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Protein

Transcription elongation factor SPT5

Gene

SUPT5H

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Component of the DRB sensitivity-inducing factor complex (DSIF complex), which regulates mRNA processing and transcription elongation by RNA polymerase II. DSIF positively regulates mRNA capping by stimulating the mRNA guanylyltransferase activity of RNGTT/CAP1A. DSIF also acts cooperatively with the negative elongation factor complex (NELF complex) to enhance transcriptional pausing at sites proximal to the promoter. Transcriptional pausing may facilitate the assembly of an elongation competent RNA polymerase II complex. DSIF and NELF promote pausing by inhibition of the transcription elongation factor TFIIS/S-II. TFIIS/S-II binds to RNA polymerase II at transcription pause sites and stimulates the weak intrinsic nuclease activity of the enzyme. Cleavage of blocked transcripts by RNA polymerase II promotes the resumption of transcription from the new 3' terminus and may allow repeated attempts at transcription through natural pause sites. DSIF can also positively regulate transcriptional elongation and is required for the efficient activation of transcriptional elongation by the HIV-1 nuclear transcriptional activator, Tat. DSIF acts to suppress transcriptional pausing in transcripts derived from the HIV-1 LTR and blocks premature release of HIV-1 transcripts at terminator sequences.19 Publications

GO - Molecular functioni

  • chromatin binding Source: Ensembl
  • enzyme binding Source: UniProtKB
  • mRNA binding Source: GO_Central
  • poly(A) RNA binding Source: UniProtKB
  • protein heterodimerization activity Source: UniProtKB
  • structure-specific DNA binding Source: GO_Central

GO - Biological processi

  • 7-methylguanosine mRNA capping Source: Reactome
  • cell cycle Source: UniProtKB
  • chromatin remodeling Source: UniProtKB
  • DNA-templated transcription, elongation Source: UniProtKB
  • negative regulation of DNA-templated transcription, elongation Source: UniProtKB
  • negative regulation of mRNA polyadenylation Source: UniProtKB
  • negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  • positive regulation of DNA-templated transcription, elongation Source: UniProtKB
  • positive regulation of macroautophagy Source: BHF-UCL
  • positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  • positive regulation of viral transcription Source: Reactome
  • response to organic substance Source: UniProtKB
  • single stranded viral RNA replication via double stranded DNA intermediate Source: UniProtKB
  • transcription elongation from RNA polymerase II promoter Source: UniProtKB
  • transcription from RNA polymerase II promoter Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Activator, Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Enzyme and pathway databases

BioCyciMetaCyc:G66-31601-MONOMER.
ZFISH:G66-31601-MONOMER.
ReactomeiR-HSA-112382. Formation of RNA Pol II elongation complex.
R-HSA-112387. Elongation arrest and recovery.
R-HSA-113418. Formation of the Early Elongation Complex.
R-HSA-167152. Formation of HIV elongation complex in the absence of HIV Tat.
R-HSA-167158. Formation of the HIV-1 Early Elongation Complex.
R-HSA-167160. RNA Pol II CTD phosphorylation and interaction with CE.
R-HSA-167200. Formation of HIV-1 elongation complex containing HIV-1 Tat.
R-HSA-167238. Pausing and recovery of Tat-mediated HIV elongation.
R-HSA-167242. Abortive elongation of HIV-1 transcript in the absence of Tat.
R-HSA-167243. Tat-mediated HIV elongation arrest and recovery.
R-HSA-167246. Tat-mediated elongation of the HIV-1 transcript.
R-HSA-167287. HIV elongation arrest and recovery.
R-HSA-167290. Pausing and recovery of HIV elongation.
R-HSA-674695. RNA Polymerase II Pre-transcription Events.
R-HSA-6796648. TP53 Regulates Transcription of DNA Repair Genes.
R-HSA-72086. mRNA Capping.
R-HSA-75955. RNA Polymerase II Transcription Elongation.
R-HSA-77075. RNA Pol II CTD phosphorylation and interaction with CE.
SIGNORiO00267.

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
Proteomesi
  • UP000005640 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:11469. SUPT5H.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi681R → A: Enhances interactions with CDK9 and RNA polymerase II and enhances transcriptional elongation; when associated with A-696 and A-698. 1 Publication1
Mutagenesisi681R → K: Increases promoter association and enhances transcriptional elongation; when associated with K-696 and K-698. 1 Publication1
Mutagenesisi696R → A: Enhances interactions with CDK9 and RNA polymerase II and enhances transcriptional elongation; when associated with A-681 and A-698. 1 Publication1
Mutagenesisi696R → K: Increases promoter association and enhances transcriptional elongation; when associated with K-681 and K-698. 1 Publication1
Mutagenesisi698R → 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 Publication1
Mutagenesisi698R → K: Increases promoter association and enhances transcriptional elongation; when associated with K-681 and K-696. 1 Publication1
Mutagenesisi1002G → D: Defective in regulation of transcriptional elongation. 1 Publication1

Organism-specific databases

OpenTargetsiENSG00000196235.
PharmGKBiPA36255.

Polymorphism and mutation databases

BioMutaiSUPT5H.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002084681 – 1087Transcription elongation factor SPT5Add BLAST1087

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei32PhosphoserineBy similarity1
Modified residuei36PhosphoserineBy similarity1
Cross-linki143Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei666PhosphoserineCombined sources1
Modified residuei681Asymmetric dimethylarginine; by PRMT1; alternate1 Publication1
Modified residuei681Omega-N-methylarginine; by PRMT1; alternate1 Publication1
Modified residuei686PhosphoserineCombined sources1
Modified residuei696Asymmetric dimethylarginine; by PRMT1; alternate1 Publication1
Modified residuei696Omega-N-methylarginine; by PRMT1; alternate1 Publication1
Modified residuei698Asymmetric dimethylarginine; by PRMT1; alternate1 Publication1
Modified residuei698Omega-N-methylarginine; by PRMT1 and PRMT5; alternate1 Publication1
Modified residuei698Symmetric dimethylarginine; by PRMT5; alternate1 Publication1
Modified residuei718N6-acetyllysineBy similarity1
Modified residuei775Phosphothreonine; by CDK91 Publication1
Modified residuei784Phosphothreonine; by CDK91 Publication1
Modified residuei789PhosphoserineCombined sources1
Modified residuei791PhosphothreonineCombined sources1
Modified residuei804PhosphoserineCombined sources1
Modified residuei806PhosphothreonineCombined sources1
Modified residuei1034PhosphothreonineCombined sources1

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, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiO00267.
MaxQBiO00267.
PaxDbiO00267.
PeptideAtlasiO00267.
PRIDEiO00267.

PTM databases

iPTMnetiO00267.
PhosphoSitePlusiO00267.

Expressioni

Tissue specificityi

Ubiquitously expressed.2 Publications

Gene expression databases

BgeeiENSG00000196235.
CleanExiHS_SUPT5H.
ExpressionAtlasiO00267. baseline and differential.
GenevisibleiO00267. HS.

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
PIN1Q135263EBI-710464,EBI-714158
POLR2AP249284EBI-710464,EBI-295301
PPIAP629372EBI-710464,EBI-437708
SUPT4H1P632729EBI-710464,EBI-727250
TERF1P542742EBI-710464,EBI-710997

GO - Molecular functioni

  • enzyme binding Source: UniProtKB
  • protein heterodimerization activity Source: UniProtKB

Protein-protein interaction databases

BioGridi112697. 134 interactors.
DIPiDIP-29014N.
IntActiO00267. 75 interactors.
MINTiMINT-1193818.
STRINGi9606.ENSP00000404029.

Structurei

Secondary structure

11087
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi178 – 183Combined sources6
Helixi189 – 203Combined sources15
Beta strandi206 – 208Combined sources3
Beta strandi214 – 217Combined sources4
Beta strandi223 – 231Combined sources9
Helixi232 – 239Combined sources8
Helixi243 – 248Combined sources6
Helixi257 – 259Combined sources3
Helixi262 – 264Combined sources3
Beta strandi424 – 428Combined sources5
Turni432 – 435Combined sources4
Beta strandi437 – 440Combined sources4
Beta strandi447 – 452Combined sources6
Beta strandi461 – 464Combined sources4
Turni465 – 467Combined sources3
Beta strandi468 – 470Combined sources3
Beta strandi477 – 483Combined sources7
Turni484 – 487Combined sources4
Beta strandi489 – 495Combined sources7
Beta strandi500 – 507Combined sources8
Beta strandi509 – 513Combined sources5
Beta strandi517 – 521Combined sources5
Beta strandi708 – 712Combined sources5
Turni716 – 719Combined sources4
Beta strandi721 – 727Combined sources7
Beta strandi732 – 739Combined sources8
Beta strandi742 – 745Combined sources4
Turni747 – 749Combined sources3
Beta strandi750 – 752Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO00267.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini273 – 306KOW 1Add BLAST34
Domaini420 – 451KOW 2Add BLAST32
Domaini472 – 503KOW 3Add BLAST32
Domaini594 – 627KOW 4Add BLAST34
Domaini704 – 737KOW 5Add BLAST34
Repeati754 – 759CTR1-1; approximate6
Repeati760 – 765CTR1-26
Repeati766 – 771CTR1-36
Repeati772 – 778CTR1-47
Repeati781 – 787CTR1-57
Repeati788 – 794CTR1-67
Repeati796 – 802CTR1-77
Repeati803 – 809CTR1-87
Repeati811 – 817CTR1-97
Repeati844 – 851CTR2-18
Repeati854 – 862CTR2-2; approximate9
Repeati863 – 869CTR2-3; approximate7
Repeati881 – 885CTR2-4; half-length5
Repeati896 – 902CTR2-5; approximate7
Repeati904 – 911CTR2-68
Repeati916 – 921CTR2-7; approximate6
Repeati924 – 930CTR2-87
Repeati932 – 939CTR2-98
Repeati943 – 950CTR2-108

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni176 – 270Interaction with SUPT4H1Add BLAST95
Regioni313 – 420Interaction with RNA polymerase IIAdd BLAST108
Regioni754 – 8179 X 7 AA approximate tandem repeats of G-S-[QR]-T-P-X-[YQ], motif CTR1Add BLAST64
Regioni844 – 95010 X 8 AA approximate tandem repeats of P-[TS]-P-S-P-[QA]-[SG]-Y, motif CTR2Add BLAST107

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi11 – 106Glu-richAdd BLAST96
Compositional biasi844 – 968Pro-richAdd BLAST125

Sequence similaritiesi

Belongs to the SPT5 family.Curated
Contains 5 KOW domains.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG1999. Eukaryota.
COG0250. LUCA.
COG5164. LUCA.
GeneTreeiENSGT00440000037640.
HOGENOMiHOG000038564.
HOVERGENiHBG079775.
InParanoidiO00267.
KOiK15172.
OMAiSAHSFSM.
OrthoDBiEOG091G0114.
PhylomeDBiO00267.
TreeFamiTF105730.

Family and domain databases

Gene3Di2.30.30.30. 1 hit.
InterProiIPR005824. KOW.
IPR006645. NGN_dom.
IPR014722. Rib_L2_dom2.
IPR024945. Spt5_C_dom.
IPR022581. Spt5_N.
IPR017071. TF_Spt5.
IPR005100. TF_Spt5_NGN-domain.
IPR008991. Translation_prot_SH3-like.
[Graphical view]
PfamiPF00467. KOW. 1 hit.
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. AlignAdd to basket

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

        10         20         30         40         50
MSDSEDSNFS EEEDSERSSD GEEAEVDEER RSAAGSEKEE EPEDEEEEEE
60 70 80 90 100
EEEYDEEEEE EDDDRPPKKP RHGGFILDEA DVDDEYEDED QWEDGAEDIL
110 120 130 140 150
EKEEIEASNI DNVVLDEDRS GARRLQNLWR DQREEELGEY YMKKYAKSSV
160 170 180 190 200
GETVYGGSDE LSDDITQQQL LPGVKDPNLW TVKCKIGEER ATAISLMRKF
210 220 230 240 250
IAYQFTDTPL QIKSVVAPEH VKGYIYVEAY KQTHVKQAIE GVGNLRLGYW
260 270 280 290 300
NQQMVPIKEM TDVLKVVKEV ANLKPKSWVR LKRGIYKDDI AQVDYVEPSQ
310 320 330 340 350
NTISLKMIPR IDYDRIKARM SLKDWFAKRK KFKRPPQRLF DAEKIRSLGG
360 370 380 390 400
DVASDGDFLI FEGNRYSRKG FLFKSFAMSA VITEGVKPTL SELEKFEDQP
410 420 430 440 450
EGIDLEVVTE STGKEREHNF QPGDNVEVCE GELINLQGKI LSVDGNKITI
460 470 480 490 500
MPKHEDLKDM LEFPAQELRK YFKMGDHVKV IAGRFEGDTG LIVRVEENFV
510 520 530 540 550
ILFSDLTMHE LKVLPRDLQL CSETASGVDV GGQHEWGELV QLDPQTVGVI
560 570 580 590 600
VRLERETFQV LNMYGKVVTV RHQAVTRKKD NRFAVALDSE QNNIHVKDIV
610 620 630 640 650
KVIDGPHSGR EGEIRHLFRS FAFLHCKKLV ENGGMFVCKT RHLVLAGGSK
660 670 680 690 700
PRDVTNFTVG GFAPMSPRIS SPMHPSAGGQ RGGFGSPGGG SGGMSRGRGR
710 720 730 740 750
RDNELIGQTV RISQGPYKGY IGVVKDATES TARVELHSTC QTISVDRQRL
760 770 780 790 800
TTVGSRRPGG MTSTYGRTPM YGSQTPMYGS GSRTPMYGSQ TPLQDGSRTP
810 820 830 840 850
HYGSQTPLHD GSRTPAQSGA WDPNNPNTPS RAEEEYEYAF DDEPTPSPQA
860 870 880 890 900
YGGTPNPQTP GYPDPSSPQV NPQYNPQTPG TPAMYNTDQF SPYAAPSPQG
910 920 930 940 950
SYQPSPSPQS YHQVAPSPAG YQNTHSPASY HPTPSPMAYQ ASPSPSPVGY
960 970 980 990 1000
SPMTPGAPSP GGYNPHTPGS GIEQNSSDWV TTDIQVKVRD TYLDTQVVGQ
1010 1020 1030 1040 1050
TGVIRSVTGG MCSVYLKDSE KVVSISSEHL EPITPTKNNK VKVILGEDRE
1060 1070 1080
ATGVLLSIDG EDGIVRMDLD EQLKILNLRF LGKLLEA
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 differs from that shown. Reason: Erroneous initiation.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti181T → I in AAC51102 (PubMed:8975720).Curated1
Sequence conflicti483G → A in AAC51102 (PubMed:8975720).Curated1
Sequence conflicti820A → G in AAC51102 (PubMed:8975720).Curated1
Sequence conflicti846P → R in BAA24075 (PubMed:9450929).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_016282103 – 106Missing in isoform 2. 1 Publication4

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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_001306919.1. NM_001319990.1. [O00267-1]
NP_001306920.1. NM_001319991.1. [O00267-2]
NP_003160.2. NM_003169.3. [O00267-1]
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.
UCSCiuc002olo.5. human. [O00267-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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_001306919.1. NM_001319990.1. [O00267-1]
NP_001306920.1. NM_001319991.1. [O00267-2]
NP_003160.2. NM_003169.3. [O00267-1]
UniGeneiHs.631604.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112697. 134 interactors.
DIPiDIP-29014N.
IntActiO00267. 75 interactors.
MINTiMINT-1193818.
STRINGi9606.ENSP00000404029.

PTM databases

iPTMnetiO00267.
PhosphoSitePlusiO00267.

Polymorphism and mutation databases

BioMutaiSUPT5H.

Proteomic databases

EPDiO00267.
MaxQBiO00267.
PaxDbiO00267.
PeptideAtlasiO00267.
PRIDEiO00267.

Protocols and materials databases

DNASUi6829.
Structural Biology KnowledgebaseSearch...

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.
UCSCiuc002olo.5. human. [O00267-1]

Organism-specific databases

CTDi6829.
GeneCardsiSUPT5H.
HGNCiHGNC:11469. SUPT5H.
HPAiCAB034370.
HPA029273.
MIMi602102. gene.
neXtProtiNX_O00267.
OpenTargetsiENSG00000196235.
PharmGKBiPA36255.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1999. Eukaryota.
COG0250. LUCA.
COG5164. LUCA.
GeneTreeiENSGT00440000037640.
HOGENOMiHOG000038564.
HOVERGENiHBG079775.
InParanoidiO00267.
KOiK15172.
OMAiSAHSFSM.
OrthoDBiEOG091G0114.
PhylomeDBiO00267.
TreeFamiTF105730.

Enzyme and pathway databases

BioCyciMetaCyc:G66-31601-MONOMER.
ZFISH:G66-31601-MONOMER.
ReactomeiR-HSA-112382. Formation of RNA Pol II elongation complex.
R-HSA-112387. Elongation arrest and recovery.
R-HSA-113418. Formation of the Early Elongation Complex.
R-HSA-167152. Formation of HIV elongation complex in the absence of HIV Tat.
R-HSA-167158. Formation of the HIV-1 Early Elongation Complex.
R-HSA-167160. RNA Pol II CTD phosphorylation and interaction with CE.
R-HSA-167200. Formation of HIV-1 elongation complex containing HIV-1 Tat.
R-HSA-167238. Pausing and recovery of Tat-mediated HIV elongation.
R-HSA-167242. Abortive elongation of HIV-1 transcript in the absence of Tat.
R-HSA-167243. Tat-mediated HIV elongation arrest and recovery.
R-HSA-167246. Tat-mediated elongation of the HIV-1 transcript.
R-HSA-167287. HIV elongation arrest and recovery.
R-HSA-167290. Pausing and recovery of HIV elongation.
R-HSA-674695. RNA Polymerase II Pre-transcription Events.
R-HSA-6796648. TP53 Regulates Transcription of DNA Repair Genes.
R-HSA-72086. mRNA Capping.
R-HSA-75955. RNA Polymerase II Transcription Elongation.
R-HSA-77075. RNA Pol II CTD phosphorylation and interaction with CE.
SIGNORiO00267.

Miscellaneous databases

ChiTaRSiSUPT5H. human.
EvolutionaryTraceiO00267.
GeneWikiiSUPT5H.
GenomeRNAii6829.
PROiO00267.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000196235.
CleanExiHS_SUPT5H.
ExpressionAtlasiO00267. baseline and differential.
GenevisibleiO00267. HS.

Family and domain databases

Gene3Di2.30.30.30. 1 hit.
InterProiIPR005824. KOW.
IPR006645. NGN_dom.
IPR014722. Rib_L2_dom2.
IPR024945. Spt5_C_dom.
IPR022581. Spt5_N.
IPR017071. TF_Spt5.
IPR005100. TF_Spt5_NGN-domain.
IPR008991. Translation_prot_SH3-like.
[Graphical view]
PfamiPF00467. KOW. 1 hit.
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.
ProtoNetiSearch...

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: November 30, 2016
This is version 160 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.