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Protein

Transcription elongation factor SPT5

Gene

Supt5h

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Component of the DRB sensitivity-inducing factor complex (DSIF complex), which regulates mRNA processing and transcription elongation by RNA polymerase II. DSIF positively regulates mRNA capping by stimulating the mRNA guanylyltransferase activity of RNGTT/CAP1A. DSIF also acts cooperatively with the negative elongation factor complex (NELF complex) to enhance transcriptional pausing at sites proximal to the promoter. Transcriptional pausing may facilitate the assembly of an elongation competent RNA polymerase II complex. DSIF and NELF promote pausing by inhibition of the transcription elongation factor TFIIS/S-II. TFIIS/S-II binds to RNA polymerase II at transcription pause sites and stimulates the weak intrinsic nuclease activity of the enzyme. Cleavage of blocked transcripts by RNA polymerase II promotes the resumption of transcription from the new 3' terminus and may allow repeated attempts at transcription through natural pause sites (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Activator, Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Enzyme and pathway databases

ReactomeiR-MMU-112382. Formation of RNA Pol II elongation complex.
R-MMU-112387. Elongation arrest and recovery.
R-MMU-113418. Formation of the Early Elongation Complex.
R-MMU-674695. RNA Polymerase II Pre-transcription Events.
R-MMU-6796648. TP53 Regulates Transcription of DNA Repair Genes.
R-MMU-72086. mRNA Capping.
R-MMU-75955. RNA Polymerase II Transcription Elongation.
R-MMU-77075. RNA Pol II CTD phosphorylation and interaction with CE.

Names & Taxonomyi

Protein namesi
Recommended name:
Transcription elongation factor SPT5
Alternative name(s):
DRB sensitivity-inducing factor large subunit
Short name:
DSIF large subunit
Gene namesi
Name:Supt5h
Synonyms:Supt5
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:1202400. Supt5.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002084691 – 1082Transcription elongation factor SPT5Add BLAST1082

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei32PhosphoserineCombined sources1
Modified residuei36PhosphoserineCombined sources1
Cross-linki141Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei661PhosphothreonineCombined sources1
Modified residuei664PhosphoserineCombined sources1
Modified residuei684PhosphoserineBy similarity1
Modified residuei690Asymmetric dimethylarginine; alternateBy similarity1
Modified residuei690Omega-N-methylarginine; alternateCombined sources1
Modified residuei690Omega-N-methylated arginine; alternateBy similarity1
Modified residuei692Asymmetric dimethylarginine; alternateBy similarity1
Modified residuei692Omega-N-methylarginine; alternateBy similarity1
Modified residuei692Omega-N-methylated arginine; alternateBy similarity1
Modified residuei692Symmetric dimethylarginine; alternateBy similarity1
Modified residuei712N6-acetyllysineCombined sources1
Modified residuei769Phosphothreonine; by CDK9By similarity1
Modified residuei778Phosphothreonine; by CDK9By similarity1
Modified residuei783PhosphoserineBy similarity1
Modified residuei785PhosphothreonineBy similarity1
Modified residuei798PhosphoserineBy similarity1
Modified residuei800PhosphothreonineBy similarity1
Modified residuei1028PhosphothreonineBy similarity1

Post-translational modificationi

Methylated by PRMT1/HRMT1L2 and PRMT5/SKB1. Methylation negatively regulates interaction with P-TEFb and RNA polymerase II (By similarity).By similarity
Phosphorylated by CDK7 and CDK9. Phosphorylation by P-TEFb alleviates transcriptional pausing. Phosphorylation may also stimulate interaction with PIN1. Bulk phosphorylation occurs predominantly in mitosis (By similarity).By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiO55201.
MaxQBiO55201.
PaxDbiO55201.
PeptideAtlasiO55201.
PRIDEiO55201.

PTM databases

iPTMnetiO55201.
PhosphoSitePlusiO55201.

Expressioni

Gene expression databases

BgeeiENSMUSG00000003435.
CleanExiMM_SUPT5H.
ExpressionAtlasiO55201. baseline and differential.
GenevisibleiO55201. MM.

Interactioni

Subunit structurei

Interacts with SUPT4H1 to form DSIF. DSIF interacts with the positive transcription elongation factor b complex (P-TEFb complex), which is composed of CDK9 and cyclin-T (CCNT1 or CCNT2). DSIF interacts with RNA polymerase II, and this interaction is reduced by phosphorylation of the C-terminal domain (CTD) of POLR2A by P-TEFb. DSIF also interacts with the NELF complex, which is composed of WHSC2/NELFA, COBRA1/NELFB, TH1L/NELFD and RDBP/NELFE, and this interaction occurs following prior binding of DSIF to RNA polymerase II. Also interacts with PRMT1/HRMT1L2, HTATSF1/TATSF1, RNGTT/CAP1A, PRMT5/SKB1, SUPT6H, and can interact with PIN1. Component of a complex which is at least composed of HTATSF1/Tat-SF1, the P-TEFb complex components CDK9 and CCNT1, RNA polymerase II, SUPT5H, and NCL/nucleolin (By similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

BioGridi203575. 14 interactors.
IntActiO55201. 1 interactor.
MINTiMINT-4105191.
STRINGi10090.ENSMUSP00000003527.

Structurei

3D structure databases

ProteinModelPortaliO55201.
SMRiO55201.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini271 – 304KOW 1Add BLAST34
Domaini418 – 449KOW 2Add BLAST32
Domaini470 – 501KOW 3Add BLAST32
Domaini592 – 625KOW 4Add BLAST34
Domaini698 – 731KOW 5Add BLAST34
Repeati748 – 753CTR1-1; approximate6
Repeati754 – 759CTR1-26
Repeati760 – 765CTR1-36
Repeati766 – 772CTR1-47
Repeati775 – 781CTR1-57
Repeati782 – 788CTR1-67
Repeati790 – 796CTR1-77
Repeati797 – 803CTR1-87
Repeati805 – 811CTR1-97
Repeati838 – 845CTR2-18
Repeati848 – 856CTR2-2; approximate9
Repeati857 – 863CTR2-3; approximate7
Repeati875 – 879CTR2-4; half-length5
Repeati890 – 896CTR2-5; approximate7
Repeati898 – 905CTR2-68
Repeati910 – 915CTR2-7; approximate6
Repeati918 – 924CTR2-87
Repeati926 – 933CTR2-98
Repeati937 – 944CTR2-108

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni174 – 268Interaction with SUPT4H1 and SUPT4H2By similarityAdd BLAST95
Regioni311 – 418Interaction with RNA polymerase IIBy similarityAdd BLAST108
Regioni748 – 8119 X 7 AA approximate tandem repeats of G-S-[QR]-T-P-X-[YQ], motif CTR1Add BLAST64
Regioni838 – 94410 X 8 AA approximate tandem repeats of P-[TS]-P-S-P-[QA]-[SG]-Y, motif CTR2Add BLAST107

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi11 – 104Glu-richAdd BLAST94

Sequence similaritiesi

Belongs to the SPT5 family.Curated
Contains 5 KOW domains.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG1999. Eukaryota.
COG0250. LUCA.
COG5164. LUCA.
GeneTreeiENSGT00440000037640.
HOVERGENiHBG079775.
InParanoidiO55201.
KOiK15172.
OMAiSAHSFSM.
OrthoDBiEOG091G0114.
PhylomeDBiO55201.
TreeFamiTF105730.

Family and domain databases

Gene3Di2.30.30.30. 1 hit.
InterProiIPR005824. KOW.
IPR006645. NGN_dom.
IPR014722. Rib_L2_dom2.
IPR024945. Spt5_C_dom.
IPR022581. Spt5_N.
IPR017071. TF_Spt5.
IPR005100. TF_Spt5_NGN-domain.
IPR008991. Translation_prot_SH3-like.
[Graphical view]
PfamiPF00467. KOW. 2 hits.
PF03439. Spt5-NGN. 1 hit.
PF11942. Spt5_N. 1 hit.
[Graphical view]
PIRSFiPIRSF036945. Spt5. 1 hit.
SMARTiSM01104. CTD. 1 hit.
SM00739. KOW. 6 hits.
SM00738. NGN. 1 hit.
[Graphical view]
SUPFAMiSSF50104. SSF50104. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: O55201-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MSDSEDSNFS EEEDSERSSE AEEAEVEEDQ RSAAGSEKEE EPEEEEEEEE
60 70 80 90 100
EYDEEEEEED DDRPPKKPRH GGFILDEADV DDEYEDEDQW EDGAEDILEK
110 120 130 140 150
EEIEASNIDN VVLDEDRSGA RRLQNLWRDQ REEELGEYYM KKYAKSSVGE
160 170 180 190 200
TVYGGSDELS DDITQQQLLP GVKDPNLWTV KCKIGEERAT AISLMRKFIA
210 220 230 240 250
YQFTDTPLQI KSVVAPEHVK GYIYVEAYKQ THVKQAIEGV GNLRLGYWNQ
260 270 280 290 300
QMVPIKEMTD VLKVVKEVAN LKPKSWVRLK RGIYKDDIAQ VDYVEPSQNT
310 320 330 340 350
ISLKMIPRID YDRIKARMSL KDWFAKRKKF KRPPQRLFDA EKIRSLGGDV
360 370 380 390 400
ASDGDFLIFE GNRYSRKGFL FKSFAMSAVI TEGVKPTLSE LEKFEDQPEG
410 420 430 440 450
IDLEVVTEST GKEREHNFQP GDNVEVCEGE LINLQGKVLS VDGNKITIMP
460 470 480 490 500
KHEDLKDMLE FPAQELRKYF KMGDHVKVIA GRFEGDTGLI VRVEENFVIL
510 520 530 540 550
FSDLTMHELK VLPRDLQLCS ETASGVDVGG QHEWGELVQL DPRTVGVIVR
560 570 580 590 600
LERETFQVLN MHGKVVTVRH QAVTQKKDNR FAVALDSDQN NIHVKDIVKV
610 620 630 640 650
IDGPHSGREG EIRHLYRSFA FLHCKKLVEN GGMFVCKARH LVLAGGSKPR
660 670 680 690 700
DVTNLTVGGF TPMSPRISSP MHPSAEGQHG GFGSPGGMSR GRGRRDNELI
710 720 730 740 750
GQTVRISQGP YKGYIGVVKD ATESTARVEL HSTCQTISVD RQRLTTVDSQ
760 770 780 790 800
RPGGMTSTYG RTPMYGSQTP MYGSGSRTPM YGSQTPLQDG SRTPHYGSQT
810 820 830 840 850
PLHDGSRTPA QSGAWDPNNP NTPSRAEEEY EYAFDDEPTP SPQAYGGTPN
860 870 880 890 900
PQTPGYPDPS SPQVNPQYNP QTPGTPAMYN TDQFSPYAAP SPQGSYQPSP
910 920 930 940 950
SPQSYHQVAP SPAGYQNTHS PASYHPTPSP MAYQASPSPS PVGYSPMTPG
960 970 980 990 1000
APSPGGYNPH TPGSGIEQNS SDWVTTDIQV KVRDTYLDTQ IVGQTGVIRS
1010 1020 1030 1040 1050
VTGGMCSVYL KDSEKVVSIS SEHLEPITPT KNNKVKVILG EDREATGVLL
1060 1070 1080
SIDGEDGIIR MDLEDQQIKI LNLRFLGKLL EA
Length:1,082
Mass (Da):120,664
Last modified:June 1, 1998 - v1
Checksum:i109D0D8D2D71DDE7
GO
Isoform 2 (identifier: O55201-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-194: Missing.

Note: No experimental confirmation available.
Show »
Length:888
Mass (Da):98,310
Checksum:i30E132908E6A5F03
GO

Sequence cautioni

The sequence AAH57449 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti30Q → R in BAE26244 (PubMed:16141072).Curated1
Sequence conflicti51E → EE in BAE26244 (PubMed:16141072).Curated1
Sequence conflicti111V → L in BAE27278 (PubMed:16141072).Curated1
Sequence conflicti229K → E in BAE27184 (PubMed:16141072).Curated1
Sequence conflicti265V → E in BAE26864 (PubMed:16141072).Curated1
Sequence conflicti416H → N in AAH58598 (PubMed:15489334).Curated1
Sequence conflicti775G → D in BAE26864 (PubMed:16141072).Curated1
Sequence conflicti1063L → I in BAE26864 (PubMed:16141072).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0162831 – 194Missing in isoform 2. 1 PublicationAdd BLAST194

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U88539 mRNA. Translation: AAC40052.1.
AK145117 mRNA. Translation: BAE26244.1.
AK146055 mRNA. Translation: BAE26864.1.
AK146453 mRNA. Translation: BAE27184.1.
AK146583 mRNA. Translation: BAE27278.1.
AK146650 mRNA. Translation: BAE27330.1.
BC007132 mRNA. Translation: AAH07132.1.
BC057449 mRNA. Translation: AAH57449.1. Different initiation.
BC058598 mRNA. Translation: AAH58598.1.
BC059849 mRNA. Translation: AAH59849.1.
CCDSiCCDS39857.1. [O55201-1]
PIRiT42204.
RefSeqiNP_038704.1. NM_013676.1. [O55201-1]
UniGeneiMm.285906.

Genome annotation databases

EnsembliENSMUST00000003527; ENSMUSP00000003527; ENSMUSG00000003435. [O55201-1]
ENSMUST00000209141; ENSMUSP00000147164; ENSMUSG00000003435. [O55201-1]
GeneIDi20924.
KEGGimmu:20924.
UCSCiuc009fyh.1. mouse. [O55201-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U88539 mRNA. Translation: AAC40052.1.
AK145117 mRNA. Translation: BAE26244.1.
AK146055 mRNA. Translation: BAE26864.1.
AK146453 mRNA. Translation: BAE27184.1.
AK146583 mRNA. Translation: BAE27278.1.
AK146650 mRNA. Translation: BAE27330.1.
BC007132 mRNA. Translation: AAH07132.1.
BC057449 mRNA. Translation: AAH57449.1. Different initiation.
BC058598 mRNA. Translation: AAH58598.1.
BC059849 mRNA. Translation: AAH59849.1.
CCDSiCCDS39857.1. [O55201-1]
PIRiT42204.
RefSeqiNP_038704.1. NM_013676.1. [O55201-1]
UniGeneiMm.285906.

3D structure databases

ProteinModelPortaliO55201.
SMRiO55201.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi203575. 14 interactors.
IntActiO55201. 1 interactor.
MINTiMINT-4105191.
STRINGi10090.ENSMUSP00000003527.

PTM databases

iPTMnetiO55201.
PhosphoSitePlusiO55201.

Proteomic databases

EPDiO55201.
MaxQBiO55201.
PaxDbiO55201.
PeptideAtlasiO55201.
PRIDEiO55201.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000003527; ENSMUSP00000003527; ENSMUSG00000003435. [O55201-1]
ENSMUST00000209141; ENSMUSP00000147164; ENSMUSG00000003435. [O55201-1]
GeneIDi20924.
KEGGimmu:20924.
UCSCiuc009fyh.1. mouse. [O55201-1]

Organism-specific databases

CTDi20924.
MGIiMGI:1202400. Supt5.

Phylogenomic databases

eggNOGiKOG1999. Eukaryota.
COG0250. LUCA.
COG5164. LUCA.
GeneTreeiENSGT00440000037640.
HOVERGENiHBG079775.
InParanoidiO55201.
KOiK15172.
OMAiSAHSFSM.
OrthoDBiEOG091G0114.
PhylomeDBiO55201.
TreeFamiTF105730.

Enzyme and pathway databases

ReactomeiR-MMU-112382. Formation of RNA Pol II elongation complex.
R-MMU-112387. Elongation arrest and recovery.
R-MMU-113418. Formation of the Early Elongation Complex.
R-MMU-674695. RNA Polymerase II Pre-transcription Events.
R-MMU-6796648. TP53 Regulates Transcription of DNA Repair Genes.
R-MMU-72086. mRNA Capping.
R-MMU-75955. RNA Polymerase II Transcription Elongation.
R-MMU-77075. RNA Pol II CTD phosphorylation and interaction with CE.

Miscellaneous databases

PROiO55201.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000003435.
CleanExiMM_SUPT5H.
ExpressionAtlasiO55201. baseline and differential.
GenevisibleiO55201. MM.

Family and domain databases

Gene3Di2.30.30.30. 1 hit.
InterProiIPR005824. KOW.
IPR006645. NGN_dom.
IPR014722. Rib_L2_dom2.
IPR024945. Spt5_C_dom.
IPR022581. Spt5_N.
IPR017071. TF_Spt5.
IPR005100. TF_Spt5_NGN-domain.
IPR008991. Translation_prot_SH3-like.
[Graphical view]
PfamiPF00467. KOW. 2 hits.
PF03439. Spt5-NGN. 1 hit.
PF11942. Spt5_N. 1 hit.
[Graphical view]
PIRSFiPIRSF036945. Spt5. 1 hit.
SMARTiSM01104. CTD. 1 hit.
SM00739. KOW. 6 hits.
SM00738. NGN. 1 hit.
[Graphical view]
SUPFAMiSSF50104. SSF50104. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiSPT5H_MOUSE
AccessioniPrimary (citable) accession number: O55201
Secondary accession number(s): Q3UJ77
, Q3UJH1, Q3UKD7, Q3UM54, Q6PB73, Q6PDP0, Q6PFR4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 22, 2005
Last sequence update: June 1, 1998
Last modified: November 30, 2016
This is version 138 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.