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O00267

- SPT5H_HUMAN

UniProt

O00267 - SPT5H_HUMAN

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Protein

Transcription elongation factor SPT5

Gene
SUPT5H, SPT5, SPT5H
Organism
Homo sapiens (Human)
Status
Reviewed - 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.19 Publications

GO - Molecular functioni

  1. chromatin binding Source: Ensembl
  2. enzyme binding Source: UniProtKB
  3. poly(A) RNA binding Source: UniProtKB
  4. protein binding Source: IntAct
  5. protein heterodimerization activity Source: UniProtKB

GO - Biological processi

  1. 7-methylguanosine mRNA capping Source: Reactome
  2. cell cycle Source: UniProtKB
  3. chromatin remodeling Source: UniProtKB
  4. DNA-templated transcription, elongation Source: UniProtKB
  5. gene expression Source: Reactome
  6. negative regulation of DNA-templated transcription, elongation Source: UniProtKB
  7. negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  8. positive regulation of DNA-templated transcription, elongation Source: UniProtKB
  9. positive regulation of macroautophagy Source: BHF-UCL
  10. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  11. positive regulation of viral transcription Source: Reactome
  12. response to organic substance Source: UniProtKB
  13. single stranded viral RNA replication via double stranded DNA intermediate Source: UniProtKB
  14. transcription elongation from RNA polymerase II promoter Source: UniProtKB
  15. transcription from RNA polymerase II promoter Source: Reactome
  16. viral process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Activator, Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Enzyme and pathway databases

BioCyciMetaCyc:G66-31601-MONOMER.
ReactomeiREACT_1470. mRNA Capping.
REACT_22107. RNA Polymerase II Pre-transcription Events.
REACT_22201. Formation of HIV elongation complex in the absence of HIV Tat.
REACT_6143. Pausing and recovery of Tat-mediated HIV elongation.
REACT_6162. Tat-mediated elongation of the HIV-1 transcript.
REACT_6237. RNA Pol II CTD phosphorylation and interaction with CE.
REACT_6244. Pausing and recovery of HIV elongation.
REACT_6259. HIV elongation arrest and recovery.
REACT_6261. Abortive elongation of HIV-1 transcript in the absence of Tat.
REACT_6319. Formation of the HIV-1 Early Elongation Complex.
REACT_6344. Tat-mediated HIV elongation arrest and recovery.
REACT_6346. Formation of HIV-1 elongation complex containing HIV-1 Tat.
REACT_833. RNA Polymerase II Transcription Elongation.
REACT_846. Formation of the Early Elongation Complex.
REACT_975. RNA Pol II CTD phosphorylation and interaction with CE.

Names & Taxonomyi

Protein namesi
Recommended name:
Transcription elongation factor SPT5
Short name:
hSPT5
Alternative name(s):
DRB sensitivity-inducing factor 160 kDa subunit
Short name:
DSIF p160
DRB sensitivity-inducing factor large subunit
Short name:
DSIF large subunit
Tat-cotransactivator 1 protein
Short name:
Tat-CT1 protein
Gene namesi
Name:SUPT5H
Synonyms:SPT5, SPT5H
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 19

Organism-specific databases

HGNCiHGNC:11469. SUPT5H.

Subcellular locationi

Nucleus 1 Publication

GO - Cellular componenti

  1. DSIF complex Source: UniProtKB
  2. nucleoplasm Source: Reactome
  3. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi681 – 6811R → A: Enhances interactions with CDK9 and RNA polymerase II and enhances transcriptional elongation; when associated with A-696 and A-698. 1 Publication
Mutagenesisi681 – 6811R → K: Increases promoter association and enhances transcriptional elongation; when associated with K-696 and K-698. 1 Publication
Mutagenesisi696 – 6961R → A: Enhances interactions with CDK9 and RNA polymerase II and enhances transcriptional elongation; when associated with A-681 and A-698. 1 Publication
Mutagenesisi696 – 6961R → K: Increases promoter association and enhances transcriptional elongation; when associated with K-681 and K-698. 1 Publication
Mutagenesisi698 – 6981R → A: Enhances transcriptional elongation. Enhances interactions with CDK9 and RNA polymerase II and enhances transcriptional elongation; when associated with A-681 and A-696. 1 Publication
Mutagenesisi698 – 6981R → K: Increases promoter association and enhances transcriptional elongation; when associated with K-681 and K-696. 1 Publication
Mutagenesisi1002 – 10021G → D: Defective in regulation of transcriptional elongation. 1 Publication

Organism-specific databases

PharmGKBiPA36255.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10871087Transcription elongation factor SPT5PRO_0000208468Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei666 – 6661Phosphoserine3 Publications
Modified residuei681 – 6811Asymmetric dimethylarginine; by PRMT1; alternate1 Publication
Modified residuei681 – 6811Omega-N-methylarginine; by PRMT1; alternate1 Publication
Modified residuei696 – 6961Asymmetric dimethylarginine; by PRMT1; alternate1 Publication
Modified residuei696 – 6961Omega-N-methylarginine; by PRMT1; alternate1 Publication
Modified residuei698 – 6981Asymmetric dimethylarginine; by PRMT1; alternate1 Publication
Modified residuei698 – 6981Omega-N-methylarginine; by PRMT1 and PRMT5; alternate1 Publication
Modified residuei698 – 6981Symmetric dimethylarginine; by PRMT5; alternate1 Publication
Modified residuei718 – 7181N6-acetyllysine By similarity
Modified residuei775 – 7751Phosphothreonine; by CDK91 Publication
Modified residuei784 – 7841Phosphothreonine; by CDK91 Publication
Modified residuei1034 – 10341Phosphothreonine2 Publications

Post-translational modificationi

Methylated by PRMT1/HRMT1L2 and PRMT5/SKB1. Methylation negatively regulates interaction with P-TEFb and RNA polymerase II.1 Publication
Phosphorylated by CDK7 and CDK9. Phosphorylation by P-TEFb alleviates transcriptional pausing and can stimulate transcriptional elongation from the HIV-1 LTR. P-TEFb dependent phosphorylation is stimulated by the HIV-1 Tat protein. Phosphorylation may also stimulate interaction with PIN1. Bulk phosphorylation occurs predominantly in mitosis.8 Publications

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein

Proteomic databases

MaxQBiO00267.
PaxDbiO00267.
PRIDEiO00267.

PTM databases

PhosphoSiteiO00267.

Expressioni

Tissue specificityi

Ubiquitously expressed.2 Publications

Gene expression databases

ArrayExpressiO00267.
BgeeiO00267.
CleanExiHS_SUPT5H.
GenevestigatoriO00267.

Organism-specific databases

HPAiCAB034370.
HPA029273.

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. DSIF 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.14 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
POLR2AP249282EBI-710464,EBI-295301
PPIAP629372EBI-710464,EBI-437708
SUPT4H1P632723EBI-710464,EBI-727250

Protein-protein interaction databases

BioGridi112697. 64 interactions.
DIPiDIP-29014N.
IntActiO00267. 28 interactions.
MINTiMINT-1193818.
STRINGi9606.ENSP00000367784.

Structurei

Secondary structure

1
1087
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi178 – 1836
Helixi189 – 20315
Beta strandi206 – 2083
Beta strandi214 – 2174
Beta strandi223 – 2319
Helixi232 – 2398
Helixi243 – 2486
Helixi257 – 2593
Helixi262 – 2643
Beta strandi424 – 4285
Turni432 – 4354
Beta strandi437 – 4404
Beta strandi447 – 4526
Beta strandi461 – 4644
Turni465 – 4673
Beta strandi468 – 4703
Beta strandi477 – 4837
Turni484 – 4874
Beta strandi489 – 4957
Beta strandi500 – 5078
Beta strandi509 – 5135
Beta strandi517 – 5215
Beta strandi708 – 7125
Turni716 – 7194
Beta strandi721 – 7277
Beta strandi732 – 7398
Beta strandi742 – 7454
Turni747 – 7493
Beta strandi750 – 7523

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2DO3NMR-A462-523[»]
2E6ZNMR-A420-471[»]
2E70NMR-A694-757[»]
3H7HX-ray1.55B176-273[»]
4L1UX-ray2.42G/H/I/J778-790[»]
ProteinModelPortaliO00267.
SMRiO00267. Positions 176-311, 413-523, 702-757.

Miscellaneous databases

EvolutionaryTraceiO00267.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini273 – 30634KOW 1Add
BLAST
Domaini420 – 45132KOW 2Add
BLAST
Domaini472 – 50332KOW 3Add
BLAST
Domaini594 – 62734KOW 4Add
BLAST
Domaini704 – 73734KOW 5Add
BLAST
Repeati754 – 7596CTR1-1; approximate
Repeati760 – 7656CTR1-2
Repeati766 – 7716CTR1-3
Repeati772 – 7787CTR1-4
Repeati781 – 7877CTR1-5
Repeati788 – 7947CTR1-6
Repeati796 – 8027CTR1-7
Repeati803 – 8097CTR1-8
Repeati811 – 8177CTR1-9
Repeati844 – 8518CTR2-1
Repeati854 – 8629CTR2-2; approximate
Repeati863 – 8697CTR2-3; approximate
Repeati881 – 8855CTR2-4; half-length
Repeati896 – 9027CTR2-5; approximate
Repeati904 – 9118CTR2-6
Repeati916 – 9216CTR2-7; approximate
Repeati924 – 9307CTR2-8
Repeati932 – 9398CTR2-9
Repeati943 – 9508CTR2-10

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni176 – 27095Interaction with SUPT4H1Add
BLAST
Regioni313 – 420108Interaction with RNA polymerase IIAdd
BLAST
Regioni754 – 817649 X 7 AA approximate tandem repeats of G-S-[QR]-T-P-X-[YQ], motif CTR1Add
BLAST
Regioni844 – 95010710 X 8 AA approximate tandem repeats of P-[TS]-P-S-P-[QA]-[SG]-Y, motif CTR2Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi11 – 10696Glu-richAdd
BLAST
Compositional biasi844 – 968125Pro-richAdd
BLAST

Sequence similaritiesi

Belongs to the SPT5 family.
Contains 5 KOW domains.

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG0250.
HOGENOMiHOG000038564.
HOVERGENiHBG079775.
InParanoidiO00267.
KOiK15172.
OMAiAFFDIEA.
OrthoDBiEOG7Z3F3Q.
PhylomeDBiO00267.
TreeFamiTF105730.

Family and domain databases

InterProiIPR005824. KOW.
IPR006645. NGN_dom.
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. Align

Isoform 1 (identifier: O00267-1) [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

MSDSEDSNFS EEEDSERSSD GEEAEVDEER RSAAGSEKEE EPEDEEEEEE     50
EEEYDEEEEE EDDDRPPKKP RHGGFILDEA DVDDEYEDED QWEDGAEDIL 100
EKEEIEASNI DNVVLDEDRS GARRLQNLWR DQREEELGEY YMKKYAKSSV 150
GETVYGGSDE LSDDITQQQL LPGVKDPNLW TVKCKIGEER ATAISLMRKF 200
IAYQFTDTPL QIKSVVAPEH VKGYIYVEAY KQTHVKQAIE GVGNLRLGYW 250
NQQMVPIKEM TDVLKVVKEV ANLKPKSWVR LKRGIYKDDI AQVDYVEPSQ 300
NTISLKMIPR IDYDRIKARM SLKDWFAKRK KFKRPPQRLF DAEKIRSLGG 350
DVASDGDFLI FEGNRYSRKG FLFKSFAMSA VITEGVKPTL SELEKFEDQP 400
EGIDLEVVTE STGKEREHNF QPGDNVEVCE GELINLQGKI LSVDGNKITI 450
MPKHEDLKDM LEFPAQELRK YFKMGDHVKV IAGRFEGDTG LIVRVEENFV 500
ILFSDLTMHE LKVLPRDLQL CSETASGVDV GGQHEWGELV QLDPQTVGVI 550
VRLERETFQV LNMYGKVVTV RHQAVTRKKD NRFAVALDSE QNNIHVKDIV 600
KVIDGPHSGR EGEIRHLFRS FAFLHCKKLV ENGGMFVCKT RHLVLAGGSK 650
PRDVTNFTVG GFAPMSPRIS SPMHPSAGGQ RGGFGSPGGG SGGMSRGRGR 700
RDNELIGQTV RISQGPYKGY IGVVKDATES TARVELHSTC QTISVDRQRL 750
TTVGSRRPGG MTSTYGRTPM YGSQTPMYGS GSRTPMYGSQ TPLQDGSRTP 800
HYGSQTPLHD GSRTPAQSGA WDPNNPNTPS RAEEEYEYAF DDEPTPSPQA 850
YGGTPNPQTP GYPDPSSPQV NPQYNPQTPG TPAMYNTDQF SPYAAPSPQG 900
SYQPSPSPQS YHQVAPSPAG YQNTHSPASY HPTPSPMAYQ ASPSPSPVGY 950
SPMTPGAPSP GGYNPHTPGS GIEQNSSDWV TTDIQVKVRD TYLDTQVVGQ 1000
TGVIRSVTGG MCSVYLKDSE KVVSISSEHL EPITPTKNNK VKVILGEDRE 1050
ATGVLLSIDG EDGIVRMDLD EQLKILNLRF LGKLLEA 1087
Length:1,087
Mass (Da):121,000
Last modified:July 1, 1997 - v1
Checksum:iEC3F402A670A5B7D
GO
Isoform 2 (identifier: O00267-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     103-106: Missing.

Show »
Length:1,083
Mass (Da):120,499
Checksum:i1B62A9E8011EB918
GO

Sequence cautioni

The sequence BAD92494.1 differs from that shown. Reason: Erroneous initiation.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei103 – 1064Missing in isoform 2. VSP_016282

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti181 – 1811T → I in AAC51102. 1 Publication
Sequence conflicti483 – 4831G → A in AAC51102. 1 Publication
Sequence conflicti820 – 8201A → G in AAC51102. 1 Publication
Sequence conflicti846 – 8461P → R in BAA24075. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U56402 mRNA. Translation: AAC51102.1.
Y12790 mRNA. Translation: CAA73326.1.
AB000516 mRNA. Translation: BAA24075.1.
AF040253 mRNA. Translation: AAD02179.1.
AB209257 mRNA. Translation: BAD92494.1. Different initiation.
BC024203 mRNA. Translation: AAH24203.1.
CCDSiCCDS12536.1. [O00267-1]
CCDS46072.1. [O00267-2]
RefSeqiNP_001104490.1. NM_001111020.2. [O00267-1]
NP_001124296.1. NM_001130824.1. [O00267-1]
NP_001124297.1. NM_001130825.1. [O00267-2]
NP_003160.2. NM_003169.3. [O00267-1]
XP_005259240.1. XM_005259183.1. [O00267-1]
XP_006723400.1. XM_006723337.1. [O00267-2]
UniGeneiHs.631604.

Genome annotation databases

EnsembliENST00000359191; ENSP00000352117; ENSG00000196235. [O00267-2]
ENST00000402194; ENSP00000384505; ENSG00000196235. [O00267-2]
ENST00000432763; ENSP00000404029; ENSG00000196235. [O00267-1]
ENST00000598725; ENSP00000469090; ENSG00000196235. [O00267-1]
ENST00000599117; ENSP00000470252; ENSG00000196235. [O00267-1]
GeneIDi6829.
KEGGihsa:6829.
UCSCiuc002oln.4. human. [O00267-1]
uc002olq.4. human. [O00267-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U56402 mRNA. Translation: AAC51102.1 .
Y12790 mRNA. Translation: CAA73326.1 .
AB000516 mRNA. Translation: BAA24075.1 .
AF040253 mRNA. Translation: AAD02179.1 .
AB209257 mRNA. Translation: BAD92494.1 . Different initiation.
BC024203 mRNA. Translation: AAH24203.1 .
CCDSi CCDS12536.1. [O00267-1 ]
CCDS46072.1. [O00267-2 ]
RefSeqi NP_001104490.1. NM_001111020.2. [O00267-1 ]
NP_001124296.1. NM_001130824.1. [O00267-1 ]
NP_001124297.1. NM_001130825.1. [O00267-2 ]
NP_003160.2. NM_003169.3. [O00267-1 ]
XP_005259240.1. XM_005259183.1. [O00267-1 ]
XP_006723400.1. XM_006723337.1. [O00267-2 ]
UniGenei Hs.631604.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2DO3 NMR - A 462-523 [» ]
2E6Z NMR - A 420-471 [» ]
2E70 NMR - A 694-757 [» ]
3H7H X-ray 1.55 B 176-273 [» ]
4L1U X-ray 2.42 G/H/I/J 778-790 [» ]
ProteinModelPortali O00267.
SMRi O00267. Positions 176-311, 413-523, 702-757.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 112697. 64 interactions.
DIPi DIP-29014N.
IntActi O00267. 28 interactions.
MINTi MINT-1193818.
STRINGi 9606.ENSP00000367784.

PTM databases

PhosphoSitei O00267.

Proteomic databases

MaxQBi O00267.
PaxDbi O00267.
PRIDEi O00267.

Protocols and materials databases

DNASUi 6829.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000359191 ; ENSP00000352117 ; ENSG00000196235 . [O00267-2 ]
ENST00000402194 ; ENSP00000384505 ; ENSG00000196235 . [O00267-2 ]
ENST00000432763 ; ENSP00000404029 ; ENSG00000196235 . [O00267-1 ]
ENST00000598725 ; ENSP00000469090 ; ENSG00000196235 . [O00267-1 ]
ENST00000599117 ; ENSP00000470252 ; ENSG00000196235 . [O00267-1 ]
GeneIDi 6829.
KEGGi hsa:6829.
UCSCi uc002oln.4. human. [O00267-1 ]
uc002olq.4. human. [O00267-2 ]

Organism-specific databases

CTDi 6829.
GeneCardsi GC19P039936.
HGNCi HGNC:11469. SUPT5H.
HPAi CAB034370.
HPA029273.
MIMi 602102. gene.
neXtProti NX_O00267.
PharmGKBi PA36255.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0250.
HOGENOMi HOG000038564.
HOVERGENi HBG079775.
InParanoidi O00267.
KOi K15172.
OMAi AFFDIEA.
OrthoDBi EOG7Z3F3Q.
PhylomeDBi O00267.
TreeFami TF105730.

Enzyme and pathway databases

BioCyci MetaCyc:G66-31601-MONOMER.
Reactomei REACT_1470. mRNA Capping.
REACT_22107. RNA Polymerase II Pre-transcription Events.
REACT_22201. Formation of HIV elongation complex in the absence of HIV Tat.
REACT_6143. Pausing and recovery of Tat-mediated HIV elongation.
REACT_6162. Tat-mediated elongation of the HIV-1 transcript.
REACT_6237. RNA Pol II CTD phosphorylation and interaction with CE.
REACT_6244. Pausing and recovery of HIV elongation.
REACT_6259. HIV elongation arrest and recovery.
REACT_6261. Abortive elongation of HIV-1 transcript in the absence of Tat.
REACT_6319. Formation of the HIV-1 Early Elongation Complex.
REACT_6344. Tat-mediated HIV elongation arrest and recovery.
REACT_6346. Formation of HIV-1 elongation complex containing HIV-1 Tat.
REACT_833. RNA Polymerase II Transcription Elongation.
REACT_846. Formation of the Early Elongation Complex.
REACT_975. RNA Pol II CTD phosphorylation and interaction with CE.

Miscellaneous databases

ChiTaRSi SUPT5H. human.
EvolutionaryTracei O00267.
GeneWikii SUPT5H.
GenomeRNAii 6829.
NextBioi 26663.
PROi O00267.
SOURCEi Search...

Gene expression databases

ArrayExpressi O00267.
Bgeei O00267.
CleanExi HS_SUPT5H.
Genevestigatori O00267.

Family and domain databases

InterProi IPR005824. KOW.
IPR006645. NGN_dom.
IPR024945. Spt5_C_dom.
IPR022581. Spt5_N.
IPR017071. TF_Spt5.
IPR005100. TF_Spt5_NGN-domain.
IPR008991. Translation_prot_SH3-like.
[Graphical view ]
Pfami PF00467. KOW. 2 hits.
PF03439. Spt5-NGN. 1 hit.
PF11942. Spt5_N. 1 hit.
[Graphical view ]
PIRSFi PIRSF036945. Spt5. 1 hit.
SMARTi SM01104. CTD. 1 hit.
SM00739. KOW. 6 hits.
SM00738. NGN. 1 hit.
[Graphical view ]
SUPFAMi SSF50104. SSF50104. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation, sequencing, and mapping of the human homologue of the yeast transcription factor, SPT5."
    Chiang P.-W., Fogel E., Jackson C.L., Lieuallen K., Lennon G., Qu X., Wang S.-Q., Kurnit D.M.
    Genomics 38:421-424(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
  2. "Human Supt5h protein, a putative modulator of chromatin structure, is reversibly phosphorylated in mitosis."
    Stachora A.A., Schaefer R.E., Pohlmeier M., Maier G., Ponstingl H.
    FEBS Lett. 409:74-78(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 116-152; 288-319; 461-471; 529-542; 580-587; 746-761; 795-809; 841-885; 888-922 AND 1068-1087, DOMAINS CTR1 AND CTR2, PHOSPHORYLATION.
  3. "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: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 277-282; 324-328; 459-470 AND 580-597, FUNCTION, INTERACTION WITH SUPT4H1 AND RNA POLYMERASE II.
  4. "Role of the human homolog of the yeast transcription factor SPT5 in HIV-1 Tat-activation."
    Wu-Baer F., Lane W.S., Gaynor R.B.
    J. Mol. Biol. 277:179-197(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 199-213; 247-258 AND 799-811, FUNCTION.
  5. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
    Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Brain.
  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] (ISOFORM 1).
    Tissue: Muscle.
  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, INTERACTION WITH RNA POLYMERASE II.
  8. "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, INTERACTION WITH THE NELF COMPLEX.
  9. "A novel RNA polymerase II-containing complex potentiates Tat-enhanced HIV-1 transcription."
    Parada C.A., Roeder R.G.
    EMBO J. 18:3688-3701(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION IN A COMPLEX WITH NCL; CCNT1; RNA POL II; HTATSF1 AND CDK9.
  10. "Transcription elongation factor hSPT5 stimulates mRNA capping."
    Wen Y., Shatkin A.J.
    Genes Dev. 13:1774-1779(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH RNGTT.
  11. "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 RNA POLYMERASE II AND SUPT4H1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  12. "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, INTERACTION WITH HTATSF1 AND RNA POLYMERASE II.
  13. "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.
  14. "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: FUNCTION, INTERACTION WITH RNA POLYMERASE II AND SUPT4H1, PHOSPHORYLATION AT THR-775 AND THR-784.
  15. "Positive transcription elongation factor B phosphorylates hSPT5 and RNA polymerase II carboxyl-terminal domain independently of cyclin-dependent kinase-activating kinase."
    Kim J.B., Sharp P.A.
    J. Biol. Chem. 276:12317-12323(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION BY CDK9.
  16. "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, PHOSPHORYLATION BY CDK9.
  17. "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.
  18. "The peptidyl-prolyl isomerase Pin1 interacts with hSpt5 phosphorylated by Cdk9."
    Lavoie S.B., Albert A.L., Handa H., Vincent M., Bensaude O.
    J. Mol. Biol. 312:675-685(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PIN1, PHOSPHORYLATION.
  19. "Spt5 cooperates with human immunodeficiency virus type 1 Tat by preventing premature RNA release at terminator sequences."
    Bourgeois C.F., Kim Y.K., Churcher M.J., West M.J., Karn J.
    Mol. Cell. Biol. 22:1079-1093(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PHOSPHORYLATION BY CDK9.
  20. "Evidence that negative elongation factor represses transcription elongation through binding to a DRB sensitivity-inducing factor/RNA polymerase II complex and RNA."
    Yamaguchi Y., Inukai N., Narita T., Wada T., Handa H.
    Mol. Cell. Biol. 22:2918-2927(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH THE NELF COMPLEX.
  21. "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 SUPT4H1.
  22. "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, INTERACTION WITH CDK9; PRMT1; RNA POLYMERASE II; PRMT5 AND SUPT4H1, METHYLATION AT ARG-681; ARG-696 AND ARG-698, MUTAGENESIS OF ARG-681; ARG-696 AND ARG-698.
  23. "Human transcription elongation factor NELF: identification of novel subunits and reconstitution of the functionally active complex."
    Narita T., Yamaguchi Y., Yano K., Sugimoto S., Chanarat S., Wada T., Kim D.-K., Hasegawa J., Omori M., Inukai N., Endoh M., Yamada T., Handa H.
    Mol. Cell. Biol. 23:1863-1873(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH THE NELF COMPLEX.
  24. "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, MUTAGENESIS OF GLY-1002.
  25. "Coordination of transcription factor phosphorylation and histone methylation by the P-TEFb kinase during human immunodeficiency virus type 1 transcription."
    Zhou M., Deng L., Lacoste V., Park H.U., Pumfery A., Kashanchi F., Brady J.N., Kumar A.
    J. Virol. 78:13522-13533(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION BY CDK9.
  26. "Dynamics of human immunodeficiency virus transcription: P-TEFb phosphorylates RD and dissociates negative effectors from the transactivation response element."
    Fujinaga K., Irwin D., Huang Y., Taube R., Kurosu T., Peterlin B.M.
    Mol. Cell. Biol. 24:787-795(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  27. Cited for: INTERACTION WITH RNA POLYMERASE II; SUPT4H1 AND SUPT6H.
  28. "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.
  29. "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.
  30. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-666, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  31. "Dichotomous but stringent substrate selection by the dual-function Cdk7 complex revealed by chemical genetics."
    Larochelle S., Batliner J., Gamble M.J., Barboza N.M., Kraybill B.C., Blethrow J.D., Shokat K.M., Fisher R.P.
    Nat. Struct. Mol. Biol. 13:55-62(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION BY CDK7.
  32. "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."
    Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.
    J. Proteome Res. 6:4150-4162(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  33. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-666 AND THR-1034, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  34. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  35. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-666 AND THR-1034, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  36. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  37. "Solution structure of KOW motifs of human transcription elongation factor SPT5."
    RIKEN structural genomics initiative (RSGI)
    Submitted (JUL-2007) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 420-523 AND 690-757.
  38. "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 176-273 IN COMPLEX WITH SPT4H1.

Entry informationi

Entry nameiSPT5H_HUMAN
AccessioniPrimary (citable) accession number: O00267
Secondary accession number(s): O43279, Q59G52, Q99639
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 22, 2005
Last sequence update: July 1, 1997
Last modified: September 3, 2014
This is version 134 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: 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

External Data

Dasty 3

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