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O00267

- SPT5H_HUMAN

UniProt

O00267 - SPT5H_HUMAN

Protein

Transcription elongation factor SPT5

Gene

SUPT5H

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 135 (01 Oct 2014)
      Sequence version 1 (01 Jul 1997)
      Previous versions | rss
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    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

    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

    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-acetyllysineBy 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.11 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.15 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.
    ModBaseiSearch...
    MobiDBiSearch...

    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.Curated
    Contains 5 KOW domains.Curated

    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.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti181 – 1811T → I in AAC51102. (PubMed:8975720)Curated
    Sequence conflicti483 – 4831G → A in AAC51102. (PubMed:8975720)Curated
    Sequence conflicti820 – 8201A → G in AAC51102. (PubMed:8975720)Curated
    Sequence conflicti846 – 8461P → R in BAA24075. (PubMed:9450929)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei103 – 1064Missing in isoform 2. 1 PublicationVSP_016282

    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

    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: October 1, 2014
    This is version 135 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