TCP4_HUMAN
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 03-AUG-2022, entry version 193.
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}.
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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; 131.
DR CORUM; P53999; -.
DR DIP; DIP-29044N; -.
DR IntAct; P53999; 46.
DR MINT; P53999; -.
DR STRING; 9606.ENSP00000265073; -.
DR GlyGen; P53999; 1 site, 1 O-linked glycan (1 site).
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; P53999; -.
DR PeptideAtlas; P53999; -.
DR PRIDE; P53999; -.
DR ProteomicsDB; 56641; -.
DR TopDownProteomics; P53999; -.
DR Antibodypedia; 681; 283 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 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; 1525616at2759; -.
DR PhylomeDB; P53999; -.
DR TreeFam; TF313859; -.
DR PathwayCommons; P53999; -.
DR SignaLink; P53999; -.
DR SIGNOR; P53999; -.
DR BioGRID-ORCS; 10923; 60 hits in 1058 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 205 other tissues.
DR ExpressionAtlas; P53999; baseline and differential.
DR Genevisible; P53999; HS.
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:0051053; P:negative regulation of DNA metabolic process; IDA:CACAO.
DR GO; GO:0060261; P:positive regulation of transcription initiation from RNA polymerase II promoter; IBA:GO_Central.
DR GO; GO:0001111; P:promoter clearance from RNA polymerase II promoter; IDA:WormBase.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0060395; P:SMAD protein signal transduction; IEA:Ensembl.
DR DisProt; DP01804; -.
DR Gene3D; 2.30.31.10; -; 1.
DR IDEAL; IID00306; -.
DR InterPro; IPR003173; PC4_C.
DR InterPro; IPR009044; ssDNA-bd_transcriptional_reg.
DR InterPro; IPR045125; Sub1/Tcp4-like.
DR PANTHER; PTHR13215; PTHR13215; 1.
DR Pfam; PF02229; PC4; 1.
DR SUPFAM; SSF54447; SSF54447; 1.
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
