Transcription elongation factor SPT5

Protein names

Recommended name:
    Transcription elongation factor SPT5
      Short name=hSPT5
Alternative name(s):
    DRB sensitivity-inducing factor large subunit
      Short name=DSIF large subunit
    DSIF p160
    Tat-cotransactivator 1 protein
      Short name=Tat-CT1 protein

Gene names

Name:	SUPT5H
Synonyms:	SPT5, SPT5H

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Sequence length	1087 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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.10 Ref.11 Ref.12 Ref.14 Ref.21 Ref.22 Ref.18 Ref.20 Ref.23 Ref.27
Subcellular location	Nucleus. Ref.11
Tissue specificity	Ubiquitously expressed. Ref.11 Ref.1
Post-translational modification	Methylated by PRMT1/HRMT1L2 and PRMT5/SKB1. Methylation negatively regulates interaction with P-TEFb and RNA polymerase II. Ref.22 Phosphorylated. 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.14 Ref.16 Ref.19 Ref.18 Ref.2 Ref.15 Ref.25 Ref.30 Ref.31 Ref.32 Ref.33
Sequence similarities	Belongs to the SPT5 family. Contains 5 KOW domains.

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing
Domain	Repeat
Molecular function	Activator Repressor
PTM	Methylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	RNA elongation from RNA polymerase II promoter Ref.3 Ref.11 Inferred from direct assay. Source: UniProtKB cell cycle Ref.11 Non-traceable author statement. Source: UniProtKB chromatin remodeling Ref.11 Non-traceable author statement. Source: UniProtKB negative regulation of transcription from RNA polymerase II promoter Ref.3 Ref.11 Inferred from direct assay. Source: UniProtKB positive regulation of RNA elongation from RNA polymerase II promoter Inferred from electronic annotation. Source: InterPro positive regulation of transcription from RNA polymerase II promoter Ref.3 Inferred from direct assay. Source: UniProtKB response to organic substance Ref.11 Traceable author statement. Source: UniProtKB retroviral genome replication Ref.11 Non-traceable author statement. Source: UniProtKB
Cellular component	nucleoplasm Inferred from Experiment. Source: Reactome
Molecular function	enzyme binding Ref.11 Inferred from physical interaction. Source: UniProtKB negative transcription elongation factor activity Ref.3 Ref.11 Inferred from direct assay. Source: UniProtKB positive transcription elongation factor activity Ref.3 Inferred from direct assay. Source: UniProtKB protein heterodimerization activity Ref.3 Inferred from physical interaction. Source: UniProtKB
Complete GO annotation...

With	Entry	#Exp.	IntAct
POLR2A	P24928	2	EBI-710464,EBI-295301
PPIA	P62937	1	EBI-710464,EBI-437708
SUPT4H1	P63272	3	EBI-710464,EBI-727250

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Chain

1 – 1087

1087

Transcription elongation factor SPT5

PRO_0000208468

Domain

273 – 306

KOW 1

Domain

420 – 451

KOW 2

Domain

472 – 503

KOW 3

Domain

594 – 627

KOW 4

Domain

704 – 737

KOW 5

Repeat

754 – 759

CTR1-1; approximate

Repeat

760 – 765

CTR1-2

Repeat

766 – 771

CTR1-3

Repeat

772 – 778

CTR1-4

Repeat

781 – 787

CTR1-5

Repeat

788 – 794

CTR1-6

Repeat

796 – 802

CTR1-7

Repeat

803 – 809

CTR1-8

Repeat

811 – 817

CTR1-9

Repeat

844 – 851

CTR2-1

Repeat

854 – 862

CTR2-2; approximate

Repeat

863 – 869

CTR2-3; approximate

Repeat

881 – 885

CTR2-4; half-length

Repeat

896 – 902

CTR2-5; approximate

Repeat

904 – 911

CTR2-6

Repeat

916 – 921

CTR2-7; approximate

Repeat

924 – 930

CTR2-8

Repeat

932 – 939

CTR2-9

Repeat

943 – 950

CTR2-10

Region

176 – 270

Interaction with SUPT4H1

Region

313 – 420

108

Interaction with RNA polymerase II

Region

754 – 817

9 X 7 AA approximate tandem repeats of G-S-[QR]-T-P-X-[YQ], motif CTR1

Region

844 – 950

107

10 X 8 AA approximate tandem repeats of P-[TS]-P-S-P-[QA]-[SG]-Y, motif CTR2

Compositional bias

11 – 106

Glu-rich

Compositional bias

844 – 968

125

Pro-rich

Modified residue

666

Phosphoserine Ref.30 Ref.31 Ref.32 Ref.33

Modified residue

Asymmetric dimethylarginine; by PRMT1; alternate Ref.22

Modified residue

Omega-N-methylarginine; by PRMT1; alternate Ref.22

Modified residue

Asymmetric dimethylarginine; by PRMT1; alternate Ref.22

Modified residue

Omega-N-methylarginine; by PRMT1; alternate Ref.22

Modified residue

Asymmetric dimethylarginine; by PRMT1; alternate Ref.22

Modified residue

Omega-N-methylarginine; by PRMT1 and PRMT5; alternate Ref.22

Modified residue

Symmetric dimethylarginine; by PRMT5; alternate Ref.22

Modified residue

709

Phosphothreonine Ref.31

Modified residue

717

Phosphotyrosine Ref.31

Modified residue

775

Phosphothreonine; by CDK9 Ref.14

Modified residue

784

Phosphothreonine; by CDK9 Ref.14

Modified residue

1034

Phosphothreonine Ref.31 Ref.33

Alternative sequence

103 – 106

Missing in isoform 2.

VSP_016282

Mutagenesis

R → A: Enhances interactions with CDK9 and RNA polymerase II and enhances transcriptional elongation; when associated with A-696 and A-698. Ref.22

Mutagenesis

R → K: Increases promoter association and enhances transcriptional elongation; when associated with K-696 and K-698. Ref.22

Mutagenesis

R → A: Enhances interactions with CDK9 and RNA polymerase II and enhances transcriptional elongation; when associated with A-681 and A-698. Ref.22

Mutagenesis

R → K: Increases promoter association and enhances transcriptional elongation; when associated with K-681 and K-698. Ref.22

Mutagenesis

R → 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

Mutagenesis

R → K: Increases promoter association and enhances transcriptional elongation; when associated with K-681 and K-696. Ref.22

Mutagenesis

1002

G → D: Defective in regulation of transcriptional elongation. Ref.24

Sequence conflict

181

T → I in AAC51102. Ref.1

Sequence conflict

483

G → A in AAC51102. Ref.1

Sequence conflict

820

A → G in AAC51102. Ref.1

Sequence conflict

846

P → R in BAA24075. Ref.3

1087

Helix Strand Turn

Details...

Sequence		Length	Mass (Da)
Isoform 1 [UniParc]. Last modified July 1, 1997. Version 1. Checksum: EC3F402A670A5B7D Show »	FASTA	1,087	121,000
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. Checksum: 1B62A9E8011EB918 Show »	FASTA	1,083	120,499
10 20 30 40 50 60 MSDSEDSNFS EEEDSERSSD GEEAEVDEER RSAAGSEKEE EPEDEEEEEE EEEYDEEEEE 70 80 90 100 110 120 EDDDRPPKKP RHGGFILDEA DVDDEYEDED QWEDGAEDIL EKASNIDNVV LDEDRSGARR 130 140 150 160 170 180 LQNLWRDQRE EELGEYYMKK YAKSSVGETV YGGSDELSDD ITQQQLLPGV KDPNLWTVKC 190 200 210 220 230 240 KIGEERATAI SLMRKFIAYQ FTDTPLQIKS VVAPEHVKGY IYVEAYKQTH VKQAIEGVGN 250 260 270 280 290 300 LRLGYWNQQM VPIKEMTDVL KVVKEVANLK PKSWVRLKRG IYKDDIAQVD YVEPSQNTIS 310 320 330 340 350 360 LKMIPRIDYD RIKARMSLKD WFAKRKKFKR PPQRLFDAEK IRSLGGDVAS DGDFLIFEGN 370 380 390 400 410 420 RYSRKGFLFK SFAMSAVITE GVKPTLSELE KFEDQPEGID LEVVTESTGK EREHNFQPGD 430 440 450 460 470 480 NVEVCEGELI NLQGKILSVD GNKITIMPKH EDLKDMLEFP AQELRKYFKM GDHVKVIAGR 490 500 510 520 530 540 FEGDTGLIVR VEENFVILFS DLTMHELKVL PRDLQLCSET ASGVDVGGQH EWGELVQLDP 550 560 570 580 590 600 QTVGVIVRLE RETFQVLNMY GKVVTVRHQA VTRKKDNRFA VALDSEQNNI HVKDIVKVID 610 620 630 640 650 660 GPHSGREGEI RHLFRSFAFL HCKKLVENGG MFVCKTRHLV LAGGSKPRDV TNFTVGGFAP 670 680 690 700 710 720 MSPRISSPMH PSAGGQRGGF GSPGGGSGGM SRGRGRRDNE LIGQTVRISQ GPYKGYIGVV 730 740 750 760 770 780 KDATESTARV ELHSTCQTIS VDRQRLTTVG SRRPGGMTST YGRTPMYGSQ TPMYGSGSRT 790 800 810 820 830 840 PMYGSQTPLQ DGSRTPHYGS QTPLHDGSRT PAQSGAWDPN NPNTPSRAEE EYEYAFDDEP 850 860 870 880 890 900 TPSPQAYGGT PNPQTPGYPD PSSPQVNPQY NPQTPGTPAM YNTDQFSPYA APSPQGSYQP 910 920 930 940 950 960 SPSPQSYHQV APSPAGYQNT HSPASYHPTP SPMAYQASPS PSPVGYSPMT PGAPSPGGYN 970 980 990 1000 1010 1020 PHTPGSGIEQ NSSDWVTTDI QVKVRDTYLD TQVVGQTGVI RSVTGGMCSV YLKDSEKVVS 1030 1040 1050 1060 1070 1080 ISSEHLEPIT PTKNNKVKVI LGEDREATGV LLSIDGEDGI VRMDLDEQLK ILNLRFLGKL LEA « Hide

	« Hide 'large scale' referencesShow '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: 8975720] [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: 9199507] [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: 9450929] [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: 9514752] [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: 15489334] [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: 9857195] [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: 10199401] [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: 10393184] [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: 10421630] [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: 10075709] [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: 10454543] [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: 10912001] [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: 10757782] [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: 11145967] [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: 11112772] [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: 11553615] [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: 11575923] [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: 11809800] [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: 11940650] [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: 12653964] [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: 12718890] [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: 12612062] [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: 15380072] [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: 15564463] [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: 14701750] [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: 15060154] [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: 15136722] [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: 16214896] [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: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-666, MASS SPECTROMETRY. Tissue: Epithelium.
[31]	"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: 17924679] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-666; THR-709; TYR-717 AND THR-1034, MASS SPECTROMETRY. Tissue: Epithelium.
[32]	"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis." Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III J. Proteome Res. 7:1346-1351(2008) [PubMed: 18220336] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-666, MASS SPECTROMETRY.
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[34]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[35]	"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 420-757.
+	Additional computationally mapped references.