PIAS1_MOUSE
ID PIAS1_MOUSE Reviewed; 651 AA.
AC O88907; Q8C6H5;
DT 05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 2.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=E3 SUMO-protein ligase PIAS1;
DE EC=2.3.2.27;
DE AltName: Full=DEAD/H box-binding protein 1;
DE AltName: Full=Protein inhibitor of activated STAT protein 1;
DE AltName: Full=RING-type E3 ubiquitin transferase PIAS1 {ECO:0000305};
GN Name=Pias1; Synonyms=Ddxbp1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=B-cell;
RX PubMed=9724754; DOI=10.1073/pnas.95.18.10626;
RA Liu B., Liao J., Rao X., Kushner S.A., Chung C.D., Chang D.D., Shuai K.;
RT "Inhibition of Stat1-mediated gene activation by PIAS1.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:10626-10631(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Lung;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N-3; TISSUE=Mammary tumor;
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 DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=10854042; DOI=10.1385/jmn:14:1-2:107;
RA Sturm S., Koch M., White F.A.;
RT "Cloning and analysis of a murine Pias family member, Pias-gamma, in
RT developing skin and neurons.";
RL J. Mol. Neurosci. 14:107-121(2000).
RN [5]
RP INTERACTION WITH AR.
RX PubMed=11117529; DOI=10.1210/mend.14.12.0569;
RA Kotaja N., Aittomaeki S., Silvennoinen O., Palvimo J.J., Jaenne O.A.;
RT "ARIP3 (androgen receptor-interacting protein 3) and other PIAS (protein
RT inhibitor of activated STAT) proteins differ in their ability to modulate
RT steroid receptor-dependent transcriptional activation.";
RL Mol. Endocrinol. 14:1986-2000(2000).
RN [6]
RP INTERACTION WITH SUMO1; UBE2I AND NCOA2, SUBCELLULAR LOCATION, SUMOYLATION
RP OF AR AND NCOA2, AND MUTAGENESIS OF TRP-372.
RX PubMed=12077349; DOI=10.1128/mcb.22.14.5222-5234.2002;
RA Kotaja N., Karvonen U., Jaenne O.A., Palvimo J.J.;
RT "PIAS proteins modulate transcription factors by functioning as SUMO-1
RT ligases.";
RL Mol. Cell. Biol. 22:5222-5234(2002).
RN [7]
RP STAT1 SUMOYLATION.
RX PubMed=12855578; DOI=10.1182/blood-2002-12-3816;
RA Ungureanu D., Vanhatupa S., Kotaja N., Yang J., Aittomaeki S., Jaenne O.A.,
RA Palvimo J.J., Silvennoinen O.;
RT "PIAS proteins promote SUMO-1 conjugation to STAT1.";
RL Blood 102:3311-3313(2003).
RN [8]
RP SUMOYLATION OF KLF1, AND MUTAGENESIS OF CYS-346; CYS-351; CYS-356; ILE-363
RP AND 375-PRO-VAL-376.
RX PubMed=17938210; DOI=10.1128/mcb.00589-07;
RA Siatecka M., Xue L., Bieker J.J.;
RT "Sumoylation of EKLF promotes transcriptional repression and is involved in
RT inhibition of megakaryopoiesis.";
RL Mol. Cell. Biol. 27:8547-8560(2007).
RN [9]
RP INTERACTION WITH NR2C1.
RX PubMed=17187077; DOI=10.1038/nsmb1185;
RA Park S.W., Hu X., Gupta P., Lin Y.P., Ha S.G., Wei L.N.;
RT "SUMOylation of Tr2 orphan receptor involves Pml and fine-tunes Oct4
RT expression in stem cells.";
RL Nat. Struct. Mol. Biol. 14:68-75(2007).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-485 AND THR-487, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-483; SER-485; THR-487;
RP SER-488 AND SER-491, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [12]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH PML.
RX PubMed=22406621; DOI=10.1158/0008-5472.can-11-3159;
RA Rabellino A., Carter B., Konstantinidou G., Wu S.Y., Rimessi A.,
RA Byers L.A., Heymach J.V., Girard L., Chiang C.M., Teruya-Feldstein J.,
RA Scaglioni P.P.;
RT "The SUMO E3-ligase PIAS1 regulates the tumor suppressor PML and its
RT oncogenic counterpart PML-RARA.";
RL Cancer Res. 72:2275-2284(2012).
RN [13]
RP FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=24061474; DOI=10.1128/mcb.00723-13;
RA Liu Y., Zhang Y.D., Guo L., Huang H.Y., Zhu H., Huang J.X., Liu Y.,
RA Zhou S.R., Dang Y.J., Li X., Tang Q.Q.;
RT "Protein inhibitor of activated STAT 1 (PIAS1) is identified as the SUMO E3
RT ligase of CCAAT/enhancer-binding protein beta (C/EBPbeta) during
RT adipogenesis.";
RL Mol. Cell. Biol. 33:4606-4617(2013).
CC -!- FUNCTION: Functions as an E3-type small ubiquitin-like modifier (SUMO)
CC ligase, stabilizing the interaction between UBE2I and the substrate,
CC and as a SUMO-tethering factor. Plays a crucial role as a
CC transcriptional coregulation in various cellular pathways, including
CC the STAT pathway, the p53 pathway and the steroid hormone signaling
CC pathway. In vitro, binds A/T-rich DNA (By similarity). The effects of
CC this transcriptional coregulation, transactivation or silencing, may
CC vary depending upon the biological context. Sumoylates PML (at'Lys-65'
CC and 'Lys-160') and PML-RAR and promotes their ubiquitin-mediated
CC degradation. PIAS1-mediated sumoylation of PML promotes its interaction
CC with CSNK2A1/CK2 which in turn promotes PML phosphorylation and
CC degradation. Enhances the sumoylation of MTA1 and may participate in
CC its paralog-selective sumoylation. Plays a dynamic role in adipogenesis
CC by promoting the SUMOylation and degradation of CEBPB
CC (PubMed:24061474). {ECO:0000250|UniProtKB:O75925,
CC ECO:0000269|PubMed:22406621, ECO:0000269|PubMed:24061474}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27;
CC -!- PATHWAY: Protein modification; protein sumoylation.
CC -!- SUBUNIT: Interacts with NR2C1; the interaction promotes its
CC sumoylation. Interacts with DDX21, CSRP2, AXIN1, JUN, SATB2, PLAG1,
CC TP53 and STAT1 (dimer), following IFNA1-stimulation. Interacts with SP3
CC (preferentially when SUMO-modified). Interacts with KLF8; the
CC interaction results in SUMO ligation and repression of KLF8
CC transcriptional activity and of its cell cycle progression into G(1)
CC phase (By similarity). Interacts with CHUK/IKKA; this interaction
CC induces PIAS1 phosphorylation. Interacts with PTK2/FAK1; the
CC interaction promotes its sumoylation (By similarity). Interacts with
CC SUMO1, UBE2I, NCOA2 and AR. Interacts with NR2C1; the interaction
CC promotes its sumoylation. Interacts with DDX5. Interacts with MTA1 (By
CC similarity). Interacts with PML (isoform PML-12). Interacts with PRDM1
CC (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:O75925,
CC ECO:0000269|PubMed:11117529, ECO:0000269|PubMed:12077349,
CC ECO:0000269|PubMed:17187077, ECO:0000269|PubMed:22406621}.
CC -!- INTERACTION:
CC O88907; Q505F1: Nr2c1; NbExp=4; IntAct=EBI-3508327, EBI-15617004;
CC O88907; Q9Z0P7: Sufu; NbExp=3; IntAct=EBI-3508327, EBI-3508336;
CC -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000250}. Nucleus, PML body
CC {ECO:0000269|PubMed:12077349, ECO:0000269|PubMed:22406621}.
CC Note=Interaction with CSRP2 may induce a partial redistribution along
CC the cytoskeleton. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in kidney, heart, spleen, brain and
CC cerebellum; weak expression, if any, in liver and lung.
CC {ECO:0000269|PubMed:10854042}.
CC -!- DEVELOPMENTAL STAGE: Expressed as early as 7.6 dpc. Expression remains
CC high through 15.5 dpc (PubMed:10854042). In 3T3-L1 cells, expression is
CC transiently induced during late adipocyte differentiation
CC (PubMed:24061474). {ECO:0000269|PubMed:10854042,
CC ECO:0000269|PubMed:24061474}.
CC -!- DOMAIN: The LXXLL motif is a transcriptional coregulator signature.
CC -!- DOMAIN: The SP-RING-type domain is required for promoting EKLF
CC sumoylation.
CC -!- PTM: Sumoylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the PIAS family. {ECO:0000305}.
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DR EMBL; AF077950; AAC36701.1; -; mRNA.
DR EMBL; AK075708; BAC35902.1; -; mRNA.
DR EMBL; BC051417; AAH51417.1; -; mRNA.
DR CCDS; CCDS40665.1; -.
DR RefSeq; NP_062637.2; NM_019663.3.
DR AlphaFoldDB; O88907; -.
DR BMRB; O88907; -.
DR SMR; O88907; -.
DR BioGRID; 208005; 38.
DR CORUM; O88907; -.
DR DIP; DIP-29277N; -.
DR IntAct; O88907; 19.
DR MINT; O88907; -.
DR STRING; 10090.ENSMUSP00000096248; -.
DR iPTMnet; O88907; -.
DR PhosphoSitePlus; O88907; -.
DR EPD; O88907; -.
DR jPOST; O88907; -.
DR PaxDb; O88907; -.
DR PeptideAtlas; O88907; -.
DR PRIDE; O88907; -.
DR ProteomicsDB; 301829; -.
DR Antibodypedia; 26284; 370 antibodies from 35 providers.
DR DNASU; 56469; -.
DR Ensembl; ENSMUST00000098651; ENSMUSP00000096248; ENSMUSG00000032405.
DR GeneID; 56469; -.
DR KEGG; mmu:56469; -.
DR UCSC; uc009qas.1; mouse.
DR CTD; 8554; -.
DR MGI; MGI:1913125; Pias1.
DR VEuPathDB; HostDB:ENSMUSG00000032405; -.
DR eggNOG; KOG2169; Eukaryota.
DR GeneTree; ENSGT01030000234539; -.
DR HOGENOM; CLU_020768_3_0_1; -.
DR InParanoid; O88907; -.
DR OMA; CFVSKQM; -.
DR OrthoDB; 1205949at2759; -.
DR PhylomeDB; O88907; -.
DR TreeFam; TF323787; -.
DR Reactome; R-MMU-3108214; SUMOylation of DNA damage response and repair proteins.
DR Reactome; R-MMU-3232118; SUMOylation of transcription factors.
DR Reactome; R-MMU-3232142; SUMOylation of ubiquitinylation proteins.
DR Reactome; R-MMU-3899300; SUMOylation of transcription cofactors.
DR Reactome; R-MMU-4090294; SUMOylation of intracellular receptors.
DR Reactome; R-MMU-4551638; SUMOylation of chromatin organization proteins.
DR Reactome; R-MMU-5696395; Formation of Incision Complex in GG-NER.
DR Reactome; R-MMU-877312; Regulation of IFNG signaling.
DR UniPathway; UPA00886; -.
DR BioGRID-ORCS; 56469; 9 hits in 74 CRISPR screens.
DR ChiTaRS; Pias1; mouse.
DR PRO; PR:O88907; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; O88907; protein.
DR Bgee; ENSMUSG00000032405; Expressed in animal zygote and 276 other tissues.
DR ExpressionAtlas; O88907; baseline and differential.
DR Genevisible; O88907; MM.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0016605; C:PML body; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IPI:UniProtKB.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0061665; F:SUMO ligase activity; ISS:UniProtKB.
DR GO; GO:0019789; F:SUMO transferase activity; EXP:Reactome.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR GO; GO:0003714; F:transcription corepressor activity; ISO:MGI.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:BHF-UCL.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0045444; P:fat cell differentiation; IDA:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:BHF-UCL.
DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IMP:UniProtKB.
DR GO; GO:0033235; P:positive regulation of protein sumoylation; ISS:UniProtKB.
DR GO; GO:0016925; P:protein sumoylation; IDA:UniProtKB.
DR GO; GO:0007259; P:receptor signaling pathway via JAK-STAT; ISO:MGI.
DR GO; GO:0042127; P:regulation of cell population proliferation; IMP:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 1.10.720.30; -; 1.
DR Gene3D; 2.60.120.780; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR027227; PIAS1.
DR InterPro; IPR023321; PINIT.
DR InterPro; IPR038654; PINIT_sf.
DR InterPro; IPR003034; SAP_dom.
DR InterPro; IPR036361; SAP_dom_sf.
DR InterPro; IPR004181; Znf_MIZ.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR10782:SF11; PTHR10782:SF11; 1.
DR Pfam; PF14324; PINIT; 1.
DR Pfam; PF02891; zf-MIZ; 1.
DR SMART; SM00513; SAP; 1.
DR SUPFAM; SSF68906; SSF68906; 1.
DR PROSITE; PS51466; PINIT; 1.
DR PROSITE; PS50800; SAP; 1.
DR PROSITE; PS51044; ZF_SP_RING; 1.
PE 1: Evidence at protein level;
KW Acetylation; DNA-binding; Isopeptide bond; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Transferase; Ubl conjugation;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:O75925"
FT CHAIN 2..651
FT /note="E3 SUMO-protein ligase PIAS1"
FT /id="PRO_0000218975"
FT DOMAIN 11..45
FT /note="SAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00186"
FT DOMAIN 124..288
FT /note="PINIT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00799"
FT REPEAT 520..523
FT /note="1"
FT REPEAT 557..560
FT /note="2"
FT REPEAT 598..601
FT /note="3; approximate"
FT REPEAT 612..615
FT /note="4; approximate"
FT ZN_FING 320..405
FT /note="SP-RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00452"
FT REGION 462..473
FT /note="SUMO1-binding"
FT /evidence="ECO:0000250"
FT REGION 465..511
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 520..615
FT /note="4 X 4 AA repeats of N-T-S-L"
FT REGION 600..630
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 19..23
FT /note="LXXLL motif"
FT MOTIF 56..64
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOTIF 368..380
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 481..511
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 351
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00452"
FT BINDING 353
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00452"
FT BINDING 374
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00452"
FT BINDING 377
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00452"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:O75925"
FT MOD_RES 467
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75925"
FT MOD_RES 468
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75925"
FT MOD_RES 483
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 485
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 487
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 488
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 491
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 503
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75925"
FT MOD_RES 510
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75925"
FT MOD_RES 522
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75925"
FT CROSSLNK 40
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O75925"
FT CROSSLNK 46
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O75925"
FT CROSSLNK 137
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O75925"
FT CROSSLNK 238
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O75925"
FT CROSSLNK 453
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O75925"
FT CROSSLNK 493
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O75925"
FT MUTAGEN 346
FT /note="C->G: Loss of promotion of EKLF sumoylation; when
FT associated with G-351 and A-356."
FT /evidence="ECO:0000269|PubMed:17938210"
FT MUTAGEN 351
FT /note="C->G: Loss of promotion of EKLF sumoylation; when
FT associated with G-346 and A-356."
FT /evidence="ECO:0000269|PubMed:17938210"
FT MUTAGEN 356
FT /note="C->A: Loss of promotion of EKLF sumoylation; when
FT associated with G-346 and G-351."
FT /evidence="ECO:0000269|PubMed:17938210"
FT MUTAGEN 363
FT /note="I->S: Loss of promotion of EKLF sumoylation."
FT /evidence="ECO:0000269|PubMed:17938210"
FT MUTAGEN 372
FT /note="W->A: Loss of promotion of NCOA2 sumoylation."
FT /evidence="ECO:0000269|PubMed:12077349"
FT MUTAGEN 375..376
FT /note="PV->AA: Loss of promotion of EKLF sumoylation."
FT /evidence="ECO:0000269|PubMed:17938210"
FT CONFLICT 320
FT /note="P -> S (in Ref. 1; AAC36701)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 651 AA; 71618 MW; 8844364E8FEE4F7F CRC64;
MADSAELKQM VMSLRVSELQ VLLGYAGRNK HGRKHELLTK ALHLLKAGCS PAVQMKIKEL
YRRRFPQKIM TPADLSIPNV HSSPMPPTLS PSTIPQLTYD GHPASSPLLP VSLLGPKHEL
ELPHLTSALH PVHPDIKLQK LPFYDLLDEL IKPTSLASDN SQRFRETCFA FALTPQQVQQ
ISSSMDISGT KCDFTVQVQL RFCLSETSCP QEDHFPPNLC VKVNTKPCSL PGYLPPTKNG
VEPKRPSRPI NITSLVRLST TVPNTIVVSW TAEIGRTYSM AVYLVKQLSS TVLLQRLRAK
GIRNPDHSRA LIKEKLTADP DSEIATTSLR VSLLCPLGKM RLTIPCRALT CSHLQCFDAT
LYIQMNEKKP TWVCPVCDKK APYEHLIIDG LFMEILKYCT DCDEIQFKED GSWAPMRSKK
EVQEVTASYN GVDGCLSSTL EHQVASHNQS SNKNKKVEVI DLTIDSSSDE EEEEPPAKRT
CPSLSPTSPL SNKGILSLPH QASPVSRTPS LPAVDTSYIN TSLIQDYRHP FHMTPMPYDL
QGLDFFPFLS GDNQHYNTSL LAAAAAAVSD DQDLLHSSRF FPYTSSQMFL DQLSAGGSTS
LPATNGSSSG SNSSLVSSNS LRESHGHGVA SRSSADTASI FGIIPDIISL D
