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Protein

Transcription elongation factor B polypeptide 3

Gene

Tceb3

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

SIII, also known as elongin, is a general transcription elongation factor that increases the RNA polymerase II transcription elongation past template-encoded arresting sites. Subunit A is transcriptionally active and its transcription activity is strongly enhanced by binding to the dimeric complex of the SIII regulatory subunits B and C (elongin BC complex) (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Transcription, Transcription regulation

Enzyme and pathway databases

ReactomeiR-MMU-112382. Formation of RNA Pol II elongation complex.
R-MMU-674695. RNA Polymerase II Pre-transcription Events.
R-MMU-6796648. TP53 Regulates Transcription of DNA Repair Genes.
R-MMU-75955. RNA Polymerase II Transcription Elongation.

Names & Taxonomyi

Protein namesi
Recommended name:
Transcription elongation factor B polypeptide 3
Alternative name(s):
Elongin 110 kDa subunit
Elongin-A
Short name:
EloA
RNA polymerase II transcription factor SIII subunit A1
SIII p110
Gene namesi
Name:Tceb3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 4

Organism-specific databases

MGIiMGI:1351315. Tceb3.

Subcellular locationi

  • Nucleus PROSITE-ProRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 773773Transcription elongation factor B polypeptide 3PRO_0000086961Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei82 – 821PhosphoserineCombined sources
Modified residuei195 – 1951PhosphoserineBy similarity
Modified residuei309 – 3091PhosphoserineCombined sources
Modified residuei379 – 3791PhosphoserineBy similarity
Modified residuei390 – 3901PhosphothreonineCombined sources
Modified residuei430 – 4301N6-acetyllysineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ8CB77.
MaxQBiQ8CB77.
PaxDbiQ8CB77.
PRIDEiQ8CB77.

PTM databases

iPTMnetiQ8CB77.
PhosphoSiteiQ8CB77.

Expressioni

Gene expression databases

BgeeiQ8CB77.
GenevisibleiQ8CB77. MM.

Interactioni

Subunit structurei

Heterotrimer of an A (A1, A2 or A3), B and C subunit.By similarity

Protein-protein interaction databases

BioGridi205145. 3 interactions.
IntActiQ8CB77. 3 interactions.
MINTiMINT-4094290.
STRINGi10090.ENSMUSP00000030427.

Structurei

3D structure databases

ProteinModelPortaliQ8CB77.
SMRiQ8CB77. Positions 573-646.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini4 – 7976TFIIS N-terminalPROSITE-ProRule annotationAdd
BLAST
Domaini565 – 60945F-boxPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni521 – 680160Activation domainBy similarityAdd
BLAST
Regioni549 – 55810Interacting with Elongin BC complexBy similarity

Domaini

The elongin BC complex binding domain is also known as BC-box with the consensus [APST]-L-x(3)-C-x(3)-[AILV].

Sequence similaritiesi

Contains 1 F-box domain.PROSITE-ProRule annotation
Contains 1 TFIIS N-terminal domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG2821. Eukaryota.
ENOG4110PG3. LUCA.
GeneTreeiENSGT00390000002428.
HOGENOMiHOG000059565.
HOVERGENiHBG051467.
InParanoidiQ8CB77.
KOiK15076.
OMAiPHKVSHS.
OrthoDBiEOG7P2XSR.
TreeFamiTF317259.

Family and domain databases

Gene3Di1.20.930.10. 1 hit.
InterProiIPR001810. F-box_dom.
IPR010684. RNA_pol_II_trans_fac_SIII_A.
IPR003617. TFIIS/CRSP70_N_sub.
IPR017923. TFIIS_N.
[Graphical view]
PfamiPF06881. Elongin_A. 1 hit.
PF08711. Med26. 1 hit.
[Graphical view]
SMARTiSM00509. TFS2N. 1 hit.
[Graphical view]
SUPFAMiSSF47676. SSF47676. 1 hit.
PROSITEiPS50181. FBOX. 1 hit.
PS51319. TFIIS_N. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8CB77-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAESALQVV EKLQARLAAN PDPKKLLKYL KKLSILPITV DILVETGVGK
60 70 80 90 100
TVNSFRKHEQ VGNFARDLVA QWKKLVPVER NSEAEDQDFE KNNSRKRPRD
110 120 130 140 150
ALQREEELEG NYQESWKPSG SRSYSPEHRQ KKHKKLSEPE RPHKVAHSHE
160 170 180 190 200
KRDERKRCHK VSPPYSSDPE SSDYGHVQSP PPSSPHQMYT DLSRSPEEDQ
210 220 230 240 250
EPIISHQKPG KVHSNTFQDR LGVSHLGEQG KGAVSHHKQH RSSHKEKHPA
260 270 280 290 300
DAREDEKISA VSREKSHKAS SKEESRRLLS GDSAKEKLPS SVVKKDKDRE
310 320 330 340 350
GSSLKKKFSP ALDVASDNHF KKPKHKDSEK AKSDKNKQSV DGVDSGRGTG
360 370 380 390 400
DPLPKAKEKV PNHLKAQEGK VRTNADGKSA GPLHPKAEET DVDDEFERPT
410 420 430 440 450
MSFESYLSYD QPRKKKKKVV KTSSTALGEK GLKKKDSKST SKNLNSAQKL
460 470 480 490 500
PKVNENKSEK LQPAGAEPTR PRKVPTDVLP ALPDIPLPAI HANYRPLPSL
510 520 530 540 550
ELIPSFQPKR KAFSSPQEEE EAGFTGRRMN SKMQVYSGSK CAYLPKMMTL
560 570 580 590 600
HQQCIRVLKN NIDSIFEVGG VPYSVLEPVL ERCTPDQLYR IEECNHVLIE
610 620 630 640 650
ETDQLWKVHC HRDFKEERPE EYESWREMYL RLQDAREQRL RLLTNNIRSA
660 670 680 690 700
HANKPKGRQA KMAFVNSVAK PPRDVRRRQE KFGTGGAAVP EKVRIKPAPY
710 720 730 740 750
TTGSSHVPAS NSSSNFHSSP EELAYDGPST SSAHLAPVAS SSVSYDPRKP
760 770
AVKKIAPMMA KTIKAFKNRF SRR
Length:773
Mass (Da):87,161
Last modified:July 27, 2011 - v3
Checksum:i7F5B33C4B6E87561
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti35 – 351I → V in BAA84994 (PubMed:10575222).Curated
Sequence conflicti142 – 1421P → R in BAA84994 (PubMed:10575222).Curated
Sequence conflicti159 – 1591H → Q in BAA84994 (PubMed:10575222).Curated
Sequence conflicti236 – 2361H → Q in BAA84994 (PubMed:10575222).Curated
Sequence conflicti382 – 3821P → L in BAA84994 (PubMed:10575222).Curated
Sequence conflicti382 – 3821P → L in AAH49885 (PubMed:15489334).Curated
Sequence conflicti609 – 6091H → P in BAA84994 (PubMed:10575222).Curated
Sequence conflicti625 – 6262WR → LE in BAA84994 (PubMed:10575222).Curated
Sequence conflicti633 – 6353QDA → SER in BAA84994 (PubMed:10575222).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB025015 mRNA. Translation: BAA84994.1.
AK036592 mRNA. Translation: BAC29497.1.
AK145994 mRNA. Translation: BAE26815.1.
AK147088 mRNA. Translation: BAE27668.1.
AL672076 Genomic DNA. Translation: CAM15908.1.
CH466552 Genomic DNA. Translation: EDL29954.1.
BC049885 mRNA. Translation: AAH49885.1.
CCDSiCCDS18798.1.
RefSeqiNP_038764.2. NM_013736.4.
UniGeneiMm.27663.

Genome annotation databases

EnsembliENSMUST00000030427; ENSMUSP00000030427; ENSMUSG00000028668.
GeneIDi27224.
KEGGimmu:27224.
UCSCiuc008vhp.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB025015 mRNA. Translation: BAA84994.1.
AK036592 mRNA. Translation: BAC29497.1.
AK145994 mRNA. Translation: BAE26815.1.
AK147088 mRNA. Translation: BAE27668.1.
AL672076 Genomic DNA. Translation: CAM15908.1.
CH466552 Genomic DNA. Translation: EDL29954.1.
BC049885 mRNA. Translation: AAH49885.1.
CCDSiCCDS18798.1.
RefSeqiNP_038764.2. NM_013736.4.
UniGeneiMm.27663.

3D structure databases

ProteinModelPortaliQ8CB77.
SMRiQ8CB77. Positions 573-646.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi205145. 3 interactions.
IntActiQ8CB77. 3 interactions.
MINTiMINT-4094290.
STRINGi10090.ENSMUSP00000030427.

PTM databases

iPTMnetiQ8CB77.
PhosphoSiteiQ8CB77.

Proteomic databases

EPDiQ8CB77.
MaxQBiQ8CB77.
PaxDbiQ8CB77.
PRIDEiQ8CB77.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000030427; ENSMUSP00000030427; ENSMUSG00000028668.
GeneIDi27224.
KEGGimmu:27224.
UCSCiuc008vhp.1. mouse.

Organism-specific databases

CTDi6924.
MGIiMGI:1351315. Tceb3.

Phylogenomic databases

eggNOGiKOG2821. Eukaryota.
ENOG4110PG3. LUCA.
GeneTreeiENSGT00390000002428.
HOGENOMiHOG000059565.
HOVERGENiHBG051467.
InParanoidiQ8CB77.
KOiK15076.
OMAiPHKVSHS.
OrthoDBiEOG7P2XSR.
TreeFamiTF317259.

Enzyme and pathway databases

ReactomeiR-MMU-112382. Formation of RNA Pol II elongation complex.
R-MMU-674695. RNA Polymerase II Pre-transcription Events.
R-MMU-6796648. TP53 Regulates Transcription of DNA Repair Genes.
R-MMU-75955. RNA Polymerase II Transcription Elongation.

Miscellaneous databases

PROiQ8CB77.
SOURCEiSearch...

Gene expression databases

BgeeiQ8CB77.
GenevisibleiQ8CB77. MM.

Family and domain databases

Gene3Di1.20.930.10. 1 hit.
InterProiIPR001810. F-box_dom.
IPR010684. RNA_pol_II_trans_fac_SIII_A.
IPR003617. TFIIS/CRSP70_N_sub.
IPR017923. TFIIS_N.
[Graphical view]
PfamiPF06881. Elongin_A. 1 hit.
PF08711. Med26. 1 hit.
[Graphical view]
SMARTiSM00509. TFS2N. 1 hit.
[Graphical view]
SUPFAMiSSF47676. SSF47676. 1 hit.
PROSITEiPS50181. FBOX. 1 hit.
PS51319. TFIIS_N. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Structural organization and chromosome location of the mouse elongin A gene (Tceb3)."
    Aso T., Amimoto K., Takebayashi S., Okumura K., Hatakeyama M.
    Cytogenet. Cell Genet. 86:259-262(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "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: Bone and Placenta.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  4. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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].
    Strain: FVB/N.
    Tissue: Mammary tumor.
  6. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82; SER-309 AND THR-390, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  8. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-430, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiELOA1_MOUSE
AccessioniPrimary (citable) accession number: Q8CB77
Secondary accession number(s): Q3UI38, Q80VB2, Q9R0Q5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 11, 2003
Last sequence update: July 27, 2011
Last modified: June 8, 2016
This is version 126 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

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.