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P62875 (RPAB5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 104. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
RNA polymerase II 7.6 kDa subunit
Short name=RPB7.6
RPB10 homolog
Gene names
Name:POLR2L
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length67 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.6

Subunit structure

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. Ref.6 Ref.7

Subcellular location

Nucleus Ref.6 Ref.7.

Sequence similarities

Belongs to the archaeal RpoN/eukaryotic RPB10 RNA polymerase subunit family.

Ontologies

Keywords
   Biological processTranscription
   Cellular componentDNA-directed RNA polymerase
Nucleus
   LigandMetal-binding
Zinc
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_process7-methylguanosine mRNA capping

Traceable author statement. Source: Reactome

DNA repair

Traceable author statement. Source: Reactome

RNA splicing

Traceable author statement. Source: Reactome

gene expression

Traceable author statement. Source: Reactome

innate immune response

Traceable author statement. Source: Reactome

mRNA splicing, via spliceosome

Traceable author statement. Source: Reactome

nucleotide-excision repair

Traceable author statement. Source: Reactome

positive regulation of type I interferon production

Traceable author statement. Source: Reactome

positive regulation of viral transcription

Traceable author statement. Source: Reactome

regulation of transcription from RNA polymerase I promoter

Traceable author statement PubMed 8786124. Source: ProtInc

termination of RNA polymerase III transcription

Traceable author statement. Source: Reactome

transcription elongation from RNA polymerase II promoter

Traceable author statement. Source: Reactome

transcription elongation from RNA polymerase III promoter

Traceable author statement. Source: Reactome

transcription from RNA polymerase I promoter

Inferred from Biological aspect of Ancestor. Source: GOC

transcription from RNA polymerase II promoter

Inferred from direct assay Ref.6. Source: UniProtKB

transcription from RNA polymerase III promoter

Traceable author statement. Source: Reactome

transcription initiation from RNA polymerase II promoter

Traceable author statement. Source: Reactome

transcription-coupled nucleotide-excision repair

Traceable author statement. Source: Reactome

viral process

Traceable author statement. Source: Reactome

   Cellular_componentDNA-directed RNA polymerase I complex

Inferred from Biological aspect of Ancestor. Source: RefGenome

DNA-directed RNA polymerase II, core complex

Inferred from direct assay Ref.6. Source: UniProtKB

DNA-directed RNA polymerase III complex

Inferred from Biological aspect of Ancestor. Source: RefGenome

cytosol

Traceable author statement. Source: Reactome

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay Ref.6. Source: UniProtKB

   Molecular_functionDNA binding

Inferred from electronic annotation. Source: InterPro

DNA-directed RNA polymerase activity

Traceable author statement Ref.1. Source: ProtInc

zinc ion binding

Inferred from Biological aspect of Ancestor. Source: RefGenome

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 6767DNA-directed RNA polymerases I, II, and III subunit RPABC5 HAMAP-Rule MF_00250
PRO_0000121333

Sites

Metal binding71Zinc By similarity
Metal binding101Zinc By similarity
Metal binding441Zinc By similarity
Metal binding451Zinc By similarity

Sequences

Sequence LengthMass (Da)Tools
P62875 [UniParc].

Last modified August 16, 2004. Version 1.
Checksum: 9E8A72F667FE7EC5

FASTA677,645
        10         20         30         40         50         60 
MIIPVRCFTC GKIVGNKWEA YLGLLQAEYT EGDALDALGL KRYCCRRMLL AHVDLIEKLL 


NYAPLEK 

« Hide

References

« Hide 'large scale' references
[1]"Six human RNA polymerase subunits functionally substitute for their yeast counterparts."
McKune K., Moore P.A., Hull M.W., Woychik N.A.
Mol. Cell. Biol. 15:6895-6900(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]"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. expand/collapse author list , 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].
Tissue: Cerebellum.
[4]"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: Bone marrow and Kidney.
[5]"Four subunits that are shared by the three classes of RNA polymerase are functionally interchangeable between Homo sapiens and Saccharomyces cerevisiae."
Shpakovski G.V., Acker J., Wintzerith M., Lacroix J.F., Thuriaux P., Vigneron M.
Mol. Cell. Biol. 15:4702-4710(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-32.
[6]"Immunoaffinity purification and functional characterization of human transcription factor IIH and RNA polymerase II from clonal cell lines that conditionally express epitope-tagged subunits of the multiprotein complexes."
Kershnar E., Wu S.-Y., Chiang C.-M.
J. Biol. Chem. 273:34444-34453(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, IDENTIFICATION IN THE RNA POLYMERASE II CORE-COMPLEX, SUBCELLULAR LOCATION.
[7]"RNA polymerase I-specific subunit CAST/hPAF49 has a role in the activation of transcription by upstream binding factor."
Panov K.I., Panova T.B., Gadal O., Nishiyama K., Saito T., Russell J., Zomerdijk J.C.B.M.
Mol. Cell. Biol. 26:5436-5448(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE RNA POL I COMPLEX, SUBCELLULAR LOCATION.
[8]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U37690 mRNA. Translation: AAA91459.1.
CR536565 mRNA. Translation: CAG38802.1.
AK311997 mRNA. Translation: BAG34935.1.
BC005903 mRNA. Translation: AAH05903.1.
BC018649 mRNA. Translation: AAH18649.1.
Z47729 Genomic DNA. Translation: CAA87658.1.
Z47728 Genomic DNA. Translation: CAA87657.1.
PIRS53015.
RefSeqNP_066951.1. NM_021128.4.
UniGeneHs.441072.

3D structure databases

ProteinModelPortalP62875.
SMRP62875. Positions 1-67.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111437. 23 interactions.
IntActP62875. 11 interactions.
MINTMINT-1132504.
STRING9606.ENSP00000324124.

PTM databases

PhosphoSiteP62875.

Polymorphism databases

DMDM51338657.

Proteomic databases

PaxDbP62875.
PRIDEP62875.

Protocols and materials databases

DNASU5441.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000322028; ENSP00000324124; ENSG00000177700.
ENST00000534030; ENSP00000432807; ENSG00000177700.
GeneID5441.
KEGGhsa:5441.
UCSCuc001lsc.3. human.

Organism-specific databases

CTD5441.
GeneCardsGC11M000829.
HGNCHGNC:9199. POLR2L.
MIM601189. gene.
neXtProtNX_P62875.
PharmGKBPA33519.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1644.
HOVERGENHBG061475.
InParanoidP62875.
KOK03007.
OMAKKYCCRR.
OrthoDBEOG79CZ2Z.
PhylomeDBP62875.
TreeFamTF103046.

Enzyme and pathway databases

ReactomeREACT_116125. Disease.
REACT_1788. Transcription.
REACT_1892. Elongation arrest and recovery.
REACT_216. DNA Repair.
REACT_6900. Immune System.
REACT_71. Gene Expression.

Gene expression databases

BgeeP62875.
CleanExHS_POLR2L.
GenevestigatorP62875.

Family and domain databases

Gene3D1.10.10.60. 1 hit.
HAMAPMF_00250. RNApol_arch_N.
InterProIPR009057. Homeodomain-like.
IPR023580. RNA_pol_su_RPB10.
IPR020789. RNA_pol_suN_Zn-BS.
IPR000268. RNAP_N/Rpb10.
[Graphical view]
PfamPF01194. RNA_pol_N. 1 hit.
[Graphical view]
PIRSFPIRSF005653. RNA_pol_N/8_sub. 1 hit.
ProDomPD006539. RNA_pol_N/8_sub. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMSSF46924. SSF46924. 1 hit.
PROSITEPS01112. RNA_POL_N_8KD. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiPOLR2L.
GenomeRNAi5441.
NextBio21055.
PROP62875.
SOURCESearch...

Entry information

Entry nameRPAB5_HUMAN
AccessionPrimary (citable) accession number: P62875
Secondary accession number(s): P52436, Q6FHX3
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: August 16, 2004
Last modified: April 16, 2014
This is version 104 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM