POLR1B
entrez
84172
canonical
uniprot
Q9H9Y6
canonical
ensembl
ENSG00000125630
resolver
ensp
ENSP00000263331
resolver
ensp
ENSP00000387143
resolver
ensp
ENSP00000405358
resolver
ensp
ENSP00000437914
resolver
ensp
ENSP00000444136
resolver
genesymbol
POLR1B
resolver
hgnc
HGNC:20454
resolver
uniprot
B7Z1W6
resolver
uniprot
B7Z6Y7
resolver
uniprot
B7Z823
resolver
uniprot
F5GZX4
resolver
uniprot
F8W898
resolver
uniprot
Q2TAM4
resolver
uniprot
Q585T5
resolver
uniprot
Q6ZRR2
resolver
uniprot
Q9H9D3
resolver
uniprot_entry
B7Z1W6_HUMAN
resolver
uniprot_entry
RPA2_HUMAN
resolver
uniprot_sec
B7Z6Y7
resolver
uniprot_sec
B7Z823
resolver
uniprot_sec
F5GZX4
resolver
uniprot_sec
F8W898
resolver
uniprot_sec
Q2TAM4
resolver
uniprot_sec
Q585T5
resolver
uniprot_sec
Q6ZRR2
resolver
uniprot_sec
Q9H9D3
resolver
amino_acid_sequence
MDPGSRWRNLPSGPSLKHLTDPSYGIPREQQKAALQELTRAHVESFNYAVHEGLGLAVQAIPPFEFAFKDERISFTILDAVISPPTVPKGTICKEANVYPAECRGRRSTYRGKLTADINWAVNGISKGIIKQFLGYVPIMVKSKLCNLRNLPPQALIEHHEEAEEMGGYFIINGIEKVIRMLIMPRRNFPIAMIRPKWKTRGPGYTQYGVSMHCVREEHSAVNMNLHYLENGTVMLNFIYRKELFFLPLGFALKALVSFSDYQIFQELIKGKEDDSFLRNSVSQMLRIVMEEGCSTQKQVLNYLGECFRVKLNVPDWYPNEQAAEFLFNQCICIHLKSNTEKFYMLCLMTRKLFALAKGECMEDNPDSLVNQEVLTPGQLFLMFLKEKLEGWLVSIKIAFDKKAQKTSVSMNTDNLMRIFTMGIDLTKPFEYLFATGNLRSKTGLGLLQDSGLCVVADKLNFIRYLSHFRCVHRGADFAKMRTTTVRRLLPESWGFLCPVHTPDGEPCGLMNHLTAVCEVVTQFVYTASIPALLCNLGVTPIDGAPHRSYSECYPVLLDGVMVGWVDKDLAPGIADSLRHFKVLREKRIPPWMEVVLIPMTGKPSLYPGLFLFTTPCRLVRPVQNLALGKEELIGTMEQIFMNVAIFEDEVFAGVTTHQELFPHSLLSVIANFIPFSDHNQSPRNMYQCQMGKQTMGFPLLTYQDRSDNKLYRLQTPQSPLVRPSMYDYYDMDNYPIGTNAIVAVISYTGYDMEDAMIVNKASWERGFAHGSVYKSEFIDLSEKIKQGDSSLVFGIKPGDPRVLQKLDDDGLPFIGAKLQYGDPYYSYLNLNTGESFVMYYKSKENCVVDNIKVCSNDTGSGKFKCVCITMRVPRNPTIGDKFASRHGQKGILSRLWPAEDMPFTESGMVPDILFNPHGFPSRMTIGMLIESMAGKSAALHGLCHDATPFIFSEENSALEYFGEMLKAAGYNFYGTERLYSGISGLELEADIFIGVVYYQRLRHMVSDKFQVRTTGARDRVTNQPIGGRNVQGGIRFGEMERDALLAHGTSFLLHDRLFNCSDRSVAHVCVKCGSLLSPLLEKPPPSWSAMRNRKYNCTLCSRSDTIDTVSVPYVFRYFVAELAAMNIKVKLDVV
uniprot
proteins
disease_involvement
DISEASE: Treacher Collins syndrome 4 (TCS4) [MIM:618939]: A form of Treacher Collins syndrome, a disorder of craniofacial development. Treacher Collins syndrome is characterized by a combination of bilateral downward slanting of the palpebral fissures, colobomas of the lower eyelids with a paucity of eyelashes medial to the defect, hypoplasia of the facial bones, cleft palate, malformation of the external ears, atresia of the external auditory canals, and bilateral conductive hearing loss. TCS4 inheritance pattern is autosomal dominant. {ECO:0000269|PubMed:31649276}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
2.7.7.6
uniprot
proteins
function
FUNCTION: Catalytic core component of RNA polymerase I (Pol I), a DNA-dependent RNA polymerase which synthesizes ribosomal RNA precursors using the four ribonucleoside triphosphates as substrates. Transcribes 47S pre-rRNAs from multicopy rRNA gene clusters, giving rise to 5.8S, 18S and 28S ribosomal RNAs (PubMed:11250903, PubMed:11283244, PubMed:16858408, PubMed:34671025, PubMed:34887565, PubMed:36271492). Pol I-mediated transcription cycle proceeds through transcription initiation, transcription elongation and transcription termination stages. During transcription initiation, Pol I pre-initiation complex (PIC) is recruited by the selectivity factor 1 (SL1/TIF-IB) complex bound to the core promoter that precedes an rDNA repeat unit. The PIC assembly bends the promoter favoring the formation of the transcription bubble and promoter escape. 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. Highly processive, assembles in structures referred to as 'Miller trees' where many elongating Pol I complexes queue and transcribe the same rDNA coding regions. At terminator sequences downstream of the rDNA gene, PTRF interacts with Pol I and halts Pol I transcription leading to the release of the RNA transcript and polymerase from the DNA (PubMed:11250903, PubMed:11283244, PubMed:16858408, PubMed:34671025, PubMed:34887565, PubMed:36271492). Forms Pol I active center together with the largest subunit POLR1A/RPA1. Appends one nucleotide at a time to the 3' end of the nascent RNA, with POLR1A/RPA1 contributing a Mg(2+)-coordinating DxDGD motif, and POLR1B/RPA2 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 the 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. Has proofreading activity: Pauses and backtracks to allow the cleavage of a missincorporated nucleotide via POLR1H/RPA12. High Pol I processivity is associated with decreased transcription fidelity (By similarity) (PubMed:11250903, PubMed:11283244, PubMed:16809778, PubMed:16858408, PubMed:34671025, PubMed:34887565, PubMed:36271492). {ECO:0000250|UniProtKB:P10964, ECO:0000269|PubMed:11250903, ECO:0000269|PubMed:11283244, ECO:0000269|PubMed:16809778, ECO:0000269|PubMed:16858408, ECO:0000269|PubMed:34671025, ECO:0000269|PubMed:34887565, ECO:0000269|PubMed:36271492}.
uniprot
proteins
mass_dalton
128229
uniprot
proteins
protein_family
RNA polymerase beta chain family
uniprot
proteins
pubmed
11250903
uniprot
proteins
pubmed
11283244
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15815621
uniprot
proteins
pubmed
16809778
uniprot
proteins
pubmed
16858408
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
31649276
uniprot
proteins
pubmed
34671025
uniprot
proteins
pubmed
34887565
uniprot
proteins
pubmed
36271492
uniprot
proteins
sequence_length
1135
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000305|PubMed:34887565, ECO:0000305|PubMed:36271492}. Chromosome {ECO:0000250|UniProtKB:P70700}.
uniprot
proteins