ID   RPA34_HUMAN             Reviewed;         510 AA.
AC   O15446; Q32N11; Q7Z5U2; Q9UPF6;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   27-MAR-2024, entry version 178.
DE   RecName: Full=DNA-directed RNA polymerase I subunit RPA34 {ECO:0000305};
DE   AltName: Full=A34.5;
DE   AltName: Full=Antisense to ERCC-1 protein {ECO:0000303|PubMed:9426281};
DE            Short=ASE-1 {ECO:0000303|PubMed:9426281};
DE   AltName: Full=CD3-epsilon-associated protein {ECO:0000303|PubMed:10373416};
DE            Short=CD3E-associated protein {ECO:0000303|PubMed:10373416};
DE   AltName: Full=DNA-directed RNA polymerase I subunit G {ECO:0000312|HGNC:HGNC:24219};
DE   AltName: Full=RNA polymerase I-associated factor PAF49 {ECO:0000305|PubMed:16809778};
GN   Name=POLR1G {ECO:0000312|HGNC:HGNC:24219};
GN   Synonyms=ASE1 {ECO:0000303|PubMed:9426281}, CAST
GN   {ECO:0000303|PubMed:10373416}, CD3EAP {ECO:0000312|HGNC:HGNC:24219},
GN   PAF49 {ECO:0000303|PubMed:16809778};
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] (ISOFORM 1), AND SUBCELLULAR LOCATION.
RC   TISSUE=Serum;
RX   PubMed=9426281; DOI=10.1007/s004120050271;
RA   Whitehead C.M., Winkfein R.J., Fritzler M.J., Rattner J.B.;
RT   "ASE-1: a novel protein of the fibrillar centres of the nucleolus and
RT   nucleolus organizer region of mitotic chromosomes.";
RL   Chromosoma 106:493-502(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION IN T-CELL RECEPTOR
RP   SIGNALING (ISOFORM 2), PHOSPHORYLATION, AND INTERACTION WITH CD3E (ISOFORM
RP   2).
RX   PubMed=10373416; DOI=10.1074/jbc.274.26.18173;
RA   Yamazaki T., Hamano Y., Tashiro H., Itoh K., Nakano H., Miyatake S.,
RA   Saito T.;
RT   "CAST, a novel CD3epsilon-binding protein transducing activation signal for
RT   interleukin-2 production in T cells.";
RL   J. Biol. Chem. 274:18173-18180(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT LYS-504.
RC   TISSUE=Skin, and Testis;
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).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA   Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT   "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT   networks.";
RL   Cell 127:635-648(2006).
RN   [5]
RP   IDENTIFICATION IN THE RNA POL I COMPLEX (ISOFORM 1), IDENTIFICATION BY MASS
RP   SPECTROMETRY, FUNCTION, INTERACTION WITH TAF1A AND UBTF, AND
RP   PHOSPHORYLATION AT TYR-80.
RX   PubMed=16809778; DOI=10.1128/mcb.00230-06;
RA   Panov K.I., Panova T.B., Gadal O., Nishiyama K., Saito T., Russell J.,
RA   Zomerdijk J.C.B.M.;
RT   "RNA polymerase I-specific subunit CAST/hPAF49 has a role in the activation
RT   of transcription by upstream binding factor.";
RL   Mol. Cell. Biol. 26:5436-5448(2006).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-309, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic kidney;
RX   PubMed=17525332; DOI=10.1126/science.1140321;
RA   Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA   Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA   Gygi S.P., Elledge S.J.;
RT   "ATM and ATR substrate analysis reveals extensive protein networks
RT   responsive to DNA damage.";
RL   Science 316:1160-1166(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27; SER-128; SER-136;
RP   SER-172; SER-205; SER-285 AND THR-287, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [8]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT   refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-136 AND SER-490, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA   Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA   Rodionov V., Han D.K.;
RT   "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT   reveals system-wide modulation of protein-protein interactions.";
RL   Sci. Signal. 2:RA46-RA46(2009).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-172 AND SER-285, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT   site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-136, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA   Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT   "System-wide temporal characterization of the proteome and phosphoproteome
RT   of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [12]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-128; SER-136; SER-172;
RP   SER-285 AND THR-287, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RC   TISSUE=Cervix carcinoma, and Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [14]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [15]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-270 AND LYS-314, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25218447; DOI=10.1038/nsmb.2890;
RA   Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA   Vertegaal A.C.;
RT   "Uncovering global SUMOylation signaling networks in a site-specific
RT   manner.";
RL   Nat. Struct. Mol. Biol. 21:927-936(2014).
RN   [16]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-270 AND LYS-314, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25114211; DOI=10.1073/pnas.1413825111;
RA   Impens F., Radoshevich L., Cossart P., Ribet D.;
RT   "Mapping of SUMO sites and analysis of SUMOylation changes induced by
RT   external stimuli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
RN   [17]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-270, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
RA   Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
RA   Vertegaal A.C.;
RT   "SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
RL   Cell Rep. 10:1778-1791(2015).
RN   [18]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-270 AND LYS-314, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA   Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA   Vertegaal A.C.;
RT   "System-wide analysis of SUMOylation dynamics in response to replication
RT   stress reveals novel small ubiquitin-like modified target proteins and
RT   acceptor lysines relevant for genome stability.";
RL   Mol. Cell. Proteomics 14:1419-1434(2015).
RN   [19]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-270 AND LYS-314, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=28112733; DOI=10.1038/nsmb.3366;
RA   Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA   Nielsen M.L.;
RT   "Site-specific mapping of the human SUMO proteome reveals co-modification
RT   with phosphorylation.";
RL   Nat. Struct. Mol. Biol. 24:325-336(2017).
RN   [20]
RP   STRUCTURE BY ELECTRON MICROSCOPY (2.81 ANGSTROMS), FUNCTION OF POL I, AND
RP   SUBUNIT.
RX   PubMed=34671025; DOI=10.1038/s41421-021-00335-5;
RA   Zhao D., Liu W., Chen K., Wu Z., Yang H., Xu Y.;
RT   "Structure of the human RNA polymerase I elongation complex.";
RL   Cell Discov. 7:97-109(2021).
RN   [21]
RP   STRUCTURE BY ELECTRON MICROSCOPY (2.70 ANGSTROMS), FUNCTION OF POL I, AND
RP   SUBUNIT.
RX   PubMed=34887565; DOI=10.1038/s41594-021-00693-4;
RA   Misiaszek A.D., Girbig M., Grotsch H., Baudin F., Murciano B., Lafita A.,
RA   Muller C.W.;
RT   "Cryo-EM structures of human RNA polymerase I.";
RL   Nat. Struct. Mol. Biol. 28:997-1008(2021).
RN   [22]
RP   STRUCTURE BY ELECTRON MICROSCOPY (4.09 ANGSTROMS), FUNCTION OF POL I, AND
RP   SUBUNIT.
RX   PubMed=36271492; DOI=10.26508/lsa.202201568;
RA   Daiss J.L., Pilsl M., Straub K., Bleckmann A., Hocherl M., Heiss F.B.,
RA   Abascal-Palacios G., Ramsay E.P., Tluckova K., Mars J.C., Furtges T.,
RA   Bruckmann A., Rudack T., Bernecky C., Lamour V., Panov K., Vannini A.,
RA   Moss T., Engel C.;
RT   "The human RNA polymerase I structure reveals an HMG-like docking domain
RT   specific to metazoans.";
RL   Life. Sci Alliance 5:1-20(2022).
CC   -!- FUNCTION: Component of RNA polymerase I (Pol I), a DNA-dependent RNA
CC       polymerase which synthesizes ribosomal RNA precursors using the four
CC       ribonucleoside triphosphates as substrates. Involved in UBTF-activated
CC       transcription, presumably at a step following PIC formation.
CC       {ECO:0000269|PubMed:34671025, ECO:0000269|PubMed:34887565,
CC       ECO:0000269|PubMed:36271492}.
CC   -!- FUNCTION: [Isoform 2]: Has been described as a component of preformed
CC       T-cell receptor (TCR) complex. {ECO:0000269|PubMed:10373416}.
CC   -!- SUBUNIT: Component of the RNA polymerase I (Pol I) complex consisting
CC       of 13 subunits: a ten-subunit catalytic core composed of POLR1A/RPA1,
CC       POLR1B/RPA2, POLR1C/RPAC1, POLR1D/RPAC2, POLR1H/RPA12, POLR2E/RPABC1,
CC       POLR2F/RPABC2, POLR2H/RPABC3, POLR2K/RPABC4 and POLR2L/RPABC5; a mobile
CC       stalk subunit POLR1F/RPA43 protruding from the core and additional
CC       subunits homologous to general transcription factors POLR1E/RPA49 and
CC       POLR1G/RPA34. Forms a heterodimer with POLR1E/RPA49 (PubMed:34671025,
CC       PubMed:34887565, PubMed:36271492). Part of Pol I pre-initiation complex
CC       (PIC), in which Pol I core assembles with RRN3 and promoter-bound UTBF
CC       and SL1/TIF-IB complex. Interacts with TAF1A thereby associates with
CC       the SL1/TIF-IB complex. Interacts with UBTF (PubMed:34887565,
CC       PubMed:16809778). Interacts with POLR1E/PRAF1 through its N-terminal
CC       region (By similarity). {ECO:0000250|UniProtKB:Q76KJ5,
CC       ECO:0000269|PubMed:16809778, ECO:0000269|PubMed:34671025,
CC       ECO:0000269|PubMed:34887565, ECO:0000269|PubMed:36271492}.
CC   -!- SUBUNIT: [Isoform 2]: Interacts with CD3E.
CC       {ECO:0000269|PubMed:10373416}.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:9426281}.
CC       Chromosome {ECO:0000269|PubMed:9426281}. Note=Found at the fibrillar
CC       centers of the nucleolus in interphase and during cell division it is
CC       localized to the nucleolus organizer regions of the chromosomes.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=O15446-1; Sequence=Displayed;
CC       Name=2; Synonyms=CAST;
CC         IsoId=O15446-2; Sequence=VSP_017673;
CC   -!- PTM: [Isoform 2]: Undergoes tyrosine phosphorylation upon T-cell
CC       receptor (TCR) stimulation. This phosphorylation has not been confirmed
CC       by other groups. {ECO:0000269|PubMed:10373416}.
CC   -!- PTM: [Isoform 1]: Phosphorylated on tyrosine residues in initiation-
CC       competent Pol I-beta complexes but not in Pol I-alpha complexes.
CC       {ECO:0000269|PubMed:16809778}.
CC   -!- MISCELLANEOUS: It is in an antisense orientation to and overlaps the
CC       gene of the DNA repair enzyme ERCC1. This gene overlap is conserved in
CC       mouse, suggesting an important biological function.
CC   -!- MISCELLANEOUS: [Isoform 2]: Has sharply different functional
CC       characteristics. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the eukaryotic RPA34 RNA polymerase subunit
CC       family. {ECO:0000305}.
CC   -!- CAUTION: It is not known whether the so-called human ASE1 and human
CC       CAST proteins represent two sides of a single gene product with sharply
CC       different functional characteristics. Experiments done with the mouse
CC       homolog protein are in favor of an implication of this gene in rRNA
CC       transcription instead of T-cell receptor signaling. {ECO:0000305}.
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DR   EMBL; U86751; AAB68608.1; -; mRNA.
DR   EMBL; AF017633; AAD41158.1; -; mRNA.
DR   EMBL; BC038992; AAH38992.1; -; mRNA.
DR   EMBL; BC054044; AAH54044.1; -; mRNA.
DR   EMBL; BC108889; AAI08890.1; -; mRNA.
DR   CCDS; CCDS12661.1; -. [O15446-1]
DR   CCDS; CCDS74397.1; -. [O15446-2]
DR   RefSeq; NP_001284519.1; NM_001297590.1. [O15446-2]
DR   RefSeq; NP_036231.1; NM_012099.1. [O15446-1]
DR   PDB; 7OB9; EM; 2.70 A; N=1-510.
DR   PDB; 7OBA; EM; 3.10 A; N=1-510.
DR   PDB; 7OBB; EM; 3.30 A; N=1-510.
DR   PDB; 7VBA; EM; 2.89 A; N=1-510.
DR   PDB; 7VBB; EM; 2.81 A; N=1-510.
DR   PDB; 7VBC; EM; 3.01 A; N=1-510.
DR   PDB; 8A43; EM; 4.09 A; M=1-510.
DR   PDBsum; 7OB9; -.
DR   PDBsum; 7OBA; -.
DR   PDBsum; 7OBB; -.
DR   PDBsum; 7VBA; -.
DR   PDBsum; 7VBB; -.
DR   PDBsum; 7VBC; -.
DR   PDBsum; 8A43; -.
DR   AlphaFoldDB; O15446; -.
DR   EMDB; EMD-12795; -.
DR   EMDB; EMD-12796; -.
DR   EMDB; EMD-12797; -.
DR   EMDB; EMD-15135; -.
DR   EMDB; EMD-31876; -.
DR   EMDB; EMD-31877; -.
DR   EMDB; EMD-31878; -.
DR   SMR; O15446; -.
DR   BioGRID; 116060; 586.
DR   ComplexPortal; CPX-2386; DNA-directed RNA polymerase I complex.
DR   CORUM; O15446; -.
DR   DIP; DIP-27616N; -.
DR   IntAct; O15446; 29.
DR   MINT; O15446; -.
DR   STRING; 9606.ENSP00000465099; -.
DR   GlyGen; O15446; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; O15446; -.
DR   MetOSite; O15446; -.
DR   PhosphoSitePlus; O15446; -.
DR   SwissPalm; O15446; -.
DR   BioMuta; CD3EAP; -.
DR   CPTAC; CPTAC-920; -.
DR   CPTAC; CPTAC-921; -.
DR   EPD; O15446; -.
DR   jPOST; O15446; -.
DR   MassIVE; O15446; -.
DR   MaxQB; O15446; -.
DR   PaxDb; 9606-ENSP00000465099; -.
DR   PeptideAtlas; O15446; -.
DR   ProteomicsDB; 48675; -. [O15446-1]
DR   ProteomicsDB; 48676; -. [O15446-2]
DR   Pumba; O15446; -.
DR   Antibodypedia; 17932; 341 antibodies from 28 providers.
DR   DNASU; 10849; -.
DR   Ensembl; ENST00000309424.8; ENSP00000310966.3; ENSG00000117877.11. [O15446-1]
DR   Ensembl; ENST00000589804.1; ENSP00000465099.1; ENSG00000117877.11. [O15446-2]
DR   GeneID; 10849; -.
DR   KEGG; hsa:10849; -.
DR   MANE-Select; ENST00000309424.8; ENSP00000310966.3; NM_012099.3; NP_036231.1.
DR   UCSC; uc002pbq.1; human. [O15446-1]
DR   AGR; HGNC:24219; -.
DR   CTD; 10849; -.
DR   DisGeNET; 10849; -.
DR   GeneCards; POLR1G; -.
DR   HGNC; HGNC:24219; POLR1G.
DR   HPA; ENSG00000117877; Low tissue specificity.
DR   MIM; 107325; gene.
DR   neXtProt; NX_O15446; -.
DR   OpenTargets; ENSG00000117877; -.
DR   PharmGKB; PA142672156; -.
DR   VEuPathDB; HostDB:ENSG00000117877; -.
DR   eggNOG; ENOG502S2W3; Eukaryota.
DR   GeneTree; ENSGT00450000040362; -.
DR   HOGENOM; CLU_035235_0_0_1; -.
DR   InParanoid; O15446; -.
DR   OMA; RIFDGPQ; -.
DR   OrthoDB; 2972198at2759; -.
DR   PhylomeDB; O15446; -.
DR   TreeFam; TF338162; -.
DR   PathwayCommons; O15446; -.
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; O15446; -.
DR   SIGNOR; O15446; -.
DR   BioGRID-ORCS; 10849; 330 hits in 1158 CRISPR screens.
DR   ChiTaRS; CD3EAP; human.
DR   GeneWiki; CD3EAP; -.
DR   GenomeRNAi; 10849; -.
DR   Pharos; O15446; Tbio.
DR   PRO; PR:O15446; -.
DR   Proteomes; UP000005640; Chromosome 19.
DR   RNAct; O15446; Protein.
DR   Bgee; ENSG00000117877; Expressed in primordial germ cell in gonad and 167 other cell types or tissues.
DR   ExpressionAtlas; O15446; baseline and differential.
DR   GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0001650; C:fibrillar center; IDA:HPA.
DR   GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR   GO; GO:0005730; C:nucleolus; TAS:ProtInc.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005736; C:RNA polymerase I complex; IDA:UniProtKB.
DR   GO; GO:0000120; C:RNA polymerase I transcription regulator complex; TAS:ProtInc.
DR   GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR   GO; GO:0009303; P:rRNA transcription; TAS:ProtInc.
DR   GO; GO:0006360; P:transcription by RNA polymerase I; IEA:InterPro.
DR   GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; TAS:ProtInc.
DR   Gene3D; 6.20.250.70; -; 1.
DR   InterPro; IPR013240; DNA-dir_RNA_pol1_su_RPA34.
DR   PANTHER; PTHR15484; DNA-DIRECTED RNA POLYMERASE I SUBUNIT RPA34; 1.
DR   PANTHER; PTHR15484:SF8; DNA-DIRECTED RNA POLYMERASE I SUBUNIT RPA34; 1.
DR   Pfam; PF08208; RNA_polI_A34; 1.
DR   Genevisible; O15446; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing; Chromosome;
KW   DNA-directed RNA polymerase; Isopeptide bond; Nucleus; Phosphoprotein;
KW   Reference proteome; Transcription; Ubl conjugation.
FT   CHAIN           1..510
FT                   /note="DNA-directed RNA polymerase I subunit RPA34"
FT                   /id="PRO_0000228120"
FT   REGION          1..31
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          120..143
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          203..510
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        205..222
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        256..274
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        283..301
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        323..338
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        383..397
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        493..510
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0007744|PubMed:19413330,
FT                   ECO:0007744|PubMed:22814378"
FT   MOD_RES         27
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         80
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000269|PubMed:16809778"
FT   MOD_RES         128
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         136
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         172
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT   MOD_RES         205
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         285
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT   MOD_RES         287
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         309
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17525332"
FT   MOD_RES         490
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19690332"
FT   CROSSLNK        270
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO1); alternate"
FT                   /evidence="ECO:0007744|PubMed:25114211"
FT   CROSSLNK        270
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2); alternate"
FT                   /evidence="ECO:0007744|PubMed:25218447,
FT                   ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:25772364,
FT                   ECO:0007744|PubMed:28112733"
FT   CROSSLNK        314
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO1); alternate"
FT                   /evidence="ECO:0007744|PubMed:25114211"
FT   CROSSLNK        314
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2); alternate"
FT                   /evidence="ECO:0007744|PubMed:25218447,
FT                   ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:28112733"
FT   VAR_SEQ         7
FT                   /note="G -> GGE (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:10373416"
FT                   /id="VSP_017673"
FT   VARIANT         259
FT                   /note="K -> T (in dbSNP:rs735482)"
FT                   /id="VAR_051875"
FT   VARIANT         282
FT                   /note="T -> A (in dbSNP:rs3212989)"
FT                   /id="VAR_051876"
FT   VARIANT         373
FT                   /note="K -> E (in dbSNP:rs762562)"
FT                   /id="VAR_051877"
FT   VARIANT         394
FT                   /note="D -> N (in dbSNP:rs2336219)"
FT                   /id="VAR_051878"
FT   VARIANT         503
FT                   /note="K -> Q (in dbSNP:rs3212986)"
FT                   /id="VAR_051879"
FT   VARIANT         504
FT                   /note="Q -> K (in dbSNP:rs3212986)"
FT                   /evidence="ECO:0000269|PubMed:15489334"
FT                   /id="VAR_051880"
FT   CONFLICT        218
FT                   /note="N -> K (in Ref. 3; AAH54044)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        422
FT                   /note="Missing (in Ref. 3; AAI08890)"
FT                   /evidence="ECO:0000305"
FT   STRAND          22..26
FT                   /evidence="ECO:0007829|PDB:7OB9"
FT   STRAND          38..47
FT                   /evidence="ECO:0007829|PDB:7OB9"
FT   TURN            53..58
FT                   /evidence="ECO:0007829|PDB:7OB9"
FT   STRAND          59..68
FT                   /evidence="ECO:0007829|PDB:7OB9"
FT   STRAND          73..75
FT                   /evidence="ECO:0007829|PDB:7OB9"
FT   STRAND          80..85
FT                   /evidence="ECO:0007829|PDB:7OB9"
FT   STRAND          93..96
FT                   /evidence="ECO:0007829|PDB:7OB9"
FT   TURN            99..103
FT                   /evidence="ECO:0007829|PDB:7OB9"
FT   STRAND          113..119
FT                   /evidence="ECO:0007829|PDB:7OB9"
FT   STRAND          123..127
FT                   /evidence="ECO:0007829|PDB:7OBB"
SQ   SEQUENCE   510 AA;  54986 MW;  D460FB944412D393 CRC64;
     MEEPQAGDAA RFSCPPNFTA KPPASESPRF SLEALTGPDT ELWLIQAPAD FAPECFNGRH
     VPLSGSQIVK GKLAGKRHRY RVLSSCPQAG EATLLAPSTE AGGGLTCASA PQGTLRILEG
     PQQSLSGSPL QPIPASPPPQ IPPGLRPRFC AFGGNPPVTG PRSALAPNLL TSGKKKKEMQ
     VTEAPVTQEA VNGHGALEVD MALGSPEMDV RKKKKKKNQQ LKEPEAAGPV GTEPTVETLE
     PLGVLFPSTT KKRKKPKGKE TFEPEDKTVK QEQINTEPLE DTVLSPTKKR KRQKGTEGME
     PEEGVTVESQ PQVKVEPLEE AIPLPPTKKR KKEKGQMAMM EPGTEAMEPV EPEMKPLESP
     GGTMAPQQPE GAKPQAQAAL AAPKKKTKKE KQQDATVEPE TEVVGPELPD DLEPQAAPTS
     TKKKKKKKER GHTVTEPIQP LEPELPGEGQ PEARATPGST KKRKKQSQES RMPETVPQEE
     MPGPPLNSES GEEAPTGRDK KRKQQQQQPV
//