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Protein

DNA-directed RNA polymerases I, II, and III subunit RPABC5

Gene

Polr2l

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

Functioni

DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Common component of RNA polymerases I, II and III which synthesize ribosomal RNA precursors, mRNA precursors and many functional non-coding RNAs, and a small RNAs, such as 5S rRNA and tRNAs, respectively. Pol II is the central component of the basal RNA polymerase II transcription machinery. Pols are composed of mobile elements that move relative to each other. In Pol II, POLR2L/RBP10 is part of the core element with the central large cleft (By similarity).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi7 – 71ZincBy similarity
Metal bindingi10 – 101ZincBy similarity
Metal bindingi44 – 441ZincBy similarity
Metal bindingi45 – 451ZincBy similarity

GO - Molecular functioni

  1. DNA binding Source: InterPro
  2. DNA-directed RNA polymerase activity Source: UniProtKB-KW
  3. zinc ion binding Source: GO_Central

GO - Biological processi

  1. transcription from RNA polymerase III promoter Source: GOC
  2. transcription from RNA polymerase II promoter Source: UniProtKB
  3. transcription from RNA polymerase I promoter Source: GOC
Complete GO annotation...

Keywords - Biological processi

Transcription

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_203462. Formation of the Early Elongation Complex.
REACT_205207. RNA Polymerase III Chain Elongation.
REACT_213655. Transcription-coupled NER (TC-NER).
REACT_221403. RNA Polymerase III Transcription Termination.
REACT_223654. Formation of transcription-coupled NER (TC-NER) repair complex.
REACT_224562. Dual incision reaction in TC-NER.
REACT_226490. RNA Polymerase II Transcription Elongation.
REACT_230204. RNA Polymerase II Transcription Initiation And Promoter Clearance.
REACT_232235. RNA Polymerase I Promoter Escape.
REACT_232708. RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
REACT_233950. Processing of Capped Intron-Containing Pre-mRNA.
REACT_235610. mRNA Splicing - Minor Pathway.
REACT_235780. RNA Polymerase I Transcription Initiation.
REACT_240508. RNA Polymerase III Transcription Initiation From Type 3 Promoter.
REACT_244380. RNA Polymerase II Transcription Initiation.
REACT_250309. RNA Polymerase III Transcription Initiation From Type 1 Promoter.
REACT_251592. RNA Polymerase III Transcription Initiation From Type 2 Promoter.
REACT_255009. RNA Polymerase II Pre-transcription Events.
REACT_255334. RNA Polymerase II Promoter Escape.
REACT_257165. RNA Polymerase I Transcription Termination.
REACT_257596. RNA Pol II CTD phosphorylation and interaction with CE.
REACT_258231. mRNA Capping.
REACT_259097. RNA Polymerase I Chain Elongation.
REACT_260226. mRNA Splicing - Major Pathway.
REACT_261233. RNA Polymerase III Abortive And Retractive Initiation.
REACT_270446. Transcriptional regulation by small RNAs.

Names & Taxonomyi

Protein namesi
Recommended name:
DNA-directed RNA polymerases I, II, and III subunit RPABC5
Short name:
RNA polymerases I, II, and III subunit ABC5
Alternative name(s):
DNA-directed RNA polymerase III subunit L
RPB10 homolog
Gene namesi
Name:Polr2l
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 7

Organism-specific databases

MGIiMGI:1913741. Polr2l.

Subcellular locationi

Nucleus By similarity

GO - Cellular componenti

  1. DNA-directed RNA polymerase I complex Source: GO_Central
  2. DNA-directed RNA polymerase II, core complex Source: UniProtKB
  3. DNA-directed RNA polymerase III complex Source: GO_Central
  4. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

DNA-directed RNA polymerase, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 6767DNA-directed RNA polymerases I, II, and III subunit RPABC5PRO_0000121334Add
BLAST

Proteomic databases

MaxQBiP62876.
PaxDbiP62876.
PRIDEiP62876.

PTM databases

PhosphoSiteiP62876.

Expressioni

Gene expression databases

BgeeiP62876.
CleanExiMM_POLR2L.
GenevestigatoriP62876.

Interactioni

Subunit structurei

Component of the RNA polymerase I (Pol I), RNA polymerase II (Pol II) and RNA polymerase III (Pol III) complexes consisting of at least 13, 12 and 17 subunits, respectively.By similarity

Protein-protein interaction databases

IntActiP62876. 2 interactions.
MINTiMINT-4133017.
STRINGi10090.ENSMUSP00000043204.

Structurei

3D structure databases

ProteinModelPortaliP62876.
SMRiP62876. Positions 1-67.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1644.
GeneTreeiENSGT00390000007087.
HOVERGENiHBG061475.
InParanoidiP62876.
KOiK03007.
OMAiLAHIELI.
OrthoDBiEOG79CZ2Z.
PhylomeDBiP62876.
TreeFamiTF103046.

Family and domain databases

Gene3Di1.10.10.60. 1 hit.
HAMAPiMF_00250. RNApol_arch_N.
InterProiIPR009057. Homeodomain-like.
IPR023580. RNA_pol_su_RPB10.
IPR020789. RNA_pol_suN_Zn-BS.
IPR000268. RNAP_N/Rpb10.
[Graphical view]
PfamiPF01194. RNA_pol_N. 1 hit.
[Graphical view]
PIRSFiPIRSF005653. RNA_pol_N/8_sub. 1 hit.
ProDomiPD006539. RNA_pol_N/8_sub. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF46924. SSF46924. 1 hit.
PROSITEiPS01112. RNA_POL_N_8KD. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P62876-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MIIPVRCFTC GKIVGNKWEA YLGLLQAEYT EGDALDALGL KRYCCRRMLL
60
AHVDLIEKLL NYAPLEK
Length:67
Mass (Da):7,645
Last modified:August 16, 2004 - v1
Checksum:i9E8A72F667FE7EC5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK011021 mRNA. Translation: BAB27338.1.
AK149137 mRNA. Translation: BAE28747.1.
AK168159 mRNA. Translation: BAE40122.1.
CCDSiCCDS52446.1.
RefSeqiNP_079869.1. NM_025593.1.
UniGeneiMm.380115.

Genome annotation databases

EnsembliENSMUST00000043870; ENSMUSP00000043204; ENSMUSG00000038489.
GeneIDi66491.
KEGGimmu:66491.
UCSCiuc009klm.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK011021 mRNA. Translation: BAB27338.1.
AK149137 mRNA. Translation: BAE28747.1.
AK168159 mRNA. Translation: BAE40122.1.
CCDSiCCDS52446.1.
RefSeqiNP_079869.1. NM_025593.1.
UniGeneiMm.380115.

3D structure databases

ProteinModelPortaliP62876.
SMRiP62876. Positions 1-67.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP62876. 2 interactions.
MINTiMINT-4133017.
STRINGi10090.ENSMUSP00000043204.

PTM databases

PhosphoSiteiP62876.

Proteomic databases

MaxQBiP62876.
PaxDbiP62876.
PRIDEiP62876.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000043870; ENSMUSP00000043204; ENSMUSG00000038489.
GeneIDi66491.
KEGGimmu:66491.
UCSCiuc009klm.2. mouse.

Organism-specific databases

CTDi5441.
MGIiMGI:1913741. Polr2l.

Phylogenomic databases

eggNOGiCOG1644.
GeneTreeiENSGT00390000007087.
HOVERGENiHBG061475.
InParanoidiP62876.
KOiK03007.
OMAiLAHIELI.
OrthoDBiEOG79CZ2Z.
PhylomeDBiP62876.
TreeFamiTF103046.

Enzyme and pathway databases

ReactomeiREACT_203462. Formation of the Early Elongation Complex.
REACT_205207. RNA Polymerase III Chain Elongation.
REACT_213655. Transcription-coupled NER (TC-NER).
REACT_221403. RNA Polymerase III Transcription Termination.
REACT_223654. Formation of transcription-coupled NER (TC-NER) repair complex.
REACT_224562. Dual incision reaction in TC-NER.
REACT_226490. RNA Polymerase II Transcription Elongation.
REACT_230204. RNA Polymerase II Transcription Initiation And Promoter Clearance.
REACT_232235. RNA Polymerase I Promoter Escape.
REACT_232708. RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
REACT_233950. Processing of Capped Intron-Containing Pre-mRNA.
REACT_235610. mRNA Splicing - Minor Pathway.
REACT_235780. RNA Polymerase I Transcription Initiation.
REACT_240508. RNA Polymerase III Transcription Initiation From Type 3 Promoter.
REACT_244380. RNA Polymerase II Transcription Initiation.
REACT_250309. RNA Polymerase III Transcription Initiation From Type 1 Promoter.
REACT_251592. RNA Polymerase III Transcription Initiation From Type 2 Promoter.
REACT_255009. RNA Polymerase II Pre-transcription Events.
REACT_255334. RNA Polymerase II Promoter Escape.
REACT_257165. RNA Polymerase I Transcription Termination.
REACT_257596. RNA Pol II CTD phosphorylation and interaction with CE.
REACT_258231. mRNA Capping.
REACT_259097. RNA Polymerase I Chain Elongation.
REACT_260226. mRNA Splicing - Major Pathway.
REACT_261233. RNA Polymerase III Abortive And Retractive Initiation.
REACT_270446. Transcriptional regulation by small RNAs.

Miscellaneous databases

NextBioi21055.
PROiP62876.
SOURCEiSearch...

Gene expression databases

BgeeiP62876.
CleanExiMM_POLR2L.
GenevestigatoriP62876.

Family and domain databases

Gene3Di1.10.10.60. 1 hit.
HAMAPiMF_00250. RNApol_arch_N.
InterProiIPR009057. Homeodomain-like.
IPR023580. RNA_pol_su_RPB10.
IPR020789. RNA_pol_suN_Zn-BS.
IPR000268. RNAP_N/Rpb10.
[Graphical view]
PfamiPF01194. RNA_pol_N. 1 hit.
[Graphical view]
PIRSFiPIRSF005653. RNA_pol_N/8_sub. 1 hit.
ProDomiPD006539. RNA_pol_N/8_sub. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF46924. SSF46924. 1 hit.
PROSITEiPS01112. RNA_POL_N_8KD. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "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 and DBA/2.
    Tissue: Liver and Sympathetic ganglion.

Entry informationi

Entry nameiRPAB5_MOUSE
AccessioniPrimary (citable) accession number: P62876
Secondary accession number(s): P52436, Q3UF14
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: August 16, 2004
Last modified: February 4, 2015
This is version 96 of the entry and version 1 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

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.