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Protein

Transcription elongation factor SPT4-A

Gene

Supt4h1a

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript 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

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri16 – 3621C4-typeSequence analysisAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Activator, Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-MMU-112382. Formation of RNA Pol II elongation complex.
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-75955. RNA Polymerase II Transcription Elongation.

Names & Taxonomyi

Protein namesi
Recommended name:
Transcription elongation factor SPT4-A
Alternative name(s):
DRB sensitivity-inducing factor small subunit 1
Short name:
DSIF small subunit 1
Transcription elongation factor SPT4 1
Gene namesi
Name:Supt4h1a
Synonyms:Spt4h, Supt4a, Supt4h
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:107416. Supt4a.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 117116Transcription elongation factor SPT4-APRO_0000210327Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

EPDiP63271.
MaxQBiP63271.
PaxDbiP63271.
PeptideAtlasiP63271.
PRIDEiP63271.

PTM databases

iPTMnetiP63271.
PhosphoSiteiP63271.

Expressioni

Tissue specificityi

Widely expressed.2 Publications

Gene expression databases

BgeeiP63271.
CleanExiMM_SUPT4H1.
ExpressionAtlasiP63271. baseline and differential.
GenevisibleiP63271. MM.

Interactioni

Subunit structurei

Interacts with SUPT5H 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. DSIF also interacts with HRMT1L2/PRMT1, HTATSF1/TATSF1, RNGTT/CAP1A, SKB1/PRMT5, SUPT6H, and can interact with PIN1 (By similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

BioGridi203573. 2 interactions.
STRINGi10090.ENSMUSP00000091487.

Structurei

3D structure databases

ProteinModelPortaliP63271.
SMRiP63271. Positions 2-117.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 4039Interaction with SUPT5HBy similarityAdd
BLAST

Sequence similaritiesi

Belongs to the SPT4 family.Curated

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri16 – 3621C4-typeSequence analysisAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG3490. Eukaryota.
COG5204. LUCA.
GeneTreeiENSGT00390000018559.
HOVERGENiHBG055988.
InParanoidiP63271.
KOiK15171.
OMAiACMLCGI.
OrthoDBiEOG7RFTK7.
PhylomeDBiP63271.
TreeFamiTF300105.

Family and domain databases

InterProiIPR029040. RPABC4/Spt4.
IPR009287. Spt4.
IPR016046. Spt4-like.
IPR022800. Spt4/RpoE2_Znf.
[Graphical view]
PANTHERiPTHR12882. PTHR12882. 1 hit.
PfamiPF06093. Spt4. 1 hit.
[Graphical view]
PIRSFiPIRSF025023. Spt4. 1 hit.
SMARTiSM01389. Spt4. 1 hit.
[Graphical view]
SUPFAMiSSF63393. SSF63393. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P63271-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALETVPKDL RHLRACLLCS LVKTIDQFEY DGCDNCDAYL QMKGNREMVY
60 70 80 90 100
DCTSSSFDGI IAMMSPEDSW VSKWQRVSNF KPGVYAVSVT GRLPQGIVRE
110
LKSRGVAYKS RDTAIKT
Length:117
Mass (Da):13,193
Last modified:October 11, 2004 - v1
Checksum:i09EDF007501D0F03
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti11 – 111R → L in BAE39944 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U43154 mRNA. Translation: AAB18730.1.
U96809 Genomic DNA. Translation: AAC71659.1.
AK167941 mRNA. Translation: BAE39944.1.
AL604022 Genomic DNA. Translation: CAI35953.1.
CU393486 Genomic DNA. Translation: CAQ52074.1.
CH466556 Genomic DNA. Translation: EDL15830.1.
BC024391 mRNA. Translation: AAH24391.1.
BC061174 mRNA. Translation: AAH61174.1.
BC087923 mRNA. Translation: AAH87923.1.
BC141092 mRNA. Translation: AAI41093.1.
CCDSiCCDS36270.1.
RefSeqiNP_033322.1. NM_009296.1.
UniGeneiMm.622.

Genome annotation databases

EnsembliENSMUST00000093955; ENSMUSP00000091487; ENSMUSG00000020485.
GeneIDi20922.
KEGGimmu:20922.
UCSCiuc007kuj.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U43154 mRNA. Translation: AAB18730.1.
U96809 Genomic DNA. Translation: AAC71659.1.
AK167941 mRNA. Translation: BAE39944.1.
AL604022 Genomic DNA. Translation: CAI35953.1.
CU393486 Genomic DNA. Translation: CAQ52074.1.
CH466556 Genomic DNA. Translation: EDL15830.1.
BC024391 mRNA. Translation: AAH24391.1.
BC061174 mRNA. Translation: AAH61174.1.
BC087923 mRNA. Translation: AAH87923.1.
BC141092 mRNA. Translation: AAI41093.1.
CCDSiCCDS36270.1.
RefSeqiNP_033322.1. NM_009296.1.
UniGeneiMm.622.

3D structure databases

ProteinModelPortaliP63271.
SMRiP63271. Positions 2-117.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi203573. 2 interactions.
STRINGi10090.ENSMUSP00000091487.

PTM databases

iPTMnetiP63271.
PhosphoSiteiP63271.

Proteomic databases

EPDiP63271.
MaxQBiP63271.
PaxDbiP63271.
PeptideAtlasiP63271.
PRIDEiP63271.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000093955; ENSMUSP00000091487; ENSMUSG00000020485.
GeneIDi20922.
KEGGimmu:20922.
UCSCiuc007kuj.1. mouse.

Organism-specific databases

CTDi20922.
MGIiMGI:107416. Supt4a.

Phylogenomic databases

eggNOGiKOG3490. Eukaryota.
COG5204. LUCA.
GeneTreeiENSGT00390000018559.
HOVERGENiHBG055988.
InParanoidiP63271.
KOiK15171.
OMAiACMLCGI.
OrthoDBiEOG7RFTK7.
PhylomeDBiP63271.
TreeFamiTF300105.

Enzyme and pathway databases

ReactomeiR-MMU-112382. Formation of RNA Pol II elongation complex.
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-75955. RNA Polymerase II Transcription Elongation.

Miscellaneous databases

PROiP63271.
SOURCEiSearch...

Gene expression databases

BgeeiP63271.
CleanExiMM_SUPT4H1.
ExpressionAtlasiP63271. baseline and differential.
GenevisibleiP63271. MM.

Family and domain databases

InterProiIPR029040. RPABC4/Spt4.
IPR009287. Spt4.
IPR016046. Spt4-like.
IPR022800. Spt4/RpoE2_Znf.
[Graphical view]
PANTHERiPTHR12882. PTHR12882. 1 hit.
PfamiPF06093. Spt4. 1 hit.
[Graphical view]
PIRSFiPIRSF025023. Spt4. 1 hit.
SMARTiSM01389. Spt4. 1 hit.
[Graphical view]
SUPFAMiSSF63393. SSF63393. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation and characterization of the human and mouse homologues (SUPT4H and Supt4h) of the yeast SPT4 gene."
    Chiang P.-W., Wang S.-Q., Smithivas P., Song W.-J., Crombez E., Akhtar A., Im R., Greenfield J., Ramamoorthy S., van Keuren M.L., Blackburn C.C., Tsai C.-H., Kurnit D.M.
    Genomics 34:368-375(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    Strain: Swiss Webster.
  2. "Comparison of murine Supt4h and a nearly identical expressed, processed gene: evidence of sequence conservation through gene conversion extending into the untranslated regions."
    Chiang P.-W., Zhang R., Stubbs L., Zhang L., Zhu L., Kurnit D.M.
    Nucleic Acids Res. 26:4960-4964(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY.
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: DBA/2J.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  5. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: FVB/N-3.
    Tissue: Brain, Liver and Mammary tumor.

Entry informationi

Entry nameiSPT4A_MOUSE
AccessioniPrimary (citable) accession number: P63271
Secondary accession number(s): B2KGH6
, Q16550, Q3TIA2, Q5NCP8, Q5NCP9, Q5NCQ0, Q62387
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: October 11, 2004
Last modified: July 6, 2016
This is version 99 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.