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Protein

Transcription elongation factor A protein 1

Gene

TCEA1

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

Functioni

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.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri259 – 29941TFIIS-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. DNA binding Source: UniProtKB-KW
  2. zinc ion binding Source: InterPro

GO - Biological processi

  1. DNA repair Source: Reactome
  2. erythrocyte differentiation Source: Ensembl
  3. gene expression Source: Reactome
  4. nucleotide-excision repair Source: Reactome
  5. positive regulation of transcription from RNA polymerase II promoter Source: Ensembl
  6. positive regulation of viral transcription Source: Reactome
  7. regulation of DNA-templated transcription, elongation Source: InterPro
  8. transcription-coupled nucleotide-excision repair Source: Reactome
  9. transcription elongation from RNA polymerase II promoter Source: Reactome
  10. transcription from RNA polymerase II promoter Source: Reactome
  11. viral process Source: Reactome
Complete GO annotation...

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_1845. Formation of RNA Pol II elongation complex.
REACT_1941. Formation of transcription-coupled NER (TC-NER) repair complex.
REACT_22107. RNA Polymerase II Pre-transcription Events.
REACT_22201. Formation of HIV elongation complex in the absence of HIV Tat.
REACT_2222. Dual incision reaction in TC-NER.
REACT_6143. Pausing and recovery of Tat-mediated HIV elongation.
REACT_6162. Tat-mediated elongation of the HIV-1 transcript.
REACT_6244. Pausing and recovery of HIV elongation.
REACT_6259. HIV elongation arrest and recovery.
REACT_6344. Tat-mediated HIV elongation arrest and recovery.
REACT_6346. Formation of HIV-1 elongation complex containing HIV-1 Tat.
REACT_833. RNA Polymerase II Transcription Elongation.

Names & Taxonomyi

Protein namesi
Recommended name:
Transcription elongation factor A protein 1
Alternative name(s):
Transcription elongation factor S-II protein 1
Transcription elongation factor TFIIS.o
Gene namesi
Name:TCEA1
Synonyms:GTF2S, TFIIS
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 8

Organism-specific databases

HGNCiHGNC:11612. TCEA1.

Subcellular locationi

GO - Cellular componenti

  1. nucleolus Source: HPA
  2. nucleoplasm Source: Reactome
  3. nucleus Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

A chromosomal aberration 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.

Organism-specific databases

PharmGKBiPA36371.

Polymorphism and mutation databases

DMDMi1174652.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 301301Transcription elongation factor A protein 1PRO_0000121446Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine3 Publications
Modified residuei97 – 971Phosphoserine2 Publications
Modified residuei100 – 1001Phosphoserine5 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP23193.
PaxDbiP23193.
PRIDEiP23193.

PTM databases

PhosphoSiteiP23193.

Miscellaneous databases

PMAP-CutDBP23193.

Expressioni

Gene expression databases

BgeeiP23193.
CleanExiHS_TCEA1.
ExpressionAtlasiP23193. baseline and differential.
GenevestigatoriP23193.

Organism-specific databases

HPAiHPA043786.

Interactioni

Subunit structurei

Interacts with EAF2 (By similarity). Associates with UBR5 and forms a transcription regulatory complex made of CDK9, RNAP II, UBR5 and TFIIS/TCEA1 that can stimulate target gene transcription (e.g. gamma fibrinogen/FGG) by recruiting their promoters.By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
LEO1Q8WVC04EBI-2608271,EBI-932432
PAF1Q8N7H54EBI-2608271,EBI-2607770

Protein-protein interaction databases

BioGridi112779. 52 interactions.
DIPiDIP-48480N.
IntActiP23193. 9 interactions.
MINTiMINT-3009864.
STRINGi9606.ENSP00000382541.

Structurei

Secondary structure

1
301
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi139 – 15113Combined sources
Helixi152 – 1565Combined sources
Helixi157 – 1615Combined sources
Helixi165 – 18016Combined sources
Beta strandi182 – 1843Combined sources
Helixi185 – 19814Combined sources
Helixi204 – 2118Combined sources
Helixi217 – 2226Combined sources
Turni225 – 2273Combined sources
Beta strandi264 – 2663Combined sources
Beta strandi271 – 2766Combined sources
Beta strandi278 – 2836Combined sources
Beta strandi286 – 2949Combined sources
Beta strandi297 – 2993Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1TFINMR-A252-301[»]
3NDQX-ray1.93A131-232[»]
ProteinModelPortaliP23193.
SMRiP23193. Positions 1-84, 132-301.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP23193.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini3 – 8078TFIIS N-terminalPROSITE-ProRule annotationAdd
BLAST
Domaini140 – 256117TFIIS centralPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the TFS-II family.Curated
Contains 1 TFIIS central domain.PROSITE-ProRule annotation
Contains 1 TFIIS N-terminal domain.PROSITE-ProRule annotation
Contains 1 TFIIS-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri259 – 29941TFIIS-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiCOG1594.
GeneTreeiENSGT00390000017794.
HOGENOMiHOG000195015.
HOVERGENiHBG055022.
InParanoidiP23193.
KOiK03145.
OMAiRAMISFW.
OrthoDBiEOG7GQXWQ.
PhylomeDBiP23193.
TreeFamiTF314970.

Family and domain databases

Gene3Di1.10.472.30. 1 hit.
1.20.930.10. 1 hit.
InterProiIPR016492. TF_IIS-rel.
IPR003617. TFIIS/CRSP70_N_sub.
IPR003618. TFIIS_cen_dom.
IPR017923. TFIIS_N.
IPR017890. TFS2M.
IPR006289. TFSII.
IPR001222. Znf_TFIIS.
[Graphical view]
PfamiPF08711. Med26. 1 hit.
PF01096. TFIIS_C. 1 hit.
PF07500. TFIIS_M. 1 hit.
[Graphical view]
PIRSFiPIRSF006704. TF_IIS. 1 hit.
SMARTiSM00510. TFS2M. 1 hit.
SM00509. TFS2N. 1 hit.
SM00440. ZnF_C2C2. 1 hit.
[Graphical view]
SUPFAMiSSF46942. SSF46942. 1 hit.
SSF47676. SSF47676. 1 hit.
TIGRFAMsiTIGR01385. TFSII. 1 hit.
PROSITEiPS51321. TFIIS_CENTRAL. 1 hit.
PS51319. TFIIS_N. 1 hit.
PS00466. ZF_TFIIS_1. 1 hit.
PS51133. ZF_TFIIS_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Note: Additional isoforms seem to exist.

Isoform 1 (identifier: P23193-1) [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
MEDEVVRFAK KMDKMVQKKN AAGALDLLKE LKNIPMTLEL LQSTRIGMSV
60 70 80 90 100
NAIRKQSTDE EVTSLAKSLI KSWKKLLDGP STEKDLDEKK KEPAITSQNS
110 120 130 140 150
PEAREESTSS GNVSNRKDET NARDTYVSSF PRAPSTSDSV RLKCREMLAA
160 170 180 190 200
ALRTGDDYIA IGADEEELGS QIEEAIYQEI RNTDMKYKNR VRSRISNLKD
210 220 230 240 250
AKNPNLRKNV LCGNIPPDLF ARMTAEEMAS DELKEMRKNL TKEAIREHQM
260 270 280 290 300
AKTGGTQTDL FTCGKCKKKN CTYTQVQTRS ADEPMTTFVV CNECGNRWKF

C
Length:301
Mass (Da):33,970
Last modified:November 1, 1995 - v2
Checksum:i8A685107A56D2DA1
GO
Isoform 2 (identifier: P23193-2) [UniParc]FASTAAdd to basket

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

Show »
Length:280
Mass (Da):31,664
Checksum:i31833641990136EF
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti127 – 1271V → L in AAA61138 (PubMed:1378807).Curated
Sequence conflicti141 – 1411R → Q in CAA51940 (PubMed:8112616).Curated
Sequence conflicti205 – 2051N → Y in CAA51940 (PubMed:8112616).Curated
Sequence conflicti237 – 2371R → W in CAA51940 (PubMed:8112616).Curated
Sequence conflicti285 – 2851M → V in CAA51940 (PubMed:8112616).Curated
Sequence conflicti300 – 3001F → I in AC100821 (Ref. 6) Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei22 – 4221Missing in isoform 2. 1 PublicationVSP_006409Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS47857.1. [P23193-2]
CCDS47858.1. [P23193-1]
PIRiS17361.
S26831.
S34159.
RefSeqiNP_006747.1. NM_006756.3. [P23193-1]
NP_958845.1. NM_201437.2. [P23193-2]
UniGeneiHs.491745.

Genome annotation databases

EnsembliENST00000396401; ENSP00000395483; ENSG00000187735. [P23193-2]
ENST00000521604; ENSP00000428426; ENSG00000187735. [P23193-1]
GeneIDi6917.
KEGGihsa:6917.
UCSCiuc003xru.3. human. [P23193-1]
uc003xrv.3. human. [P23193-2]

Keywords - Coding sequence diversityi

Alternative splicing, Chromosomal rearrangement

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS47857.1. [P23193-2]
CCDS47858.1. [P23193-1]
PIRiS17361.
S26831.
S34159.
RefSeqiNP_006747.1. NM_006756.3. [P23193-1]
NP_958845.1. NM_201437.2. [P23193-2]
UniGeneiHs.491745.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1TFINMR-A252-301[»]
3NDQX-ray1.93A131-232[»]
ProteinModelPortaliP23193.
SMRiP23193. Positions 1-84, 132-301.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112779. 52 interactions.
DIPiDIP-48480N.
IntActiP23193. 9 interactions.
MINTiMINT-3009864.
STRINGi9606.ENSP00000382541.

PTM databases

PhosphoSiteiP23193.

Polymorphism and mutation databases

DMDMi1174652.

Proteomic databases

MaxQBiP23193.
PaxDbiP23193.
PRIDEiP23193.

Protocols and materials databases

DNASUi6917.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000396401; ENSP00000395483; ENSG00000187735. [P23193-2]
ENST00000521604; ENSP00000428426; ENSG00000187735. [P23193-1]
GeneIDi6917.
KEGGihsa:6917.
UCSCiuc003xru.3. human. [P23193-1]
uc003xrv.3. human. [P23193-2]

Organism-specific databases

CTDi6917.
GeneCardsiGC08M054879.
H-InvDBHIX0057264.
HGNCiHGNC:11612. TCEA1.
HPAiHPA043786.
MIMi601425. gene.
neXtProtiNX_P23193.
PharmGKBiPA36371.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG1594.
GeneTreeiENSGT00390000017794.
HOGENOMiHOG000195015.
HOVERGENiHBG055022.
InParanoidiP23193.
KOiK03145.
OMAiRAMISFW.
OrthoDBiEOG7GQXWQ.
PhylomeDBiP23193.
TreeFamiTF314970.

Enzyme and pathway databases

ReactomeiREACT_1845. Formation of RNA Pol II elongation complex.
REACT_1941. Formation of transcription-coupled NER (TC-NER) repair complex.
REACT_22107. RNA Polymerase II Pre-transcription Events.
REACT_22201. Formation of HIV elongation complex in the absence of HIV Tat.
REACT_2222. Dual incision reaction in TC-NER.
REACT_6143. Pausing and recovery of Tat-mediated HIV elongation.
REACT_6162. Tat-mediated elongation of the HIV-1 transcript.
REACT_6244. Pausing and recovery of HIV elongation.
REACT_6259. HIV elongation arrest and recovery.
REACT_6344. Tat-mediated HIV elongation arrest and recovery.
REACT_6346. Formation of HIV-1 elongation complex containing HIV-1 Tat.
REACT_833. RNA Polymerase II Transcription Elongation.

Miscellaneous databases

EvolutionaryTraceiP23193.
GeneWikiiTCEA1.
GenomeRNAii6917.
NextBioi27057.
PMAP-CutDBP23193.
PROiP23193.
SOURCEiSearch...

Gene expression databases

BgeeiP23193.
CleanExiHS_TCEA1.
ExpressionAtlasiP23193. baseline and differential.
GenevestigatoriP23193.

Family and domain databases

Gene3Di1.10.472.30. 1 hit.
1.20.930.10. 1 hit.
InterProiIPR016492. TF_IIS-rel.
IPR003617. TFIIS/CRSP70_N_sub.
IPR003618. TFIIS_cen_dom.
IPR017923. TFIIS_N.
IPR017890. TFS2M.
IPR006289. TFSII.
IPR001222. Znf_TFIIS.
[Graphical view]
PfamiPF08711. Med26. 1 hit.
PF01096. TFIIS_C. 1 hit.
PF07500. TFIIS_M. 1 hit.
[Graphical view]
PIRSFiPIRSF006704. TF_IIS. 1 hit.
SMARTiSM00510. TFS2M. 1 hit.
SM00509. TFS2N. 1 hit.
SM00440. ZnF_C2C2. 1 hit.
[Graphical view]
SUPFAMiSSF46942. SSF46942. 1 hit.
SSF47676. SSF47676. 1 hit.
TIGRFAMsiTIGR01385. TFSII. 1 hit.
PROSITEiPS51321. TFIIS_CENTRAL. 1 hit.
PS51319. TFIIS_N. 1 hit.
PS00466. ZF_TFIIS_1. 1 hit.
PS51133. ZF_TFIIS_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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, IDENTIFICATION BY 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] [Europe PMC] [Abstract]
    Cited for: CHROMOSOMAL TRANSLOCATION WITH PLAG1.
  11. "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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-100, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. "Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment."
    Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.
    J. Proteome Res. 7:5167-5176(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: T-cell.
  13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-97 AND SER-100, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-100, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "Transcription factor IIS cooperates with the E3 ligase UBR5 to ubiquitinate the CDK9 subunit of the positive transcription elongation factor B."
    Cojocaru M., Bouchard A., Cloutier P., Cooper J.J., Varzavand K., Price D.H., Coulombe B.
    J. Biol. Chem. 286:5012-5022(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH UBR5 AND CDK9.
  18. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-97 AND SER-100, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  20. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-100, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  21. "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] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 256-301.

Entry informationi

Entry nameiTCEA1_HUMAN
AccessioniPrimary (citable) accession number: P23193
Secondary accession number(s): A6NF25
, A8K339, Q15563, Q6FG87
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: November 1, 1995
Last modified: April 1, 2015
This is version 162 of the entry and version 2 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

Miscellaneous

S-II binds to RNA-polymerase II in the absence of transcription.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 8
    Human chromosome 8: 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

External Data

Dasty 3

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 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.