RPA34_HUMAN
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 03-AUG-2022, entry version 169.
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},
GN CAST {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, PHOSPHORYLATION, AND INTERACTION WITH CD3E.
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, 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).
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. Isoform 1 is involved in UBTF-activated transcription,
CC presumably at a step following PIC formation.
CC -!- FUNCTION: Isoform 2 has been described as a component of preformed T-
CC cell receptor (TCR) complex.
CC -!- SUBUNIT: Component of the RNA polymerase I (Pol I) complex consisting
CC of at least 13 subunits. Interacts with TAF1A thereby associates with
CC the SL1 complex. Interacts with UBTF. Interacts with POLR1E/PRAF1
CC through its N-terminal region (By similarity). Isoform 2 interacts with
CC CD3E. {ECO:0000250, ECO:0000269|PubMed:10373416,
CC ECO:0000269|PubMed:16809778}.
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 receptor
CC (TCR) stimulation. This phosphorylation has not been confirmed by other
CC groups.
CC -!- PTM: Isoform 1 is phosphorylated on tyrosine residues in initiation-
CC competent Pol I-beta complexes but not in Pol I-alpha complexes.
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 PDBsum; 7OB9; -.
DR PDBsum; 7OBA; -.
DR PDBsum; 7OBB; -.
DR PDBsum; 7VBA; -.
DR PDBsum; 7VBB; -.
DR PDBsum; 7VBC; -.
DR AlphaFoldDB; O15446; -.
DR SMR; O15446; -.
DR BioGRID; 116060; 557.
DR CORUM; O15446; -.
DR DIP; DIP-27616N; -.
DR IntAct; O15446; 27.
DR MINT; O15446; -.
DR STRING; 9606.ENSP00000465099; -.
DR iPTMnet; O15446; -.
DR MetOSite; O15446; -.
DR PhosphoSitePlus; 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; O15446; -.
DR PeptideAtlas; O15446; -.
DR PRIDE; O15446; -.
DR ProteomicsDB; 48675; -. [O15446-1]
DR ProteomicsDB; 48676; -. [O15446-2]
DR Antibodypedia; 17932; 307 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 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; QVMMEPG; -.
DR OrthoDB; 984661at2759; -.
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; 304 hits in 1086 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 oocyte and 166 other tissues.
DR ExpressionAtlas; O15446; baseline and differential.
DR Genevisible; O15446; HS.
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; IBA:GO_Central.
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 InterPro; IPR013240; DNA-dir_RNA_pol1_su_RPA34.
DR PANTHER; PTHR15484; PTHR15484; 1.
DR Pfam; PF08208; RNA_polI_A34; 1.
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
