UniProt Accession

 TCEA1_HUMAN; P23193; A6NF25; A8K339; Q15563; Q6FG87 

Genbank Protein ID

 X62585; X57198; M81601; X73534; AK290454; CR542221; BT019995; AC100821; BC072460 

Genbank Nucleotide ID

 CAA44470.1; CAA40484.1; AAA61138.1; CAA51940.1; BAF83143.1; CAG47017.1; AAV38798.1; AAH72460.1 

Protein Name

 Transcription elongation factor A protein 1 

Protein Synonyms/Alias

 Transcription elongation factor S-II protein 1; Transcription elongation factor TFIIS.o 

Gene Name

 TCEA1 

Gene Synonyms/Alias

 GTF2S; TFIIS 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
29	AGALDLLKELKNIPM	ubiquitination	[1, 2, 3]
67	EEVTSLAKSLIKSWK	ubiquitination	[1, 3, 4]
84	LDGPSTEKDLDEKKK	acetylation	[5]
199	RSRISNLKDAKNPNL	acetylation	[6]
242	EMRKNLTKEAIREHQ	ubiquitination	[4]
265	TDLFTCGKCKKKNCT	ubiquitination	[2, 7]

Reference

 [1] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [2] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [3] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [4] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [5] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [6] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [7] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724] 

Functional Description

 Necessary for efficient RNA polymerase II transcription elongation past template-encoded arresting sites. The arresting sites in DNA have the property of trapping a certain fraction of elongating RNA polymerases that pass through, resulting in locked ternary complexes. Cleavage of the nascent transcript by S-II allows the resumption of elongation from the new 3'-terminus. 

Sequence Annotation

 DOMAIN 3 80 TFIIS N-terminal.
 DOMAIN 140 256 TFIIS central.
 ZN_FING 259 299 TFIIS-type.
 MOD_RES 1 1 N-acetylmethionine.
 MOD_RES 97 97 Phosphoserine.
 MOD_RES 100 100 Phosphoserine.  

Keyword

 3D-structure; Acetylation; Alternative splicing; Chromosomal rearrangement; Complete proteome; Direct protein sequencing; DNA-binding; Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Transcription; Transcription regulation; Zinc; Zinc-finger. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 301 AA 

Protein Sequence

Gene Ontology

 GO:0005730; C:nucleolus; IDA:HPA.
 GO:0005654; C:nucleoplasm; TAS:Reactome.
 GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0030218; P:erythrocyte differentiation; IEA:Compara.
 GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IEA:Compara.
 GO:0050434; P:positive regulation of viral transcription; TAS:Reactome.
 GO:0032784; P:regulation of DNA-dependent transcription, elongation; IEA:InterPro.
 GO:0006368; P:transcription elongation from RNA polymerase II promoter; TAS:Reactome.
 GO:0006283; P:transcription-coupled nucleotide-excision repair; TAS:Reactome.
 GO:0022415; P:viral reproductive process; TAS:Reactome. 

Interpro

 IPR016492; TF_IIS-rel.
 IPR003617; TFIIS/CRSP70_N_sub.
 IPR003618; TFIIS_cen_dom.
 IPR017923; TFIIS_N.
 IPR017890; TFS2M.
 IPR006289; TFSII.
 IPR001222; Znf_TFIIS. 

Pfam

 PF08711; Med26
 PF01096; TFIIS_C
 PF07500; TFIIS_M 

SMART

 SM00510; TFS2M
 SM00509; TFS2N
 SM00440; ZnF_C2C2 

PROSITE

 PS51321; TFIIS_CENTRAL
 PS51319; TFIIS_N
 PS00466; ZF_TFIIS_1
 PS51133; ZF_TFIIS_2 

PRINTS