O95602 (RPA1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
DNA-directed RNA polymerase I subunit RPA1
Short name=RNA polymerase I subunit A1
EC=2.7.7.6

Alternative name(s):
A190
DNA-directed RNA polymerase I largest subunit
DNA-directed RNA polymerase I subunit A
RNA polymerase I 194 kDa subunit
Short name=RPA194

Gene names

Name:

POLR1A

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	1720 AA.
Sequence status	Complete.
Protein existence	Evidence 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. Largest and catalytic core component of RNA polymerase I which synthesizes ribosomal RNA precursors. Forms the polymerase active center together with the second largest subunit. A single stranded DNA template strand of the promoter is positioned within the central active site cleft of Pol I. A bridging helix emanates from RPA1 and crosses the cleft near the catalytic site and is thought to promote translocation of Pol I by acting as a ratchet that moves the RNA-DNA hybrid through the active site by switching from straight to bent conformations at each step of nucleotide addition By similarity.
Catalytic activity	Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1).
Subunit structure	Component of the RNA polymerase I (Pol I) complex consisting of at least 13 subunits. Interacts with MYO1C. Interacts with ERBB2 By similarity. Ref.10
Subcellular location	Nucleus › nucleolus By similarity.
Sequence similarities	Belongs to the RNA polymerase beta' chain family.
Sequence caution	The sequence AAC99959.1 differs from that shown. Reason: Frameshift at positions 1114 and 1469. The sequence AAD09356.1 differs from that shown. Reason: Frameshift at position 1114.

Ontologies

Keywords
Biological process	Transcription
Cellular component	DNA-directed RNA polymerase Nucleus
Coding sequence diversity	Polymorphism
Ligand	Magnesium Metal-binding Zinc
Molecular function	Nucleotidyltransferase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	termination of RNA polymerase I transcription Traceable author statement. Source: Reactome transcription elongation from RNA polymerase I promoter Traceable author statement. Source: Reactome transcription initiation from RNA polymerase I promoter Traceable author statement. Source: Reactome
Cellular component	DNA-directed RNA polymerase I complex Non-traceable author statement. Source: UniProtKB nucleoplasm Traceable author statement. Source: Reactome
Molecular function	DNA binding Inferred from electronic annotation. Source: InterPro DNA-directed RNA polymerase activity Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction Ref.10. Source: IntAct zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ERBB2	P04626	16	EBI-359472,EBI-641062

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1720	1720	DNA-directed RNA polymerase I subunit RPA1		PRO_0000073923
Regions
	Region	961 – 973	13	Bridging helix By similarity
Sites
	Metal binding	64	1	Zinc By similarity
	Metal binding	67	1	Zinc By similarity
	Metal binding	74	1	Zinc By similarity
	Metal binding	77	1	Zinc By similarity
	Metal binding	588	1	Magnesium; catalytic By similarity
	Metal binding	590	1	Magnesium; catalytic By similarity
	Metal binding	592	1	Magnesium; catalytic By similarity
Amino acid modifications
	Modified residue	1386	1	Phosphoserine Ref.8
	Modified residue	1580	1	Phosphothreonine Ref.7
Natural variations
	Natural variant	150	1	P → A. Ref.1 Ref.3 Corresponds to variant rs4832242 [ dbSNP | Ensembl ].		VAR_047493
	Natural variant	349	1	Q → E. Corresponds to variant rs17026866 [ dbSNP | Ensembl ].		VAR_047494
	Natural variant	364	1	K → E. Corresponds to variant rs35239368 [ dbSNP | Ensembl ].		VAR_047495
	Natural variant	396	1	S → N. Corresponds to variant rs35443467 [ dbSNP | Ensembl ].		VAR_047496
	Natural variant	815	1	I → V. Corresponds to variant rs34302587 [ dbSNP | Ensembl ].		VAR_047497
	Natural variant	1141	1	A → T. Corresponds to variant rs34892520 [ dbSNP | Ensembl ].		VAR_047498
	Natural variant	1608	1	I → M. Corresponds to variant rs35093541 [ dbSNP | Ensembl ].		VAR_047499
Experimental info
	Sequence conflict	143	1	N → S in AAC99959. Ref.1
	Sequence conflict	309	1	Y → S in AAC99959. Ref.1
	Sequence conflict	411	1	M → R in AAC99959. Ref.1
	Sequence conflict	439 – 440	2	YA → ST in AAC99959. Ref.1
	Sequence conflict	808	1	A → R in AAC99959. Ref.1
	Sequence conflict	893	1	S → T in AAC99959. Ref.1
	Sequence conflict	896	1	M → L in AAC99959. Ref.1
	Sequence conflict	925 – 926	2	RP → ST in AAC99959. Ref.1
	Sequence conflict	986	1	G → A in AAD09356. Ref.1
	Sequence conflict	1371 – 1373	3	RAT → TRI in AAD09356. Ref.1
	Sequence conflict	1470 – 1471	2	Missing in AAC99959. Ref.1
	Sequence conflict	1616	1	Missing in AAC99959. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	O95602 [UniParc]. Last modified November 25, 2008. Version 2. Checksum: AD4BA543FFB98DC6	FASTA	1,720	194,811
	10 20 30 40 50 60 MLISKNMPWR RLQGISFGMY SAEELKKLSV KSITNPRYLD SLGNPSANGL YDLALGPADS 70 80 90 100 110 120 KEVCSTCVQD FSNCSGHLGH IELPLTVYNP LLFDKLYLLL RGSCLNCHML TCPRAVIHLL 130 140 150 160 170 180 LCQLRVLEVG ALQAVYELER ILNRFLEENP DPSASEIREE LEQYTTEIVQ NNLLGSQGAH 190 200 210 220 230 240 VKNVCESKSK LIALFWKAHM NAKRCPHCKT GRSVVRKEHN SKLTITFPAM VHRTAGQKDS 250 260 270 280 290 300 EPLGIEEAQI GKRGYLTPTS AREHLSALWK NEGFFLNYLF SGMDDDGMES RFNPSVFFLD 310 320 330 340 350 360 FLVVPPSRYR PVSRLGDQMF TNGQTVNLQA VMKDVVLIRK LLALMAQEQK LPEEVATPTT 370 380 390 400 410 420 DEEKDSLIAI DRSFLSTLPG QSLIDKLYNI WIRLQSHVNI VFDSEMDKLM MDKYPGIRQI 430 440 450 460 470 480 LEKKEGLFRK HMMGKRVDYA ARSVICPDMY INTNEIGIPM VFATKLTYPQ PVTPWNVQEL 490 500 510 520 530 540 RQAVINGPNV HPGASMVINE DGSRTALSAV DMTQREAVAK QLLTPATGAP KPQGTKIVCR 550 560 570 580 590 600 HVKNGDILLL NRQPTLHRPS IQAHRARILP EEKVLRLHYA NCKAYNADFD GDEMNAHFPQ 610 620 630 640 650 660 SELGRAEAYV LACTDQQYLV PKDGQPLAGL IQDHMVSGAS MTTRGCFFTR EHYMELVYRG 670 680 690 700 710 720 LTDKVGRVKL LSPSILKPFP LWTGKQVVST LLINIIPEDH IPLNLSGKAK ITGKAWVKET 730 740 750 760 770 780 PRSVPGFNPD SMCESQVIIR EGELLCGVLD KAHYGSSAYG LVHCCYEIYG GETSGKVLTC 790 800 810 820 830 840 LARLFTAYLQ LYRGFTLGVE DILVKPKADV KRQRIIEEST HCGPQAVRAA LNLPEAASYD 850 860 870 880 890 900 EVRGKWQDAH LGKDQRDFNM IDLKFKEEVN HYSNEINKAC MPFGLHRQFP ENSLQMMVQS 910 920 930 940 950 960 GAKGSTVNTM QISCLLGQIE LEGRRPPLMA SGKSLPCFEP YEFTPRAGGF VTGRFLTGIK 970 980 990 1000 1010 1020 PPEFFFHCMA GREGLVDTAV KTSRSGYLQR CIIKHLEGLV VQYDLTVRDS DGSVVQFLYG 1030 1040 1050 1060 1070 1080 EDGLDIPKTQ FLQPKQFPFL ASNYEVIMKS QHLHEVLSRA DPKKALHHFR AIKKWQSKHP 1090 1100 1110 1120 1130 1140 NTLLRRGAFL SYSQKIQEAV KALKLESENR NGRSPGTQEM LRMWYELDEE SRRKYQKKAA 1150 1160 1170 1180 1190 1200 ACPDPSLSVW RPDIYFASVS ETFETKVDDY SQEWAAQTEK SYEKSELSLD RLRTLLQLKW 1210 1220 1230 1240 1250 1260 QRSLCEPGEA VGLLAAQSIG EPSTQMTLNT FHFAGRGEMN VTLGIPRLRE ILMVASANIK 1270 1280 1290 1300 1310 1320 TPMMSVPVLN TKKALKRVKS LKKQLTRVCL GEVLQKIDVQ ESFCMEEKQN KFQVYQLRFQ 1330 1340 1350 1360 1370 1380 FLPHAYYQQE KCLRPEDILR FMETRFFKLL MESIKKKNNK ASAFRNVNTR RATQRDLDNA 1390 1400 1410 1420 1430 1440 GELGRSRGEQ EGDEEEEGHI VDAEAEEGDA DASDAKRKEK QEEEVDYESE EEEEREGEEN 1450 1460 1470 1480 1490 1500 DDEDMQEERN PHREGARKTQ EQDEEVGLGT EEDPSLPALL TQPRKPTHSQ EPQGPEAMER 1510 1520 1530 1540 1550 1560 RVQAVREIHP FIDDYQYDTE ESLWCQVTVK LPLMKINFDM SSLVVSLAHG AVIYATKGIT 1570 1580 1590 1600 1610 1620 RCLLNETTNN KNEKELVLNT EGINLPELFK YAEVLDLRRL YSNDIHAIAN TYGIEAALRV 1630 1640 1650 1660 1670 1680 IEKEIKDVFA VYGIAVDPRH LSLVADYMCF EGVYKPLNRF GIRSNSSPLQ QMTFETSFQF 1690 1700 1710 1720 LKQATMLGSH DELRSPSACL VVGKVVRGGT GLFELKQPLR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	Wang D., Stetler D.A. Submitted (AUG-1995) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ALA-150.
[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. , 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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Testis.
[3]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT ALA-150.
[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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Colon.
[5]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed: 17974005] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1626-1720. Tissue: Uterus.
[6]	"RNA polymerase I-specific subunit CAST/hPAF49 has a role in the activation of transcription by upstream binding factor." Panov K.I., Panova T.B., Gadal O., Nishiyama K., Saito T., Russell J., Zomerdijk J.C.B.M. Mol. Cell. Biol. 26:5436-5448(2006) [PubMed: 16809778] [Abstract] Cited for: IDENTIFICATION IN THE RNA POL I COMPLEX.
[7]	"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column." Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y. Anal. Sci. 24:161-166(2008) [PubMed: 18187866] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1580, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[8]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1386, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[9]	"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: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]	"Nuclear ErbB2 enhances translation and cell growth by activating transcription of ribosomal RNA genes." Li L.Y., Chen H., Hsieh Y.H., Wang Y.N., Chu H.J., Chen Y.H., Chen H.Y., Chien P.J., Ma H.T., Tsai H.C., Lai C.C., Sher Y.P., Lien H.C., Tsai C.H., Hung M.C. Cancer Res. 71:4269-4279(2011) [PubMed: 21555369] [Abstract] Cited for: INTERACTION WITH ERBB2.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U33460 mRNA. Translation: AAC99959.1. Frameshift. U33823, U33824 Transcribed RNA. Translation: AAD09356.1. Frameshift. AK302458 mRNA. Translation: BAH13716.1. CH471053 Genomic DNA. Translation: EAW99467.1. CH471053 Genomic DNA. Translation: EAW99469.1. BC117173 mRNA. Translation: AAI17174.1. BC126303 mRNA. Translation: AAI26304.1. AL117467 mRNA. Translation: CAB55942.1.
IPI	IPI00031960.
PIR	T17252.
RefSeq	NP_056240.2. NM_015425.3.
UniGene	Hs.531818.
3D structure databases
ProteinModelPortal	O95602.
SMR	O95602. Positions 5-1720.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-27537N.
IntAct	O95602. 9 interactions.
MINT	MINT-111492.
STRING	O95602.
PTM databases
PhosphoSite	O95602.
2D gel databases
SWISS-2DPAGE	O95602.
Proteomic databases
PRIDE	O95602.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000263857; ENSP00000263857; ENSG00000068654.
GeneID	25885.
KEGG	hsa:25885.
Organism-specific databases
CTD	25885.
GeneCards	GC02M086253.
H-InvDB	HIX0002233.
HGNC	HGNC:17264. POLR1A.
HPA	CAB010145.
neXtProt	NX_O95602.
PharmGKB	PA134891380.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG08294.
HOGENOM	HBG598940.
HOVERGEN	HBG017741.
InParanoid	O95602.
OMA	VPPTRFR.
OrthoDB	EOG41VK23.
PhylomeDB	O95602.
Enzyme and pathway databases
Reactome	REACT_1788. Transcription.
Gene expression databases
ArrayExpress	O95602.
Bgee	O95602.
CleanEx	HS_POLR1A.
Genevestigator	O95602.
GermOnline	ENSG00000068654. Homo sapiens.
Family and domain databases
InterPro	IPR015699. DNA-dir_RNA_pol1_lsu. IPR000722. RNA_pol_asu. IPR006592. RNA_pol_N. IPR007080. RNA_pol_Rpb1_1. IPR007066. RNA_pol_Rpb1_3. IPR007083. RNA_pol_Rpb1_4. IPR007081. RNA_pol_Rpb1_5. [Graphical view]
KO	K02999.
PANTHER	PTHR19376:SF11. RNA_polyI. 1 hit.
Pfam	PF04997. RNA_pol_Rpb1_1. 1 hit. PF00623. RNA_pol_Rpb1_2. 1 hit. PF04983. RNA_pol_Rpb1_3. 1 hit. PF05000. RNA_pol_Rpb1_4. 1 hit. PF04998. RNA_pol_Rpb1_5. 1 hit. [Graphical view]
SMART	SM00663. RPOLA_N. 1 hit. [Graphical view]
ProtoNet	Search...
Other
PMAP-CutDB	O95602.

Entry information

Entry name

RPA1_HUMAN

Accession

Primary (citable) accession number: O95602
Secondary accession number(s): B7Z7T0 , D6W5M0, Q0VG05, Q9UEH0, Q9UFT9

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	November 25, 2008
Last modified:	January 25, 2012
This is version 108 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.