ID TCP4_HUMAN Reviewed; 127 AA. AC P53999; Q96L29; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 27-MAR-2024, entry version 202. DE RecName: Full=Activated RNA polymerase II transcriptional coactivator p15; DE AltName: Full=Positive cofactor 4; DE Short=PC4; DE AltName: Full=SUB1 homolog; DE AltName: Full=p14; GN Name=SUB1; Synonyms=PC4, RPO2TC1; 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], PARTIAL PROTEIN SEQUENCE, AND FUNCTION. RX PubMed=8062392; DOI=10.1016/0092-8674(94)90429-4; RA Kretzschmar M., Kaiser K., Lottspeich F., Meisterernst M.; RT "A novel mediator of class II gene transcription with homology to viral RT immediate-early transcriptional regulators."; RL Cell 78:525-534(1994). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 2-11 AND 81-97, AND RP FUNCTION. RX PubMed=8062391; DOI=10.1016/0092-8674(94)90428-6; RA Ge H., Roeder R.G.; RT "Purification, cloning, and characterization of a human coactivator, PC4, RT that mediates transcriptional activation of class II genes."; RL Cell 78:513-523(1994). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLY-11. RC TISSUE=Bone marrow, Cervix, Lung, and Prostate; 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 PHOSPHORYLATION, AND MASS SPECTROMETRY. RX PubMed=7809103; DOI=10.1073/pnas.91.26.12691; RA Ge H., Zhao Y., Chait B.T., Roeder R.G.; RT "Phosphorylation negatively regulates the function of coactivator PC4."; RL Proc. Natl. Acad. Sci. U.S.A. 91:12691-12695(1994). RN [5] RP FUNCTION, AND DNA-BINDING. RX PubMed=7628453; DOI=10.1002/j.1460-2075.1995.tb07358.x; RA Kaiser K., Stelzer G., Meisterernst M.; RT "The coactivator p15 (PC4) initiates transcriptional activation during RT TFIIA-TFIID-promoter complex formation."; RL EMBO J. 14:3520-3527(1995). RN [6] RP FUNCTION, AND PHOSPHORYLATION BY CK2. RX PubMed=9482861; DOI=10.1073/pnas.95.5.2192; RA Malik S., Guermah M., Roeder R.G.; RT "A dynamic model for PC4 coactivator function in RNA polymerase II RT transcription."; RL Proc. Natl. Acad. Sci. U.S.A. 95:2192-2197(1998). RN [7] RP INTERACTION WITH CSTF2. RX PubMed=11389848; DOI=10.1016/s1097-2765(01)00236-2; RA Calvo O., Manley J.L.; RT "Evolutionarily conserved interaction between CstF-64 and PC4 links RT transcription, polyadenylation, and termination."; RL Mol. Cell 7:1013-1023(2001). RN [8] RP MASS SPECTROMETRY, FUNCTION, DNA-BINDING, AND PHOSPHORYLATION AT SER-11; RP SER-13; SER-15; SER-17 AND SER-19. RX PubMed=16689930; DOI=10.1111/j.1742-4658.2006.05165.x; RA Jonker H.R.A., Wechselberger R.W., Pinkse M., Kaptein R., Folkers G.E.; RT "Gradual phosphorylation regulates PC4 coactivator function."; RL FEBS J. 273:1430-1444(2006). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17 AND SER-19, AND RP IDENTIFICATION BY MASS 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 [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-118, AND IDENTIFICATION BY RP 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 [11] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-35 AND LYS-68, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-118, AND IDENTIFICATION BY RP 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 [13] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-118, 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 [15] RP IDENTIFICATION BY MASS 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 [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17; SER-19; SER-55; SER-56; RP SER-57; SER-58 AND SER-118, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE RP SCALE 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 [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4; SER-9; SER-10; SER-13; RP SER-15; SER-17; SER-19 AND SER-118, AND IDENTIFICATION BY MASS SPECTROMETRY RP [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 [18] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-68, AND IDENTIFICATION BY MASS RP 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 [19] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [20] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-68, AND IDENTIFICATION BY MASS RP 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 [21] RP X-RAY CRYSTALLOGRAPHY (1.74 ANGSTROMS) OF 63-127, FUNCTION, AND SUBUNIT. RX PubMed=9360603; DOI=10.1038/nsb1197-900; RA Brandsen J., Werten S., van der Vliet P.C., Meisterernst M., Kroon J., RA Gros P.; RT "C-terminal domain of transcription cofactor PC4 reveals dimeric ssDNA RT binding site."; RL Nat. Struct. Biol. 4:900-903(1997). RN [22] RP STRUCTURE BY NMR, FUNCTION, AND MUTAGENESIS OF LYS-68; ARG-75; RP 77-PHE--LYS-80; ARG-86 AND LYS-101. RX PubMed=16605275; DOI=10.1021/bi052531b; RA Jonker H.R.A., Wechselberger R.W., Boelens R., Kaptein R., Folkers G.E.; RT "The intrinsically unstructured domain of PC4 modulates the activity of the RT structured core through inter- and intramolecular interactions."; RL Biochemistry 45:5067-5081(2006). RN [23] RP X-RAY CRYSTALLOGRAPHY (1.74 ANGSTROMS) OF 63-127 IN COMPLEX WITH RP SINGLE-STRANDED DNA, AND SUBUNIT. RX PubMed=16415882; DOI=10.1038/nsmb1044; RA Werten S., Moras D.; RT "A global transcription cofactor bound to juxtaposed strands of unwound RT DNA."; RL Nat. Struct. Biol. 13:181-182(2006). CC -!- FUNCTION: General coactivator that functions cooperatively with TAFs CC and mediates functional interactions between upstream activators and CC the general transcriptional machinery. May be involved in stabilizing CC the multiprotein transcription complex. Binds single-stranded DNA. Also CC binds, in vitro, non-specifically to double-stranded DNA (ds DNA). CC {ECO:0000269|PubMed:16605275, ECO:0000269|PubMed:16689930, CC ECO:0000269|PubMed:7628453, ECO:0000269|PubMed:8062391, CC ECO:0000269|PubMed:8062392, ECO:0000269|PubMed:9360603, CC ECO:0000269|PubMed:9482861}. CC -!- SUBUNIT: Homodimer. Interacts with CSTF2. {ECO:0000269|PubMed:11389848, CC ECO:0000269|PubMed:16415882, ECO:0000269|PubMed:9360603}. CC -!- INTERACTION: CC P53999; P28288-2: ABCD3; NbExp=3; IntAct=EBI-998260, EBI-25889034; CC P53999; P33240-1: CSTF2; NbExp=3; IntAct=EBI-998260, EBI-711374; CC P53999; Q6P4D5-2: PABIR3; NbExp=3; IntAct=EBI-998260, EBI-9091052; CC P53999; O00560: SDCBP; NbExp=3; IntAct=EBI-998260, EBI-727004; CC P53999; P53999: SUB1; NbExp=5; IntAct=EBI-998260, EBI-998260; CC P53999; P03132: Rep68; Xeno; NbExp=3; IntAct=EBI-998260, EBI-7387242; CC -!- SUBCELLULAR LOCATION: Nucleus. CC -!- PTM: Activity is controlled by protein kinases that target the CC regulatory region. Phosphorylation inactivates both ds DNA-binding and CC cofactor function, but does not affect binding to ssDNA. Seems to be CC phosphorylated in vivo by CK2 in at least 7 sites in the N-terminal CC Ser-rich region. {ECO:0000269|PubMed:16689930, CC ECO:0000269|PubMed:7809103, ECO:0000269|PubMed:9482861}. CC -!- MASS SPECTROMETRY: Mass=14266; Mass_error=4; Method=MALDI; CC Evidence={ECO:0000269|PubMed:7809103}; CC -!- MASS SPECTROMETRY: Mass=14263; Method=Electrospray; CC Evidence={ECO:0000269|PubMed:16689930}; CC -!- SIMILARITY: Belongs to the transcriptional coactivator PC4 family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X79805; CAA56200.1; -; mRNA. DR EMBL; U12979; AAA20980.1; -; mRNA. DR EMBL; BC009610; AAH09610.1; -; mRNA. DR EMBL; BC010537; AAH10537.1; -; mRNA. DR EMBL; BC018189; AAH18189.1; -; mRNA. DR EMBL; BC022339; AAH22339.1; -; mRNA. DR CCDS; CCDS3897.1; -. DR PIR; A54670; A54670. DR RefSeq; NP_006704.3; NM_006713.3. DR RefSeq; XP_011512246.1; XM_011513944.2. DR RefSeq; XP_016864475.1; XM_017008986.1. DR RefSeq; XP_016864476.1; XM_017008987.1. DR PDB; 1PCF; X-ray; 1.74 A; A/B/C/D/E/F/G/H=63-127. DR PDB; 2C62; X-ray; 1.74 A; A/B=63-127. DR PDB; 2PHE; NMR; -; A/B=63-127. DR PDB; 4USG; X-ray; 1.97 A; A/B=63-127. DR PDB; 6YCS; X-ray; 3.05 A; A/B/C/D=61-127. DR PDB; 7E4W; X-ray; 2.90 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P=63-127. DR PDBsum; 1PCF; -. DR PDBsum; 2C62; -. DR PDBsum; 2PHE; -. DR PDBsum; 4USG; -. DR PDBsum; 6YCS; -. DR PDBsum; 7E4W; -. DR AlphaFoldDB; P53999; -. DR BMRB; P53999; -. DR SMR; P53999; -. DR BioGRID; 116127; 222. DR CORUM; P53999; -. DR DIP; DIP-29044N; -. DR IntAct; P53999; 48. DR MINT; P53999; -. DR STRING; 9606.ENSP00000265073; -. DR GlyGen; P53999; 3 sites, 1 O-linked glycan (3 sites). DR iPTMnet; P53999; -. DR MetOSite; P53999; -. DR PhosphoSitePlus; P53999; -. DR SwissPalm; P53999; -. DR BioMuta; SUB1; -. DR DMDM; 1709514; -. DR EPD; P53999; -. DR jPOST; P53999; -. DR MassIVE; P53999; -. DR PaxDb; 9606-ENSP00000265073; -. DR PeptideAtlas; P53999; -. DR ProteomicsDB; 56641; -. DR Pumba; P53999; -. DR TopDownProteomics; P53999; -. DR Antibodypedia; 681; 318 antibodies from 32 providers. DR DNASU; 10923; -. DR Ensembl; ENST00000265073.9; ENSP00000265073.4; ENSG00000113387.12. DR Ensembl; ENST00000502897.5; ENSP00000427100.1; ENSG00000113387.12. DR Ensembl; ENST00000506237.5; ENSP00000422078.1; ENSG00000113387.12. DR Ensembl; ENST00000512913.5; ENSP00000422806.1; ENSG00000113387.12. DR Ensembl; ENST00000515355.5; ENSP00000426850.1; ENSG00000113387.12. DR GeneID; 10923; -. DR KEGG; hsa:10923; -. DR MANE-Select; ENST00000265073.9; ENSP00000265073.4; NM_006713.4; NP_006704.3. DR AGR; HGNC:19985; -. DR CTD; 10923; -. DR DisGeNET; 10923; -. DR GeneCards; SUB1; -. DR HGNC; HGNC:19985; SUB1. DR HPA; ENSG00000113387; Low tissue specificity. DR MIM; 600503; gene. DR neXtProt; NX_P53999; -. DR OpenTargets; ENSG00000113387; -. DR PharmGKB; PA142670858; -. DR VEuPathDB; HostDB:ENSG00000113387; -. DR eggNOG; KOG2712; Eukaryota. DR GeneTree; ENSGT00390000008802; -. DR HOGENOM; CLU_104273_1_1_1; -. DR InParanoid; P53999; -. DR OMA; WMNPDGE; -. DR OrthoDB; 5489415at2759; -. DR PhylomeDB; P53999; -. DR TreeFam; TF313859; -. DR PathwayCommons; P53999; -. DR SignaLink; P53999; -. DR SIGNOR; P53999; -. DR BioGRID-ORCS; 10923; 62 hits in 1131 CRISPR screens. DR ChiTaRS; SUB1; human. DR EvolutionaryTrace; P53999; -. DR GeneWiki; SUB1; -. DR GenomeRNAi; 10923; -. DR Pharos; P53999; Tbio. DR PRO; PR:P53999; -. DR Proteomes; UP000005640; Chromosome 5. DR RNAct; P53999; Protein. DR Bgee; ENSG00000113387; Expressed in epithelium of nasopharynx and 207 other cell types or tissues. DR ExpressionAtlas; P53999; baseline and differential. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005730; C:nucleolus; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0005667; C:transcription regulator complex; IDA:UniProtKB. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IEA:Ensembl. DR GO; GO:0003697; F:single-stranded DNA binding; IDA:UniProtKB. DR GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB. DR GO; GO:1905463; P:negative regulation of DNA duplex unwinding; IDA:DisProt. DR GO; GO:0051053; P:negative regulation of DNA metabolic process; IDA:CACAO. DR GO; GO:0060261; P:positive regulation of transcription initiation by RNA polymerase II; IEA:InterPro. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:UniProtKB. DR GO; GO:0001111; P:RNA polymerase II promoter clearance; IDA:WormBase. DR DisProt; DP01804; -. DR IDEAL; IID00306; -. DR InterPro; IPR003173; PC4_C. DR InterPro; IPR009044; ssDNA-bd_transcriptional_reg. DR InterPro; IPR045125; Sub1/Tcp4-like. DR PANTHER; PTHR13215:SF0; ACTIVATED RNA POLYMERASE II TRANSCRIPTIONAL COACTIVATOR P15; 1. DR PANTHER; PTHR13215; RNA POLYMERASE II TRANSCRIPTIONAL COACTIVATOR; 1. DR Pfam; PF02229; PC4; 1. DR SUPFAM; SSF54447; ssDNA-binding transcriptional regulator domain; 1. DR Genevisible; P53999; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Activator; Direct protein sequencing; KW DNA-binding; Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome; KW Transcription; Transcription regulation; Ubl conjugation. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:8062391" FT CHAIN 2..127 FT /note="Activated RNA polymerase II transcriptional FT coactivator p15" FT /id="PRO_0000215944" FT REGION 1..64 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2..50 FT /note="Regulatory" FT REGION 77..101 FT /note="Interaction with ssDNA" FT COMPBIAS 1..16 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 17..42 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 43..63 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT SITE 50..51 FT /note="Cleavage" FT MOD_RES 4 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 9 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 10 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 11 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:16689930" FT MOD_RES 13 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:16689930, FT ECO:0007744|PubMed:24275569" FT MOD_RES 15 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:16689930, FT ECO:0007744|PubMed:24275569" FT MOD_RES 17 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:16689930, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 19 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:16689930, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 35 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 53 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P11031" FT MOD_RES 55 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 56 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 57 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 58 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 68 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 118 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT CROSSLNK 68 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO1); alternate" FT /evidence="ECO:0007744|PubMed:25114211" FT CROSSLNK 68 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0007744|PubMed:28112733" FT VARIANT 11 FT /note="S -> G (in dbSNP:rs17850527)" FT /evidence="ECO:0000269|PubMed:15489334" FT /id="VAR_032870" FT MUTAGEN 68 FT /note="K->G: Reduced ssDNA binding." FT /evidence="ECO:0000269|PubMed:16605275" FT MUTAGEN 75 FT /note="R->G: Reduced ssDNA binding." FT /evidence="ECO:0000269|PubMed:16605275" FT MUTAGEN 77..80 FT /note="FKGK->AGG: Loss of ssDNA binding." FT /evidence="ECO:0000269|PubMed:16605275" FT MUTAGEN 86 FT /note="R->G: Loss of ssDNA binding." FT /evidence="ECO:0000269|PubMed:16605275" FT MUTAGEN 101 FT /note="K->G: Loss of ssDNA binding." FT /evidence="ECO:0000269|PubMed:16605275" FT STRAND 63..67 FT /evidence="ECO:0007829|PDB:1PCF" FT STRAND 70..77 FT /evidence="ECO:0007829|PDB:1PCF" FT STRAND 80..90 FT /evidence="ECO:0007829|PDB:1PCF" FT STRAND 92..94 FT /evidence="ECO:0007829|PDB:2PHE" FT STRAND 96..105 FT /evidence="ECO:0007829|PDB:1PCF" FT HELIX 107..126 FT /evidence="ECO:0007829|PDB:1PCF" SQ SEQUENCE 127 AA; 14395 MW; 0DAE0CAAAD5E4E15 CRC64; MPKSKELVSS SSSGSDSDSE VDKKLKRKKQ VAPEKPVKKQ KTGETSRALS SSKQSSSSRD DNMFQIGKMR YVSVRDFKGK VLIDIREYWM DPEGEMKPGR KGISLNPEQW SQLKEQISDI DDAVRKL //