RNA Polymerase II Transcription (Homo sapiens)

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Bibliography

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1. Martinez E, Ge H, Tao Y, Yuan CX, Palhan V, Roeder RG.; ''Novel cofactors and TFIIA mediate functional core promoter selectivity by the human TAFII150-containing TFIID complex.''; PubMed Europe PMC Scholia
2. Mandal SS, Cho H, Kim S, Cabane K, Reinberg D.; ''FCP1, a phosphatase specific for the heptapeptide repeat of the largest subunit of RNA polymerase II, stimulates transcription elongation.''; PubMed Europe PMC Scholia
3. Dvir A, Conaway RC, Conaway JW.; ''A role for TFIIH in controlling the activity of early RNA polymerase II elongation complexes.''; PubMed Europe PMC Scholia
4. Kibel A, Iliopoulos O, DeCaprio JA, Kaelin WG.; ''Binding of the von Hippel-Lindau tumor suppressor protein to Elongin B and C.''; PubMed Europe PMC Scholia
5. Roeder RG.; ''Transcriptional regulation and the role of diverse coactivators in animal cells.''; PubMed Europe PMC Scholia
6. Rosenfeld MG, Lunyak VV, Glass CK.; ''Sensors and signals: a coactivator/corepressor/epigenetic code for integrating signal-dependent programs of transcriptional response.''; PubMed Europe PMC Scholia
7. Mousson F, Kolkman A, Pijnappel WW, Timmers HT, Heck AJ.; ''Quantitative proteomics reveals regulation of dynamic components within TATA-binding protein (TBP) transcription complexes.''; PubMed Europe PMC Scholia
8. Gnatt AL, Cramer P, Fu J, Bushnell DA, Kornberg RD.; ''Structural basis of transcription: an RNA polymerase II elongation complex at 3.3 A resolution.''; PubMed Europe PMC Scholia
9. Yu M, Yang W, Ni T, Tang Z, Nakadai T, Zhu J, Roeder RG.; ''RNA polymerase II-associated factor 1 regulates the release and phosphorylation of paused RNA polymerase II.''; PubMed Europe PMC Scholia
10. Yao C, Choi EA, Weng L, Xie X, Wan J, Xing Y, Moresco JJ, Tu PG, Yates JR, Shi Y.; ''Overlapping and distinct functions of CstF64 and CstF64τ in mammalian mRNA 3' processing.''; PubMed Europe PMC Scholia
11. Hernandez N.; ''Small nuclear RNA genes: a model system to study fundamental mechanisms of transcription.''; PubMed Europe PMC Scholia
12. Bray SJ.; ''Notch signalling: a simple pathway becomes complex.''; PubMed Europe PMC Scholia
13. Yamazaki K, Guo L, Sugahara K, Zhang C, Enzan H, Nakabeppu Y, Kitajima S, Aso T.; ''Identification and biochemical characterization of a novel transcription elongation factor, Elongin A3.''; PubMed Europe PMC Scholia
14. Justice NJ, Jan YN.; ''Variations on the Notch pathway in neural development.''; PubMed Europe PMC Scholia
15. Sims RJ, Belotserkovskaya R, Reinberg D.; ''Elongation by RNA polymerase II: the short and long of it.''; PubMed Europe PMC Scholia
16. Pal M, McKean D, Luse DS.; ''Promoter clearance by RNA polymerase II is an extended, multistep process strongly affected by sequence.''; PubMed Europe PMC Scholia
17. Holstege FC, Fiedler U, Timmers HT.; ''Three transitions in the RNA polymerase II transcription complex during initiation.''; PubMed Europe PMC Scholia
18. Kadonaga JT.; ''Regulation of RNA polymerase II transcription by sequence-specific DNA binding factors.''; PubMed Europe PMC Scholia
19. Dvir A, Tan S, Conaway JW, Conaway RC.; ''Promoter escape by RNA polymerase II. Formation of an escape-competent transcriptional intermediate is a prerequisite for exit of polymerase from the promoter.''; PubMed Europe PMC Scholia
20. Jawdekar GW, Henry RW.; ''Transcriptional regulation of human small nuclear RNA genes.''; PubMed Europe PMC Scholia
21. Tirode F, Busso D, Coin F, Egly JM.; ''Reconstitution of the transcription factor TFIIH: assignment of functions for the three enzymatic subunits, XPB, XPD, and cdk7.''; PubMed Europe PMC Scholia
22. Yoh SM, Cho H, Pickle L, Evans RM, Jones KA.; ''The Spt6 SH2 domain binds Ser2-P RNAPII to direct Iws1-dependent mRNA splicing and export.''; PubMed Europe PMC Scholia
23. Wahle E, Rüegsegger U.; ''3'-End processing of pre-mRNA in eukaryotes.''; PubMed Europe PMC Scholia
24. Van Arsdell SW, Weiner AM.; ''Human genes for U2 small nuclear RNA are tandemly repeated.''; PubMed Europe PMC Scholia
25. Bertolotti A, Melot T, Acker J, Vigneron M, Delattre O, Tora L.; ''EWS, but not EWS-FLI-1, is associated with both TFIID and RNA polymerase II: interactions between two members of the TET family, EWS and hTAFII68, and subunits of TFIID and RNA polymerase II complexes.''; PubMed Europe PMC Scholia
26. Duan DR, Pause A, Burgess WH, Aso T, Chen DY, Garrett KP, Conaway RC, Conaway JW, Linehan WM, Klausner RD.; ''Inhibition of transcription elongation by the VHL tumor suppressor protein.''; PubMed Europe PMC Scholia
27. Maston GA, Evans SK, Green MR.; ''Transcriptional regulatory elements in the human genome.''; PubMed Europe PMC Scholia
28. Gangloff YG, Pointud JC, Thuault S, Carré L, Romier C, Muratoglu S, Brand M, Tora L, Couderc JL, Davidson I.; ''The TFIID components human TAF(II)140 and Drosophila BIP2 (TAF(II)155) are novel metazoan homologues of yeast TAF(II)47 containing a histone fold and a PHD finger.''; PubMed Europe PMC Scholia
29. Jacob GA, Luse SW, Luse DS.; ''Abortive initiation is increased only for the weakest members of a set of down mutants of the adenovirus 2 major late promoter.''; PubMed Europe PMC Scholia
30. Kamakaka RT, Bulger M, Kadonaga JT.; ''Potentiation of RNA polymerase II transcription by Gal4-VP16 during but not after DNA replication and chromatin assembly.''; PubMed Europe PMC Scholia
31. Frontini M, Soutoglou E, Argentini M, Bole-Feysot C, Jost B, Scheer E, Tora L.; ''TAF9b (formerly TAF9L) is a bona fide TAF that has unique and overlapping roles with TAF9.''; PubMed Europe PMC Scholia
32. Yamaguchi Y, Takagi T, Wada T, Yano K, Furuya A, Sugimoto S, Hasegawa J, Handa H.; ''NELF, a multisubunit complex containing RD, cooperates with DSIF to repress RNA polymerase II elongation.''; PubMed Europe PMC Scholia
33. Chen J, Wagner EJ.; ''snRNA 3' end formation: the dawn of the Integrator complex.''; PubMed Europe PMC Scholia
34. O'Reilly D, Kuznetsova OV, Laitem C, Zaborowska J, Dienstbier M, Murphy S.; ''Human snRNA genes use polyadenylation factors to promote efficient transcription termination.''; PubMed Europe PMC Scholia
35. Takagaki Y, Manley JL.; ''Complex protein interactions within the human polyadenylation machinery identify a novel component.''; PubMed Europe PMC Scholia
36. Zhao J, Hyman L, Moore C.; ''Formation of mRNA 3' ends in eukaryotes: mechanism, regulation, and interrelationships with other steps in mRNA synthesis.''; PubMed Europe PMC Scholia
37. Schultz P, Fribourg S, Poterszman A, Mallouh V, Moras D, Egly JM.; ''Molecular structure of human TFIIH.''; PubMed Europe PMC Scholia
38. Zhou Z, Licklider LJ, Gygi SP, Reed R.; ''Comprehensive proteomic analysis of the human spliceosome.''; PubMed Europe PMC Scholia
39. Egloff S, Dienstbier M, Murphy S.; ''Updating the RNA polymerase CTD code: adding gene-specific layers.''; PubMed Europe PMC Scholia
40. Orphanides G, Lagrange T, Reinberg D.; ''The general transcription factors of RNA polymerase II.''; PubMed Europe PMC Scholia
41. Hu D, Smith ER, Garruss AS, Mohaghegh N, Varberg JM, Lin C, Jackson J, Gao X, Saraf A, Florens L, Washburn MP, Eissenberg JC, Shilatifard A.; ''The little elongation complex functions at initiation and elongation phases of snRNA gene transcription.''; PubMed Europe PMC Scholia
42. Barolo S, Posakony JW.; ''Three habits of highly effective signaling pathways: principles of transcriptional control by developmental cell signaling.''; PubMed Europe PMC Scholia
43. Giglia-Mari G, Giglia-Mari G, Coin F, Ranish JA, Hoogstraten D, Theil A, Wijgers N, Jaspers NG, Raams A, Argentini M, van der Spek PJ, Botta E, Stefanini M, Egly JM, Aebersold R, Hoeijmakers JH, Vermeulen W.; ''A new, tenth subunit of TFIIH is responsible for the DNA repair syndrome trichothiodystrophy group A.''; PubMed Europe PMC Scholia
44. Morris DP, Michelotti GA, Schwinn DA.; ''Evidence that phosphorylation of the RNA polymerase II carboxyl-terminal repeats is similar in yeast and humans.''; PubMed Europe PMC Scholia
45. Bourbon HM, Aguilera A, Ansari AZ, Asturias FJ, Berk AJ, Bjorklund S, Blackwell TK, Borggrefe T, Carey M, Carlson M, Conaway JW, Conaway RC, Emmons SW, Fondell JD, Freedman LP, Fukasawa T, Gustafsson CM, Han M, He X, Herman PK, Hinnebusch AG, Holmberg S, Holstege FC, Jaehning JA, Kim YJ, Kuras L, Leutz A, Lis JT, Meisterernest M, Naar AM, Nasmyth K, Parvin JD, Ptashne M, Reinberg D, Ronne H, Sadowski I, Sakurai H, Sipiczki M, Sternberg PW, Stillman DJ, Strich R, Struhl K, Svejstrup JQ, Tuck S, Winston F, Roeder RG, Kornberg RD.; ''A unified nomenclature for protein subunits of mediator complexes linking transcriptional regulators to RNA polymerase II.''; PubMed Europe PMC Scholia
46. Egloff S, Murphy S.; ''Role of the C-terminal domain of RNA polymerase II in expression of small nuclear RNA genes.''; PubMed Europe PMC Scholia
47. Aso T, Lane WS, Conaway JW, Conaway RC.; ''Elongin (SIII): a multisubunit regulator of elongation by RNA polymerase II.''; PubMed Europe PMC Scholia
48. Cramer P.; ''Structure and function of RNA polymerase II.''; PubMed Europe PMC Scholia
49. Baillat D, Wagner EJ.; ''Integrator: surprisingly diverse functions in gene expression.''; PubMed Europe PMC Scholia
50. Woudstra EC, Gilbert C, Fellows J, Jansen L, Brouwer J, Erdjument-Bromage H, Tempst P, Svejstrup JQ.; ''A Rad26-Def1 complex coordinates repair and RNA pol II proteolysis in response to DNA damage.''; PubMed Europe PMC Scholia
51. Rachez C, Lemon BD, Suldan Z, Bromleigh V, Gamble M, Näär AM, Erdjument-Bromage H, Tempst P, Freedman LP.; ''Ligand-dependent transcription activation by nuclear receptors requires the DRIP complex.''; PubMed Europe PMC Scholia
52. Louvi A, Artavanis-Tsakonas S.; ''Notch signalling in vertebrate neural development.''; PubMed Europe PMC Scholia
53. Wada T, Takagi T, Yamaguchi Y, Ferdous A, Imai T, Hirose S, Sugimoto S, Yano K, Hartzog GA, Winston F, Buratowski S, Handa H.; ''DSIF, a novel transcription elongation factor that regulates RNA polymerase II processivity, is composed of human Spt4 and Spt5 homologs.''; PubMed Europe PMC Scholia
54. Goodrich JA, Tjian R.; ''Transcription factors IIE and IIH and ATP hydrolysis direct promoter clearance by RNA polymerase II.''; PubMed Europe PMC Scholia
55. Conaway JW, Florens L, Sato S, Tomomori-Sato C, Parmely TJ, Yao T, Swanson SK, Banks CA, Washburn MP, Conaway RC.; ''The mammalian Mediator complex.''; PubMed Europe PMC Scholia
56. Shilatifard A, Conaway RC, Conaway JW.; ''The RNA polymerase II elongation complex.''; PubMed Europe PMC Scholia
57. Fiedler U, Marc Timmers HT.; ''Peeling by binding or twisting by cranking: models for promoter opening and transcription initiation by RNA polymerase II.''; PubMed Europe PMC Scholia
58. Bunick D, Zandomeni R, Ackerman S, Weinmann R.; ''Mechanism of RNA polymerase II--specific initiation of transcription in vitro: ATP requirement and uncapped runoff transcripts.''; PubMed Europe PMC Scholia
59. Chen Y, Yamaguchi Y, Tsugeno Y, Yamamoto J, Yamada T, Nakamura M, Hisatake K, Handa H.; ''DSIF, the Paf1 complex, and Tat-SF1 have nonredundant, cooperative roles in RNA polymerase II elongation.''; PubMed Europe PMC Scholia
60. Lin X, Taube R, Fujinaga K, Peterlin BM.; ''P-TEFb containing cyclin K and Cdk9 can activate transcription via RNA.''; PubMed Europe PMC Scholia
61. Conaway RC, Conaway JW.; ''ATP activates transcription initiation from promoters by RNA polymerase II in a reversible step prior to RNA synthesis.''; PubMed Europe PMC Scholia
62. Blazek E, Mittler G, Meisterernst M.; ''The mediator of RNA polymerase II.''; PubMed Europe PMC Scholia
63. Wang W, Carey M, Gralla JD.; ''Polymerase II promoter activation: closed complex formation and ATP-driven start site opening.''; PubMed Europe PMC Scholia
64. Hoffmann A, Roeder RG.; ''Cloning and characterization of human TAF20/15. Multiple interactions suggest a central role in TFIID complex formation.''; PubMed Europe PMC Scholia
65. Gonatopoulos-Pournatzis T, Cowling VH.; ''Cap-binding complex (CBC).''; PubMed Europe PMC Scholia
66. Rossignol M, Kolb-Cheynel I, Egly JM.; ''Substrate specificity of the cdk-activating kinase (CAK) is altered upon association with TFIIH.''; PubMed Europe PMC Scholia
67. Orphanides G, LeRoy G, Chang CH, Luse DS, Reinberg D.; ''FACT, a factor that facilitates transcript elongation through nucleosomes.''; PubMed Europe PMC Scholia
68. Egloff S, O'Reilly D, Murphy S.; ''Expression of human snRNA genes from beginning to end.''; PubMed Europe PMC Scholia
69. Pavelitz T, Bailey AD, Elco CP, Weiner AM.; ''Human U2 snRNA genes exhibit a persistently open transcriptional state and promoter disassembly at metaphase.''; PubMed Europe PMC Scholia
70. Malik S, Roeder RG.; ''Dynamic regulation of pol II transcription by the mammalian Mediator complex.''; PubMed Europe PMC Scholia
71. Dominski Z, Erkmann JA, Yang X, Sànchez R, Marzluff WF.; ''A novel zinc finger protein is associated with U7 snRNP and interacts with the stem-loop binding protein in the histone pre-mRNP to stimulate 3'-end processing.''; PubMed Europe PMC Scholia
72. Archambault J, Pan G, Dahmus GK, Cartier M, Marshall N, Zhang S, Dahmus ME, Greenblatt J.; ''FCP1, the RAP74-interacting subunit of a human protein phosphatase that dephosphorylates the carboxyl-terminal domain of RNA polymerase IIO.''; PubMed Europe PMC Scholia
73. Buratowski S.; ''Progression through the RNA polymerase II CTD cycle.''; PubMed Europe PMC Scholia
74. Schweisguth F.; ''Regulation of notch signaling activity.''; PubMed Europe PMC Scholia
75. Aso T, Yamazaki K, Amimoto K, Kuroiwa A, Higashi H, Matsuda Y, Kitajima S, Hatakeyama M.; ''Identification and characterization of Elongin A2, a new member of the Elongin family of transcription elongation factors, specifically expressed in the testis.''; PubMed Europe PMC Scholia
76. Pal M, Luse DS.; ''Strong natural pausing by RNA polymerase II within 10 bases of transcription start may result in repeated slippage and reextension of the nascent RNA.''; PubMed Europe PMC Scholia
77. Parvin JD, Sharp PA.; ''DNA topology and a minimal set of basal factors for transcription by RNA polymerase II.''; PubMed Europe PMC Scholia
78. Fiedler U, Timmers HT.; ''Analysis of the open region of RNA polymerase II transcription complexes in the early phase of elongation.''; PubMed Europe PMC Scholia
79. Lin C, Smith ER, Takahashi H, Lai KC, Martin-Brown S, Florens L, Washburn MP, Conaway JW, Conaway RC, Shilatifard A.; ''AFF4, a component of the ELL/P-TEFb elongation complex and a shared subunit of MLL chimeras, can link transcription elongation to leukemia.''; PubMed Europe PMC Scholia
80. Bernstein LB, Manser T, Weiner AM.; ''Human U1 small nuclear RNA genes: extensive conservation of flanking sequences suggests cycles of gene amplification and transposition.''; PubMed Europe PMC Scholia
81. Kugel JF, Goodrich JA.; ''Translocation after synthesis of a four-nucleotide RNA commits RNA polymerase II to promoter escape.''; PubMed Europe PMC Scholia
82. Hernandez N.; ''TBP, a universal eukaryotic transcription factor?''; PubMed Europe PMC Scholia
83. Näär AM, Lemon BD, Tjian R.; ''Transcriptional coactivator complexes.''; PubMed Europe PMC Scholia
84. Zawel L, Kumar KP, Reinberg D.; ''Recycling of the general transcription factors during RNA polymerase II transcription.''; PubMed Europe PMC Scholia
85. Cramer P, Bushnell DA, Kornberg RD.; ''Structural basis of transcription: RNA polymerase II at 2.8 angstrom resolution.''; PubMed Europe PMC Scholia
86. Schaeffer L, Roy R, Humbert S, Moncollin V, Vermeulen W, Hoeijmakers JH, Chambon P, Egly JM.; ''DNA repair helicase: a component of BTF2 (TFIIH) basic transcription factor.''; PubMed Europe PMC Scholia

History

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Compare	Revision	Action	Time	User	Comment
	115030	view	16:57, 25 January 2021	ReactomeTeam	Reactome version 75
	113475	view	11:55, 2 November 2020	ReactomeTeam	Reactome version 74
	112674	view	16:06, 9 October 2020	ReactomeTeam	Reactome version 73
	101591	view	11:46, 1 November 2018	ReactomeTeam	reactome version 66
	101127	view	21:31, 31 October 2018	ReactomeTeam	reactome version 65
	100655	view	20:04, 31 October 2018	ReactomeTeam	reactome version 64
	100205	view	16:49, 31 October 2018	ReactomeTeam	reactome version 63
	99756	view	15:15, 31 October 2018	ReactomeTeam	reactome version 62 (2nd attempt)
	99318	view	12:47, 31 October 2018	ReactomeTeam	reactome version 62
	93793	view	13:36, 16 August 2017	ReactomeTeam	reactome version 61
	93329	view	11:20, 9 August 2017	ReactomeTeam	reactome version 61
	86414	view	09:17, 11 July 2016	ReactomeTeam	reactome version 56
	83471	view	13:23, 18 November 2015	ReactomeTeam	Version54
	81416	view	12:56, 21 August 2015	ReactomeTeam	Version53
	76887	view	08:16, 17 July 2014	ReactomeTeam	Fixed remaining interactions
	76592	view	11:57, 16 July 2014	ReactomeTeam	Fixed remaining interactions
	75625	view	10:49, 10 June 2014	ReactomeTeam	Reactome 48 Update
	74980	view	13:50, 8 May 2014	Anwesha	Fixing comment source for displaying WikiPathways description
	74624	view	08:40, 30 April 2014	ReactomeTeam	Reactome46
	45042	view	18:59, 6 October 2011	Thomas	Ontology Term : 'RNA Polymerase II transcription pathway' added !
	42122	view	21:58, 4 March 2011	MaintBot	Automatic update
	39932	view	05:57, 21 January 2011	MaintBot	New pathway

External references

DataNodes

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Name	Type	Database reference	Comment
3' end cleaved, ligated exon containing complex	Complex	REACT_3092 (Reactome)
ADP	Metabolite	CHEBI:16761 (ChEBI)
ALYREF [nucleoplasm]	Protein	Q86V81 (Uniprot-TrEMBL)
ATP [nucleoplasm]	Metabolite	CHEBI:15422 (ChEBI)
ATP	Metabolite	CHEBI:15422 (ChEBI)
Aborted early elongation complex	Complex	REACT_3362 (Reactome)
Aborted elongation complex after arrest	Complex	REACT_6654 (Reactome)
Arrested processive elongation complex	Complex	REACT_4675 (Reactome)
CCNH [nucleoplasm]	Protein	P51946 (Uniprot-TrEMBL)
CCNT1 [nucleoplasm]	Protein	O60563 (Uniprot-TrEMBL)
CCNT1	Protein	O60563 (Uniprot-TrEMBL)
CCNT2 [nucleoplasm]	Protein	O60583 (Uniprot-TrEMBL)
CCNT2	Protein	O60583 (Uniprot-TrEMBL)
CDC40 [nucleoplasm]	Protein	O60508 (Uniprot-TrEMBL)
CDK7 [nucleoplasm]	Protein	P50613 (Uniprot-TrEMBL)
CDK9 [nucleoplasm]	Protein	P50750 (Uniprot-TrEMBL)
CDK9	Protein	P50750 (Uniprot-TrEMBL)
CE:Pol II CTD:Spt5 complex	Complex	REACT_2332 (Reactome)	Spt5 reacts with Guanyl Transferase (GT) of the capping enzyme (CE).
CF II	Complex	REACT_3772 (Reactome)
CF I	Complex	REACT_4896 (Reactome)
CLP1 [nucleoplasm]	Protein	Q92989 (Uniprot-TrEMBL)
CPSF1 [nucleoplasm]	Protein	Q10570 (Uniprot-TrEMBL)
CPSF2 [nucleoplasm]	Protein	Q9P2I0 (Uniprot-TrEMBL)
CPSF3 [nucleoplasm]	Protein	Q9UKF6 (Uniprot-TrEMBL)
CPSF7 [nucleoplasm]	Protein	Q8N684 (Uniprot-TrEMBL)
CSTF1 [nucleoplasm]	Protein	Q05048 (Uniprot-TrEMBL)
CSTF2(2-577) [nucleoplasm]	Protein	P33240 (Uniprot-TrEMBL)
CSTF3 [nucleoplasm]	Protein	Q12996 (Uniprot-TrEMBL)
CTDP1 [nucleoplasm]	Protein	Q9Y5B0 (Uniprot-TrEMBL)
CTDP1	Protein	Q9Y5B0 (Uniprot-TrEMBL)
CTP [nucleoplasm]	Metabolite	CHEBI:17677 (ChEBI)
Cap Binding Complex (CBC)	Complex	REACT_3884 (Reactome)
Capped Intronless Histone pre-mRNA:CBC:ZFP100 Complex	Complex	REACT_5338 (Reactome)
Capped Intronless Histone pre-mRNA:CBP80:CBP20:SLBP:ZFP100 Complex	Complex	REACT_3667 (Reactome)
CstF	Complex	REACT_3503 (Reactome)
DHX38 [nucleoplasm]	Protein	Q92620 (Uniprot-TrEMBL)
DNA containing Pol II promoter with transcript with 2 or 3 nucleotides		REACT_3936 (Reactome)
DNA containing RNA Polymerase II promoter		REACT_2835 (Reactome)
DSIF complex	Complex	REACT_2797 (Reactome)
DSIF:NELF:early elongation complex	Complex	REACT_4575 (Reactome)
ELL [nucleoplasm]	Protein	P55199 (Uniprot-TrEMBL)
ELL	Protein	P55199 (Uniprot-TrEMBL)
ERCC2 [nucleoplasm]	Protein	P18074 (Uniprot-TrEMBL)
ERCC3 [nucleoplasm]	Protein	P19447 (Uniprot-TrEMBL)
Early elongation complex with hyperphosphorylated Pol II CTD	Complex	REACT_2481 (Reactome)
Elongation complex prior to separation	Complex	REACT_5853 (Reactome)
Elongation complex with separated and uncleaved transcript	Complex	REACT_5512 (Reactome)
Elongation complex	Complex	REACT_3511 (Reactome)
Elongin B:C complex	Complex	REACT_2434 (Reactome)
Elongin Complex	Complex	REACT_5616 (Reactome)
FACT complex	Complex	REACT_4314 (Reactome)
GTF2A1(1-274) [nucleoplasm]	Protein	P52655 (Uniprot-TrEMBL)
GTF2A1(275-376) [nucleoplasm]	Protein	P52655 (Uniprot-TrEMBL)
GTF2A2 [nucleoplasm]	Protein	P52657 (Uniprot-TrEMBL)
GTF2B [nucleoplasm]	Protein	Q00403 (Uniprot-TrEMBL)
GTF2B	Protein	Q00403 (Uniprot-TrEMBL)
GTF2E1 [nucleoplasm]	Protein	P29083 (Uniprot-TrEMBL)
GTF2E2 [nucleoplasm]	Protein	P29084 (Uniprot-TrEMBL)
GTF2F1(2-517) [nucleoplasm]	Protein	P35269 (Uniprot-TrEMBL)
GTF2F2(2-249) [nucleoplasm]	Protein	P13984 (Uniprot-TrEMBL)
GTF2H1(2-548) [nucleoplasm]	Protein	P32780 (Uniprot-TrEMBL)
GTF2H2 [nucleoplasm]	Protein	Q13888 (Uniprot-TrEMBL)
GTF2H3 [nucleoplasm]	Protein	Q13889 (Uniprot-TrEMBL)
GTF2H4 [nucleoplasm]	Protein	Q92759 (Uniprot-TrEMBL)
GTP [nucleoplasm]	Metabolite	CHEBI:15996 (ChEBI)
LSM10 [nucleoplasm]	Protein	Q969L4 (Uniprot-TrEMBL)
LSM11 [nucleoplasm]	Protein	P83369 (Uniprot-TrEMBL)
Ligated exon containing complex	Complex	REACT_5472 (Reactome)
MAGOH [nucleoplasm]	Protein	P61326 (Uniprot-TrEMBL)
MNAT1 [nucleoplasm]	Protein	P51948 (Uniprot-TrEMBL)
Mature Intronless transcript derived Histone mRNA:SLBP:CBP80:CBP20	Complex	REACT_3802 (Reactome)
Mature intronless transcript derived Histone pre-mRNA:CBC complex	Complex	REACT_5592 (Reactome)
NCBP1 [nucleoplasm]	Protein	Q09161 (Uniprot-TrEMBL)
NCBP2 [nucleoplasm]	Protein	P52298 (Uniprot-TrEMBL)
NELF complex	Complex	REACT_2737 (Reactome)
NELFA(2-528) [nucleoplasm]	Protein	Q9H3P2 (Uniprot-TrEMBL)
NELFA(2-528)	Protein	Q9H3P2 (Uniprot-TrEMBL)
NELFB [nucleoplasm]	Protein	Q8WX92 (Uniprot-TrEMBL)
NELFB	Protein	Q8WX92 (Uniprot-TrEMBL)
NELFCD [nucleoplasm]	Protein	Q8IXH7 (Uniprot-TrEMBL)
NELFCD	Protein	Q8IXH7 (Uniprot-TrEMBL)
NELFE [nucleoplasm]	Protein	P18615 (Uniprot-TrEMBL)
NELFE	Protein	P18615 (Uniprot-TrEMBL)
NFX.1 [nucleoplasm]	Protein	O43831 (Uniprot-TrEMBL)
NTP	Metabolite	REACT_4491 (Reactome)
NUDT21 [nucleoplasm]	Protein	O43809 (Uniprot-TrEMBL)
P-TEFb complex	Complex	REACT_3433 (Reactome)
PABPN1 [nucleoplasm]	Protein	Q86U42 (Uniprot-TrEMBL)
PAPOLA(2-745) [nucleoplasm]	Protein	P51003 (Uniprot-TrEMBL)
PCF11 [nucleoplasm]	Protein	O94913 (Uniprot-TrEMBL)
POLR2A [nucleoplasm]	Protein	P24928 (Uniprot-TrEMBL)
POLR2B [nucleoplasm]	Protein	P30876 (Uniprot-TrEMBL)
POLR2C [nucleoplasm]	Protein	P19387 (Uniprot-TrEMBL)
POLR2D(2-142) [nucleoplasm]	Protein	O15514 (Uniprot-TrEMBL)
POLR2E [nucleoplasm]	Protein	P19388 (Uniprot-TrEMBL)
POLR2F(1-127) [nucleoplasm]	Protein	P61218 (Uniprot-TrEMBL)
POLR2G [nucleoplasm]	Protein	P62487 (Uniprot-TrEMBL)
POLR2H [nucleoplasm]	Protein	P52434 (Uniprot-TrEMBL)
POLR2I [nucleoplasm]	Protein	P36954 (Uniprot-TrEMBL)
POLR2J [nucleoplasm]	Protein	P52435 (Uniprot-TrEMBL)
POLR2K [nucleoplasm]	Protein	P53803 (Uniprot-TrEMBL)
POLR2L [nucleoplasm]	Protein	P62875 (Uniprot-TrEMBL)
PPi	Metabolite	CHEBI:29888 (ChEBI)
Paused processive elongation complex	Complex	REACT_3066 (Reactome)
Pi	Metabolite	CHEBI:18367 (ChEBI)
Pol II Initiation complex with phosphodiester-PPi intermediate	Complex	REACT_2410 (Reactome)
Pol II Promoter Escape Complex	Complex	REACT_3851 (Reactome)
Pol II initiation complex	Complex	REACT_5487 (Reactome)
Pol II transcription complex containing extruded transcript to +30	Complex	REACT_4335 (Reactome)
Pol II transcription complex containing transcript to +30	Complex	REACT_4399 (Reactome)
Pol II transcription complex with (ser5) phosphorylated CTD containing extruded transcript to +30	Complex	REACT_2595 (Reactome)
Processive elongation complex	Complex	REACT_3018 (Reactome)
RBM8A [nucleoplasm]	Protein	Q9Y5S9 (Uniprot-TrEMBL)
RNA Pol II (hypophosphorylated) complex bound to DSIF protein	Complex	REACT_4417 (Reactome)
RNA Pol II (hypophosphorylated):capped pre-mRNA complex	Complex	REACT_5658 (Reactome)
RNA Pol II with phosphorylated CTD: CE complex with activated GT	Complex	REACT_3171 (Reactome)
RNA Pol II with phosphorylated CTD: CE complex	Complex	REACT_2371 (Reactome)
RNA Polymerase II (unphosphorylated):TFIIF complex	Complex	REACT_2692 (Reactome)
RNA Polymerase II holoenzyme complex (hyperphosphorylated)	Complex	REACT_4889 (Reactome)
RNGTT [nucleoplasm]	Protein	O60942 (Uniprot-TrEMBL)
RNGTT	Protein	O60942 (Uniprot-TrEMBL)
RNMT [nucleoplasm]	Protein	O43148 (Uniprot-TrEMBL)
RNMT	Protein	O43148 (Uniprot-TrEMBL)
RNPS1 [nucleoplasm]	Protein	Q15287 (Uniprot-TrEMBL)
SLBP [nucleoplasm]	Protein	Q14493 (Uniprot-TrEMBL)
SNRPB [nucleoplasm]	Protein	P14678 (Uniprot-TrEMBL)
SNRPD3 [nucleoplasm]	Protein	P62318 (Uniprot-TrEMBL)
SNRPE [nucleoplasm]	Protein	P62304 (Uniprot-TrEMBL)
SNRPF [nucleoplasm]	Protein	P62306 (Uniprot-TrEMBL)
SNRPG [nucleoplasm]	Protein	P62308 (Uniprot-TrEMBL)
SRRM1 [nucleoplasm]	Protein	Q8IYB3 (Uniprot-TrEMBL)
SRSF1 [nucleoplasm]	Protein	Q07955 (Uniprot-TrEMBL)
SRSF11 [nucleoplasm]	Protein	Q05519 (Uniprot-TrEMBL)
SRSF2 [nucleoplasm]	Protein	Q01130 (Uniprot-TrEMBL)
SRSF3 [nucleoplasm]	Protein	P84103 (Uniprot-TrEMBL)
SRSF4 [nucleoplasm]	Protein	Q08170 (Uniprot-TrEMBL)
SRSF5 [nucleoplasm]	Protein	Q13243 (Uniprot-TrEMBL)
SRSF6 [nucleoplasm]	Protein	Q13247 (Uniprot-TrEMBL)
SRSF7 [nucleoplasm]	Protein	Q16629 (Uniprot-TrEMBL)
SRSF9 [nucleoplasm]	Protein	Q13242 (Uniprot-TrEMBL)
SSRP1 [nucleoplasm]	Protein	Q08945 (Uniprot-TrEMBL)
SSRP1	Protein	Q08945 (Uniprot-TrEMBL)
SUPT16H [nucleoplasm]	Protein	Q9Y5B9 (Uniprot-TrEMBL)	DSIF is a heterodimer consisting of hSPT4 (human homolog of yeast Spt4- p14) and hSPT5 (human homolog of yeast Spt5-p160). DSIF association with Pol II may be enabled by Spt5 binding to Pol II creating a scaffold for NELF binding (Wada et al.,1998). Spt5 subunit of DSIF can be phosphorylated by P-TEFb.
SUPT16H	Protein	Q9Y5B9 (Uniprot-TrEMBL)	DSIF is a heterodimer consisting of hSPT4 (human homolog of yeast Spt4- p14) and hSPT5 (human homolog of yeast Spt5-p160). DSIF association with Pol II may be enabled by Spt5 binding to Pol II creating a scaffold for NELF binding (Wada et al.,1998). Spt5 subunit of DSIF can be phosphorylated by P-TEFb.
SUPT4H1 [nucleoplasm]	Protein	P63272 (Uniprot-TrEMBL)
SUPT4H1	Protein	P63272 (Uniprot-TrEMBL)
TAF1 [nucleoplasm]	Protein	P21675 (Uniprot-TrEMBL)
TAF10 [nucleoplasm]	Protein	Q12962 (Uniprot-TrEMBL)
TAF11 [nucleoplasm]	Protein	Q15544 (Uniprot-TrEMBL)
TAF12 [nucleoplasm]	Protein	Q16514 (Uniprot-TrEMBL)
TAF13 [nucleoplasm]	Protein	Q15543 (Uniprot-TrEMBL)
TAF4 [nucleoplasm]	Protein	O00268 (Uniprot-TrEMBL)
TAF4B [nucleoplasm]	Protein	Q92750 (Uniprot-TrEMBL)
TAF5 [nucleoplasm]	Protein	Q15542 (Uniprot-TrEMBL)
TAF6 [nucleoplasm]	Protein	P49848 (Uniprot-TrEMBL)
TAF9 [nucleoplasm]	Protein	Q16594 (Uniprot-TrEMBL)
TBP [nucleoplasm]	Protein	P20226 (Uniprot-TrEMBL)
TCEA1 [nucleoplasm]	Protein	P23193 (Uniprot-TrEMBL)
TCEA1	Protein	P23193 (Uniprot-TrEMBL)
TCEB1 [nucleoplasm]	Protein	Q15369 (Uniprot-TrEMBL)
TCEB1	Protein	Q15369 (Uniprot-TrEMBL)
TCEB2 [nucleoplasm]	Protein	Q15370 (Uniprot-TrEMBL)
TCEB2	Protein	Q15370 (Uniprot-TrEMBL)
TCEB3 [nucleoplasm]	Protein	Q14241 (Uniprot-TrEMBL)
TCEB3	Protein	Q14241 (Uniprot-TrEMBL)
TFIIA	Complex	REACT_5743 (Reactome)
TFIID	Complex	REACT_5886 (Reactome)
TFIIE	Complex	REACT_2368 (Reactome)
TFIIF	Complex	REACT_4708 (Reactome)
TFIIH	Complex	REACT_3832 (Reactome)
U2AF1 [nucleoplasm]	Protein	Q01081 (Uniprot-TrEMBL)
U2AF2 [nucleoplasm]	Protein	P26368 (Uniprot-TrEMBL)
U7 snRNP:ZNF473	Complex	REACT_5001 (Reactome)
UPF3B [nucleoplasm]	Protein	Q9BZI7 (Uniprot-TrEMBL)
UTP [nucleoplasm]	Metabolite	CHEBI:15713 (ChEBI)
ZNF473 [nucleoplasm]	Protein	Q8WTR7 (Uniprot-TrEMBL)
capped pre-mRNA:CBC:RNA Pol II (phosphorylated) complex	Complex	REACT_3243 (Reactome)
damaged DNA substrate:nascent mRNA hybrid		REACT_3022 (Reactome)
downstream intronless mRNA fragment		REACT_3064 (Reactome)
intronless pre-mRNA cleavage complex	Complex	REACT_3895 (Reactome)
mRNA 3'-end cleavage factor	Complex	REACT_2642 (Reactome)
p-S2,S5-POLR2A [nucleoplasm]	Protein	P24928 (Uniprot-TrEMBL)
p-S5-POLR2A [nucleoplasm]	Protein	P24928 (Uniprot-TrEMBL)
p-SUPT5H [nucleoplasm]	Protein	O00267 (Uniprot-TrEMBL)
p-SUPT5H	Protein	O00267 (Uniprot-TrEMBL)
pol II promoter:TFIID complex	Complex	REACT_5906 (Reactome)
pol II promoter:TFIID:TFIIA:TFIIB complex	Complex	REACT_2339 (Reactome)
pol II promoter:TFIID:TFIIA:TFIIB:Pol II:TFIIF complex	Complex	REACT_2469 (Reactome)
pol II promoter:TFIID:TFIIA:TFIIB:Pol II:TFIIF:TFIIE complex	Complex	REACT_4404 (Reactome)
pol II closed pre-initiation complex	Complex	REACT_5734 (Reactome)
pol II open pre-initiation complex	Complex	REACT_4930 (Reactome)
pol II transcription complex containing 11 nucleotide long transcript	Complex	REACT_3183 (Reactome)
pol II transcription complex containing 4-9 nucleotide long transcript	Complex	REACT_3928 (Reactome)
pol II transcription complex containing 3 Nucleotide long transcript	Complex	REACT_3251 (Reactome)
pol II transcription complex containing 4 nucleotide long transcript	Complex	REACT_4148 (Reactome)
pol II transcription complex containing 9 nucleotide long transcript	Complex	REACT_5212 (Reactome)
pol II transcription complex	Complex	REACT_2954 (Reactome)
template DNA with first transcript dinucleotide, opened to +8 position		REACT_3318 (Reactome)
template DNA:4-9 nucleotide transcript hybrid		REACT_3607 (Reactome)
upstream mRNA fragment:CPSF:PAP:PABPN1 complex	Complex	REACT_3436 (Reactome)

Annotated Interactions

View all...

Source	Target	Type	Database reference	Comment
	3' end cleaved, ligated exon containing complex	Arrow	REACT_1914 (Reactome)
	ADP	Arrow	REACT_1844 (Reactome)
ATP			REACT_1844 (Reactome)
	Aborted early elongation complex	Arrow	REACT_989 (Reactome)
	Aborted elongation complex after arrest	Arrow	REACT_6355 (Reactome)
	Arrested processive elongation complex	Arrow	REACT_1645 (Reactome)
Arrested processive elongation complex			REACT_1094 (Reactome)
Arrested processive elongation complex			REACT_6355 (Reactome)
CCNT1			REACT_307 (Reactome)
CCNT2			REACT_307 (Reactome)
CDK9			REACT_307 (Reactome)
	CE:Pol II CTD:Spt5 complex	Arrow	REACT_423 (Reactome)
	CF I	Arrow	REACT_1914 (Reactome)
	CF I	Arrow	REACT_460 (Reactome)
	CF II	Arrow	REACT_1914 (Reactome)
	CF II	Arrow	REACT_460 (Reactome)
	CTDP1	Arrow	REACT_1138 (Reactome)
CTDP1			REACT_1251 (Reactome)
CTDP1		mim-catalysis	REACT_1251 (Reactome)
	Cap Binding Complex (CBC)	Arrow	REACT_2066 (Reactome)
Capped Intronless Histone pre-mRNA:CBC:ZFP100 Complex			REACT_1222 (Reactome)
Capped Intronless Histone pre-mRNA:CBP80:CBP20:SLBP:ZFP100 Complex			REACT_888 (Reactome)
	CstF	Arrow	REACT_1914 (Reactome)
	CstF	Arrow	REACT_460 (Reactome)
	DNA containing Pol II promoter with transcript with 2 or 3 nucleotides	Arrow	REACT_543 (Reactome)
DNA containing RNA Polymerase II promoter			REACT_745 (Reactome)
	DSIF complex	Arrow	REACT_1138 (Reactome)
	DSIF complex	Arrow	REACT_1635 (Reactome)
DSIF complex			REACT_802 (Reactome)
	DSIF:NELF:early elongation complex	Arrow	REACT_981 (Reactome)
DSIF:NELF:early elongation complex			REACT_2066 (Reactome)
DSIF:NELF:early elongation complex			REACT_989 (Reactome)
	ELL	Arrow	REACT_1138 (Reactome)
ELL			REACT_949 (Reactome)
	Early elongation complex with hyperphosphorylated Pol II CTD	Arrow	REACT_2066 (Reactome)
Early elongation complex with hyperphosphorylated Pol II CTD			REACT_949 (Reactome)
	Elongation complex prior to separation	Arrow	REACT_2053 (Reactome)
Elongation complex prior to separation			REACT_2030 (Reactome)
	Elongation complex with separated and uncleaved transcript	Arrow	REACT_2030 (Reactome)
	Elongation complex	Arrow	REACT_949 (Reactome)
Elongation complex			REACT_751 (Reactome)
	Elongin B:C complex	Arrow	REACT_936 (Reactome)
Elongin B:C complex			REACT_51 (Reactome)
	Elongin Complex	Arrow	REACT_1138 (Reactome)
	Elongin Complex	Arrow	REACT_51 (Reactome)
Elongin Complex			REACT_949 (Reactome)
	FACT complex	Arrow	REACT_1138 (Reactome)
	FACT complex	Arrow	REACT_294 (Reactome)
FACT complex			REACT_949 (Reactome)
	GTF2B	Arrow	REACT_1817 (Reactome)
	GTF2B	Arrow	REACT_543 (Reactome)
	GTF2B	Arrow	REACT_653 (Reactome)
GTF2B			REACT_266 (Reactome)
Ligated exon containing complex			REACT_1914 (Reactome)
	Mature Intronless transcript derived Histone mRNA:SLBP:CBP80:CBP20	Arrow	REACT_888 (Reactome)
	Mature intronless transcript derived Histone pre-mRNA:CBC complex	Arrow	REACT_1222 (Reactome)
	NELF complex	Arrow	REACT_1138 (Reactome)
	NELF complex	Arrow	REACT_168 (Reactome)
NELF complex			REACT_981 (Reactome)
NELFA(2-528)			REACT_168 (Reactome)
NELFB			REACT_168 (Reactome)
NELFCD			REACT_168 (Reactome)
NELFE			REACT_168 (Reactome)
	NTP	Arrow	REACT_1138 (Reactome)
	NTP	Arrow	REACT_2053 (Reactome)
	NTP	Arrow	REACT_981 (Reactome)
NTP			REACT_1082 (Reactome)
NTP			REACT_1160 (Reactome)
NTP			REACT_1817 (Reactome)
NTP			REACT_2053 (Reactome)
NTP			REACT_209 (Reactome)
NTP			REACT_40 (Reactome)
NTP			REACT_581 (Reactome)
NTP			REACT_751 (Reactome)
NTP			REACT_981 (Reactome)
	P-TEFb complex	Arrow	REACT_1138 (Reactome)
	P-TEFb complex	Arrow	REACT_307 (Reactome)
P-TEFb complex			REACT_2066 (Reactome)
P-TEFb complex		mim-catalysis	REACT_2066 (Reactome)
	PPi	Arrow	REACT_1055 (Reactome)
	PPi	Arrow	REACT_1082 (Reactome)
	PPi	Arrow	REACT_1817 (Reactome)
	PPi	Arrow	REACT_209 (Reactome)
	PPi	Arrow	REACT_40 (Reactome)
	PPi	Arrow	REACT_581 (Reactome)
	Paused processive elongation complex	Arrow	REACT_234 (Reactome)
Paused processive elongation complex			REACT_1638 (Reactome)
	Pi	Arrow	REACT_1844 (Reactome)
	Pol II Initiation complex with phosphodiester-PPi intermediate	Arrow	REACT_1467 (Reactome)
Pol II Initiation complex with phosphodiester-PPi intermediate			REACT_1055 (Reactome)
Pol II Promoter Escape Complex			REACT_543 (Reactome)
	Pol II initiation complex	Arrow	REACT_1160 (Reactome)
Pol II initiation complex			REACT_1467 (Reactome)
	Pol II transcription complex containing extruded transcript to +30	Arrow	REACT_1567 (Reactome)
Pol II transcription complex containing extruded transcript to +30			REACT_1185 (Reactome)
	Pol II transcription complex containing transcript to +30	Arrow	REACT_209 (Reactome)
Pol II transcription complex containing transcript to +30			REACT_1567 (Reactome)
	Pol II transcription complex with (ser5) phosphorylated CTD containing extruded transcript to +30	Arrow	REACT_1185 (Reactome)
Pol II transcription complex with (ser5) phosphorylated CTD containing extruded transcript to +30			REACT_2233 (Reactome)
	Processive elongation complex	Arrow	REACT_1094 (Reactome)
	Processive elongation complex	Arrow	REACT_1638 (Reactome)
	Processive elongation complex	Arrow	REACT_751 (Reactome)
Processive elongation complex			REACT_1138 (Reactome)
Processive elongation complex			REACT_1645 (Reactome)
Processive elongation complex			REACT_2053 (Reactome)
Processive elongation complex			REACT_234 (Reactome)
			REACT_1055 (Reactome)	At the beginning of this reaction, 1 molecule of 'Pol II Initiation complex with phosphodiester-PPi intermediate' is present. At the end of this reaction, 1 molecule of 'pyrophosphate', and 1 molecule of 'pol II transcription complex' are present. This reaction takes place in the 'nucleus'.
			REACT_1082 (Reactome)	Formation of phosphodiester bonds nine and ten creates RNA products, which do not dissociate from the RNA pol II initiation complex. The transcription complex has enter the productive elongation phase. TFIIH and ATP-hydrolysis are required for efficient promoter escape. The open region (“transcription bubble�) expands concomitant with the site of RNA-extension. The region upstream from the transcription start site (-9 to -3) collapses to the double-stranded state. TFIIH remains associated to the RNA pol II initiation complex.
			REACT_1094 (Reactome)	TFIIS reactivates arrested RNA Pol II directly interacting with the enzyme resulting in endonucleolytic excision of nascent transcript ~7-14 nucleotides upstream of the 3' end. This reaction is catalyzed by the catalytic site and results in the generation of a new 3'-OH terminus that could be used for re-extension from the correctly base paired site (reviewed by Shilatifard et al., 2003).
			REACT_1138 (Reactome)	At the beginning of this reaction, 1 molecule of 'Processive elongation complex' is present. At the end of this reaction, 1 molecule of 'DSIF complex', 1 molecule of 'FACT complex', 1 molecule of 'RNA Polymerase II holoenzyme complex (hyperphosphorylated)', 1 molecule of 'damaged DNA substrate:nascent mRNA hybrid', 1 molecule of 'Elongin Complex', 1 molecule of 'FCP1P protein', 1 molecule of 'P-TEFb complex', 1 molecule of 'NELF complex', 1 molecule of 'RNA polymerase II elongation factor ELL', 1 molecule of 'NTP', 1 molecule of 'TFIIS protein', and 1 molecule of 'TFIIF' are present. This reaction takes place in the 'nucleus'.
			REACT_1160 (Reactome)	At the beginning of this reaction, 1 molecule of 'pol II open pre-initiation complex', and 2 molecules of 'NTP' are present. At the end of this reaction, 1 molecule of 'Pol II initiation complex' is present. This reaction takes place in the 'nucleus'.
			REACT_1185 (Reactome)	Phosphorylation of serine 5 residue at the CTD of pol II largest subunit is an important step signaling the end of initiation and escape into processive elongation processes. Cdk7 protein subunit of TFIIH phosphorylates RNA Pol II CTD serine 5 residues on its heptad repeats.
			REACT_1222 (Reactome)	Processing is initiated once the U7 snRNP is loaded onto the pre-mRNA. The pre-mRNA HDE makes base-pairing contacts with the 5′ end of U7 snRNA. Binding of the U7 snRNP to the pre-mRNA is stabilized by interactions between a U7 snRNP protein, hZFP100 and other trans-acting factors, including the factor that catalyzes the cleavage reaction, which have yet to be defined. The cleavage occurs in the presence of EDTA as does the cleavage reaction in polyadenylation, it is likely that this reaction is catalyzed by a protein. There may well be additional proteins associated with the U7 snRNP, since the in vitro processing occurs in the absence of SLBP, it is possible that all the other factors required for processing are associated with the active form of the U7 snRNP.
			REACT_1251 (Reactome)	FCP1 dephosphorylates RNAP II in ternary elongation complexes as well as in solution and, therefore, is thought to function in the recycling of RNAP II during the transcription cycle. Biochemical experiments suggest that human FCP1 targets CTDs that are phosphorylated at serine 2 (CTD-serine 2) and/or CTD-serine 5. It is also observed to stimulate elongation independent of its catalytic activity. Dephosphorylation of Ser2 - phosphorylated Pol II results in hypophosphorylated form that disengages capping enzymes (CE).
			REACT_1467 (Reactome)	At the beginning of this reaction, 1 molecule of 'Pol II initiation complex' is present. At the end of this reaction, 1 molecule of 'Pol II Initiation complex with phosphodiester-PPi intermediate' is present. This reaction takes place in the 'nucleus'.
			REACT_1567 (Reactome)	At the beginning of this reaction, 1 molecule of 'Pol II transcription complex containing transcript to +30' is present. At the end of this reaction, 1 molecule of 'Pol II transcription complex containing extruded transcript to +30' is present. This reaction takes place in the 'nucleus'.
			REACT_1635 (Reactome)	At the beginning of this reaction, 1 molecule of 'SUPT5H protein', and 1 molecule of 'SPT4H1 protein' are present. At the end of this reaction, 1 molecule of 'DSIF complex' is present. This reaction takes place in the 'nucleus'.
			REACT_1638 (Reactome)	Recovery from pausing occurs spontaneously after a variable length of time as the enzyme spontaneously slides forward again. This renders the transcript's 3'-OH terminus realigned with the catalytic Mg2+ site of the enzyme. TFIIS is capable of excising the nascent transcript at 2 or 3 nucleotides upstream of the transcript's 3'-end to reinitiate processive elongation (reviewed by Shilatifard et al., 2003).
			REACT_1645 (Reactome)	RNA Pol II arrest is believed to be a result of irreversible backsliding of the enzyme by ~7-14 nucleotides. It is suggested that, arrest leads to extrusion of displaced transcripts 3'-end through the small pore near the Mg2+ ion. Pol II arrest may lead to abortive termination of elongation due to irreversible trapping of the 3'-end of the displaced transcript in the pore (reviewed by Shilatifard et al., 2003).
			REACT_1684 (Reactome)	The general transcription factor TFIIF has a high affinity for the RNA Polymerase II holoenzyme. TFIIF stabilizes the preinitiation complex, and suppresses non-specific binding of RNA Pol II to DNA, and is thus critical for start site recognition.
			REACT_168 (Reactome)	At the beginning of this reaction, 1 molecule of 'NELF-A protein', 1 molecule of 'RD protein', 1 molecule of 'NELF-B protein', and 1 molecule of 'NELF-C/D protein' are present. At the end of this reaction, 1 molecule of 'NELF complex' is present. This reaction takes place in the 'nucleus'.
			REACT_1702 (Reactome)	At the beginning of this reaction, 1 molecule of 'pol II open pre-initiation complex' is present. At the end of this reaction, 1 molecule of 'pol II closed pre-initiation complex' is present. This reaction takes place in the 'nucleus'.
			REACT_1793 (Reactome)	At the beginning of this reaction, 1 molecule of 'pol II transcription complex containing 4-9 nucleotide long transcript' is present. At the end of this reaction, 1 molecule of 'template DNA:4-9 nucleotide transcript hybrid', 1 molecule of 'TFIIH', 1 molecule of 'TFIIE', and 1 molecule of 'RNA Polymerase II (unphosphorylated):TFIIF complex' are present. This reaction takes place in the 'nucleus'.
			REACT_1817 (Reactome)	Formation of the third phosphodiester bond creates a 4-nt product. This commits the initiation complex to promoter escape. The short 4-nt transcript is still loosely associated with the RNA polymerase II initiation complex and can dissociate to yield abortive products, which are not further extended. Inhibition of ATP-hydrolysis by TFIIH does not lead to collapse of the open region any longer. The transcription complex has lost the sensitivity to single-stranded oligo-nucleotide inhibition. However, ATP-hydrolysis and TFIIH are required for efficient promoter escape. The open region (“transcription bubble�) expands concomitant with the site of RNA-extension. In this case this region spans positions -9 to +4.
			REACT_1821 (Reactome)	Factor TFIIE enters the preinitiation complex after TFIIF recruits RNA Polymerase II. TFIIE is composed of two subunits of 56 kDA and 34 kDa. TFIIE facilitates the recruitment of factor TFIIH to the preinitiation complex, and it also stimulates the phosphorylation of the RNA Polymerase II CTD by TFIIH.
			REACT_1844 (Reactome)	After assembly of the complete RNA polymerase II-preinitiation complex, the next step is separation of the two DNA strands. This isomerization step is known as the closed-to-open complex transition and occurs prior to the initiation of mRNA synthesis. In the RNA polymerase II system this step requires the hydrolysis of ATP or dATP into Pi and ADP or dADP (in contrast to the other RNA polymerase systems) and is catalyzed by the XPB subunit of TFIIH. The region of the promoter, which becomes single-stranded , spans from –10 to +2 relative to the transcription start site. Negative supercoiling in the promoter region probably induces transient opening events and can alleviate requirement of TFIIE, TFIIH and ATP-hydrolysis for open complex formation. ATP is also used in this step by the cdk7-subunit of TFIIH to phosphorylate the heptad repeats of the C-terminal domain of the largest subunit of RNA polymerase II (RPB1) on serine-2
			REACT_1914 (Reactome)	Endonucleolytic cleavage separates the pre-mRNA into an upstream fragment destined to become the mature mRNA, and a downstream fragment that is rapidly degraded. Cleavage depends on two signals in the RNA, a highly conserved hexanucleotide, AAUAAA, 10 to 30 nucleotides upstream of the cleavage site, and a poorly conserved GU- or U-rich downstream element. Additional sequences, often upstream of AAUAAA, can enhance the efficiency of the reaction. Cleavage occurs most often after a CA dinucleotide. A single gene can have more than one 3' processing site. Cleavage is preceded by the assembly of a large processing complex, the composition of which is poorly defined. ATP, but not its hydrolysis, is required for assembly. Cleavage at the 3'-end of mRNAs depends on a number of protein factors. CPSF, a heterotetramer, binds specifically to the AAUAAA sequence. The heterotrimer CstF binds the downstream element. CF I, which appears to be composed of two subunits, one of several related larger polypeptides and a common smaller one, also binds RNA, but with unknown specificity. RNA recognition by these proteins is cooperative. Cleavage also requires CF II, composed of at least two subunits, and poly(A) polymerase, the enzyme synthesizing the poly(A) tail in the second step of the reaction. The polypeptide catalyzing the hydrolysis of the phosphodiester bond remains to be identified. Cleavage produces a 3'-OH on the upstream fragment and a 5'-phosphate on the downstream fragment. At some unknown point after cleavage, the downstream RNA fragment, CstF, CF I and CF II are thought to be released, whereas CPSF and poly(A) polymerase remain to carry out polyadenylation.
			REACT_2030 (Reactome)	At the beginning of this reaction, 1 molecule of 'Elongation complex prior to separation' is present. At the end of this reaction, 1 molecule of 'Elongation complex with separated and uncleaved transcript' is present. This reaction takes place in the 'nucleus'.
			REACT_2053 (Reactome)	At the beginning of this reaction, 1 molecule of 'Processive elongation complex', and 1 molecule of 'NTP' are present. At the end of this reaction, 1 molecule of 'Elongation complex prior to separation', and 1 molecule of 'NTP' are present. This reaction takes place in the 'nucleus'.
			REACT_2066 (Reactome)	Cdk-9 is the kinase subunit of P-TEFb that phosphorylates Serine 2 on the heptapeptide repeats of Pol II CTD alleviating the negative action of DSIF-NELF complex. This reaction is considered to be a rate limiting step for processive elongation. P-TEFb complex, that has a DRB-sensitive cyclin-dependent kinase activity, is composed of ~43 kDa, Cdk9 kinase (PITALRE), and either Cyclin T1, Cyclin T2a, Cyclin T2b, or Cyclin K. The exact mechanism by which P-TEFb removes the inhibition of elongation by DSIF-NELF is not yet known. P-TEFb is also capable of phosphorylating Spt5 subunit of DSIF complex. A P-TEFb complex (which contains only the Cyclin T1) is implicated in the efficient synthesis of human immunodeficiency virus-1 (HIV-1) transcripts. Cyclin T1 subunit of the P-TEFb(Cyclin T1:Cdk9) complex interacts with HIV-1 encoded Tat protein that binds to the transactivation response (TAR) element in the nascent HIV-1 transcript (reviewed in Price,2000). The mechanism by which DSIF, NELF and P-TEFb or TAK/P-TEFb act together in Pol II-regulated elongation is yet to be fully understood. Various biochemical evidences point to a model in which DSIF and NELF negatively regulate elongation through interactions with polymerase containing a hypophosphorylated CTD. Subsequent phosphorylation of the Pol II CTD by P-TEFb might promote elongation by inhibiting interactions of DSIF and NELF with the elongation complex.
			REACT_209 (Reactome)	RNA polymerase II transcription complexes are susceptible to transcriptional stalling and arrest, when extending nascent transcripts to 30-nt. This susceptibility depends on presence on down-stream DNA, the particular DNA-sequence of the template and presence of transcription factors. Transcription factor TFIIH remains associated to the RNA pol II elongation complex until position +30. At this stage transcription elongation factor TFIIS can rescue stalled transcription elongation complexes. The transcription bubble varies between 13- and 22-nt in size.
			REACT_2233 (Reactome)	At the beginning of this reaction, 1 molecule of 'mRNA capping enzyme', and 1 molecule of 'Pol II transcription complex with (ser5) phosphorylated CTD containing extruded transcript to +30' are present. At the end of this reaction, 1 molecule of 'RNA Pol II with phosphorylated CTD: CE complex' is present. This reaction takes place in the 'nucleus'.
			REACT_234 (Reactome)	Pol II pausing is believed to result from reversible backtracking of the Pol II enzyme complex by ~2 to 4 nucleotides. This leads to misaligned 3'-OH terminus that is unable to be an acceptor for the incoming NTPs in synthesis of next phosphodiester bond (reviewed by Shilatifard et al., 2003).
			REACT_266 (Reactome)	The general transcription factor TFIIB is a single polypeptide of approximately 35 kDa. There is a Zn-binding domain near the N terminus of TFIIB, and the C-terminal domain encompasses two imperfect repeats; between the N and C termini is a phylogenetically conserved region. The C terminus interacts with TBP and RNA Polymerase II, whereas the N terminus interacts with factor TFIIF and RNA polymerase II. TFIIB is a sequence-specific factor, and it interacts with the BRE element within the promoter. TFIIB interacts with the Rpb1 subunit of RNA polymerase II to define transcription strat sites. Several activators directly bind TFIIB, and stimulate transcription. The N-terminus and the C-terminus can participate in intramolecular interactions, and this can be disrupted by specific activators by causing a conformational change in TFIIB. TFIIA also binds the preinitiation complex along with TFIIB. However, TFIIA is not required for accurate initiation, but rather functions as a coactivator of transcription.
			REACT_294 (Reactome)	At the beginning of this reaction, 1 molecule of 'FACT 140 kDa subunit', and 1 molecule of 'FACT 80 kDa subunit' are present. At the end of this reaction, 1 molecule of 'FACT complex' is present. This reaction takes place in the 'nucleus'.
			REACT_307 (Reactome)	At the beginning of this reaction, 1 molecule of 'Cdk 9 protein', 1 molecule of 'Cyclin T1', and 1 molecule of 'Cyclin T2' are present. At the end of this reaction, 1 molecule of 'P-TEFb complex' is present. This reaction takes place in the 'nucleus'.
			REACT_40 (Reactome)	Formation of the second phosphodiester bond creates a 3-nt product. This short transcript is still loosely associated with the RNA polymerase II initiation complex and can dissociate to yield abortive products, which are not further extended. The transcription complex still requires continued ATP-hydrolysis by TFIIH and remains sensitive to single-stranded oligo-nucleotide inhibition. The open region (“transcription bubble�) expands concomitant with the site of RNA-extension. In this case this region spans positions -9 to +3.
			REACT_423 (Reactome)	The capping enzyme interacts with the Spt5 subunit of transcription elongation factor DSIF. This interaction may couple the capping reaction with promoter escape or elongation, thereby acting as a “checkpoint� to assure that capping has occurred before the polymerase proceeds to make the rest of the transcript.
			REACT_460 (Reactome)	The polypeptide catalyzing the hydrolysis of the phosphodiester bond remains to be identified. Cleavage produces a 3'-OH on the upstream fragment and a 5'-phosphate on the downstream fragment. At some unknown point after cleavage, the downstream fragment, CstF, CF I and CF II are thought to be released, whereas CPSF and poly(A) polymerase remain to carry out polyadenylation.
			REACT_51 (Reactome)	At the beginning of this reaction, 1 molecule of 'Elongin A1 protein', and 1 molecule of 'Elongin B:C complex' are present. At the end of this reaction, 1 molecule of 'Elongin Complex' is present. This reaction takes place in the 'nucleus'.
			REACT_543 (Reactome)	At the beginning of this reaction, 1 molecule of 'Pol II Promoter Escape Complex' is present. At the end of this reaction, 1 molecule of 'TFIIA', 1 molecule of 'TFIIH', 1 molecule of 'TFIIE', 1 molecule of 'TFIID', 1 molecule of 'TFIIB', 1 molecule of 'RNA Polymerase II (unphosphorylated):TFIIF complex', and 1 molecule of 'DNA containing Pol II promoter with transcript with 2 or 3 nucleotides' are present. This reaction takes place in the 'nucleus'.
			REACT_581 (Reactome)	Formation of the second phosphodiester bond creates a 3-nt product. This transcript is still loosely associated with the RNA polymerase II initiation complex and can dissociate to yield abortive products, which are not further extended. At this stage pausing by RNA polymerase II may result in repeated slippage and reextension of the nascent RNA. The transcription complex still requires continued ATP-hydrolysis by TFIIH for efficient promoter escape. Basal transcription factor TFIIE dissociates from the initiation complex before position +10. Basal transcription factor TFIIF may reassociate and can stimulate transcription elongation at multiple stages. The open region (“transcription bubble�) expands concomitant with the site of RNA-extension, eventually reaching an open region from -9 to +9.
			REACT_632 (Reactome)	The binding of TFIIH completes the assembly of the preinitiation complex (PIC) for RNA Polymerase II transcription. Although RNA polymerase binds the TATA box on the promoter DNA, no initiation of transcription occurs until TFIIH is bound to the PIC. TFIIH is the only factor with known enzymatic activities.
			REACT_6355 (Reactome)	At the beginning of this reaction, 1 molecule of 'Arrested processive elongation complex' is present. At the end of this reaction, 1 molecule of 'Aborted elongation complex after arrest' is present. This reaction takes place in the 'nucleus'.
			REACT_653 (Reactome)	At the beginning of this reaction, 1 molecule of 'pol II transcription complex' is present. At the end of this reaction, 1 molecule of 'TFIIA', 1 molecule of 'TFIIH', 1 molecule of 'TFIIE', 1 molecule of 'TFIID', 1 molecule of 'TFIIB', 1 molecule of 'RNA Polymerase II (unphosphorylated):TFIIF complex', and 1 molecule of 'template DNA with first transcript dinucleotide, opened to +8 position' are present. This reaction takes place in the 'nucleus'.
			REACT_745 (Reactome)	Although TBP (TATA box binding factor) is necessary and sufficient for initiation of basal transcription, the other subunits of the general transcription factor TFIID, the TBP-associated factors, are required for response to transcriptional activators. TBP binds to the TATA box (a core promoter element), and bends the DNA 80 degrees toward the major groove. This conformation of TBP-TATA box provides the proper topology for the binding of the general transcription factor TFIIB. Transcriptional activators function by affecting the kinetics of binding of TBP to the promoter DNA.
			REACT_751 (Reactome)	High-resolution structures of free, catalytically active yeast Pol II and of an elongating form reveal that Pol II elongation complex includes features like: - RNA-DNA hybrid, an unwound template ahead of 3'-OH terminus of growing transcript and an exit groove at the base of the CTD, possibly for dynamic interaction of processing and transcriptional factors. - a cleft or channel created by Rpb1 and Rpb2 subunits to accommodate DNA template, extending to Mg2+ ion located deep in the enzyme core -a 50 kDa "clamp" with open confirmation in free polymerase, allowing entry of DNA strands but closed in the processive elongation phase. The clamp is composed of portions of Rpb1,Rpb2 and Rpb3 , five loops or "switches" that change from unfolded to well-folded structures stabilizing the elongation complex, and a long "bridging helix" that emanates from Rpb1 subunit, crossing near the Mg2+ ion. The bridging helix is thought to "bend" to push on the base pair at the 3'-end of RNA-DNA hybrid like a ratchet, translocating Pol II along the DNA (Cramer et al.,2001; Gnatt et al.,2001).In addition to its dynamic biochemical potential, Pol II possess a repertoire of functions to serve as a critical platform of recruiting and coordinating the actions of a host of additional enzyme and proteins involved in various pathways.
			REACT_802 (Reactome)	DSIF is a heterodimer consisting of hSPT4 (human homolog of yeast Spt4- p14) and hSPT5 (human homolog of yeast Spt5-p160). DSIF association with Pol II may be enabled by Spt5 binding to Pol II creating a scaffold for NELF binding (Wada et al.,1998). Spt5 subunit of DSIF can be phosphorylated by P-TEFb.
			REACT_888 (Reactome)	Processing is initiated once the SLBP (bound to the stem loop) and the U7 snRNP (bound to the HDE) are both loaded onto the pre-mRNA. The pre-mRNA HDE makes base-pairing contacts with the 5′ end of U7 snRNA. Binding of the U7 snRNP to the pre-mRNA is stabilized by interactions between a U7 snRNP protein, hZFP100 and SLBP. It should be noted that there must be other trans-acting factors, including the factor that catalyzes the cleavage reaction, which have yet to be defined. The cleavage occurs in the presence of EDTA as does the cleavage reaction in polyadenylation, it is likely that this reaction is catalyzed by a protein. There may well be additional proteins associated with the U7 snRNP, and since in some conditions in vitro processing occurs in the absence of SLBP, it is possible that all the other factors required for processing are associated with the active form of the U7 snRNP.
			REACT_893 (Reactome)	At the beginning of this reaction, 1 molecule of 'RNA Pol II with phosphorylated CTD: CE complex' is present. At the end of this reaction, 1 molecule of 'RNA Pol II with phosphorylated CTD: CE complex with activated GT' is present. This reaction takes place in the 'nucleus'.
			REACT_936 (Reactome)	At the beginning of this reaction, 1 molecule of 'Elongin B protein', and 1 molecule of 'Elongin C protein' are present. At the end of this reaction, 1 molecule of 'Elongin B:C complex' is present. This reaction takes place in the 'nucleus'.
			REACT_949 (Reactome)	At the beginning of this reaction, 1 molecule of 'FACT complex', 1 molecule of 'Elongin Complex', 1 molecule of 'Early elongation complex with hyperphosphorylated Pol II CTD', 1 molecule of 'TFIIH', 1 molecule of 'RNA polymerase II elongation factor ELL', and 1 molecule of 'TFIIS protein' are present. At the end of this reaction, 1 molecule of 'Elongation complex' is present. This reaction takes place in the 'nucleus'.
			REACT_981 (Reactome)	NELF complex is a ~ 300 kDa multiprotein complex composed of 5 peptides (A - E): ~66,61,59,58 and 46 kDa. All these peptides are required for NELF-mediated inhibition of Pol II elongation. NELF complex has been reported to bind to the pre-formed DSIF:RNA Pol II complex that may act as a scaffold for its binding. NELF-A is suspected to be involved in Wolf-Hirschhorn syndrome. Binding of DSIF:NELF to RNA Pol II CTD results in abortive termination of early elongation steps by the growing transcripts.
			REACT_989 (Reactome)	In the early elongation phase, shorter transcripts typically of ~30 nt in length are generated due to random termination of elongating nascent transcripts. This abortive cessation of elongation has been observed mainly in the presence of DSIF-NELF bound to Pol II complex. (Reviewed in Conaway et al.,2000; Shilatifard et al., 2003 ).
	RNA Pol II (hypophosphorylated) complex bound to DSIF protein	Arrow	REACT_802 (Reactome)
RNA Pol II (hypophosphorylated) complex bound to DSIF protein			REACT_981 (Reactome)
	RNA Pol II (hypophosphorylated):capped pre-mRNA complex	Arrow	REACT_1251 (Reactome)
RNA Pol II (hypophosphorylated):capped pre-mRNA complex			REACT_802 (Reactome)
	RNA Pol II with phosphorylated CTD: CE complex with activated GT	Arrow	REACT_893 (Reactome)
RNA Pol II with phosphorylated CTD: CE complex with activated GT			REACT_423 (Reactome)
	RNA Pol II with phosphorylated CTD: CE complex	Arrow	REACT_2233 (Reactome)
RNA Pol II with phosphorylated CTD: CE complex			REACT_893 (Reactome)
	RNA Polymerase II (unphosphorylated):TFIIF complex	Arrow	REACT_1793 (Reactome)
	RNA Polymerase II (unphosphorylated):TFIIF complex	Arrow	REACT_543 (Reactome)
	RNA Polymerase II (unphosphorylated):TFIIF complex	Arrow	REACT_653 (Reactome)
RNA Polymerase II (unphosphorylated):TFIIF complex			REACT_1684 (Reactome)
RNA Polymerase II (unphosphorylated):TFIIF complex		mim-catalysis	REACT_1082 (Reactome)
RNA Polymerase II (unphosphorylated):TFIIF complex		mim-catalysis	REACT_1817 (Reactome)
RNA Polymerase II (unphosphorylated):TFIIF complex		mim-catalysis	REACT_209 (Reactome)
RNA Polymerase II (unphosphorylated):TFIIF complex		mim-catalysis	REACT_40 (Reactome)
RNA Polymerase II (unphosphorylated):TFIIF complex		mim-catalysis	REACT_581 (Reactome)
	RNA Polymerase II holoenzyme complex (hyperphosphorylated)	Arrow	REACT_1138 (Reactome)
RNGTT			REACT_2233 (Reactome)
RNMT			REACT_423 (Reactome)
SSRP1			REACT_294 (Reactome)
SUPT16H			REACT_294 (Reactome)
SUPT4H1			REACT_1635 (Reactome)
	TCEA1	Arrow	REACT_1138 (Reactome)
TCEA1			REACT_949 (Reactome)
TCEB1			REACT_936 (Reactome)
TCEB2			REACT_936 (Reactome)
TCEB3			REACT_51 (Reactome)
	TFIIA	Arrow	REACT_543 (Reactome)
	TFIIA	Arrow	REACT_581 (Reactome)
	TFIIA	Arrow	REACT_653 (Reactome)
TFIIA			REACT_266 (Reactome)
	TFIID	Arrow	REACT_543 (Reactome)
	TFIID	Arrow	REACT_581 (Reactome)
	TFIID	Arrow	REACT_653 (Reactome)
TFIID			REACT_745 (Reactome)
	TFIIE	Arrow	REACT_1793 (Reactome)
	TFIIE	Arrow	REACT_543 (Reactome)
	TFIIE	Arrow	REACT_581 (Reactome)
	TFIIE	Arrow	REACT_653 (Reactome)
TFIIE			REACT_1821 (Reactome)
	TFIIF	Arrow	REACT_1138 (Reactome)
	TFIIH	Arrow	REACT_1251 (Reactome)
	TFIIH	Arrow	REACT_1793 (Reactome)
	TFIIH	Arrow	REACT_543 (Reactome)
	TFIIH	Arrow	REACT_653 (Reactome)
	TFIIH	Arrow	REACT_751 (Reactome)
TFIIH			REACT_1251 (Reactome)
TFIIH			REACT_632 (Reactome)
TFIIH			REACT_949 (Reactome)
TFIIH		mim-catalysis	REACT_1185 (Reactome)
TFIIH		mim-catalysis	REACT_1817 (Reactome)
TFIIH		mim-catalysis	REACT_1844 (Reactome)
TFIIH		mim-catalysis	REACT_40 (Reactome)
	U7 snRNP:ZNF473	Arrow	REACT_1222 (Reactome)
	U7 snRNP:ZNF473	Arrow	REACT_888 (Reactome)
capped pre-mRNA:CBC:RNA Pol II (phosphorylated) complex			REACT_1251 (Reactome)
	damaged DNA substrate:nascent mRNA hybrid	Arrow	REACT_1138 (Reactome)
	downstream intronless mRNA fragment	Arrow	REACT_460 (Reactome)
intronless pre-mRNA cleavage complex			REACT_460 (Reactome)
mRNA 3'-end cleavage factor		mim-catalysis	REACT_1914 (Reactome)
p-SUPT5H			REACT_1635 (Reactome)
p-SUPT5H			REACT_423 (Reactome)
	pol II promoter:TFIID complex	Arrow	REACT_745 (Reactome)
pol II promoter:TFIID complex			REACT_266 (Reactome)
	pol II promoter:TFIID:TFIIA:TFIIB complex	Arrow	REACT_266 (Reactome)
pol II promoter:TFIID:TFIIA:TFIIB complex			REACT_1684 (Reactome)
	pol II promoter:TFIID:TFIIA:TFIIB:Pol II:TFIIF complex	Arrow	REACT_1684 (Reactome)
pol II promoter:TFIID:TFIIA:TFIIB:Pol II:TFIIF complex			REACT_1821 (Reactome)
	pol II promoter:TFIID:TFIIA:TFIIB:Pol II:TFIIF:TFIIE complex	Arrow	REACT_1821 (Reactome)
pol II promoter:TFIID:TFIIA:TFIIB:Pol II:TFIIF:TFIIE complex			REACT_632 (Reactome)
	pol II closed pre-initiation complex	Arrow	REACT_1702 (Reactome)
	pol II closed pre-initiation complex	Arrow	REACT_632 (Reactome)
pol II closed pre-initiation complex			REACT_1844 (Reactome)
	pol II open pre-initiation complex	Arrow	REACT_1844 (Reactome)
pol II open pre-initiation complex			REACT_1160 (Reactome)
pol II open pre-initiation complex			REACT_1702 (Reactome)
	pol II transcription complex containing 11 nucleotide long transcript	Arrow	REACT_1082 (Reactome)
pol II transcription complex containing 11 nucleotide long transcript			REACT_209 (Reactome)
pol II transcription complex containing 4-9 nucleotide long transcript			REACT_1793 (Reactome)
	pol II transcription complex containing 3 Nucleotide long transcript	Arrow	REACT_40 (Reactome)
pol II transcription complex containing 3 Nucleotide long transcript			REACT_1817 (Reactome)
	pol II transcription complex containing 4 nucleotide long transcript	Arrow	REACT_1817 (Reactome)
pol II transcription complex containing 4 nucleotide long transcript			REACT_581 (Reactome)
	pol II transcription complex containing 9 nucleotide long transcript	Arrow	REACT_581 (Reactome)
pol II transcription complex containing 9 nucleotide long transcript			REACT_1082 (Reactome)
	pol II transcription complex	Arrow	REACT_1055 (Reactome)
pol II transcription complex			REACT_40 (Reactome)
pol II transcription complex			REACT_653 (Reactome)
	template DNA with first transcript dinucleotide, opened to +8 position	Arrow	REACT_653 (Reactome)
	template DNA:4-9 nucleotide transcript hybrid	Arrow	REACT_1793 (Reactome)
	upstream mRNA fragment:CPSF:PAP:PABPN1 complex	Arrow	REACT_460 (Reactome)