Overview
| Uniprot ID | O95602 |
| Protein Name | DNA-directed RNA polymerase I subunit RPA1 |
| Gene Name | POLR1A |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position |
Flanking peptide |
| 1360 |
SIKKKNNKASAFRNV |
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 second largest subunit POLR1B/RPA2. 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:16858408, PubMed:34671025, PubMed:34887565, PubMed:36271492)
Protein Sequence
10
MLISKNMPWR
20
RLQGISFGMY
30
SAEELKKLSV
40
KSITNPRYLD
50
SLGNPSANGL
60
YDLALGPADS
70
KEVCSTCVQD
80
FSNCSGHLGH
90
IELPLTVYNP
100
LLFDKLYLLL
110
RGSCLNCHML
120
TCPRAVIHLL
130
LCQLRVLEVG
140
ALQAVYELER
150
ILNRFLEENP
160
DPSASEIREE
170
LEQYTTEIVQ
180
NNLLGSQGAH
190
VKNVCESKSK
200
LIALFWKAHM
210
NAKRCPHCKT
220
GRSVVRKEHN
230
SKLTITFPAM
240
VHRTAGQKDS
250
EPLGIEEAQI
260
GKRGYLTPTS
270
AREHLSALWK
280
NEGFFLNYLF
290
SGMDDDGMES
300
RFNPSVFFLD
310
FLVVPPSRYR
320
PVSRLGDQMF
330
TNGQTVNLQA
340
VMKDVVLIRK
350
LLALMAQEQK
360
LPEEVATPTT
370
DEEKDSLIAI
380
DRSFLSTLPG
390
QSLIDKLYNI
400
WIRLQSHVNI
410
VFDSEMDKLM
420
MDKYPGIRQI
430
LEKKEGLFRK
440
HMMGKRVDYA
450
ARSVICPDMY
460
INTNEIGIPM
470
VFATKLTYPQ
480
PVTPWNVQEL
490
RQAVINGPNV
500
HPGASMVINE
510
DGSRTALSAV
520
DMTQREAVAK
530
QLLTPATGAP
540
KPQGTKIVCR
550
HVKNGDILLL
560
NRQPTLHRPS
570
IQAHRARILP
580
EEKVLRLHYA
590
NCKAYNADFD
600
GDEMNAHFPQ
610
SELGRAEAYV
620
LACTDQQYLV
630
PKDGQPLAGL
640
IQDHMVSGAS
650
MTTRGCFFTR
660
EHYMELVYRG
670
LTDKVGRVKL
680
LSPSILKPFP
690
LWTGKQVVST
700
LLINIIPEDH
710
IPLNLSGKAK
720
ITGKAWVKET
730
PRSVPGFNPD
740
SMCESQVIIR
750
EGELLCGVLD
760
KAHYGSSAYG
770
LVHCCYEIYG
780
GETSGKVLTC
790
LARLFTAYLQ
800
LYRGFTLGVE
810
DILVKPKADV
820
KRQRIIEEST
830
HCGPQAVRAA
840
LNLPEAASYD
850
EVRGKWQDAH
860
LGKDQRDFNM
870
IDLKFKEEVN
880
HYSNEINKAC
890
MPFGLHRQFP
900
ENSLQMMVQS
910
GAKGSTVNTM
920
QISCLLGQIE
930
LEGRRPPLMA
940
SGKSLPCFEP
950
YEFTPRAGGF
960
VTGRFLTGIK
970
PPEFFFHCMA
980
GREGLVDTAV
990
KTSRSGYLQR
1000
CIIKHLEGLV
1010
VQYDLTVRDS
1020
DGSVVQFLYG
1030
EDGLDIPKTQ
1040
FLQPKQFPFL
1050
ASNYEVIMKS
1060
QHLHEVLSRA
1070
DPKKALHHFR
1080
AIKKWQSKHP
1090
NTLLRRGAFL
1100
SYSQKIQEAV
1110
KALKLESENR
1120
NGRSPGTQEM
1130
LRMWYELDEE
1140
SRRKYQKKAA
1150
ACPDPSLSVW
1160
RPDIYFASVS
1170
ETFETKVDDY
1180
SQEWAAQTEK
1190
SYEKSELSLD
1200
RLRTLLQLKW
1210
QRSLCEPGEA
1220
VGLLAAQSIG
1230
EPSTQMTLNT
1240
FHFAGRGEMN
1250
VTLGIPRLRE
1260
ILMVASANIK
1270
TPMMSVPVLN
1280
TKKALKRVKS
1290
LKKQLTRVCL
1300
GEVLQKIDVQ
1310
ESFCMEEKQN
1320
KFQVYQLRFQ
1330
FLPHAYYQQE
1340
KCLRPEDILR
1350
FMETRFFKLL
1360
MESIKKKNNK
1370
ASAFRNVNTR
1380
RATQRDLDNA
1390
GELGRSRGEQ
1400
EGDEEEEGHI
1410
VDAEAEEGDA
1420
DASDAKRKEK
1430
QEEEVDYESE
1440
EEEEREGEEN
1450
DDEDMQEERN
1460
PHREGARKTQ
1470
EQDEEVGLGT
1480
EEDPSLPALL
1490
TQPRKPTHSQ
1500
EPQGPEAMER
1510
RVQAVREIHP
1520
FIDDYQYDTE
1530
ESLWCQVTVK
1540
LPLMKINFDM
1550
SSLVVSLAHG
1560
AVIYATKGIT
1570
RCLLNETTNN
1580
KNEKELVLNT
1590
EGINLPELFK
1600
YAEVLDLRRL
1610
YSNDIHAIAN
1620
TYGIEAALRV
1630
IEKEIKDVFA
1640
VYGIAVDPRH
1650
LSLVADYMCF
1660
EGVYKPLNRF
1670
GIRSNSSPLQ
1680
QMTFETSFQF
1690
LKQATMLGSH
1700
DELRSPSACL
1710
VVGKVVRGGT
1720
GLFELKQPLR
Gene Ontology
| Classification |
GO ID |
Description |
| Cellular Component |
GO:0000785 |
chromatin |
| Cellular Component |
GO:0005694 |
chromosome |
| Cellular Component |
GO:0001650 |
fibrillar center |
| Cellular Component |
GO:0005654 |
nucleoplasm |
| Cellular Component |
GO:0005634 |
nucleus |
| Cellular Component |
GO:0005736 |
RNA polymerase I complex |
| Molecular Function |
GO:0003682 |
chromatin binding |
| Molecular Function |
GO:0003677 |
DNA binding |
| Molecular Function |
GO:0003899 |
DNA-directed RNA polymerase activity |
| Molecular Function |
GO:0071667 |
DNA/RNA hybrid binding |
| Molecular Function |
GO:0000287 |
magnesium ion binding |
| Molecular Function |
GO:0008270 |
zinc ion binding |
| Biological Process |
GO:1904750 |
negative regulation of protein localization to nucleolus |
| Biological Process |
GO:0042790 |
nucleolar large rRNA transcription by RNA polymerase I |
| Biological Process |
GO:0006363 |
termination of RNA polymerase I transcription |
| Biological Process |
GO:0006360 |
transcription by RNA polymerase I |
| Biological Process |
GO:0006362 |
transcription elongation by RNA polymerase I |
| Biological Process |
GO:0006361 |
transcription initiation at RNA polymerase I promoter |
Reference
PMID: N/A