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 27-MAR-2024, entry version 198. 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 FUNCTION, INTERACTION WITH MSX1, SUBCELLULAR LOCATION, AND MUTAGENESIS OF RP CYS-351 AND TRP-372. RX PubMed=16600910; DOI=10.1101/gad.1392006; RA Lee H., Quinn J.C., Prasanth K.V., Swiss V.A., Economides K.D., RA Camacho M.M., Spector D.L., Abate-Shen C.; RT "PIAS1 confers DNA-binding specificity on the Msx1 homeoprotein."; RL Genes Dev. 20:784-794(2006). RN [9] 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 [10] 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 [11] 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 [12] 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, RC Pancreas, 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 [13] 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 [14] 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). Mediates the nuclear mobility and localization of CC MSX1 to the nuclear periphery, whereby MSX1 is brought into the CC proximity of target myoblast differentiation factor genes CC (PubMed:16600910). Also required for the binding of MSX1 to the core CC enhancer region in target gene promoter regions, independent of its CC sumolyation activity (PubMed:16600910). Capable of binding to the core CC enhancer region TAAT box in the MYOD1 gene promoter (PubMed:16600910). CC {ECO:0000250|UniProtKB:O75925, ECO:0000269|PubMed:16600910, 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). Interacts (via N-terminus) with MSX1 (via C-terminus); CC the interaction is required for the localization of both proteins to CC the nuclear periphery and specific binding of MSX1 to the core enhancer CC region in target gene promoters (PubMed:16600910). {ECO:0000250, CC ECO:0000250|UniProtKB:O75925, ECO:0000269|PubMed:11117529, CC ECO:0000269|PubMed:12077349, ECO:0000269|PubMed:16600910, 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 {ECO:0000269|PubMed:16600910}. Nucleus CC speckle {ECO:0000250|UniProtKB:O75925}. Nucleus, PML body CC {ECO:0000269|PubMed:12077349, ECO:0000269|PubMed:22406621}. Cytoplasm, CC cytoskeleton {ECO:0000250|UniProtKB:O75925}. Note=Interaction with CC CSRP2 may induce a partial redistribution along the cytoskeleton (By CC similarity). Interaction with MSX1 is required for localization to the CC nuclear periphery (PubMed:16600910). {ECO:0000250|UniProtKB:O75925, CC ECO:0000269|PubMed:16600910}. 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|UniProtKB:O75925}. CC -!- SIMILARITY: Belongs to the PIAS family. {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; 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; 10090-ENSMUSP00000096248; -. DR PeptideAtlas; O88907; -. DR ProteomicsDB; 301829; -. DR Pumba; O88907; -. DR Antibodypedia; 26284; 404 antibodies from 35 providers. DR DNASU; 56469; -. DR Ensembl; ENSMUST00000098651.6; ENSMUSP00000096248.5; ENSMUSG00000032405.11. DR GeneID; 56469; -. DR KEGG; mmu:56469; -. DR UCSC; uc009qas.1; mouse. DR AGR; MGI:1913125; -. 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; LRIVTPC; -. DR OrthoDB; 20246at2759; -. 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 79 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 280 other cell types or tissues. DR ExpressionAtlas; O88907; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW. DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell. DR GO; GO:0034399; C:nuclear periphery; IDA:UniProtKB. 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:0140297; F:DNA-binding transcription factor binding; IPI:UniProtKB. DR GO; GO:0019899; F:enzyme binding; ISO:MGI. DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI. DR GO; GO:0061665; F:SUMO ligase activity; IDA:UniProtKB. DR GO; GO:0019789; F:SUMO transferase activity; EXP:Reactome. DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:UniProtKB. 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:0000082; P:G1/S transition of mitotic cell cycle; ISO:MGI. DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:BHF-UCL. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; ISO:MGI. DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IMP:UniProtKB. DR GO; GO:1904377; P:positive regulation of protein localization to cell periphery; IDA:UniProtKB. DR GO; GO:0033235; P:positive regulation of protein sumoylation; ISS:UniProtKB. DR GO; GO:0051152; P:positive regulation of smooth muscle cell differentiation; ISO:MGI. DR GO; GO:0016925; P:protein sumoylation; IDA:UniProtKB. DR GO; GO:0065004; P:protein-DNA complex assembly; ISO:MGI. 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 GO; GO:0007283; P:spermatogenesis; IEA:Ensembl. DR GO; GO:0008542; P:visual learning; ISO:MGI. DR CDD; cd16818; SP-RING_PIAS1; 1. DR Gene3D; 2.60.120.780; PINIT domain; 1. DR Gene3D; 1.10.720.30; SAP domain; 1. DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1. 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; E3 SUMO-PROTEIN LIGASE PIAS1; 1. DR PANTHER; PTHR10782; ZINC FINGER MIZ DOMAIN-CONTAINING PROTEIN; 1. DR Pfam; PF14324; PINIT; 1. DR Pfam; PF02891; zf-MIZ; 1. DR SMART; SM00513; SAP; 1. DR SUPFAM; SSF68906; SAP domain; 1. DR PROSITE; PS51466; PINIT; 1. DR PROSITE; PS50800; SAP; 1. DR PROSITE; PS51044; ZF_SP_RING; 1. DR Genevisible; O88907; MM. PE 1: Evidence at protein level; KW Acetylation; Cytoplasm; Cytoskeleton; DNA-binding; Isopeptide bond; KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat; KW Transcription; 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 2..200 FT /note="Required for interaction with MSX1" FT /evidence="ECO:0000269|PubMed:16600910" 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 351 FT /note="C->S: No effect on interaction with MSX1 or FT localization of either protein at the nuclear periphery." FT /evidence="ECO:0000269|PubMed:16600910" 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. No FT effect on interaction with MSX1 or localization of either FT protein at the nuclear periphery." FT /evidence="ECO:0000269|PubMed:12077349, FT ECO:0000269|PubMed:16600910" 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 //