLED EEEYDEEEEE
DDDRPRKKAR HGGFILDEAD VDDEYEDEDP WEDGAEDILE KEEAEVSNLD HVVLDEDHSG
SRRLQNLWRD SREEALGEYY MRKYAKSSGG EHFYGGSEDL SDDITQQQLL PGVKDPNLWT
VKCKIGEERA TAISLMRKFV AYQCTDTPLQ IKSVVAPEHV KGYIYVEAYK QTHVKAAIEG
VGNLRMGFWN QQMVPIKEMT DVLKVVKEVT NLKPKSWVRL KRGLYKDDIA QVDYVEPSQN
TISLKMIPRI DLDRIKARMS MKDWFAKRKK FKRPPQRLFD AEKIRSLGGE VSHDGDFMIF
EANRYSRKGF LFKSFAMSAV ITEGVKPTLS ELEKFEDQPE GIDLEVVTET TGKEREHNLQ
AGDNVEVCEG ELINLQGKIL SVDGNKITIM PKHEDLKDPL EFPAHELRKY FRMGDHVKVI
AGRYEGDTGL IVRVEENFVI LFSDLTMHEL KVLPRDLQLC SETASGVDAG GQHEWGELVQ
LDPQTVGVIV RLERETFQVL NMHGKVLTVR HQAVNRRKDN RFAVALDSEQ NNIHVKDIVK
VIDGPHSGRE GEIRHIFRGF AFLHCKKLVE NGGMFVCKAR HLVLAGGSKP RDVTNFTVGG
FAPMSPRISS PMHPGGGGQP QRGGGGGGGG GMGRGRGRRD NDLIGQTVRI SQGPYKGYIG
VVKDATESTA RVELHSTCQT ISVDRQRLTT VGGKERQGRS STHLRTPMYG SQTPIYGTGS
RTPMYGSQTP LHDGSRTPHY GSQTPLHDGS RTPGQSGAWD PNNPNTPSRP DDEYEFAYDD
EPSPSPQGYG GTPNPQTPGY PEVPSPQVNP QYNPQTPGTP AMYNTDQYSP YAAPSPQGSY
QPSPSPQSYH QVAPSPVGYQ NTHSPASYHP TPSPMAYQAS PSPSPVGYSP MTPGAPSPGG
YNPHTPGSNI DQASNDWVTT DIMVRVKDTF LDGGVINQTG IIRSVTGGMC SVFLQDTEKV
VSISSEHLEP VTPTKNNKVK VILGEDREAT GVLLSIDGED GIVRMELDEQ LKILNLRFLG
KLEV
