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P19388 (RPAB1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 154. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·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 RPABC1

Short name=RNA polymerases I, II, and III subunit ABC1
Alternative name(s):
DNA-directed RNA polymerase II 23 kDa polypeptide
DNA-directed RNA polymerase II subunit E
RPB5 homolog
XAP4
Gene names
Name:POLR2E
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length210 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 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, POLR2E/RPB5 is part of the lower jaw surrounding the central large cleft and thought to grab the incoming DNA template. Seems to be the major component in this process By similarity. Ref.8

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. In RNA Pol II, this subunit is present in 2-fold molar excess over the other subunits. Interacts with URI1. Interacts with HBV protein X. Ref.3 Ref.8 Ref.9 Ref.10

Subcellular location

Nucleus Ref.8.

Sequence similarities

Belongs to the archaeal RpoH/eukaryotic RPB5 RNA polymerase subunit family.

Ontologies

Keywords
   Biological processHost-virus interaction
Transcription
   Cellular componentDNA-directed RNA polymerase
Nucleus
   Coding sequence diversityPolymorphism
   PTMAcetylation
   Technical termComplete proteome
Direct protein sequencing
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

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.8. 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.8. 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.8. Source: UniProtKB

   Molecular_functionDNA binding

Inferred from electronic annotation. Source: InterPro

DNA-directed RNA polymerase activity

Traceable author statement Ref.3. Source: ProtInc

protein binding

Inferred from physical interaction PubMed 12737519. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

URI1O947632EBI-395189,EBI-357067

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 210210DNA-directed RNA polymerases I, II, and III subunit RPABC1 HAMAP-Rule MF_00025
PRO_0000146075

Amino acid modifications

Modified residue11N-acetylmethionine Ref.11 Ref.13

Natural variations

Natural variant441S → F. Ref.1 Ref.3 Ref.4 Ref.6 Ref.7
Corresponds to variant rs12459404 [ dbSNP | Ensembl ].
VAR_028259

Experimental info

Sequence conflict1321Q → E Ref.1
Sequence conflict1321Q → E Ref.3
Sequence conflict1571T → S in BAA07406. Ref.3
Sequence conflict1851I → V in AAH34144. Ref.7
Sequence conflict1861K → R in BAA07406. Ref.3

Sequences

Sequence LengthMass (Da)Tools
P19388 [UniParc].

Last modified October 17, 2006. Version 4.
Checksum: 1E88AFDBCF9C8535

FASTA21024,551
        10         20         30         40         50         60 
MDDEEETYRL WKIRKTIMQL CHDRGYLVTQ DELDQTLEEF KAQSGDKPSE GRPRRTDLTV 

        70         80         90        100        110        120 
LVAHNDDPTD QMFVFFPEEP KVGIKTIKVY CQRMQEENIT RALIVVQQGM TPSAKQSLVD 

       130        140        150        160        170        180 
MAPKYILEQF LQQELLINIT EHELVPEHVV MTKEEVTELL ARYKLRENQL PRIQAGDPVA 

       190        200        210 
RYFGIKRGQV VKIIRPSETA GRYITYRLVQ 

« Hide

References

« Hide 'large scale' references
[1]"Isolation and molecular characterization of a cDNA encoding the 23-kDa subunit of human RNA polymerase II."
Pati U.K., Weissman S.M.
J. Biol. Chem. 264:13114-13121(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, VARIANT PHE-44.
[2]Erratum
Pati U.K., Weissman S.M.
J. Biol. Chem. 266:13468-13468(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: SEQUENCE REVISION.
[3]"Human RPB5, a subunit shared by eukaryotic nuclear RNA polymerases, binds human hepatitis B virus X protein and may play a role in X transactivation."
Cheong J.H., Yi M., Lin Y., Murakami S.
EMBO J. 14:143-150(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT PHE-44, INTERACTION WITH HBV PROTEIN X.
[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. 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], VARIANT PHE-44.
Tissue: Heart.
[5]"The DNA sequence and biology of human chromosome 19."
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V. expand/collapse author list , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT PHE-44.
[7]"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], VARIANT PHE-44.
Tissue: Lung.
[8]"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.
[9]"RMP, a novel RNA polymerase II subunit 5-interacting protein, counteracts transactivation by hepatitis B virus X protein."
Dorjsuren D., Lin Y., Wei W., Yamashita T., Nomura T., Hayashi N., Murakami S.
Mol. Cell. Biol. 18:7546-7555(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH URI1.
[10]"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.
[11]"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].
[12]"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].
[13]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J04965 mRNA. Translation: AAA62401.1. Sequence problems.
S42643 mRNA. Translation: AAB19339.1.
D38251 mRNA. Translation: BAA07406.1.
AK312625 mRNA. Translation: BAG35511.1.
AC004151 Genomic DNA. Translation: AAC03238.1.
CH471139 Genomic DNA. Translation: EAW69548.1.
CH471139 Genomic DNA. Translation: EAW69549.1.
BC004441 mRNA. Translation: AAH04441.1.
BC034144 mRNA. Translation: AAH34144.1.
CCDSCCDS12056.1.
PIRA32618. S52002.
RefSeqNP_002686.2. NM_002695.3.
UniGeneHs.24301.

3D structure databases

ProteinModelPortalP19388.
SMRP19388. Positions 3-210.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111430. 83 interactions.
DIPDIP-56N.
IntActP19388. 25 interactions.
MINTMINT-193645.
STRING9606.ENSP00000215587.

PTM databases

PhosphoSiteP19388.

Polymorphism databases

DMDM116242767.

2D gel databases

REPRODUCTION-2DPAGEIPI00291093.
SWISS-2DPAGEP19388.

Proteomic databases

MaxQBP19388.
PaxDbP19388.
PeptideAtlasP19388.
PRIDEP19388.

Protocols and materials databases

DNASU5434.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000215587; ENSP00000215587; ENSG00000099817.
ENST00000586746; ENSP00000464739; ENSG00000099817.
GeneID5434.
KEGGhsa:5434.
UCSCuc002lre.4. human.

Organism-specific databases

CTD5434.
GeneCardsGC19M001086.
HGNCHGNC:9192. POLR2E.
MIM180664. gene.
neXtProtNX_P19388.
PharmGKBPA33512.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2012.
HOGENOMHOG000205213.
HOVERGENHBG057019.
InParanoidP19388.
KOK03013.
OMADEAETYK.
OrthoDBEOG7M6D8D.
PhylomeDBP19388.

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

ArrayExpressP19388.
BgeeP19388.
CleanExHS_POLR2E.
GenevestigatorP19388.

Family and domain databases

Gene3D3.40.1340.10. 1 hit.
3.90.940.20. 1 hit.
HAMAPMF_00025. RNApol_RpoH_RPB5.
InterProIPR014381. DNA_RNA_pol_RPB5_euk/virus.
IPR005571. RNA_pol_Rpb5_N.
IPR000783. RNA_pol_subH/Rpb5_C.
IPR020608. RNA_pol_subH/Rpb5_CS.
IPR020609. RpoH/RPB5.
[Graphical view]
PfamPF01191. RNA_pol_Rpb5_C. 1 hit.
PF03871. RNA_pol_Rpb5_N. 1 hit.
[Graphical view]
PIRSFPIRSF000747. RPB5. 1 hit.
ProDomPD005155. RNA_pol_subH/Rpb5_C. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMSSF53036. SSF53036. 1 hit.
SSF55287. SSF55287. 1 hit.
PROSITEPS01110. RNA_POL_H_23KD. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiPOLR2E.
GenomeRNAi5434.
NextBio21025.
PROP19388.
SOURCESearch...

Entry information

Entry nameRPAB1_HUMAN
AccessionPrimary (citable) accession number: P19388
Secondary accession number(s): B2R6L4 expand/collapse secondary AC list , D6W5Y1, O43380, Q6PIH5, Q9BT06
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: October 17, 2006
Last modified: July 9, 2014
This is version 154 of the entry and version 4 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 polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM