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P36954 (RPB9_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 141. 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 polymerase II subunit RPB9

Short name=RNA polymerase II subunit B9
Alternative name(s):
DNA-directed RNA polymerase II subunit I
RNA polymerase II 14.5 kDa subunit
Short name=RPB14.5
Gene names
Name:POLR2I
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length125 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. Component of RNA polymerase II which synthesizes mRNA precursors and many functional non-coding RNAs. Pol II is the central component of the basal RNA polymerase II transcription machinery. It is composed of mobile elements that move relative to each other. RPB9 is part of the upper jaw surrounding the central large cleft and thought to grab the incoming DNA template By similarity. Ref.5

Subunit structure

Component of the RNA polymerase II (Pol II) complex consisting of 12 subunits. Ref.5

Subcellular location

Nucleus Ref.5.

Sequence similarities

Belongs to the archaeal RpoM/eukaryotic RPA12/RPB9/RPC11 RNA polymerase family.

Contains 1 TFIIS-type zinc finger.

Ontologies

Keywords
   Biological processTranscription
   Cellular componentDNA-directed RNA polymerase
Nucleus
   DomainZinc-finger
   LigandMetal-binding
Zinc
   PTMAcetylation
   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

mRNA splicing, via spliceosome

Traceable author statement. Source: Reactome

maintenance of transcriptional fidelity during DNA-templated transcription elongation from RNA polymerase II promoter

Inferred from Biological aspect of Ancestor. Source: RefGenome

nucleotide-excision repair

Traceable author statement. Source: Reactome

positive regulation of viral transcription

Traceable author statement. Source: Reactome

transcription elongation from RNA polymerase II promoter

Traceable author statement. Source: Reactome

transcription from RNA polymerase II promoter

Inferred from direct assay Ref.5. Source: UniProtKB

transcription initiation from RNA polymerase II promoter

Inferred from Biological aspect of Ancestor. Source: RefGenome

transcription-coupled nucleotide-excision repair

Inferred from Biological aspect of Ancestor. Source: RefGenome

viral process

Traceable author statement. Source: Reactome

   Cellular_componentDNA-directed RNA polymerase II, core complex

Inferred from direct assay Ref.5. Source: UniProtKB

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay Ref.5. 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

Traceable author statement Ref.1. Source: ProtInc

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 125125DNA-directed RNA polymerase II subunit RPB9
PRO_0000121467

Regions

Zinc finger17 – 4226C4-type Potential
Zinc finger82 – 12443TFIIS-type

Sites

Metal binding171Zinc 1 By similarity
Metal binding201Zinc 1 By similarity
Metal binding391Zinc 1 By similarity
Metal binding421Zinc 1 By similarity
Metal binding861Zinc 2 By similarity
Metal binding891Zinc 2 By similarity
Metal binding1141Zinc 2 By similarity
Metal binding1191Zinc 2 By similarity

Amino acid modifications

Modified residue11N-acetylmethionine Ref.7

Sequences

Sequence LengthMass (Da)Tools
P36954 [UniParc].

Last modified June 1, 1994. Version 1.
Checksum: 6520687BB57EE018

FASTA12514,523
        10         20         30         40         50         60 
MEPDGTYEPG FVGIRFCQEC NNMLYPKEDK ENRILLYACR NCDYQQEADN SCIYVNKITH 

        70         80         90        100        110        120 
EVDELTQIIA DVSQDPTLPR TEDHPCQKCG HKEAVFFQSH SARAEDAMRL YYVCTAPHCG 


HRWTE 

« Hide

References

« Hide 'large scale' references
[1]"Structure of the gene encoding the 14.5 kDa subunit of human RNA polymerase II."
Acker J., Wintzerith M., Vigneron M., Kedinger C.
Nucleic Acids Res. 21:5345-5350(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"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].
[3]"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].
[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: Brain and Uterus.
[5]"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.
[6]"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].
[7]"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
Z23102 Genomic DNA. Translation: CAA80649.1.
AK312206 mRNA. Translation: BAG35139.1.
AD001527 Genomic DNA. Translation: AAB51181.1.
BC017112 mRNA. Translation: AAH17112.1.
BC067794 mRNA. Translation: AAH67794.1.
PIRS41621.
RefSeqNP_006224.1. NM_006233.4.
UniGeneHs.47062.

3D structure databases

ProteinModelPortalP36954.
SMRP36954. Positions 15-125.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111434. 19 interactions.
DIPDIP-32917N.
IntActP36954. 6 interactions.
STRING9606.ENSP00000221859.

PTM databases

PhosphoSiteP36954.

Polymorphism databases

DMDM548702.

Proteomic databases

PaxDbP36954.
PeptideAtlasP36954.
PRIDEP36954.

Protocols and materials databases

DNASU5438.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000221859; ENSP00000221859; ENSG00000105258.
GeneID5438.
KEGGhsa:5438.
UCSCuc002ode.3. human.

Organism-specific databases

CTD5438.
GeneCardsGC19M036604.
HGNCHGNC:9196. POLR2I.
HPAHPA045156.
MIM180662. gene.
neXtProtNX_P36954.
PharmGKBPA33516.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1594.
HOGENOMHOG000228134.
HOVERGENHBG009981.
InParanoidP36954.
KOK03017.
OMAMHEIDEL.
OrthoDBEOG7BW0M6.
PhylomeDBP36954.
TreeFamTF103032.

Enzyme and pathway databases

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

Gene expression databases

ArrayExpressP36954.
BgeeP36954.
CleanExHS_POLR2I.
GenevestigatorP36954.

Family and domain databases

InterProIPR019761. DNA-dir_RNA_pol-M_15_CS.
IPR001529. DNA-dir_RNA_pol_M/15kDasu.
IPR012164. DNA-dir_RNApol_C11.
IPR001222. Znf_TFIIS.
[Graphical view]
PfamPF02150. RNA_POL_M_15KD. 1 hit.
PF01096. TFIIS_C. 1 hit.
[Graphical view]
PIRSFPIRSF005586. RNApol_RpoM. 1 hit.
SMARTSM00661. RPOL9. 1 hit.
SM00440. ZnF_C2C2. 1 hit.
[Graphical view]
PROSITEPS01030. RNA_POL_M_15KD. 1 hit.
PS00466. ZF_TFIIS_1. 1 hit.
PS51133. ZF_TFIIS_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPOLR2I. human.
GeneWikiPOLR2I.
GenomeRNAi5438.
NextBio21041.
PMAP-CutDBP36954.
PROP36954.
SOURCESearch...

Entry information

Entry nameRPB9_HUMAN
AccessionPrimary (citable) accession number: P36954
Secondary accession number(s): B2R5J2, Q6NW05
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: April 16, 2014
This is version 141 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 19

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