RPA12_HUMAN
ID RPA12_HUMAN Reviewed; 126 AA.
AC Q9P1U0;
DT 02-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=DNA-directed RNA polymerase I subunit RPA12 {ECO:0000305|Ref.2};
DE AltName: Full=DNA-directed RNA polymerase I subunit H {ECO:0000312|HGNC:HGNC:13182};
DE AltName: Full=Zinc ribbon domain-containing protein 1 {ECO:0000303|PubMed:10662553};
GN Name=POLR1H {ECO:0000312|HGNC:HGNC:13182};
GN Synonyms=RPA12 {ECO:0000303|Ref.2}, ZNRD1 {ECO:0000303|PubMed:10662553};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10662553; DOI=10.1006/geno.1999.6040;
RA Fan W., Wang Z., Kyzysztof F., Prange C., Lennon G.;
RT "A new zinc ribbon gene (ZNRD1) is cloned from the human MHC class I
RT region.";
RL Genomics 63:139-141(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RA Shematorova E.K., Lebedenko E.N., Shpakovski G.V.;
RT "Complementation studies of Rpa12, small specific subunit of nuclear RNA
RT polymerase I.";
RL Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skeletal muscle, and Skin;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC Component of RNA polymerase I which synthesizes ribosomal RNA
CC precursors.
CC -!- SUBUNIT: Component of the RNA polymerase I (Pol I) complex consisting
CC of at least 13 subunits. {ECO:0000250}.
CC -!- INTERACTION:
CC Q9P1U0; P54253: ATXN1; NbExp=3; IntAct=EBI-355434, EBI-930964;
CC Q9P1U0; P06396: GSN; NbExp=3; IntAct=EBI-355434, EBI-351506;
CC Q9P1U0; Q8N7C3: TRIML2; NbExp=3; IntAct=EBI-355434, EBI-11059915;
CC Q9P1U0; Q9Y649; NbExp=3; IntAct=EBI-355434, EBI-25900580;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:P32529}.
CC -!- SIMILARITY: Belongs to the archaeal RpoM/eukaryotic RPA12/RPB9/RPC11
CC RNA polymerase family. {ECO:0000305}.
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DR EMBL; AF024617; AAF40469.1; -; mRNA.
DR EMBL; AF230337; AAG50159.1; -; mRNA.
DR EMBL; AF230338; AAG50160.1; -; Genomic_DNA.
DR EMBL; CR457109; CAG33390.1; -; mRNA.
DR EMBL; AL669914; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL671859; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL845439; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX088647; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC010898; AAH10898.1; -; mRNA.
DR EMBL; BC050608; AAH50608.1; -; mRNA.
DR CCDS; CCDS4670.1; -.
DR RefSeq; NP_001265714.1; NM_001278785.1.
DR RefSeq; NP_001265715.1; NM_001278786.1.
DR RefSeq; NP_055411.1; NM_014596.5.
DR RefSeq; NP_740753.1; NM_170783.3.
DR PDB; 7OB9; EM; 2.70 A; I=1-126.
DR PDB; 7OBA; EM; 3.10 A; I=1-126.
DR PDB; 7OBB; EM; 3.30 A; I=1-126.
DR PDB; 7VBA; EM; 2.89 A; I=1-126.
DR PDB; 7VBB; EM; 2.81 A; I=1-126.
DR PDB; 7VBC; EM; 3.01 A; I=1-126.
DR PDBsum; 7OB9; -.
DR PDBsum; 7OBA; -.
DR PDBsum; 7OBB; -.
DR PDBsum; 7VBA; -.
DR PDBsum; 7VBB; -.
DR PDBsum; 7VBC; -.
DR AlphaFoldDB; Q9P1U0; -.
DR SMR; Q9P1U0; -.
DR BioGRID; 119050; 72.
DR IntAct; Q9P1U0; 24.
DR MINT; Q9P1U0; -.
DR STRING; 9606.ENSP00000331111; -.
DR GlyGen; Q9P1U0; 1 site, 1 O-linked glycan (1 site).
DR BioMuta; ZNRD1; -.
DR DMDM; 71649339; -.
DR EPD; Q9P1U0; -.
DR jPOST; Q9P1U0; -.
DR MassIVE; Q9P1U0; -.
DR MaxQB; Q9P1U0; -.
DR PaxDb; Q9P1U0; -.
DR PeptideAtlas; Q9P1U0; -.
DR PRIDE; Q9P1U0; -.
DR ProteomicsDB; 83665; -.
DR Antibodypedia; 26188; 155 antibodies from 21 providers.
DR DNASU; 30834; -.
DR Ensembl; ENST00000332435.10; ENSP00000331111.5; ENSG00000066379.15.
DR Ensembl; ENST00000359374.8; ENSP00000352333.4; ENSG00000066379.15.
DR Ensembl; ENST00000376782.6; ENSP00000365978.2; ENSG00000066379.15.
DR Ensembl; ENST00000376785.2; ENSP00000365981.2; ENSG00000066379.15.
DR Ensembl; ENST00000383613.6; ENSP00000373108.2; ENSG00000206502.8.
DR Ensembl; ENST00000400659.1; ENSP00000383500.1; ENSG00000206502.8.
DR Ensembl; ENST00000400660.7; ENSP00000383501.3; ENSG00000206502.8.
DR Ensembl; ENST00000400662.7; ENSP00000383503.3; ENSG00000206502.8.
DR Ensembl; ENST00000412396.1; ENSP00000396922.1; ENSG00000233795.6.
DR Ensembl; ENST00000417275.6; ENSP00000397636.2; ENSG00000233795.6.
DR Ensembl; ENST00000417738.6; ENSP00000407715.2; ENSG00000235176.6.
DR Ensembl; ENST00000420100.5; ENSP00000410530.1; ENSG00000236808.6.
DR Ensembl; ENST00000428913.5; ENSP00000414110.1; ENSG00000224859.6.
DR Ensembl; ENST00000429558.5; ENSP00000410954.1; ENSG00000235176.6.
DR Ensembl; ENST00000431032.5; ENSP00000416599.1; ENSG00000236949.6.
DR Ensembl; ENST00000431416.1; ENSP00000395065.1; ENSG00000235176.6.
DR Ensembl; ENST00000432227.6; ENSP00000399302.2; ENSG00000236808.6.
DR Ensembl; ENST00000432545.1; ENSP00000405264.1; ENSG00000236949.6.
DR Ensembl; ENST00000432904.6; ENSP00000414720.2; ENSG00000236808.6.
DR Ensembl; ENST00000433264.6; ENSP00000393236.2; ENSG00000236949.6.
DR Ensembl; ENST00000437373.6; ENSP00000410127.2; ENSG00000236949.6.
DR Ensembl; ENST00000437507.5; ENSP00000412369.1; ENSG00000235443.6.
DR Ensembl; ENST00000441251.6; ENSP00000413265.2; ENSG00000235176.6.
DR Ensembl; ENST00000442585.6; ENSP00000394779.2; ENSG00000233795.6.
DR Ensembl; ENST00000443142.6; ENSP00000391809.2; ENSG00000235443.6.
DR Ensembl; ENST00000443494.6; ENSP00000395397.2; ENSG00000235443.6.
DR Ensembl; ENST00000444027.1; ENSP00000396661.1; ENSG00000236808.6.
DR Ensembl; ENST00000444794.5; ENSP00000407364.1; ENSG00000233795.6.
DR Ensembl; ENST00000446493.6; ENSP00000399966.2; ENSG00000224859.6.
DR Ensembl; ENST00000451875.1; ENSP00000387914.1; ENSG00000224859.6.
DR Ensembl; ENST00000453694.1; ENSP00000405636.1; ENSG00000235443.6.
DR Ensembl; ENST00000455948.6; ENSP00000402198.2; ENSG00000224859.6.
DR GeneID; 30834; -.
DR KEGG; hsa:30834; -.
DR MANE-Select; ENST00000332435.10; ENSP00000331111.5; NM_170783.4; NP_740753.1.
DR UCSC; uc003noz.5; human.
DR CTD; 30834; -.
DR DisGeNET; 30834; -.
DR GeneCards; POLR1H; -.
DR HGNC; HGNC:13182; POLR1H.
DR HPA; ENSG00000066379; Low tissue specificity.
DR MIM; 607525; gene.
DR neXtProt; NX_Q9P1U0; -.
DR OpenTargets; ENSG00000066379; -.
DR PharmGKB; PA37754; -.
DR VEuPathDB; HostDB:ENSG00000066379; -.
DR eggNOG; KOG2907; Eukaryota.
DR GeneTree; ENSGT00390000008126; -.
DR HOGENOM; CLU_093932_1_2_1; -.
DR InParanoid; Q9P1U0; -.
DR OMA; EMQYHTL; -.
DR OrthoDB; 1456544at2759; -.
DR PhylomeDB; Q9P1U0; -.
DR TreeFam; TF313881; -.
DR PathwayCommons; Q9P1U0; -.
DR Reactome; R-HSA-427413; NoRC negatively regulates rRNA expression.
DR Reactome; R-HSA-5250924; B-WICH complex positively regulates rRNA expression.
DR Reactome; R-HSA-73762; RNA Polymerase I Transcription Initiation.
DR Reactome; R-HSA-73772; RNA Polymerase I Promoter Escape.
DR Reactome; R-HSA-73863; RNA Polymerase I Transcription Termination.
DR SignaLink; Q9P1U0; -.
DR SIGNOR; Q9P1U0; -.
DR BioGRID-ORCS; 30834; 644 hits in 1090 CRISPR screens.
DR ChiTaRS; ZNRD1; human.
DR GeneWiki; ZNRD1; -.
DR GenomeRNAi; 30834; -.
DR Pharos; Q9P1U0; Tbio.
DR PRO; PR:Q9P1U0; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q9P1U0; protein.
DR Bgee; ENSG00000066379; Expressed in granulocyte and 97 other tissues.
DR ExpressionAtlas; Q9P1U0; baseline and differential.
DR Genevisible; Q9P1U0; HS.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005736; C:RNA polymerase I complex; IBA:GO_Central.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006379; P:mRNA cleavage; IEA:InterPro.
DR GO; GO:0006139; P:nucleobase-containing compound metabolic process; TAS:ProtInc.
DR GO; GO:0006363; P:termination of RNA polymerase I transcription; IBA:GO_Central.
DR CDD; cd10507; Zn-ribbon_RPA12; 1.
DR InterPro; IPR019761; DNA-dir_RNA_pol-M_15_CS.
DR InterPro; IPR012164; Rpa12/Rpb9/Rpc10/TFS.
DR InterPro; IPR034004; Zn_ribbon_RPA12_C.
DR InterPro; IPR001222; Znf_TFIIS.
DR PANTHER; PTHR11239; PTHR11239; 1.
DR Pfam; PF01096; TFIIS_C; 1.
DR PIRSF; PIRSF005586; RNApol_RpoM; 1.
DR SMART; SM00440; ZnF_C2C2; 1.
DR PROSITE; PS01030; RNA_POL_M_15KD; 1.
DR PROSITE; PS00466; ZF_TFIIS_1; 1.
DR PROSITE; PS51133; ZF_TFIIS_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA-directed RNA polymerase; Metal-binding; Nucleus;
KW Reference proteome; Transcription; Zinc; Zinc-finger.
FT CHAIN 1..126
FT /note="DNA-directed RNA polymerase I subunit RPA12"
FT /id="PRO_0000121460"
FT ZN_FING 20..41
FT /note="C4-type"
FT /evidence="ECO:0000255"
FT ZN_FING 83..123
FT /note="TFIIS-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00472"
FT BINDING 87
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00472"
FT BINDING 90
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00472"
FT BINDING 115
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00472"
FT BINDING 118
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00472"
FT VARIANT 14
FT /note="Q -> H (in dbSNP:rs17187658)"
FT /id="VAR_052287"
FT STRAND 12..14
FT /evidence="ECO:0007829|PDB:7OBB"
FT TURN 21..23
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 32..37
FT /evidence="ECO:0007829|PDB:7OB9"
FT TURN 39..41
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 44..46
FT /evidence="ECO:0007829|PDB:7OB9"
FT HELIX 47..52
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 57..62
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 88..90
FT /evidence="ECO:0007829|PDB:7OBA"
FT STRAND 95..99
FT /evidence="ECO:0007829|PDB:7OBA"
FT STRAND 105..107
FT /evidence="ECO:0007829|PDB:7OBB"
FT STRAND 111..118
FT /evidence="ECO:0007829|PDB:7OBA"
FT STRAND 121..124
FT /evidence="ECO:0007829|PDB:7OBA"
SQ SEQUENCE 126 AA; 13904 MW; C678AC7132A91432 CRC64;
MSVMDLANTC SSFQSDLDFC SDCGSVLPLP GAQDTVTCIR CGFNINVRDF EGKVVKTSVV
FHQLGTAMPM SVEEGPECQG PVVDRRCPRC GHEGMAYHTR QMRSADEGQT VFYTCTNCKF
QEKEDS
