Reviewed, UniProtKB/Swiss-Prot P23193 (TCEA1_HUMAN)

Names and origin

Protein names

Recommended name:
    Transcription elongation factor A protein 1
Alternative name(s):
    Transcription elongation factor S-II protein 1
    Transcription elongation factor TFIIS.o

Gene names

Name:	TCEA1
Synonyms:	GTF2S, TFIIS

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	301 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	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.
Subunit structure	Interacts with EAF2 By similarity.
Subcellular location	Nucleus.
Post-translational modification	Phosphorylated upon DNA damage, probably by ATM or ATR. Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17
Involvement in disease	A chromosomal rearrangement involving TCEA1 may be a cause of salivary gland pleiomorphic adenomas (PA) [181030]. Pleiomorphic adenomas are the most common benign epithelial tumors of the salivary gland. Translocation t(3;8)(p21;q12) with PLAG1.
Miscellaneous	S-II binds to RNA-polymerase II in the absence of transcription.
Sequence similarities	Belongs to the TFS-II family. Contains 1 TFIIS central domain. Contains 1 TFIIS N-terminal domain. Contains 1 TFIIS-type zinc finger.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Chromosomal rearrangement
Domain	Zinc-finger
Ligand	DNA-binding Metal-binding Zinc
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	RNA elongation Inferred from electronic annotation. Source: InterPro transcription from RNA polymerase II promoter Ref.1 Traceable author statement. Source: ProtInc
Cellular component	nucleoplasm Inferred from Experiment. Source: Reactome
Molecular function	DNA binding Inferred from electronic annotation. Source: UniProtKB-KW general RNA polymerase II transcription factor activity Ref.1 Traceable author statement. Source: ProtInc transcription elongation regulator activity Inferred from electronic annotation. Source: InterPro translation elongation factor activity Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.

Isoform 1 (identifier: P23193-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: P23193-2)

The sequence of this isoform differs from the canonical sequence as follows:
     22-42: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 301

301

Transcription elongation factor A protein 1

PRO_0000121446

Regions

Domain

3 – 80

78

TFIIS N-terminal

Domain

140 – 256

117

TFIIS central

Zinc finger

259 – 299

41

TFIIS-type

Amino acid modifications

Modified residue

1

1

N-acetylmethionine Ref.8

Modified residue

81

1

Phosphoserine Ref.14

Modified residue

97

1

Phosphoserine Ref.15 Ref.16 Ref.17

Modified residue

100

1

Phosphoserine Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.17

Modified residue

108

1

Phosphothreonine Ref.14

Modified residue

110

1

Phosphoserine Ref.14

Modified residue

126

1

Phosphotyrosine Ref.14

Natural variations

Alternative sequence

22 – 42

21

Missing in isoform 2.

VSP_006409

Experimental info

Sequence conflict

127

1

V → L in AAA61138. Ref.2

Sequence conflict

141

1

R → Q in CAA51940. Ref.3

Sequence conflict

205

1

N → Y in CAA51940. Ref.3

Sequence conflict

237

1

R → W in CAA51940. Ref.3

Sequence conflict

285

1

M → V in CAA51940. Ref.3

Sequence conflict

300

1

F → I in AC100821. Ref.6

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

301

Helix Strand Turn

Details...

Beta strand

264 – 266

3

Beta strand

271 – 276

6

Beta strand

278 – 283

6

Beta strand

286 – 294

9

Beta strand

297 – 299

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 1, 1995. Version 2. Checksum: 8A685107A56D2DA1	FASTA	301	33,970
	10 20 30 40 50 60 MEDEVVRFAK KMDKMVQKKN AAGALDLLKE LKNIPMTLEL LQSTRIGMSV NAIRKQSTDE 70 80 90 100 110 120 EVTSLAKSLI KSWKKLLDGP STEKDLDEKK KEPAITSQNS PEAREESTSS GNVSNRKDET 130 140 150 160 170 180 NARDTYVSSF PRAPSTSDSV RLKCREMLAA ALRTGDDYIA IGADEEELGS QIEEAIYQEI 190 200 210 220 230 240 RNTDMKYKNR VRSRISNLKD AKNPNLRKNV LCGNIPPDLF ARMTAEEMAS DELKEMRKNL 250 260 270 280 290 300 TKEAIREHQM AKTGGTQTDL FTCGKCKKKN CTYTQVQTRS ADEPMTTFVV CNECGNRWKF C
	Isoform 2. Checksum: 31833641990136EF	FASTA	280	31,664
	10 20 30 40 50 60 MEDEVVRFAK KMDKMVQKKN ASTRIGMSVN AIRKQSTDEE VTSLAKSLIK SWKKLLDGPS 70 80 90 100 110 120 TEKDLDEKKK EPAITSQNSP EAREESTSSG NVSNRKDETN ARDTYVSSFP RAPSTSDSVR 130 140 150 160 170 180 LKCREMLAAA LRTGDDYIAI GADEEELGSQ IEEAIYQEIR NTDMKYKNRV RSRISNLKDA 190 200 210 220 230 240 KNPNLRKNVL CGNIPPDLFA RMTAEEMASD ELKEMRKNLT KEAIREHQMA KTGGTQTDLF 250 260 270 280 TCGKCKKKNC TYTQVQTRSA DEPMTTFVVC NECGNRWKFC

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning, expression and characterization of the human transcription elongation factor, TFIIS." Yoo O., Yoon H., Baek K., Jeon C., Miyamoto K., Ueno A., Agarwal K. Nucleic Acids Res. 19:1073-1079(1991) [PubMed: 1708494] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2). Tissue: Kidney.
[2]	"Characterization of a HeLa cDNA clone encoding the human SII protein, an elongation factor for RNA polymerase II." Chen H.C., England L., Kane C.M. Gene 116:253-258(1992) [PubMed: 1378807] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]	"Characterization of the gene encoding the human transcriptional elongation factor TFIIS." Park H.R., Baek K.H., Jeon C.J., Agarwal K., Yoo O. Gene 139:263-267(1994) [PubMed: 8112616] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Tissue: Placenta.
[4]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Brain.
[5]	"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J. Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[6]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A. Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[7]	"DNA sequence and analysis of human chromosome 8." Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T. , Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., Lander E.S. Nature 439:331-335(2006) [PubMed: 16421571] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Uterus.
[9]	Bienvenut W.V., Kanor S., Tissot J.-D., Quadroni M. Submitted (MAY-2006) to UniProtKB Cited for: PROTEIN SEQUENCE OF 1-9 AND 32-44, ACETYLATION AT MET-1, MASS SPECTROMETRY. Tissue: T-cell.
[10]	"Conserved mechanism of PLAG1 activation in salivary gland tumors with and without chromosome 8q12 abnormalities: identification of SII as a new fusion partner gene." Astroem A.-K., Voz M.L., Kas K., Roeijer E., Wedell B., Mandahl N., Van de Ven W., Mark J., Stenman G. Cancer Res. 59:918-923(1999) [PubMed: 10029085] [Abstract] Cited for: CHROMOSOMAL TRANSLOCATION WITH PLAG1.
[11]	"Large-scale characterization of HeLa cell nuclear phosphoproteins." Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-100, MASS SPECTROMETRY. Tissue: Epithelium.
[12]	"Global phosphoproteome of HT-29 human colon adenocarcinoma cells." Kim J.-E., Tannenbaum S.R., White F.M. J. Proteome Res. 4:1339-1346(2005) [PubMed: 16083285] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-100, MASS SPECTROMETRY.
[13]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-100, MASS SPECTROMETRY. Tissue: Epithelium.
[14]	"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry." Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A. Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-81; SER-100; THR-108; SER-110 AND TYR-126, MASS SPECTROMETRY.
[15]	"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage." Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J. Science 316:1160-1166(2007) [PubMed: 17525332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-97 AND SER-100, MASS SPECTROMETRY.
[16]	"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column." Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y. Anal. Sci. 24:161-166(2008) [PubMed: 18187866] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-97, MASS SPECTROMETRY.
[17]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-97 AND SER-100, MASS SPECTROMETRY.
[18]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[19]	"Structure of a new nucleic-acid-binding motif in eukaryotic transcriptional elongation factor TFIIS." Qian X., Jeon C., Yoon H., Agarwal K., Weiss M.A. Nature 365:277-279(1993) [PubMed: 7626141] [Abstract] Cited for: STRUCTURE BY NMR OF 256-301.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

X62585 mRNA. Translation: CAA44470.1.
X57198 mRNA. Translation: CAA40484.1.
M81601 mRNA. Translation: AAA61138.1.
X73534 Genomic DNA. Translation: CAA51940.1.
AK290454 mRNA. Translation: BAF83143.1.
CR542221 mRNA. Translation: CAG47017.1.
BT019995 mRNA. Translation: AAV38798.1.
AC100821 Genomic DNA. No translation available.
BC072460 mRNA. Translation: AAH72460.1.

IPI

IPI00218106.
IPI00333215.

PIR

S17361.
S26831.
S34159.

RefSeq

NP_006747.1.
NP_958845.1.

UniGene

Hs.491745

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1TFI	NMR	-	A	252-301	[»]

ModBase

Search...

PTM databases

PhosphoSite

P23193.

Proteomic databases

PRIDE

P23193.

Genome annotation databases

Ensembl

ENSG00000187735. Homo sapiens. [Contig view]

GeneID

6917.

KEGG

hsa:6917.

Organism-specific databases

GeneCards

GC08M055041.

H-InvDB

HIX0025573.
HIX0057264.

HGNC

HGNC:11612. TCEA1.

MIM

601425. gene.

PharmGKB

PA36371.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

P23193.

HOVERGEN

P23193.

Enzyme and pathway databases

Reactome

REACT_1788. Transcription.
REACT_1892. Elongation arrest and recovery.
REACT_216. DNA Repair.
REACT_6143. Pausing and recovery of Tat-mediated HIV-1 elongation.
REACT_6185. HIV Infection.
REACT_6244. Pausing and recovery of HIV-1 elongation.
REACT_6259. HIV-1 elongation arrest and recovery.
REACT_6344. Tat-mediated HIV-1 elongation arrest and recovery.
REACT_71. Gene Expression.
REACT_769. Pausing and recovery of elongation.

Gene expression databases

Bgee

P23193.

CleanEx

HS_TCEA1.

GermOnline

ENSG00000197214. Homo sapiens.

Family and domain databases

InterPro

IPR016492. TF_IIS.
IPR014765. TFIIS/CRSP70_N.
IPR003617. TFIIS/CRSP70_N_sub.
IPR010990. TFIIS/elonginA/CRSP70_N.
IPR003618. TFIIS_centre.
IPR017923. TFIIS_N.
IPR017890. TFS2M.
IPR006289. TFSII.
IPR001222. Znf_TFIIS.
[Graphical view]

Gene3D

G3DSA:1.25.40.260. TFIIS/CRSP70_N. 1 hit.
G3DSA:1.10.472.30. TFIIS_centre. 1 hit.

Pfam

PF08711. TFIIS. 1 hit.
PF01096. TFIIS_C. 1 hit.
PF07500. TFIIS_M. 1 hit.
[Graphical view]

PIRSF

PIRSF006704. TF_IIS. 1 hit.

SMART

SM00510. TFS2M. 1 hit.
SM00509. TFS2N. 1 hit.
SM00440. ZnF_C2C2. 1 hit.
[Graphical view]

TIGRFAMs

TIGR01385. TFSII. 1 hit.

PROSITE

PS51321. TFIIS_CENTRAL. 1 hit.
PS51319. TFIIS_N. 1 hit.
PS00466. ZF_TFIIS_1. 1 hit.
PS51133. ZF_TFIIS_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

27057.

PMAP-CutDB

P23193.

SOURCE

Search...

Entry information

Entry name

TCEA1_HUMAN

Accession

Primary (citable) accession number: P23193
Secondary accession number(s): A6NF25 , A8K339, Q15563, Q6FG87

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1991
Last sequence update:	November 1, 1995
Last modified:	June 16, 2009
This is version 101 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)