ID ZN263_HUMAN Reviewed; 683 AA. AC O14978; B2R634; O43387; Q96H95; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 25-OCT-2002, sequence version 2. DT 05-FEB-2025, entry version 205. DE RecName: Full=Zinc finger protein 263 {ECO:0000312|HGNC:HGNC:13056}; DE AltName: Full=Zinc finger protein FPM315 {ECO:0000312|HGNC:HGNC:13056}; DE AltName: Full=Zinc finger protein with KRAB and SCAN domains 12 {ECO:0000312|HGNC:HGNC:13056}; GN Name=ZNF263 {ECO:0000312|HGNC:HGNC:13056}; GN Synonyms=FPM315 {ECO:0000303|PubMed:9256059}, GN ZKSCAN12 {ECO:0000312|HGNC:HGNC:13056}; 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 {ECO:0000312|Proteomes:UP000005640}; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY. RX PubMed=9256059; DOI=10.1016/s0167-4781(97)00074-2; RA Yokoyama M., Nakamura M., Okudo K., Matsubara K., Nishi Y., Matsumoto T., RA Fukushima A.; RT "Isolation of a cDNA encoding a widely expressed novel zinc finger protein RT with the LeR and KRAB-A domains."; RL Biochim. Biophys. Acta 1353:13-17(1997). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15616553; DOI=10.1038/nature03187; RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M., RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., RA Myers R.M., Rubin E.M., Pennacchio L.A.; RT "The sequence and analysis of duplication-rich human chromosome 16."; RL Nature 432:988-994(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Lung; 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 [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-166 AND SER-178, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE 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 [7] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-17; LYS-157; LYS-285; LYS-299; RP LYS-376; LYS-573 AND LYS-582, AND IDENTIFICATION BY MASS SPECTROMETRY RP [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 [8] RP FUNCTION, INTERACTION WITH DNMT1; DNMT3A; PHF8; TRIM28; SETDB1; EZH2; RP UHRF1; CBX3; CBX5; ERK1; ERK2 AND HDAC2, SUBCELLULAR LOCATION, AND RP UBIQUITINATION. RX PubMed=32051553; DOI=10.1038/s41388-020-1206-7; RA Yu Z., Feng J., Wang W., Deng Z., Zhang Y., Xiao L., Wang Z., Liu C., RA Liu Q., Chen S., Wu M.; RT "The EGFR-ZNF263 signaling axis silences SIX3 in glioblastoma RT epigenetically."; RL Oncogene 39:3163-3178(2020). RN [9] RP FUNCTION. RX PubMed=32277030; DOI=10.1073/pnas.1920880117; RA Weiss R.J., Spahn P.N., Toledo A.G., Chiang A.W.T., Kellman B.P., Li J., RA Benner C., Glass C.K., Gordts P.L.S.M., Lewis N.E., Esko J.D.; RT "ZNF263 is a transcriptional regulator of heparin and heparan sulfate RT biosynthesis."; RL Proc. Natl. Acad. Sci. U.S.A. 117:9311-9317(2020). RN [10] RP VARIANT TRP-646. RX PubMed=27231705; DOI=10.1002/acn3.300; RA Saitsu H., Sonoda M., Higashijima T., Shirozu H., Masuda H., Tohyama J., RA Kato M., Nakashima M., Tsurusaki Y., Mizuguchi T., Miyatake S., Miyake N., RA Kameyama S., Matsumoto N.; RT "Somatic mutations in GLI3 and OFD1 involved in sonic hedgehog signaling RT cause hypothalamic hamartoma."; RL Ann. Clin. Transl. Neurol. 3:356-365(2016). CC -!- FUNCTION: Transcription factor that binds to the consensus sequence 5'- CC TCCTCCC-3' and acts as a transcriptional repressor (PubMed:32051553). CC Binds to the promoter region of SIX3 and recruits other proteins CC involved in chromatin modification and transcriptional corepression, CC resulting in methylation of the promoter and transcriptional repression CC (PubMed:32051553). Acts as a transcriptional repressor of HS3ST1 and CC HS3ST3A1 via binding to gene promoter regions (PubMed:32277030). CC {ECO:0000269|PubMed:32051553, ECO:0000269|PubMed:32277030}. CC -!- SUBUNIT: Interacts with a number of proteins involved in chromatin CC modification and transcriptional corepression including DNMT1, DNMT3A, CC HDAC2, PHF8, TRIM28/KAP1, SETDB1, EZH2, UHRF1, CBX3/HP1-gamma, and CC CBX5/HP1-alpha; recruits these proteins to the SIX3 promoter region, CC leading to SIX3 transcriptional repression (PubMed:32051553). Interacts CC with MAPK3/ERK1 and MAPK1/ERK2 (PubMed:32051553). CC {ECO:0000269|PubMed:32051553}. CC -!- INTERACTION: CC O14978; P49760: CLK2; NbExp=3; IntAct=EBI-744493, EBI-750020; CC O14978; P49761: CLK3; NbExp=3; IntAct=EBI-744493, EBI-745579; CC O14978; Q9NWQ4: GPATCH2L; NbExp=3; IntAct=EBI-744493, EBI-5666657; CC O14978; Q9NWQ4-1: GPATCH2L; NbExp=3; IntAct=EBI-744493, EBI-11959863; CC O14978; Q96AA8: JAKMIP2; NbExp=3; IntAct=EBI-744493, EBI-752007; CC O14978; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-744493, EBI-739832; CC O14978; O60437: PPL; NbExp=3; IntAct=EBI-744493, EBI-368321; CC O14978; P57086: SCAND1; NbExp=7; IntAct=EBI-744493, EBI-745846; CC O14978; Q9Y4C2: TCAF1; NbExp=3; IntAct=EBI-744493, EBI-750484; CC O14978; Q8WV44: TRIM41; NbExp=7; IntAct=EBI-744493, EBI-725997; CC O14978; P49910: ZNF165; NbExp=3; IntAct=EBI-744493, EBI-741694; CC O14978; P10073: ZSCAN22; NbExp=3; IntAct=EBI-744493, EBI-10178224; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:32051553}. CC -!- TISSUE SPECIFICITY: Expressed in heart, brain, placenta, lung, liver, CC skeletal muscle, kidney, pancreas, spleen, thymus, prostate, testis, CC ovary, small intestine, colon and leukocyte. CC {ECO:0000269|PubMed:9256059}. CC -!- PTM: Ubiquitinated, leading to proteasomal degradation. CC {ECO:0000269|PubMed:32051553}. CC -!- MISCELLANEOUS: May be involved in the EGFR-mediated promotion of CC invasion and anchorage-independent growth in glioblastomas via CC silencing of SIX3 (PubMed:32051553). May act as a prognostic indicator CC in glioblastoma patients, with increased expression correlating with CC poor prognosis (PubMed:32051553). {ECO:0000269|PubMed:32051553}. CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein CC 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; D88827; BAA21853.1; -; mRNA. DR EMBL; AK312421; BAG35331.1; -; mRNA. DR EMBL; AC004232; AAC24490.1; -; Genomic_DNA. DR EMBL; CH471112; EAW85379.1; -; Genomic_DNA. DR EMBL; BC008805; AAH08805.1; -; mRNA. DR CCDS; CCDS10499.1; -. DR RefSeq; NP_005732.2; NM_005741.4. DR AlphaFoldDB; O14978; -. DR SMR; O14978; -. DR BioGRID; 115431; 149. DR IntAct; O14978; 80. DR STRING; 9606.ENSP00000219069; -. DR GlyGen; O14978; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; O14978; -. DR PhosphoSitePlus; O14978; -. DR BioMuta; ZNF263; -. DR jPOST; O14978; -. DR MassIVE; O14978; -. DR PaxDb; 9606-ENSP00000219069; -. DR PeptideAtlas; O14978; -. DR ProteomicsDB; 48352; -. DR Antibodypedia; 24089; 282 antibodies from 24 providers. DR DNASU; 10127; -. DR Ensembl; ENST00000219069.6; ENSP00000219069.5; ENSG00000006194.11. DR GeneID; 10127; -. DR KEGG; hsa:10127; -. DR MANE-Select; ENST00000219069.6; ENSP00000219069.5; NM_005741.5; NP_005732.2. DR UCSC; uc002cuq.4; human. DR AGR; HGNC:13056; -. DR CTD; 10127; -. DR DisGeNET; 10127; -. DR GeneCards; ZNF263; -. DR HGNC; HGNC:13056; ZNF263. DR HPA; ENSG00000006194; Low tissue specificity. DR MIM; 604191; gene. DR neXtProt; NX_O14978; -. DR OpenTargets; ENSG00000006194; -. DR PharmGKB; PA37634; -. DR VEuPathDB; HostDB:ENSG00000006194; -. DR eggNOG; KOG1721; Eukaryota. DR GeneTree; ENSGT00940000159965; -. DR HOGENOM; CLU_002678_49_8_1; -. DR InParanoid; O14978; -. DR OMA; QQVTNQG; -. DR PhylomeDB; O14978; -. DR TreeFam; TF350829; -. DR PathwayCommons; O14978; -. DR Reactome; R-HSA-212436; Generic Transcription Pathway. DR SignaLink; O14978; -. DR BioGRID-ORCS; 10127; 15 hits in 1187 CRISPR screens. DR ChiTaRS; ZNF263; human. DR GenomeRNAi; 10127; -. DR Pharos; O14978; Tbio. DR PRO; PR:O14978; -. DR Proteomes; UP000005640; Chromosome 16. DR RNAct; O14978; protein. DR Bgee; ENSG00000006194; Expressed in calcaneal tendon and 199 other cell types or tissues. DR ExpressionAtlas; O14978; baseline and differential. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0003700; F:DNA-binding transcription factor activity; TAS:ProtInc. DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central. DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:NTNU_SB. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central. DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:NTNU_SB. DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL. DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:UniProtKB. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:UniProtKB. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB. DR GO; GO:0006355; P:regulation of DNA-templated transcription; TAS:ProtInc. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central. DR CDD; cd07765; KRAB_A-box; 1. DR CDD; cd07936; SCAN; 1. DR FunFam; 3.30.160.60:FF:001772; Uncharacterized protein; 1. DR FunFam; 3.30.160.60:FF:001024; Zinc finger and SCAN domain-containing protein 20; 1. DR FunFam; 3.30.160.60:FF:000620; Zinc finger protein 263; 1. DR FunFam; 3.30.160.60:FF:001749; Zinc finger protein 263; 1. DR FunFam; 3.30.160.60:FF:003262; Zinc finger protein 263; 1. DR FunFam; 1.10.4020.10:FF:000001; zinc finger protein 263 isoform X1; 1. DR FunFam; 3.30.160.60:FF:000540; zinc finger protein 263 isoform X1; 1. DR FunFam; 3.30.160.60:FF:002887; Zinc finger protein 263 isoform X2; 1. DR FunFam; 3.30.160.60:FF:002343; Zinc finger protein 33A; 1. DR FunFam; 3.30.160.60:FF:000953; Zinc finger protein 691; 1. DR Gene3D; 6.10.140.140; -; 1. DR Gene3D; 3.30.160.60; Classic Zinc Finger; 9. DR Gene3D; 1.10.4020.10; DNA breaking-rejoining enzymes; 1. DR InterPro; IPR001909; KRAB. DR InterPro; IPR036051; KRAB_dom_sf. DR InterPro; IPR003309; SCAN_dom. DR InterPro; IPR038269; SCAN_sf. DR InterPro; IPR036236; Znf_C2H2_sf. DR InterPro; IPR013087; Znf_C2H2_type. DR PANTHER; PTHR23235; KRUEPPEL-LIKE TRANSCRIPTION FACTOR; 1. DR PANTHER; PTHR23235:SF120; KRUPPEL-LIKE FACTOR 15; 1. DR Pfam; PF01352; KRAB; 1. DR Pfam; PF02023; SCAN; 1. DR Pfam; PF00096; zf-C2H2; 7. DR Pfam; PF13465; zf-H2C2_2; 1. DR SMART; SM00349; KRAB; 1. DR SMART; SM00431; SCAN; 1. DR SMART; SM00355; ZnF_C2H2; 9. DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 6. DR SUPFAM; SSF109640; KRAB domain (Kruppel-associated box); 1. DR SUPFAM; SSF47353; Retrovirus capsid dimerization domain-like; 1. DR PROSITE; PS50805; KRAB; 1. DR PROSITE; PS50804; SCAN_BOX; 1. DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 9. DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 9. PE 1: Evidence at protein level; KW DNA-binding; Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein; KW Proteomics identification; Reference proteome; Repeat; Repressor; KW Transcription; Transcription regulation; Ubl conjugation; Zinc; KW Zinc-finger. FT CHAIN 1..683 FT /note="Zinc finger protein 263" FT /id="PRO_0000047491" FT DOMAIN 41..123 FT /note="SCAN box" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00187" FT DOMAIN 217..289 FT /note="KRAB" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00119" FT ZN_FING 378..400 FT /note="C2H2-type 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 434..456 FT /note="C2H2-type 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 462..484 FT /note="C2H2-type 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 490..512 FT /note="C2H2-type 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 518..540 FT /note="C2H2-type 5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 575..597 FT /note="C2H2-type 6" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 603..625 FT /note="C2H2-type 7" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 631..653 FT /note="C2H2-type 8" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 659..681 FT /note="C2H2-type 9" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT REGION 147..185 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 230..301 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 322..368 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 230..246 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 166 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 178 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT CROSSLNK 17 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 157 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 285 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 299 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 376 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 573 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 582 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT VARIANT 310 FT /note="C -> S (in dbSNP:rs220379)" FT /id="VAR_052801" FT VARIANT 534 FT /note="V -> I (in dbSNP:rs34236132)" FT /id="VAR_052802" FT VARIANT 646 FT /note="R -> Q (in dbSNP:rs57710602)" FT /id="VAR_061943" FT VARIANT 646 FT /note="R -> W (found in a patient with hypothalamic FT hamartoma; uncertain significance; dbSNP:rs747714553)" FT /evidence="ECO:0000269|PubMed:27231705" FT /id="VAR_084704" FT CONFLICT 118 FT /note="D -> G (in Ref. 1; BAA21853)" FT /evidence="ECO:0000305" SQ SEQUENCE 683 AA; 77299 MW; 1E02C862FCE69265 CRC64; MASGPGSQER EGLLIVKLEE DCAWSQELPP PDPGPSPEAS HLRFRRFRFQ EAAGPREALS RLQELCHGWL RPEMRTKEQI LELLVLEQFL TILPQEIQSR VQELHPESGE EAVTLVEDMQ RELGRLRQQV TNHGRGTEVL LEEPLPLETA RESPSFKLEP METERSPGPR LQELLGPSPQ RDPQAVKERA LSAPWLSLFP PEGNMEDKEM TGPQLPESLE DVAMYISQEE WGHQDPSKRA LSRDTVQESY ENVDSLESHI PSQEVPGTQV GQGGKLWDPS VQSCKEGLSP RGPAPGEEKF ENLEGVPSVC SENIHPQVLL PDQARGEVPW SPELGRPHDR SQGDWAPPPE GGMEQALAGA SSGRELGRPK ELQPKKLHLC PLCGKNFSNN SNLIRHQRIH AAERLCMGVD CTEIFGGNPR FLSLHRAHLG EEAHKCLECG KCFSQNTHLT RHQRTHTGEK PYQCNICGKC FSCNSNLHRH QRTHTGEKPY KCPECGEIFA HSSNLLRHQR IHTGERPYKC PECGKSFSRS SHLVIHERTH ERERLYPFSE CGEAVSDSTP FLTNHGAHKA EKKLFECLTC GKSFRQGMHL TRHQRTHTGE KPYKCTLCGE NFSHRSNLIR HQRIHTGEKP YTCHECGDSF SHSSNRIRHL RTHTGERPYK CSECGESFSR SSRLMSHQRT HTG //