SPT6H_DANRE
ID SPT6H_DANRE Reviewed; 1726 AA.
AC Q8UVK2; Q4V961; Q6P4U2;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Transcription elongation factor SPT6;
DE AltName: Full=Protein pandora;
GN Name=supt6h; Synonyms=pan, spt6;
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], 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo, and Larva;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION.
RX PubMed=17570355; DOI=10.1016/j.ydbio.2007.04.039;
RA Kok F.O., Oster E., Mentzer L., Hsieh J.C., Henry C.A., Sirotkin H.I.;
RT "The role of the SPT6 chromatin remodeling factor in zebrafish
RT embryogenesis.";
RL Dev. Biol. 307:214-226(2007).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90; THR-1522 AND SER-1525,
RP AND IDENTIFICATION BY 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).
RN [5]
RP FUNCTION.
RX PubMed=23503590; DOI=10.1038/emboj.2013.54;
RA Wang A.H., Zare H., Mousavi K., Wang C., Moravec C.E., Sirotkin H.I.,
RA Ge K., Gutierrez-Cruz G., Sartorelli V.;
RT "The histone chaperone Spt6 coordinates histone H3K27 demethylation and
RT myogenesis.";
RL EMBO J. 32:1075-1086(2013).
CC -!- FUNCTION: Transcription elongation factor which binds histone H3 and
CC enhances transcription elongation by RNA polymerase II (RNAPII).
CC Promotes the activation of the myogenic gene program by entailing
CC erasure of the repressive H3K27me3 epigenetic mark through
CC stabilization of the chromatin interaction of the H3K27 demethylase
CC KDM6A. Plays an important role during early patterning and
CC somitogenesis of the embryo. {ECO:0000269|PubMed:11923199,
CC ECO:0000269|PubMed:17570355, ECO:0000269|PubMed:23503590}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout the blastoderm early in
CC development. Highly expressed in the developing brain at 24 hours post-
CC fertilization (hpf), and at lower levels in the rest of the embryo.
CC {ECO:0000269|PubMed:11923199}.
CC -!- SIMILARITY: Belongs to the SPT6 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH97046.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
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DR EMBL; AF421378; AAL73392.1; -; mRNA.
DR EMBL; BC063248; AAH63248.1; -; mRNA.
DR EMBL; BC097046; AAH97046.1; ALT_SEQ; mRNA.
DR RefSeq; NP_660094.1; NM_145118.1.
DR AlphaFoldDB; Q8UVK2; -.
DR SMR; Q8UVK2; -.
DR STRING; 7955.ENSDARP00000013353; -.
DR iPTMnet; Q8UVK2; -.
DR PaxDb; Q8UVK2; -.
DR PRIDE; Q8UVK2; -.
DR Ensembl; ENSDART00000028007; ENSDARP00000013353; ENSDARG00000006524.
DR GeneID; 337866; -.
DR KEGG; dre:337866; -.
DR CTD; 6830; -.
DR ZFIN; ZDB-GENE-030131-7949; supt6h.
DR eggNOG; KOG1856; Eukaryota.
DR GeneTree; ENSGT00510000047446; -.
DR HOGENOM; CLU_001680_4_0_1; -.
DR InParanoid; Q8UVK2; -.
DR OMA; LCNGFKT; -.
DR OrthoDB; 56990at2759; -.
DR PhylomeDB; Q8UVK2; -.
DR TreeFam; TF105956; -.
DR Reactome; R-DRE-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-DRE-75955; RNA Polymerase II Transcription Elongation.
DR PRO; PR:Q8UVK2; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 21.
DR Bgee; ENSDARG00000006524; Expressed in gastrula and 28 other tissues.
DR GO; GO:0008023; C:transcription elongation factor complex; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0042393; F:histone binding; ISS:UniProtKB.
DR GO; GO:0031491; F:nucleosome binding; IBA:GO_Central.
DR GO; GO:0035050; P:embryonic heart tube development; IMP:ZFIN.
DR GO; GO:0007507; P:heart development; IMP:ZFIN.
DR GO; GO:0042789; P:mRNA transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0061086; P:negative regulation of histone H3-K27 methylation; IMP:UniProtKB.
DR GO; GO:0034728; P:nucleosome organization; IBA:GO_Central.
DR GO; GO:0071599; P:otic vesicle development; IMP:ZFIN.
DR GO; GO:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; ISS:UniProtKB.
DR GO; GO:0001756; P:somitogenesis; IMP:ZFIN.
DR GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; IBA:GO_Central.
DR CDD; cd09928; SH2_Cterm_SPT6_like; 1.
DR CDD; cd09918; SH2_Nterm_SPT6_like; 1.
DR Gene3D; 1.10.10.2740; -; 1.
DR Gene3D; 1.10.10.650; -; 1.
DR Gene3D; 1.10.3500.10; -; 1.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.30.420.140; -; 1.
DR Gene3D; 3.30.505.10; -; 2.
DR InterPro; IPR041692; HHH_9.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR010994; RuvA_2-like.
DR InterPro; IPR003029; S1_domain.
DR InterPro; IPR000980; SH2.
DR InterPro; IPR036860; SH2_dom_sf.
DR InterPro; IPR028083; Spt6_acidic_N_dom.
DR InterPro; IPR042066; Spt6_death-like.
DR InterPro; IPR032706; Spt6_HHH.
DR InterPro; IPR028088; Spt6_HTH_DNA-bd_dom.
DR InterPro; IPR035420; Spt6_SH2.
DR InterPro; IPR035018; Spt6_SH2_C.
DR InterPro; IPR035019; Spt6_SH2_N.
DR InterPro; IPR028231; Spt6_YqgF.
DR InterPro; IPR023323; Tex-like_dom_sf.
DR InterPro; IPR023319; Tex-like_HTH_dom_sf.
DR InterPro; IPR017072; TF_Spt6.
DR InterPro; IPR006641; YqgF/RNaseH-like_dom.
DR InterPro; IPR037027; YqgF/RNaseH-like_dom_sf.
DR PANTHER; PTHR10145; PTHR10145; 1.
DR Pfam; PF14635; HHH_7; 1.
DR Pfam; PF17674; HHH_9; 1.
DR Pfam; PF14641; HTH_44; 1.
DR Pfam; PF00575; S1; 1.
DR Pfam; PF14633; SH2_2; 1.
DR Pfam; PF14632; SPT6_acidic; 1.
DR Pfam; PF14639; YqgF; 1.
DR PIRSF; PIRSF036947; Spt6; 1.
DR SMART; SM00252; SH2; 1.
DR SMART; SM00732; YqgFc; 1.
DR SUPFAM; SSF47781; SSF47781; 2.
DR SUPFAM; SSF50249; SSF50249; 1.
DR SUPFAM; SSF53098; SSF53098; 1.
DR SUPFAM; SSF55550; SSF55550; 1.
DR PROSITE; PS50126; S1; 1.
DR PROSITE; PS50001; SH2; 1.
PE 1: Evidence at protein level;
KW Chaperone; Coiled coil; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..1726
FT /note="Transcription elongation factor SPT6"
FT /id="PRO_0000072167"
FT DOMAIN 1204..1273
FT /note="S1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT DOMAIN 1316..1426
FT /note="SH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT REGION 1..196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 219..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 482..512
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1611..1726
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 806..865
FT /evidence="ECO:0000255"
FT COMPBIAS 1..16
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..31
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 55..71
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..95
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 128..154
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 163..183
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 224..238
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 487..502
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1611..1667
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1678..1694
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 90
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18307296"
FT MOD_RES 1522
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18307296"
FT MOD_RES 1525
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18307296"
FT CONFLICT 8
FT /note="E -> G (in Ref. 2; AAH97046)"
FT /evidence="ECO:0000305"
FT CONFLICT 207
FT /note="E -> G (in Ref. 2; AAH97046)"
FT /evidence="ECO:0000305"
FT CONFLICT 242
FT /note="D -> G (in Ref. 2; AAH97046)"
FT /evidence="ECO:0000305"
FT CONFLICT 262
FT /note="E -> D (in Ref. 2; AAH63248)"
FT /evidence="ECO:0000305"
FT CONFLICT 1250
FT /note="P -> L (in Ref. 2; AAH63248)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1726 AA; 198167 MW; 7A503A7AE7D2DF07 CRC64;
MSDFIESEAE ESEEEFEEKD LKPKKTQRFM EEDEEEEEEN TEDQDEHGNL RGLIDDDDVE
EEEEEERGEP PAGEDSDSGE EVRHRRRKRS FDDYLDDDDL DLIEENLGVK VKRRKKKYSR
VKTMDDEGDD DDEKDLIADE IFTGDGDGEG EVEDGEAVDT LHPRDDEEEE DDEESDIDDF
IVDDDGQPIT KKKGKKFSGY TDAALQEAQE IFGGDFDFAE FDTEAYDHAE EEEEDQDDES
WDRPKKQTKR RVSRRSIFEI YEPSELESSH MTDQDNEIRS TDMPERFQLR AIPVKPAEDD
ELEEEAEWIY RNAFSTPTIS MQESTDYLDR GTTTNFSRKG PSTIAKIKEA LNFMRNQHFE
VPFIAFYRKE YVEPELNIND LWKVWQWDEK WTQLKTRKQN LTRLFQRMQS YQFEQISADP
DKPLADSTRP LDTADMERLK DVQSIDELGD VYNHFLLYYG RDIPKMQNAA KGGKKKLKKI
KEVSEEDGEE AEVEEEEEEE EQKGPDLKQA SRRDMYSICQ SAGLDGLAKK FGLTPEQFGE
NLRDSYQRHE TEQFPAEPLE LAKDYVCSQF NTPEAVLEGA RYMVAMQIAR EPLVRHVLRQ
TFQERAKINI KPTKKGKKDV DEAHFAYSFK YLKNKPVKEL SGDQFLKMCL AEEEGLLAID
ICIDLVGVKG YGDQTYFDEI KQFYYRDEFS HQVQEWNKQR TLAIERSLQQ FLYPQMAKEL
KNKLIAEAKD NIVKSCCKKL YNWLKVAPYR PDQQVEEDDD LMDESQGKGI RVLGVAFASG
RDTPVFCSLI NGEGEVVDFL RLPYFLKRRN AWREDEREKK QQDVENLKKF LLSKKPHVVA
VSGENRDAHM VMEDIKRTIS ELEQNSSLPV VGVELVDNEL AVLYMNSKKS EADFRDYPPL
LRQAVSVARK IQDPLVEFAQ VCSTDDDILC LKLHPLQEHV VKEELLSALY CEFINRVNEV
GVDVNRAIAH PYTQSLVQYI CGLGPRKGSH LLKILKQNNT RLENRTQLVT MCHMGPKVFI
NCAGFIKIDT ASLGDSTDSY IEVLDGSRVH PETYEWARKM AVDALEYDES AEDANPAGAL
EEILENPERL KDLDLDAFAE ELERQGYGNK GITLYDIRAE LSCRYKDLRA PYRPPNTEEV
FNMLTKETPE TFYIGKLITC VVTNIAHRRP QGESYDQAIR NDETGLWQCP FCQQDNFPEL
SEVWNHFDSG SCPGQAIGVR TRLDNAVMGF IPTKFLSDKV VKHPEERVKP GMTVHCRIMK
IDIEKFNVDL TCRTSDLSDK NNEWKLPKDT YYDFDAETDD VKQEEEQKKK QQRTTYIKRV
IAHPSFHNIN FKQAEKMMES MDQGDVVIRP SSKGENHLTV TWKVADGIYQ HVDVREEGKE
NAFSLGHTLW INTEEFEDLD EITARYVQPM AAFARDLLGH KYFHECNGGD RKKMEELLVR
TKKEKPTFIP YYISACRDLP GKFLLGYQPR GKPRIEYVTI TPDGFRYRSQ IFPTVNGLFR
WFKDHYQDPV PGVTPASSRT RTPASVNATP ANINIADLTR AVNSLPRNMT SQMFNAIAAV
TGQGQNPNTT PAQWASSQYG YSGGSSAGGG GGSSSAYHVF ATPQQPMATP LMTPSYSYTT
PGQQQAMTTP QYPSSTPQSS HGHHQHSSST PSSSSSRVRT PQPKASSHTA VDWGKMAEQW
LQEKEAERRK QKTPRMTPRP SPSPMIESTP MSIAGDATPL LDEMDR
