Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Transcription elongation factor SPT4

Gene

SUPT4H1

Organism
Homo sapiens (Human)
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. DSIF can also positively regulate transcriptional elongation and is required for the efficient activation of transcriptional elongation by the HIV-1 nuclear transcriptional activator, Tat. DSIF acts to suppress transcriptional pausing in transcripts derived from the HIV-1 LTR and blocks premature release of HIV-1 transcripts at terminator sequences.13 Publications

Regions

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

GO - Molecular functioni

  • protein heterodimerization activity Source: UniProtKB
  • transcription factor activity, sequence-specific DNA binding Source: ProtInc
  • zinc ion binding Source: InterPro

GO - Biological processi

  • chromatin remodeling Source: ProtInc
  • negative regulation of DNA-templated transcription, elongation Source: UniProtKB
  • negative regulation of transcription elongation from RNA polymerase II promoter Source: Ensembl
  • negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  • positive regulation of DNA-templated transcription, elongation Source: UniProtKB
  • positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  • positive regulation of viral transcription Source: Reactome
  • regulation of transcription, DNA-templated Source: ProtInc
  • regulation of transcription from RNA polymerase II promoter Source: ProtInc
  • transcription elongation from RNA polymerase II promoter Source: UniProtKB
  • transcription from RNA polymerase II promoter Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Activator, Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-HSA-112382. Formation of RNA Pol II elongation complex.
R-HSA-113418. Formation of the Early Elongation Complex.
R-HSA-167152. Formation of HIV elongation complex in the absence of HIV Tat.
R-HSA-167158. Formation of the HIV-1 Early Elongation Complex.
R-HSA-167200. Formation of HIV-1 elongation complex containing HIV-1 Tat.
R-HSA-167238. Pausing and recovery of Tat-mediated HIV elongation.
R-HSA-167242. Abortive elongation of HIV-1 transcript in the absence of Tat.
R-HSA-167243. Tat-mediated HIV elongation arrest and recovery.
R-HSA-167246. Tat-mediated elongation of the HIV-1 transcript.
R-HSA-167287. HIV elongation arrest and recovery.
R-HSA-167290. Pausing and recovery of HIV elongation.
R-HSA-674695. RNA Polymerase II Pre-transcription Events.
R-HSA-6796648. TP53 Regulates Transcription of DNA Repair Genes.
R-HSA-75955. RNA Polymerase II Transcription Elongation.

Names & Taxonomyi

Protein namesi
Recommended name:
Transcription elongation factor SPT4
Short name:
hSPT4
Alternative name(s):
DRB sensitivity-inducing factor 14 kDa subunit
Short name:
DSIF p14
DRB sensitivity-inducing factor small subunit
Short name:
DSIF small subunit
Gene namesi
Name:SUPT4H1
Synonyms:SPT4H, SUPT4H
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:11467. SUPT4H1.

Subcellular locationi

  • Nucleus 1 Publication

GO - Cellular componenti

  • DSIF complex Source: UniProtKB
  • nucleoplasm Source: Reactome
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA36253.

Polymorphism and mutation databases

DMDMi54039624.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 117116Transcription elongation factor SPT4PRO_0000210325Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineCombined sources

Keywords - PTMi

Acetylation

Proteomic databases

EPDiP63272.
MaxQBiP63272.
PaxDbiP63272.
PeptideAtlasiP63272.
PRIDEiP63272.

PTM databases

iPTMnetiP63272.
PhosphoSiteiP63272.

Expressioni

Tissue specificityi

Widely expressed.2 Publications

Gene expression databases

BgeeiP63272.
CleanExiHS_SUPT4H1.
ExpressionAtlasiP63272. baseline and differential.
GenevisibleiP63272. HS.

Organism-specific databases

HPAiHPA059748.

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 PIN1.7 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
SUPT5HO002675EBI-727250,EBI-710464

GO - Molecular functioni

  • protein heterodimerization activity Source: UniProtKB

Protein-protein interaction databases

BioGridi112695. 25 interactions.
DIPiDIP-40644N.
IntActiP63272. 7 interactions.
MINTiMINT-1382313.
STRINGi9606.ENSP00000225504.

Structurei

Secondary structure

1
117
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 53Combined sources
Beta strandi8 – 103Combined sources
Beta strandi13 – 164Combined sources
Turni17 – 193Combined sources
Beta strandi21 – 244Combined sources
Helixi25 – 317Combined sources
Turni34 – 363Combined sources
Helixi37 – 404Combined sources
Helixi46 – 527Combined sources
Beta strandi53 – 553Combined sources
Beta strandi57 – 648Combined sources
Helixi66 – 683Combined sources
Helixi70 – 745Combined sources
Beta strandi82 – 898Combined sources
Helixi95 – 1039Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3H7HX-ray1.55A2-117[»]
ProteinModelPortaliP63272.
SMRiP63272. Positions 2-117.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP63272.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 4039Interaction with SUPT5HAdd
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.
HOGENOMiHOG000172685.
HOVERGENiHBG055988.
InParanoidiP63272.
KOiK15171.
OMAiACMLCGI.
PhylomeDBiP63272.
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.

P63272-1 [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 conflicti95 – 11723QGIVR…TAIKT → HAKDSRSNVNKYEPRESSEG HDTCLASLFHSLRHSNSLFA L in BAC85230 (PubMed:14702039).CuratedAdd
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U38818 mRNA. Translation: AAB18674.1.
U38817 mRNA. Translation: AAB18675.1.
U43923 mRNA. Translation: AAB07814.1.
AK129758 mRNA. Translation: BAC85230.1.
AK311986 mRNA. Translation: BAG34925.1.
CR407663 mRNA. Translation: CAG28591.1.
CH471109 Genomic DNA. Translation: EAW94464.1.
CH471109 Genomic DNA. Translation: EAW94466.1.
BC002802 mRNA. Translation: AAH02802.1.
CCDSiCCDS11606.1.
RefSeqiNP_003159.1. NM_003168.2.
UniGeneiHs.439481.
Hs.718477.

Genome annotation databases

EnsembliENST00000225504; ENSP00000225504; ENSG00000213246.
ENST00000580947; ENSP00000462670; ENSG00000213246.
GeneIDi6827.
KEGGihsa:6827.
UCSCiuc002iwe.3. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U38818 mRNA. Translation: AAB18674.1.
U38817 mRNA. Translation: AAB18675.1.
U43923 mRNA. Translation: AAB07814.1.
AK129758 mRNA. Translation: BAC85230.1.
AK311986 mRNA. Translation: BAG34925.1.
CR407663 mRNA. Translation: CAG28591.1.
CH471109 Genomic DNA. Translation: EAW94464.1.
CH471109 Genomic DNA. Translation: EAW94466.1.
BC002802 mRNA. Translation: AAH02802.1.
CCDSiCCDS11606.1.
RefSeqiNP_003159.1. NM_003168.2.
UniGeneiHs.439481.
Hs.718477.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3H7HX-ray1.55A2-117[»]
ProteinModelPortaliP63272.
SMRiP63272. Positions 2-117.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112695. 25 interactions.
DIPiDIP-40644N.
IntActiP63272. 7 interactions.
MINTiMINT-1382313.
STRINGi9606.ENSP00000225504.

PTM databases

iPTMnetiP63272.
PhosphoSiteiP63272.

Polymorphism and mutation databases

DMDMi54039624.

Proteomic databases

EPDiP63272.
MaxQBiP63272.
PaxDbiP63272.
PeptideAtlasiP63272.
PRIDEiP63272.

Protocols and materials databases

DNASUi6827.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000225504; ENSP00000225504; ENSG00000213246.
ENST00000580947; ENSP00000462670; ENSG00000213246.
GeneIDi6827.
KEGGihsa:6827.
UCSCiuc002iwe.3. human.

Organism-specific databases

CTDi6827.
GeneCardsiSUPT4H1.
H-InvDBHIX0014028.
HGNCiHGNC:11467. SUPT4H1.
HPAiHPA059748.
MIMi603555. gene.
neXtProtiNX_P63272.
PharmGKBiPA36253.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3490. Eukaryota.
COG5204. LUCA.
GeneTreeiENSGT00390000018559.
HOGENOMiHOG000172685.
HOVERGENiHBG055988.
InParanoidiP63272.
KOiK15171.
OMAiACMLCGI.
PhylomeDBiP63272.
TreeFamiTF300105.

Enzyme and pathway databases

ReactomeiR-HSA-112382. Formation of RNA Pol II elongation complex.
R-HSA-113418. Formation of the Early Elongation Complex.
R-HSA-167152. Formation of HIV elongation complex in the absence of HIV Tat.
R-HSA-167158. Formation of the HIV-1 Early Elongation Complex.
R-HSA-167200. Formation of HIV-1 elongation complex containing HIV-1 Tat.
R-HSA-167238. Pausing and recovery of Tat-mediated HIV elongation.
R-HSA-167242. Abortive elongation of HIV-1 transcript in the absence of Tat.
R-HSA-167243. Tat-mediated HIV elongation arrest and recovery.
R-HSA-167246. Tat-mediated elongation of the HIV-1 transcript.
R-HSA-167287. HIV elongation arrest and recovery.
R-HSA-167290. Pausing and recovery of HIV elongation.
R-HSA-674695. RNA Polymerase II Pre-transcription Events.
R-HSA-6796648. TP53 Regulates Transcription of DNA Repair Genes.
R-HSA-75955. RNA Polymerase II Transcription Elongation.

Miscellaneous databases

EvolutionaryTraceiP63272.
GeneWikiiSUPT4H1.
GenomeRNAii6827.
PROiP63272.
SOURCEiSearch...

Gene expression databases

BgeeiP63272.
CleanExiHS_SUPT4H1.
ExpressionAtlasiP63272. baseline and differential.
GenevisibleiP63272. HS.

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.
  2. "Identification and analysis of a functional human homolog of the SPT4 gene of Saccharomyces cerevisiae."
    Hartzog G.A., Basrai M.A., Ricupero-Hovasse S.L., Hieter P., Winston F.
    Mol. Cell. Biol. 16:2848-2856(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Dermoid cancer and Testis.
  4. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  5. 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].
    Tissue: Placenta.
  7. "Evidence that P-TEFb alleviates the negative effect of DSIF on RNA polymerase II-dependent transcription in vitro."
    Wada T., Takagi T., Yamaguchi Y., Watanabe D., Handa H.
    EMBO J. 17:7395-7403(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. "DSIF, a novel transcription elongation factor that regulates RNA polymerase II processivity, is composed of human Spt4 and Spt5 homologs."
    Wada T., Takagi T., Yamaguchi Y., Ferdous A., Imai T., Hirose S., Sugimoto S., Yano K., Hartzog G.A., Winston F., Buratowski S., Handa H.
    Genes Dev. 12:343-356(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH SUPT5H.
  9. "NELF, a multisubunit complex containing RD, cooperates with DSIF to repress RNA polymerase II elongation."
    Yamaguchi Y., Takagi T., Wada T., Yano K., Furuya A., Sugimoto S., Hasegawa J., Handa H.
    Cell 97:41-51(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  10. "Structure and function of the human transcription elongation factor DSIF."
    Yamaguchi Y., Wada T., Watanabe D., Takagi T., Hasegawa J., Handa H.
    J. Biol. Chem. 274:8085-8092(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH SUPT5H.
  11. "Tat-SF1 protein associates with RAP30 and human SPT5 proteins."
    Kim J.B., Yamaguchi Y., Wada T., Handa H., Sharp P.A.
    Mol. Cell. Biol. 19:5960-5968(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  12. "FACT relieves DSIF/NELF-mediated inhibition of transcriptional elongation and reveals functional differences between P-TEFb and TFIIH."
    Wada T., Orphanides G., Hasegawa J., Kim D.-K., Shima D., Yamaguchi Y., Fukuda A., Hisatake K., Oh S., Reinberg D., Handa H.
    Mol. Cell 5:1067-1072(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  13. "Domains in the SPT5 protein that modulate its transcriptional regulatory properties."
    Ivanov D., Kwak Y.T., Guo J., Gaynor R.B.
    Mol. Cell. Biol. 20:2970-2983(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SUPT5H.
  14. "DSIF and NELF interact with RNA polymerase II elongation complex and HIV-1 Tat stimulates P-TEFb-mediated phosphorylation of RNA polymerase II and DSIF during transcription elongation."
    Ping Y.-H., Rana T.M.
    J. Biol. Chem. 276:12951-12958(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  15. "A highly purified RNA polymerase II elongation control system."
    Renner D.B., Yamaguchi Y., Wada T., Handa H., Price D.H.
    J. Biol. Chem. 276:42601-42609(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  16. "Structure-function analysis of human Spt4: evidence that hSpt4 and hSpt5 exert their roles in transcriptional elongation as parts of the DSIF complex."
    Kim D.-K., Inukai N., Yamada T., Furuya A., Sato H., Yamaguchi Y., Wada T., Handa H.
    Genes Cells 8:371-378(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH SUPT5H.
  17. "Methylation of SPT5 regulates its interaction with RNA polymerase II and transcriptional elongation properties."
    Kwak Y.T., Guo J., Prajapati S., Park K.-J., Surabhi R.M., Miller B., Gehrig P., Gaynor R.B.
    Mol. Cell 11:1055-1066(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH SUPT5H.
  18. "Locus-specific requirements for Spt5 in transcriptional activation and repression in Drosophila."
    Jennings B.H., Shah S., Yamaguchi Y., Seki M., Phillips R.G., Handa H., Ish-Horowicz D.
    Curr. Biol. 14:1680-1684(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  19. Cited for: INTERACTION WITH SUPT5H.
  20. "Functional interactions of RNA-capping enzyme with factors that positively and negatively regulate promoter escape by RNA polymerase II."
    Mandal S.S., Chu C., Wada T., Handa H., Shatkin A.J., Reinberg D.
    Proc. Natl. Acad. Sci. U.S.A. 101:7572-7577(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  21. "A negative elongation factor for human RNA polymerase II inhibits the anti-arrest transcript-cleavage factor TFIIS."
    Palangat M., Renner D.B., Price D.H., Landick R.
    Proc. Natl. Acad. Sci. U.S.A. 102:15036-15041(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  22. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  23. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  24. "Crystal structure of the human transcription elongation factor DSIF hSpt4 subunit in complex with the hSpt5 dimerization interface."
    Wenzel S., Martins B.M., Rosch P., Wohrl B.M.
    Biochem. J. 425:373-380(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 2-117 IN COMPLEX WITH SPT5H.

Entry informationi

Entry nameiSPT4H_HUMAN
AccessioniPrimary (citable) accession number: P63272
Secondary accession number(s): B2R4X8
, D3DTZ4, Q16550, Q62387, Q6ZP89
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: October 11, 2004
Last modified: June 8, 2016
This is version 118 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.