ZN263_HUMAN
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 03-AUG-2022, entry version 191.
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 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=5; IntAct=EBI-744493, EBI-745846;
CC O14978; Q9Y4C2: TCAF1; NbExp=3; IntAct=EBI-744493, EBI-750484;
CC O14978; Q8WV44: TRIM41; NbExp=5; 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}.
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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; 147.
DR IntAct; O14978; 74.
DR STRING; 9606.ENSP00000219069; -.
DR iPTMnet; O14978; -.
DR PhosphoSitePlus; O14978; -.
DR BioMuta; ZNF263; -.
DR EPD; O14978; -.
DR jPOST; O14978; -.
DR MassIVE; O14978; -.
DR MaxQB; O14978; -.
DR PaxDb; O14978; -.
DR PeptideAtlas; O14978; -.
DR PRIDE; O14978; -.
DR Antibodypedia; 24089; 233 antibodies from 23 providers.
DR DNASU; 10127; -.
DR Ensembl; ENST00000219069.6; ENSP00000219069.5; ENSG00000006194.10.
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 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; NVEDKEM; -.
DR PhylomeDB; O14978; -.
DR TreeFam; TF350829; -.
DR PathwayCommons; O14978; -.
DR Reactome; R-HSA-212436; Generic Transcription Pathway.
DR SignaLink; O14978; -.
DR BioGRID-ORCS; 10127; 13 hits in 1100 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 197 other tissues.
DR ExpressionAtlas; O14978; baseline and differential.
DR Genevisible; O14978; HS.
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:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; TAS:ProtInc.
DR CDD; cd07765; KRAB_A-box; 1.
DR CDD; cd07936; SCAN; 1.
DR Gene3D; 1.10.4020.10; -; 1.
DR InterPro; IPR001909; KRAB.
DR InterPro; IPR036051; KRAB_dom_sf.
DR InterPro; IPR003309; SCAN_dom.
DR InterPro; IPR038269; SCAN_sf.
DR InterPro; IPR030752; ZNF263.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR23226:SF224; PTHR23226:SF224; 1.
DR Pfam; PF01352; KRAB; 1.
DR Pfam; PF02023; SCAN; 1.
DR Pfam; PF00096; zf-C2H2; 9.
DR SMART; SM00349; KRAB; 1.
DR SMART; SM00431; SCAN; 1.
DR SMART; SM00355; ZnF_C2H2; 9.
DR SUPFAM; SSF109640; SSF109640; 1.
DR SUPFAM; SSF57667; SSF57667; 6.
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 Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; 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 246..269
FT /note="Polar 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; unknown pathological significance;
FT 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
