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Protein

Transcription elongation factor A protein 3

Gene

Tcea3

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 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 fingeri305 – 34541TFIIS-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Transcription elongation factor A protein 3
Alternative name(s):
Transcription elongation factor S-II protein 3
Transcription elongation factor TFIIS.h
Gene namesi
Name:Tcea3
Synonyms:Tfiish
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 4

Organism-specific databases

MGIiMGI:1196908. Tcea3.

Subcellular locationi

GO - Cellular componenti

  • nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 347347Transcription elongation factor A protein 3PRO_0000121453Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei113 – 1131PhosphoserineCombined sources
Modified residuei139 – 1391PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP23881.
PaxDbiP23881.
PeptideAtlasiP23881.
PRIDEiP23881.

PTM databases

iPTMnetiP23881.
PhosphoSiteiP23881.

Expressioni

Tissue specificityi

Liver, kidney and heart.

Gene expression databases

BgeeiP23881.
CleanExiMM_TCEA3.
ExpressionAtlasiP23881. baseline and differential.
GenevisibleiP23881. MM.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000099592.

Structurei

Secondary structure

1
347
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 1916Combined sources
Helixi26 – 349Combined sources
Helixi40 – 456Combined sources
Helixi48 – 5811Combined sources
Helixi63 – 7816Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WJTNMR-A1-90[»]
ProteinModelPortaliP23881.
SMRiP23881. Positions 3-90, 182-347.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP23881.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini5 – 8278TFIIS N-terminalPROSITE-ProRule annotationAdd
BLAST
Domaini186 – 302117TFIIS 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 fingeri305 – 34541TFIIS-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG1105. Eukaryota.
COG1594. LUCA.
GeneTreeiENSGT00390000017794.
HOGENOMiHOG000195015.
HOVERGENiHBG055022.
InParanoidiP23881.
OMAiFAPSMCL.
OrthoDBiEOG7GQXWQ.
PhylomeDBiP23881.
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.
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]

Sequencei

Sequence statusi: Complete.

P23881-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGLEEELLRI AKKLEKMVSR KKTEGALDLL KKLNSCQMSI QLLQTTRIGV
60 70 80 90 100
AVNGVRKHCS DKEVVSLAKV LIKNWKRLLD SPRTTKGERE EREKAKKEKG
110 120 130 140 150
LGCSDWKPEA GLSPPRKKGG GEPKTRRDSV DSRSSTTSSP KRPSLERSNS
160 170 180 190 200
SKSKVETPTT PSSPSTPTFA PAVCLLAPCY LTGDSVRDKC VEMLSAALKA
210 220 230 240 250
EDNFKDYGVN CDKLASEIED HIYQELKSTD MKYRNRVRSR ISNLKDPRNP
260 270 280 290 300
GLRRNVLSGA ISPELIAKMT AEEMASDELR ELRNAMTQEA IREHQMAKTG
310 320 330 340
GTTTDLLRCS KCKKKNCTYN QVQTRSADEP MTTFVLCNEC GNRWKFC
Length:347
Mass (Da):38,850
Last modified:February 12, 2003 - v3
Checksum:iA1711D4C5DAF8CC8
GO

Sequence cautioni

The sequence BAA28177.1 differs from that shown.Chimeric cDNA. The sequence from position 1 to 95 is due to a chimeric cDNA.Curated
The sequence BAB31514.2 differs from that shown. Reason: Erroneous translation. Wrong choice of frame.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti7 – 71L → P in BAB25037 (PubMed:16141072).Curated
Sequence conflicti63 – 642EV → VL in BAB25037 (PubMed:16141072).Curated
Sequence conflicti96 – 994KKEK → RREE in BAB25037 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D00926 mRNA. Translation: BAA28177.1. Sequence problems.
AJ223472 mRNA. Translation: CAA11392.1.
AK002319 mRNA. Translation: BAB22010.1.
AK007437 mRNA. Translation: BAB25037.1.
AK019024 mRNA. Translation: BAB31514.2. Sequence problems.
AL935264 Genomic DNA. Translation: CAM13835.1.
BC010807 mRNA. Translation: AAH10807.1.
CCDSiCCDS18803.1.
RefSeqiNP_035672.1. NM_011542.2.
UniGeneiMm.112.

Genome annotation databases

EnsembliENSMUST00000102533; ENSMUSP00000099592; ENSMUSG00000001604.
GeneIDi21401.
KEGGimmu:21401.
UCSCiuc008vhv.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D00926 mRNA. Translation: BAA28177.1. Sequence problems.
AJ223472 mRNA. Translation: CAA11392.1.
AK002319 mRNA. Translation: BAB22010.1.
AK007437 mRNA. Translation: BAB25037.1.
AK019024 mRNA. Translation: BAB31514.2. Sequence problems.
AL935264 Genomic DNA. Translation: CAM13835.1.
BC010807 mRNA. Translation: AAH10807.1.
CCDSiCCDS18803.1.
RefSeqiNP_035672.1. NM_011542.2.
UniGeneiMm.112.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WJTNMR-A1-90[»]
ProteinModelPortaliP23881.
SMRiP23881. Positions 3-90, 182-347.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000099592.

PTM databases

iPTMnetiP23881.
PhosphoSiteiP23881.

Proteomic databases

MaxQBiP23881.
PaxDbiP23881.
PeptideAtlasiP23881.
PRIDEiP23881.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000102533; ENSMUSP00000099592; ENSMUSG00000001604.
GeneIDi21401.
KEGGimmu:21401.
UCSCiuc008vhv.2. mouse.

Organism-specific databases

CTDi6920.
MGIiMGI:1196908. Tcea3.

Phylogenomic databases

eggNOGiKOG1105. Eukaryota.
COG1594. LUCA.
GeneTreeiENSGT00390000017794.
HOGENOMiHOG000195015.
HOVERGENiHBG055022.
InParanoidiP23881.
OMAiFAPSMCL.
OrthoDBiEOG7GQXWQ.
PhylomeDBiP23881.
TreeFamiTF314970.

Miscellaneous databases

ChiTaRSiTcea3. mouse.
EvolutionaryTraceiP23881.
PROiP23881.
SOURCEiSearch...

Gene expression databases

BgeeiP23881.
CleanExiMM_TCEA3.
ExpressionAtlasiP23881. baseline and differential.
GenevisibleiP23881. MM.

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.
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. "Heterogeneity and tissue-specific expression of eukaryotic transcription factor S-II-related protein mRNA."
    Kanai A., Kuzuhara T., Sekimizu K., Natori S.
    J. Biochem. 109:674-677(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Liver.
  2. Hirashima S., Hirai H., Nakanishi Y., Natori S.
    Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Identification of novel genes encoding transcription elongation factor TFIIS (TCEA) in vertebrates: conservation of three distinct TFIIS isoforms in frog, mouse, and human."
    Labhart P., Morgan G.T.
    Genomics 52:278-288(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Fetus.
  4. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Kidney and Pancreas.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  6. "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].
    Tissue: Kidney.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Kidney and Pancreas.
  8. "Solution structure of the N-terminal domain I of mouse transcription elongation factor S-II protein 3."
    RIKEN structural genomics initiative (RSGI)
    Submitted (NOV-2004) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 1-90.

Entry informationi

Entry nameiTCEA3_MOUSE
AccessioniPrimary (citable) accession number: P23881
Secondary accession number(s): A2AW46
, O88710, Q9CTZ8, Q9DCZ5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: February 12, 2003
Last modified: July 6, 2016
This is version 140 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

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