SPT5H_PONAB
ID SPT5H_PONAB Reviewed; 1083 AA.
AC Q5R405;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 104.
DE RecName: Full=Transcription elongation factor SPT5;
DE AltName: Full=DRB sensitivity-inducing factor large subunit;
DE Short=DSIF large subunit;
GN Name=SUPT5H;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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 SUPT4H1 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 NELFA,
CC NELFB, NELFD and NELFE, and this interaction occurs following prior
CC binding of DSIF to RNA polymerase II. Also interacts with
CC PRMT1/HRMT1L2, HTATSF1/TATSF1, RNGTT/CAP1A, PRMT5/SKB1, SUPT6H, and can
CC interact with PIN1. Component of a complex which is at least composed
CC of HTATSF1/Tat-SF1, the P-TEFb complex components CDK9 and CCNT1, RNA
CC polymerase II, SUPT5H, and NCL/nucleolin (By similarity). Interacts
CC with MCM3AP (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:O00267}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- PTM: Methylated by PRMT1/HRMT1L2 and PRMT5/SKB1. Methylation negatively
CC regulates interaction with P-TEFb and RNA polymerase II (By
CC similarity). {ECO:0000250}.
CC -!- PTM: Phosphorylated by CDK7 and CDK9. Phosphorylation by P-TEFb
CC alleviates transcriptional pausing. Phosphorylation may also stimulate
CC interaction with PIN1. Bulk phosphorylation occurs predominantly in
CC mitosis (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SPT5 family. {ECO:0000305}.
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DR EMBL; CR861455; CAH93511.1; -; mRNA.
DR RefSeq; NP_001127053.1; NM_001133581.1.
DR AlphaFoldDB; Q5R405; -.
DR SMR; Q5R405; -.
DR STRING; 9601.ENSPPYP00000011160; -.
DR PRIDE; Q5R405; -.
DR GeneID; 100174081; -.
DR KEGG; pon:100174081; -.
DR CTD; 6829; -.
DR eggNOG; KOG1999; Eukaryota.
DR InParanoid; Q5R405; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0032044; C:DSIF complex; ISS:UniProtKB.
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; IEA:InterPro.
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 2: Evidence at transcript level;
KW Acetylation; Activator; Isopeptide bond; Methylation; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..1083
FT /note="Transcription elongation factor SPT5"
FT /id="PRO_0000208470"
FT DOMAIN 269..302
FT /note="KOW 1"
FT DOMAIN 416..447
FT /note="KOW 2"
FT DOMAIN 468..499
FT /note="KOW 3"
FT DOMAIN 590..623
FT /note="KOW 4"
FT DOMAIN 700..733
FT /note="KOW 5"
FT REPEAT 750..755
FT /note="CTR1-1; approximate"
FT REPEAT 756..761
FT /note="CTR1-2"
FT REPEAT 762..767
FT /note="CTR1-3"
FT REPEAT 768..774
FT /note="CTR1-4"
FT REPEAT 777..783
FT /note="CTR1-5"
FT REPEAT 784..790
FT /note="CTR1-6"
FT REPEAT 792..798
FT /note="CTR1-7"
FT REPEAT 799..805
FT /note="CTR1-8"
FT REPEAT 807..813
FT /note="CTR1-9"
FT REPEAT 840..847
FT /note="CTR2-1"
FT REPEAT 850..858
FT /note="CTR2-2; approximate"
FT REPEAT 859..865
FT /note="CTR2-3; approximate"
FT REPEAT 877..881
FT /note="CTR2-4; half-length"
FT REPEAT 892..898
FT /note="CTR2-5; approximate"
FT REPEAT 900..907
FT /note="CTR2-6"
FT REPEAT 912..917
FT /note="CTR2-7; approximate"
FT REPEAT 920..926
FT /note="CTR2-8"
FT REPEAT 928..935
FT /note="CTR2-9"
FT REPEAT 939..946
FT /note="CTR2-10"
FT REGION 1..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 172..266
FT /note="Interaction with SUPT4H1"
FT /evidence="ECO:0000250"
FT REGION 309..416
FT /note="Interaction with RNA polymerase II"
FT /evidence="ECO:0000250"
FT REGION 666..696
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 743..974
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 750..813
FT /note="9 X 7 AA approximate tandem repeats of G-S-[QR]-T-P-
FT X-[YQ], motif CTR1"
FT REGION 840..946
FT /note="10 X 8 AA approximate tandem repeats of P-[TS]-P-S-
FT P-[QA]-[SG]-Y, motif CTR2"
FT COMPBIAS 1..23
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..38
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..63
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..79
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 743..827
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 846..868
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 869..943
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 944..958
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 32
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O55201"
FT MOD_RES 36
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O55201"
FT MOD_RES 662
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00267"
FT MOD_RES 677
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:O00267"
FT MOD_RES 677
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:O00267"
FT MOD_RES 682
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00267"
FT MOD_RES 692
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:O00267"
FT MOD_RES 692
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:O00267"
FT MOD_RES 694
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:O00267"
FT MOD_RES 694
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:O00267"
FT MOD_RES 694
FT /note="Symmetric dimethylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:O00267"
FT MOD_RES 714
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O55201"
FT MOD_RES 771
FT /note="Phosphothreonine; by CDK9"
FT /evidence="ECO:0000250|UniProtKB:O00267"
FT MOD_RES 780
FT /note="Phosphothreonine; by CDK9"
FT /evidence="ECO:0000250|UniProtKB:O00267"
FT MOD_RES 785
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00267"
FT MOD_RES 787
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O00267"
FT MOD_RES 800
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00267"
FT MOD_RES 802
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O00267"
FT MOD_RES 1030
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O00267"
FT CROSSLNK 139
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O00267"
FT CROSSLNK 1033
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O00267"
SQ SEQUENCE 1083 AA; 120549 MW; 441C4A36114DDC69 CRC64;
MSDSEDSNFS EEEDSERSSD GEEAEVEEER RSAAGSEKEE EPEEEEEEEE EEEYDEEEEE
EDDDRPPKKP RHGGFILDEA DVDDEYEDED QWEDGAEDIL EKAPNIDNVV LDEDRSGARR
LQNLWRDQRE EELGEYYMKK YAKSSVGETV YGGSDELSDD ITQQQLLPGV KDPNLWTVKC
KIGEERATAI SLMRKFIAYQ FTDTPLQIKS VVAPEHVKGY IYVEAYKQTH VKQAIEGVGN
LRLGYWNQQM VPIKEMTDVL KVVKEVANLK PKSWVRLKRG IYKDDIAQVD YVEPSQNTIS
LKMIPRIDYD RIKARMSLKD WFAKRKKFKR PPQRLFDAEK IRSLGGDVAS DGDFLIFEGN
RYSRKGFLFK SFAMSAVITE GVKPTLSELE KFEDQPEGID LEVVTESTGR EREHNFQPGD
NVEVCEGELI NLQGKILSVD GNKITIMPKH EDLKDMLEFP AQELRKYFKM GDHVKVIAGR
FEGDTGLIVR VEENFVILFS DLTMHELKVL PRDLQLCSET ASGVDVGGQH EWGELVQLDP
QTVGVIVRLE RETFQVLNMY GKVVTVRHQA VTRKKDNRFA VALDSEQNNI HVKDIVKVID
GPHSGREGEI RHLFRSFAFL HCKKLVENGG MFVCKTRHLV LAGGSKPRDV TNFTVGGFAP
MSPRISSPMH PSAGGQRGGF GSPGGGSGGM SRGRGRRDNE LIGQTVRISQ GPYKGYIGVV
KDATESTARV ELHSTCQTIS VDRQRLTTVG SRRPGGMTST YGRTPMYGSQ TPMYGSGSRT
PMYGSQTPLQ DGSRTPHYGS QTPLHDGSRT PAQSGAWDPN NPNTPSRAEE EYEYAFDDEP
TPSPQAYGGT PNPQTPGYPD PSSPQVNPQY NPQTPGTPAM YNTDQFSPYA APSPQGSYQP
SPSPQSYHQV APSPAGYQNT HSPASYHPTP SPMAYQASPS PSPVGYSPMT PGAPSPGGYN
PHTPGSGIEQ NSSDWVTTDI QVKVRDTYLD TQVVGQTGVI RSVTGGMCSV YLKDSEKVVS
ISSEHLEPIT PTKNNKVKVI LGEDREATGV LLSIDGEDGI VRMDPDEQLK ILNLRFLGKL
LEA
