P19388 (RPAB1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	210 AA.
Sequence status	Complete.
Protein existence	Evidence 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 process	Host-virus interaction Transcription
Cellular component	DNA-directed RNA polymerase Nucleus
Coding sequence diversity	Polymorphism
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	7-methylguanosine mRNA capping Traceable author statement. Source: Reactome mRNA splicing, via spliceosome Traceable author statement. Source: Reactome positive regulation of viral transcription Traceable author statement. Source: Reactome protein phosphorylation Inferred from direct assay Ref.8. Source: GOC 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 initiation from RNA polymerase II promoter Traceable author statement. Source: Reactome transcription-coupled nucleotide-excision repair Traceable author statement. Source: Reactome viral reproduction Traceable author statement. Source: Reactome virus-host interaction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	DNA-directed RNA polymerase II, core complex Inferred from direct assay Ref.8. Source: UniProtKB
Molecular_function	DNA binding Inferred from electronic annotation. Source: InterPro DNA-directed RNA polymerase activity Traceable author statement Ref.3. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
URI1	O94763	2	EBI-395189,EBI-357067

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 210	210	DNA-directed RNA polymerases I, II, and III subunit RPABC1		PRO_0000146075
Natural variations
	Natural variant	44	1	S → F. Ref.1 Ref.3 Ref.4 Ref.6 Ref.7 Corresponds to variant rs12459404 [ dbSNP | Ensembl ].		VAR_028259
Experimental info
	Sequence conflict	132	1	Q → E Ref.1
	Sequence conflict	132	1	Q → E Ref.3
	Sequence conflict	157	1	T → S in BAA07406. Ref.3
	Sequence conflict	185	1	I → V in AAH34144. Ref.7
	Sequence conflict	186	1	K → R in BAA07406. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	P19388 [UniParc]. Last modified October 17, 2006. Version 4. Checksum: 1E88AFDBCF9C8535	FASTA	210	24,551
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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. , 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]	"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	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.
IPI	IPI00291093.
PIR	A32618. S52002.
RefSeq	NP_002686.2. NM_002695.3.
UniGene	Hs.24301.
3D structure databases
ProteinModelPortal	P19388.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-56N.
IntAct	P19388. 17 interactions.
MINT	MINT-193645.
STRING	9606.ENSP00000215587.
PTM databases
PhosphoSite	P19388.
Polymorphism databases
DMDM	116242767.
2D gel databases
REPRODUCTION-2DPAGE	IPI00291093.
SWISS-2DPAGE	P19388.
Proteomic databases
PaxDb	P19388.
PeptideAtlas	P19388.
PRIDE	P19388.
Protocols and materials databases
DNASU	5434.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000215587; ENSP00000215587; ENSG00000099817. ENST00000586746; ENSP00000464739; ENSG00000099817.
GeneID	5434.
KEGG	hsa:5434.
UCSC	uc002lre.4. human.
Organism-specific databases
CTD	5434.
GeneCards	GC19M001086.
HGNC	HGNC:9192. POLR2E.
MIM	180664. gene.
neXtProt	NX_P19388.
PharmGKB	PA33512.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG2012.
HOGENOM	HOG000205213.
HOVERGEN	HBG057019.
InParanoid	P19388.
KO	K03013.
OMA	DEAETYK.
OrthoDB	EOG479F81.
PhylomeDB	P19388.
Enzyme and pathway databases
Reactome	REACT_116125. Disease. REACT_1675. mRNA Processing. REACT_1788. Transcription. REACT_1892. Elongation arrest and recovery. REACT_216. DNA Repair. REACT_71. Gene Expression.
Gene expression databases
ArrayExpress	P19388.
Bgee	P19388.
CleanEx	HS_POLR2E.
Genevestigator	P19388.
GermOnline	ENSG00000099817. Homo sapiens.
Family and domain databases
Gene3D	3.40.1340.10. 1 hit. 3.90.940.20. 1 hit.
InterPro	IPR014381. DNA-dir_RNA_pol_RPB5_su. IPR005571. RNA_pol_Rpb5_N. IPR000783. RNA_pol_subH/Rpb5_C. IPR020608. RNA_pol_subH/Rpb5_CS. [Graphical view]
Pfam	PF01191. RNA_pol_Rpb5_C. 1 hit. PF03871. RNA_pol_Rpb5_N. 1 hit. [Graphical view]
PIRSF	PIRSF000747. RPB5. 1 hit.
ProDom	PD005155. RNA_pol_subH/Rpb5_C. 1 hit. [Graphical view] [Entries sharing at least one domain]
SUPFAM	SSF53036. RNA_pol_Rpb5_N. 1 hit. SSF55287. RNApol_RPB5_like. 1 hit.
PROSITE	PS01110. RNA_POL_H_23KD. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	5434.
NextBio	21025.
SOURCE	Search...

Entry information

Entry name

RPAB1_HUMAN

Accession

Primary (citable) accession number: P19388
Secondary accession number(s): B2R6L4 , D6W5Y1, O43380, Q6PIH5, Q9BT06

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1990
Last sequence update:	October 17, 2006
Last modified:	May 1, 2013
This is version 140 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.