P08518 · RPB2_YEAST

Function

function

DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Second largest component of RNA polymerases II which synthesizes mRNA precursors and many functional non-coding RNAs. Proposed to contribute to the polymerase catalytic activity and forms the polymerase active center together with the largest subunit. Pol II is the central component of the basal RNA polymerase II transcription machinery. During a transcription cycle, Pol II, general transcription factors and the Mediator complex assemble as the preinitiation complex (PIC) at the promoter. 11-15 base pairs of DNA surrounding the transcription start site are melted and the single-stranded DNA template strand of the promoter is positioned deeply within the central active site cleft of Pol II to form the open complex. After synthesis of about 30 bases of RNA, Pol II releases its contacts with the core promoter and the rest of the transcription machinery (promoter clearance) and enters the stage of transcription elongation in which it moves on the template as the transcript elongates. Pol II appears to oscillate between inactive and active conformations at each step of nucleotide addition. Pol II is composed of mobile elements that move relative to each other. The core element with the central large cleft comprises RPB3, RBP10, RPB11, RPB12 and regions of RPB1 and RPB2 forming the active center. The clamp element (portions of RPB1, RPB2 and RPB3) is connected to the core through a set of flexible switches and moves to open and close the cleft. The cleft is surrounded by jaws: an upper jaw formed by portions of RBP1, RPB2 and RPB9, and a lower jaw. The jaws are thought to grab the incoming DNA template. The fork loop 1 (RPB2) interacts with the RNA-DNA hybrid, possibly stabilizing it.

Miscellaneous

The binding of ribonucleoside triphosphate to the RNA polymerase II transcribing complex probably involves a two-step mechanism. The initial binding seems to occur at the entry (E) site and involves a magnesium ion coordinated by three conserved aspartate residues of the two largest RNA Pol II subunits.
Present with 18700 molecules/cell in log phase SD medium.

Catalytic activity

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site837Mg2+ (UniProtKB | ChEBI); ligand shared with RPB1
Binding site1163Zn2+ (UniProtKB | ChEBI)
Binding site1166Zn2+ (UniProtKB | ChEBI)
Binding site1182Zn2+ (UniProtKB | ChEBI)
Binding site1185Zn2+ (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasmic stress granule
Cellular Componentmitochondrion
Cellular Componentnucleus
Cellular ComponentRNA polymerase II, core complex
Molecular FunctionDNA binding
Molecular FunctionDNA-directed 5'-3' RNA polymerase activity
Molecular Functionmetal ion binding
Molecular FunctionmRNA binding
Molecular Functionribonucleoside binding
Biological ProcessRNA-templated transcription
Biological Processtranscription by RNA polymerase II
Biological Processtranscription elongation by RNA polymerase II
Biological Processtranscription initiation at RNA polymerase II promoter

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    DNA-directed RNA polymerase II subunit RPB2
  • EC number
  • Short names
    RNA polymerase II subunit 2
  • Alternative names
    • B150
    • DNA-directed RNA polymerase II 140 kDa polypeptide

Gene names

    • Name
      RPB2
    • Synonyms
      RPB150, RPO22
    • Ordered locus names
      YOR151C

Organism names

Accessions

  • Primary accession
    P08518
  • Secondary accessions
    • D6W2K8
    • Q12738
    • Q7Z9Y0

Proteomes

Organism-specific databases

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_00000480911-1224DNA-directed RNA polymerase II subunit RPB2
Modified residue919Phosphoserine

Keywords

Proteomic databases

PTM databases

Interaction

Subunit

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

Binary interactions

View interactors in UniProtKB
View CPX-2662 in Complex Portal

Protein-protein interaction databases

Miscellaneous

Family & Domains

Features

Showing features for region, zinc finger.

TypeIDPosition(s)Description
Region467-478Fork loop 1
Zinc finger1163-1185C4-type

Sequence similarities

Belongs to the RNA polymerase beta chain family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    1,224
  • Mass (Da)
    138,751
  • Last updated
    1997-11-01 v2
  • Checksum
    BABD03212C0A583E
MSDLANSEKYYDEDPYGFEDESAPITAEDSWAVISAFFREKGLVSQQLDSFNQFVDYTLQDIICEDSTLILEQLAQHTTESDNISRKYEISFGKIYVTKPMVNESDGVTHALYPQEARLRNLTYSSGLFVDVKKRTYEAIDVPGRELKYELIAEESEDDSESGKVFIGRLPIMLRSKNCYLSEATESDLYKLKECPFDMGGYFIINGSEKVLIAQERSAGNIVQVFKKAAPSPISHVAEIRSALEKGSRFISTLQVKLYGREGSSARTIKATLPYIKQDIPIVIIFRALGIIPDGEILEHICYDVNDWQMLEMLKPCVEDGFVIQDRETALDFIGRRGTALGIKKEKRIQYAKDILQKEFLPHITQLEGFESRKAFFLGYMINRLLLCALDRKDQDDRDHFGKKRLDLAGPLLAQLFKTLFKKLTKDIFRYMQRTVEEAHDFNMKLAINAKTITSGLKYALATGNWGEQKKAMSSRAGVSQVLNRYTYSSTLSHLRRTNTPIGRDGKLAKPRQLHNTHWGLVCPAETPEGQACGLVKNLSLMSCISVGTDPMPIITFLSEWGMEPLEDYVPHQSPDATRVFVNGVWHGVHRNPARLMETLRTLRRKGDINPEVSMIRDIREKELKIFTDAGRVYRPLFIVEDDESLGHKELKVRKGHIAKLMATEYQDIEGGFEDVEEYTWSSLLNEGLVEYIDAEEEESILIAMQPEDLEPAEANEENDLDVDPAKRIRVSHHATTFTHCEIHPSMILGVAASIIPFPDHNQSPRNTYQSAMGKQAMGVFLTNYNVRMDTMANILYYPQKPLGTTRAMEYLKFRELPAGQNAIVAIACYSGYNQEDSMIMNQSSIDRGLFRSLFFRSYMDQEKKYGMSITETFEKPQRTNTLRMKHGTYDKLDDDGLIAPGVRVSGEDVIIGKTTPISPDEEELGQRTAYHSKRDASTPLRSTENGIVDQVLVTTNQDGLKFVKVRVRTTKIPQIGDKFASRHGQKGTIGITYRREDMPFTAEGIVPDLIINPHAIPSRMTVAHLIECLLSKVAALSGNEGDASPFTDITVEGISKLLREHGYQSRGFEVMYNGHTGKKLMAQIFFGPTYYQRLRHMVDDKIHARARGPMQVLTRQPVEGRSRDGGLRFGEMERDCMIAHGAASFLKERLMEASDAFRVHICGICGLMTVIAKLNHNQFECKGCDNKIDIYQIHIPYAAKLLFQELMAMNITPRLYTDRSRDF

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict1003-1006in Ref. 1; AAA68096

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
M15693
EMBL· GenBank· DDBJ
AAA68096.1
EMBL· GenBank· DDBJ
Genomic DNA
U55020
EMBL· GenBank· DDBJ
AAC49637.1
EMBL· GenBank· DDBJ
Genomic DNA
Z75059
EMBL· GenBank· DDBJ
CAA99357.1
EMBL· GenBank· DDBJ
Genomic DNA
AF527884
EMBL· GenBank· DDBJ
AAP57849.1
EMBL· GenBank· DDBJ
Genomic DNA
BK006948
EMBL· GenBank· DDBJ
DAA10924.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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