Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

O00267 (SPT5H_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 133. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:SUPT5H
Synonyms:SPT5, SPT5H
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1087 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.3 Ref.4 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.16 Ref.17 Ref.19 Ref.21 Ref.22 Ref.24 Ref.26 Ref.28 Ref.29

Subunit structure

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. Ref.3 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.14 Ref.18 Ref.20 Ref.21 Ref.22 Ref.23 Ref.27

Subcellular location

Nucleus Ref.11.

Tissue specificity

Ubiquitously expressed. Ref.1 Ref.11

Post-translational modification

Methylated by PRMT1/HRMT1L2 and PRMT5/SKB1. Methylation negatively regulates interaction with P-TEFb and RNA polymerase II. Ref.22

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. Ref.2 Ref.14 Ref.15 Ref.16 Ref.18 Ref.19 Ref.25 Ref.31

Sequence similarities

Belongs to the SPT5 family.

Contains 5 KOW domains.

Sequence caution

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

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
   DomainRepeat
   Molecular functionActivator
Repressor
   PTMAcetylation
Methylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_process7-methylguanosine mRNA capping

Traceable author statement. Source: Reactome

DNA-templated transcription, elongation

Inferred from direct assay Ref.11. Source: UniProtKB

cell cycle

Non-traceable author statement Ref.11. Source: UniProtKB

chromatin remodeling

Non-traceable author statement Ref.11. Source: UniProtKB

gene expression

Traceable author statement. Source: Reactome

negative regulation of DNA-templated transcription, elongation

Inferred from direct assay Ref.11Ref.3. Source: UniProtKB

negative regulation of transcription from RNA polymerase II promoter

Inferred from direct assay Ref.11Ref.3. Source: UniProtKB

positive regulation of DNA-templated transcription, elongation

Inferred from direct assay Ref.3. Source: UniProtKB

positive regulation of macroautophagy

Inferred from mutant phenotype PubMed 22354037. Source: BHF-UCL

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay Ref.3. Source: UniProtKB

positive regulation of viral transcription

Traceable author statement. Source: Reactome

response to organic substance

Traceable author statement Ref.11. Source: UniProtKB

single stranded viral RNA replication via double stranded DNA intermediate

Non-traceable author statement Ref.11. Source: UniProtKB

transcription elongation from RNA polymerase II promoter

Inferred from direct assay Ref.11Ref.3. Source: UniProtKB

transcription from RNA polymerase II promoter

Traceable author statement. Source: Reactome

viral process

Traceable author statement. Source: Reactome

   Cellular_componentDSIF complex

Inferred from direct assay Ref.3. Source: UniProtKB

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay Ref.11. Source: UniProtKB

   Molecular_functionchromatin binding

Inferred from electronic annotation. Source: Ensembl

enzyme binding

Inferred from physical interaction Ref.11. Source: UniProtKB

poly(A) RNA binding

Inferred from direct assay PubMed 22658674PubMed 22681889. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.11PubMed 16169070. Source: IntAct

protein heterodimerization activity

Inferred from physical interaction Ref.3. Source: UniProtKB

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O00267-1)

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.
Isoform 2 (identifier: O00267-2)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10871087Transcription elongation factor SPT5
PRO_0000208468

Regions

Domain273 – 30634KOW 1
Domain420 – 45132KOW 2
Domain472 – 50332KOW 3
Domain594 – 62734KOW 4
Domain704 – 73734KOW 5
Repeat754 – 7596CTR1-1; approximate
Repeat760 – 7656CTR1-2
Repeat766 – 7716CTR1-3
Repeat772 – 7787CTR1-4
Repeat781 – 7877CTR1-5
Repeat788 – 7947CTR1-6
Repeat796 – 8027CTR1-7
Repeat803 – 8097CTR1-8
Repeat811 – 8177CTR1-9
Repeat844 – 8518CTR2-1
Repeat854 – 8629CTR2-2; approximate
Repeat863 – 8697CTR2-3; approximate
Repeat881 – 8855CTR2-4; half-length
Repeat896 – 9027CTR2-5; approximate
Repeat904 – 9118CTR2-6
Repeat916 – 9216CTR2-7; approximate
Repeat924 – 9307CTR2-8
Repeat932 – 9398CTR2-9
Repeat943 – 9508CTR2-10
Region176 – 27095Interaction with SUPT4H1
Region313 – 420108Interaction with RNA polymerase II
Region754 – 817649 X 7 AA approximate tandem repeats of G-S-[QR]-T-P-X-[YQ], motif CTR1
Region844 – 95010710 X 8 AA approximate tandem repeats of P-[TS]-P-S-P-[QA]-[SG]-Y, motif CTR2
Compositional bias11 – 10696Glu-rich
Compositional bias844 – 968125Pro-rich

Amino acid modifications

Modified residue6661Phosphoserine Ref.30 Ref.33 Ref.35
Modified residue6811Asymmetric dimethylarginine; by PRMT1; alternate Ref.22
Modified residue6811Omega-N-methylarginine; by PRMT1; alternate Ref.22
Modified residue6961Asymmetric dimethylarginine; by PRMT1; alternate Ref.22
Modified residue6961Omega-N-methylarginine; by PRMT1; alternate Ref.22
Modified residue6981Asymmetric dimethylarginine; by PRMT1; alternate Ref.22
Modified residue6981Omega-N-methylarginine; by PRMT1 and PRMT5; alternate Ref.22
Modified residue6981Symmetric dimethylarginine; by PRMT5; alternate Ref.22
Modified residue7181N6-acetyllysine By similarity
Modified residue7751Phosphothreonine; by CDK9 Ref.14
Modified residue7841Phosphothreonine; by CDK9 Ref.14
Modified residue10341Phosphothreonine Ref.33 Ref.35

Natural variations

Alternative sequence103 – 1064Missing in isoform 2.
VSP_016282

Experimental info

Mutagenesis6811R → A: Enhances interactions with CDK9 and RNA polymerase II and enhances transcriptional elongation; when associated with A-696 and A-698. Ref.22
Mutagenesis6811R → K: Increases promoter association and enhances transcriptional elongation; when associated with K-696 and K-698. Ref.22
Mutagenesis6961R → A: Enhances interactions with CDK9 and RNA polymerase II and enhances transcriptional elongation; when associated with A-681 and A-698. Ref.22
Mutagenesis6961R → K: Increases promoter association and enhances transcriptional elongation; when associated with K-681 and K-698. Ref.22
Mutagenesis6981R → A: Enhances transcriptional elongation. Enhances interactions with CDK9 and RNA polymerase II and enhances transcriptional elongation; when associated with A-681 and A-696. Ref.22
Mutagenesis6981R → K: Increases promoter association and enhances transcriptional elongation; when associated with K-681 and K-696. Ref.22
Mutagenesis10021G → D: Defective in regulation of transcriptional elongation. Ref.24
Sequence conflict1811T → I in AAC51102. Ref.1
Sequence conflict4831G → A in AAC51102. Ref.1
Sequence conflict8201A → G in AAC51102. Ref.1
Sequence conflict8461P → R in BAA24075. Ref.3

Secondary structure

...................................................... 1087
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified July 1, 1997. Version 1.
Checksum: EC3F402A670A5B7D

FASTA1,087121,000
        10         20         30         40         50         60 
MSDSEDSNFS EEEDSERSSD GEEAEVDEER RSAAGSEKEE EPEDEEEEEE EEEYDEEEEE 

        70         80         90        100        110        120 
EDDDRPPKKP RHGGFILDEA DVDDEYEDED QWEDGAEDIL EKEEIEASNI DNVVLDEDRS 

       130        140        150        160        170        180 
GARRLQNLWR DQREEELGEY YMKKYAKSSV GETVYGGSDE LSDDITQQQL LPGVKDPNLW 

       190        200        210        220        230        240 
TVKCKIGEER ATAISLMRKF IAYQFTDTPL QIKSVVAPEH VKGYIYVEAY KQTHVKQAIE 

       250        260        270        280        290        300 
GVGNLRLGYW NQQMVPIKEM TDVLKVVKEV ANLKPKSWVR LKRGIYKDDI AQVDYVEPSQ 

       310        320        330        340        350        360 
NTISLKMIPR IDYDRIKARM SLKDWFAKRK KFKRPPQRLF DAEKIRSLGG DVASDGDFLI 

       370        380        390        400        410        420 
FEGNRYSRKG FLFKSFAMSA VITEGVKPTL SELEKFEDQP EGIDLEVVTE STGKEREHNF 

       430        440        450        460        470        480 
QPGDNVEVCE GELINLQGKI LSVDGNKITI MPKHEDLKDM LEFPAQELRK YFKMGDHVKV 

       490        500        510        520        530        540 
IAGRFEGDTG LIVRVEENFV ILFSDLTMHE LKVLPRDLQL CSETASGVDV GGQHEWGELV 

       550        560        570        580        590        600 
QLDPQTVGVI VRLERETFQV LNMYGKVVTV RHQAVTRKKD NRFAVALDSE QNNIHVKDIV 

       610        620        630        640        650        660 
KVIDGPHSGR EGEIRHLFRS FAFLHCKKLV ENGGMFVCKT RHLVLAGGSK PRDVTNFTVG 

       670        680        690        700        710        720 
GFAPMSPRIS SPMHPSAGGQ RGGFGSPGGG SGGMSRGRGR RDNELIGQTV RISQGPYKGY 

       730        740        750        760        770        780 
IGVVKDATES TARVELHSTC QTISVDRQRL TTVGSRRPGG MTSTYGRTPM YGSQTPMYGS 

       790        800        810        820        830        840 
GSRTPMYGSQ TPLQDGSRTP HYGSQTPLHD GSRTPAQSGA WDPNNPNTPS RAEEEYEYAF 

       850        860        870        880        890        900 
DDEPTPSPQA YGGTPNPQTP GYPDPSSPQV NPQYNPQTPG TPAMYNTDQF SPYAAPSPQG 

       910        920        930        940        950        960 
SYQPSPSPQS YHQVAPSPAG YQNTHSPASY HPTPSPMAYQ ASPSPSPVGY SPMTPGAPSP 

       970        980        990       1000       1010       1020 
GGYNPHTPGS GIEQNSSDWV TTDIQVKVRD TYLDTQVVGQ TGVIRSVTGG MCSVYLKDSE 

      1030       1040       1050       1060       1070       1080 
KVVSISSEHL EPITPTKNNK VKVILGEDRE ATGVLLSIDG EDGIVRMDLD EQLKILNLRF 


LGKLLEA 

« Hide

Isoform 2 [UniParc].

Checksum: 1B62A9E8011EB918
Show »

FASTA1,083120,499

References

« Hide 'large scale' references
[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]"Human Spt6 stimulates transcription elongation by RNA polymerase II in vitro."
Endoh M., Zhu W., Hasegawa J., Watanabe H., Kim D.-K., Aida M., Inukai N., Narita T., Yamada T., Furuya A., Sato H., Yamaguchi Y., Mandal S.S., Reinberg D., Wada T., Handa H.
Mol. Cell. Biol. 24:3324-3336(2004) [PubMed] [Europe PMC] [Abstract]
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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [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.
[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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS12536.1. [O00267-1]
CCDS46072.1. [O00267-2]
RefSeqNP_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]
UniGeneHs.631604.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2DO3NMR-A462-523[»]
2E6ZNMR-A420-471[»]
2E70NMR-A694-757[»]
3H7HX-ray1.55B176-273[»]
4L1UX-ray2.42G/H/I/J778-790[»]
ProteinModelPortalO00267.
SMRO00267. Positions 176-311, 413-523, 702-757.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112697. 64 interactions.
DIPDIP-29014N.
IntActO00267. 28 interactions.
MINTMINT-1193818.
STRING9606.ENSP00000367784.

PTM databases

PhosphoSiteO00267.

Proteomic databases

MaxQBO00267.
PaxDbO00267.
PRIDEO00267.

Protocols and materials databases

DNASU6829.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000359191; ENSP00000352117; ENSG00000196235. [O00267-2]
ENST00000402194; ENSP00000384505; ENSG00000196235. [O00267-2]
ENST00000432763; ENSP00000404029; ENSG00000196235. [O00267-1]
ENST00000598725; ENSP00000469090; ENSG00000196235. [O00267-1]
ENST00000599117; ENSP00000470252; ENSG00000196235. [O00267-1]
GeneID6829.
KEGGhsa:6829.
UCSCuc002oln.4. human. [O00267-1]
uc002olq.4. human. [O00267-2]

Organism-specific databases

CTD6829.
GeneCardsGC19P039936.
HGNCHGNC:11469. SUPT5H.
HPACAB034370.
HPA029273.
MIM602102. gene.
neXtProtNX_O00267.
PharmGKBPA36255.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0250.
HOGENOMHOG000038564.
HOVERGENHBG079775.
InParanoidO00267.
KOK15172.
OMAAFFDIEA.
OrthoDBEOG7Z3F3Q.
PhylomeDBO00267.
TreeFamTF105730.

Enzyme and pathway databases

BioCycMetaCyc:G66-31601-MONOMER.
ReactomeREACT_116125. Disease.
REACT_1788. Transcription.
REACT_1892. Elongation arrest and recovery.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpressO00267.
BgeeO00267.
CleanExHS_SUPT5H.
GenevestigatorO00267.

Family and domain databases

InterProIPR005824. 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]
PfamPF00467. KOW. 2 hits.
PF03439. Spt5-NGN. 1 hit.
PF11942. Spt5_N. 1 hit.
[Graphical view]
PIRSFPIRSF036945. Spt5. 1 hit.
SMARTSM01104. CTD. 1 hit.
SM00739. KOW. 6 hits.
SM00738. NGN. 1 hit.
[Graphical view]
SUPFAMSSF50104. SSF50104. 1 hit.
ProtoNetSearch...

Other

ChiTaRSSUPT5H. human.
EvolutionaryTraceO00267.
GeneWikiSUPT5H.
GenomeRNAi6829.
NextBio26663.
PROO00267.
SOURCESearch...

Entry information

Entry nameSPT5H_HUMAN
AccessionPrimary (citable) accession number: O00267
Secondary accession number(s): O43279, Q59G52, Q99639
Entry history
Integrated into UniProtKB/Swiss-Prot: November 22, 2005
Last sequence update: July 1, 1997
Last modified: July 9, 2014
This is version 133 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM