POLR2B
entrez
5431
canonical
uniprot
P30876
canonical
ensembl
ENSG00000047315
resolver
ensp
ENSP00000312735
resolver
ensp
ENSP00000370625
resolver
ensp
ENSP00000391096
resolver
ensp
ENSP00000391452
resolver
enst
ENST00000314595
resolver
enst
ENST00000381227
resolver
enst
ENST00000441246
resolver
genesymbol
POLR2B
resolver
hgnc
HGNC:9188
resolver
uniprot
A8K1A8
resolver
uniprot
B4DH29
resolver
uniprot
B4DHJ3
resolver
uniprot
C9J2Y9
resolver
uniprot
Q8IZ61
resolver
uniprot_entry
B4DH29_HUMAN
resolver
uniprot_entry
B4DHJ3_HUMAN
resolver
uniprot_entry
C9J2Y9_HUMAN
resolver
uniprot_entry
RPB2_HUMAN
resolver
uniprot_sec
A8K1A8
resolver
uniprot_sec
Q8IZ61
resolver
activity_regulation
ACTIVITY REGULATION: Pol II enzymatic activities are inhibited by alpha-amanitin. 3'->5' exonuclease activity is stimulated by TFIIS, whereas pyrophosphorolysis is enhanced by TFIIF. {ECO:0000269|PubMed:8381534}.
uniprot
proteins
amino_acid_sequence
MYDADEDMQYDEDDDEITPDLWQEACWIVISSYFDEKGLVRQQLDSFDEFIQMSVQRIVEDAPPIDLQAEAQHASGEVEEPPRYLLKFEQIYLSKPTHWERDGAPSPMMPNEARLRNLTYSAPLYVDITKTVIKEGEEQLQTQHQKTFIGKIPIMLRSTYCLLNGLTDRDLCELNECPLDPGGYFIINGSEKVLIAQEKMATNTVYVFAKKDSKYAYTGECRSCLENSSRPTSTIWVSMLARGGQGAKKSAIGQRIVATLPYIKQEVPIIIVFRALGFVSDRDILEHIIYDFEDPEMMEMVKPSLDEAFVIQEQNVALNFIGSRGAKPGVTKEKRIKYAKEVLQKEMLPHVGVSDFCETKKAYFLGYMVHRLLLAALGRRELDDRDHYGNKRLDLAGPLLAFLFRGMFKNLLKEVRIYAQKFIDRGKDFNLELAIKTRIISDGLKYSLATGNWGDQKKAHQARAGVSQVLNRLTFASTLSHLRRLNSPIGRDGKLAKPRQLHNTLWGMVCPAETPEGHAVGLVKNLALMAYISVGSQPSPILEFLEEWSMENLEEISPAAIADATKIFVNGCWVGIHKDPEQLMNTLRKLRRQMDIIVSEVSMIRDIREREIRIYTDAGRICRPLLIVEKQKLLLKKRHIDQLKEREYNNYSWQDLVASGVVEYIDTLEEETVMLAMTPDDLQEKEVAYCSTYTHCEIHPSMILGVCASIIPFPDHNQSPRNTYQSAMGKQAMGVYITNFHVRMDTLAHVLYYPQKPLVTTRSMEYLRFRELPAGINSIVAIASYTGYNQEDSVIMNRSAVDRGFFRSVFYRSYKEQESKKGFDQEEVFEKPTRETCQGMRHAIYDKLDDDGLIAPGVRVSGDDVIIGKTVTLPENEDELESTNRRYTKRDCSTFLRTSETGIVDQVMVTLNQEGYKFCKIRVRSVRIPQIGDKFASRHGQKGTCGIQYRQEDMPFTCEGITPDIIINPHAIPSRMTIGHLIECLQGKVSANKGEIGDATPFNDAVNVQKISNLLSDYGYHLRGNEVLYNGFTGRKITSQIFIGPTYYQRLKHMVDDKIHSRARGPIQILNRQPMEGRSRDGGLRFGEMERDCQIAHGAAQFLRERLFEASDPYQVHVCNLCGIMAIANTRTHTYECRGCRNKTQISLVRMPYACKLLFQELMSMSIAPRMMSV
uniprot
proteins
ec_number
2.7.7.48
uniprot
proteins
ec_number
2.7.7.6
uniprot
proteins
ec_number
3.1.13.-
uniprot
proteins
function
FUNCTION: Catalytic core component of RNA polymerase II (Pol II), a DNA-dependent RNA polymerase which synthesizes mRNA precursors and many functional non-coding RNAs using the four ribonucleoside triphosphates as substrates (By similarity) (PubMed:27193682, PubMed:30190596, PubMed:9852112). Pol II-mediated transcription cycle proceeds through transcription initiation, transcription elongation and transcription termination stages. During transcription initiation, Pol II pre-initiation complex (PIC) is recruited to DNA promoters, with focused-type promoters containing either the initiator (Inr) element, or the TATA-box found in cell-type specific genes and dispersed-type promoters that often contain hypomethylated CpG islands usually found in housekeeping genes. Once the polymerase has escaped from the promoter it enters the elongation phase during which RNA is actively polymerized, based on complementarity with the template DNA strand. Transcription termination involves the release of the RNA transcript and polymerase from the DNA (PubMed:27193682, PubMed:30190596, PubMed:9852112). Forms Pol II active center together with the largest subunit POLR2A/RPB1. Appends one nucleotide at a time to the 3' end of the nascent RNA, with POLR2A/RPB1 most likely contributing a Mg(2+)-coordinating DxDGD motif and POLR2B/RPB2 participating in the coordination of a second Mg(2+) ion and providing lysine residues believed to facilitate Watson-Crick base pairing between the incoming nucleotide and template base. Typically, Mg(2+) ions direct a 5' nucleoside triphosphate to form a phosphodiester bond with the 3' hydroxyl of the preceding nucleotide of the nascent RNA, with the elimination of pyrophosphate. The reversible pyrophosphorolysis can occur at high pyrophosphate concentrations (By similarity) (PubMed:30190596, PubMed:9852112). Can proofread the nascent RNA transcript by means of a 3' -> 5' exonuclease activity. If a ribonucleotide is mis-incorporated, backtracks along the template DNA and cleaves the phosphodiester bond releasing the mis-incorporated 5'-ribonucleotide (By similarity) (PubMed:8381534). {ECO:0000250|UniProtKB:A5PJW8, ECO:0000269|PubMed:27193682, ECO:0000269|PubMed:30190596, ECO:0000269|PubMed:8381534, ECO:0000269|PubMed:9852112}.; FUNCTION: RNA-dependent RNA polymerase that catalyzes the extension of a non-coding RNA (ncRNA) at the 3'-end using the four ribonucleoside triphosphates as substrates. An internal ncRNA sequence near the 3'-end serves as a template in a single-round Pol II-mediated RNA polymerization reaction. May decrease the stability of ncRNAs that repress Pol II-mediated gene transcription. {ECO:0000269|PubMed:23395899}.
uniprot
proteins
mass_dalton
133897
uniprot
proteins
protein_family
RNA polymerase beta chain family
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
14992727
uniprot
proteins
pubmed
1518060
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
17998332
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23395899
uniprot
proteins
pubmed
24129315
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
27193682
uniprot
proteins
pubmed
30190596
uniprot
proteins
pubmed
8381534
uniprot
proteins
pubmed
9110174
uniprot
proteins
pubmed
9852112
uniprot
proteins
sequence_length
1174
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9852112}.
uniprot
proteins