FOXC2_HUMAN
ID FOXC2_HUMAN Reviewed; 501 AA.
AC Q99958; C6KMR9; Q14DA6;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 206.
DE RecName: Full=Forkhead box protein C2;
DE AltName: Full=Forkhead-related protein FKHL14;
DE AltName: Full=Mesenchyme fork head protein 1;
DE Short=MFH-1 protein;
DE AltName: Full=Transcription factor FKH-14;
GN Name=FOXC2; Synonyms=FKHL14, MFH1;
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 [GENOMIC DNA], AND FUNCTION.
RX PubMed=9169153; DOI=10.1006/geno.1997.4695;
RA Miura N., Iida K., Kakinuma H., Yang X.-L., Sugiyama T.;
RT "Isolation of the mouse (MFH-1) and human (FKHL 14) mesenchyme fork head-1
RT genes reveals conservation of their gene and protein structures.";
RL Genomics 41:489-492(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT PHE-191.
RG NIEHS SNPs program;
RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 INVOLVEMENT IN LYD.
RX PubMed=11078474; DOI=10.1086/316915;
RA Fang J., Dagenais S.L., Erickson R.P., Arlt M.F., Glynn M.W., Gorski J.L.,
RA Seaver L.H., Glover T.W.;
RT "Mutations in FOXC2 (MFH-1), a forkhead family transcription factor, are
RT responsible for the hereditary lymphedema-distichiasis syndrome.";
RL Am. J. Hum. Genet. 67:1382-1388(2000).
RN [5]
RP INVOLVEMENT IN LYD.
RX PubMed=11371511; DOI=10.1093/hmg/10.11.1185;
RA Finegold D.N., Kimak M.A., Lawrence E.C., Levinson K.L., Cherniske E.M.,
RA Pober B.R., Dunlap J.W., Ferrell R.E.;
RT "Truncating mutations in FOXC2 cause multiple lymphedema syndromes.";
RL Hum. Mol. Genet. 10:1185-1189(2001).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-240, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-235 AND SER-240, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-219, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-215; SER-219; SER-232;
RP SER-240 AND SER-288, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-232 AND SER-240, AND
RP IDENTIFICATION BY 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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-240, 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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-215; SER-219; SER-232;
RP SER-240 AND SER-288, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma;
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 [14]
RP SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-219; SER-232; SER-240;
RP THR-247; SER-251; SER-281; SER-288 AND SER-367, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=23878394; DOI=10.1128/mcb.01387-12;
RA Ivanov K.I., Agalarov Y., Valmu L., Samuilova O., Liebl J., Houhou N.,
RA Maby-El Hajjami H., Norrmen C., Jaquet M., Miura N., Zangger N.,
RA Yla-Herttuala S., Delorenzi M., Petrova T.V.;
RT "Phosphorylation regulates FOXC2-mediated transcription in lymphatic
RT endothelial cells.";
RL Mol. Cell. Biol. 33:3749-3761(2013).
RN [15]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-214, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [16]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-184 AND LYS-214, AND
RP IDENTIFICATION BY MASS 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 [17]
RP STRUCTURE BY NMR OF 70-162.
RX PubMed=10669593; DOI=10.1006/jmbi.1999.3476;
RA van Dongen M.J., Cederberg A., Carlsson P., Enerback S., Wikstrom M.;
RT "Solution structure and dynamics of the DNA-binding domain of the
RT adipocyte-transcription factor FREAC-11.";
RL J. Mol. Biol. 296:351-359(2000).
RN [18]
RP VARIANT LPHDST LEU-125.
RX PubMed=11499682; DOI=10.1007/s004390100528;
RA Bell R., Brice G., Child A.H., Murday V.A., Mansour S., Sandy C.J.,
RA Collin J.R.O., Brady A.F., Callen D.F., Burnand K., Mortimer P.,
RA Jeffery S.;
RT "Analysis of lymphoedema-distichiasis families for FOXC2 mutations reveals
RT small insertions and deletions throughout the gene.";
RL Hum. Genet. 108:546-551(2001).
CC -!- FUNCTION: Transcriptional activator. Might be involved in the formation
CC of special mesenchymal tissues. {ECO:0000269|PubMed:9169153}.
CC -!- INTERACTION:
CC Q99958; Q99958: FOXC2; NbExp=2; IntAct=EBI-3956892, EBI-3956892;
CC Q99958; Q08379: GOLGA2; NbExp=3; IntAct=EBI-3956892, EBI-618309;
CC Q99958; Q9BYR6: KRTAP3-3; NbExp=3; IntAct=EBI-3956892, EBI-3957694;
CC Q99958; Q8N6F8: METTL27; NbExp=3; IntAct=EBI-3956892, EBI-8487781;
CC Q99958; Q93062: RBPMS; NbExp=3; IntAct=EBI-3956892, EBI-740322;
CC Q99958; Q86VP1: TAX1BP1; NbExp=3; IntAct=EBI-3956892, EBI-529518;
CC Q99958; P14373: TRIM27; NbExp=3; IntAct=EBI-3956892, EBI-719493;
CC Q99958; Q96IQ6; NbExp=3; IntAct=EBI-3956892, EBI-10295632;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00089,
CC ECO:0000269|PubMed:23878394}.
CC -!- PTM: Phosphorylation regulates FOXC2 transcriptional activity by
CC promoting its recruitment to chromatin. {ECO:0000269|PubMed:23878394}.
CC -!- DISEASE: Lymphedema-distichiasis syndrome (LPHDST) [MIM:153400]: An
CC autosomal dominant disorder characterized by primary limb lymphedema
CC associated with distichiasis (double rows of eyelashes, with extra
CC eyelashes growing from the Meibomian gland orifices). Swelling of the
CC extremities, due to altered lymphatic flow, usually appears in late
CC childhood or puberty. Most affected individuals have ocular findings
CC including corneal irritation, recurrent conjunctivitis, and
CC photophobia. Drooping of the upper eyelid (ptosis) is a variable
CC feature of the lymphedema-distichiasis syndrome, occurring in about 30%
CC of patients. {ECO:0000269|PubMed:11078474, ECO:0000269|PubMed:11371511,
CC ECO:0000269|PubMed:11499682}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/foxc2/";
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DR EMBL; Y08223; CAA69400.1; -; Genomic_DNA.
DR EMBL; GQ282998; ACS83751.1; -; Genomic_DNA.
DR EMBL; BC113437; AAI13438.1; -; mRNA.
DR EMBL; BC113439; AAI13440.1; -; mRNA.
DR CCDS; CCDS10958.1; -.
DR RefSeq; NP_005242.1; NM_005251.2.
DR PDB; 1D5V; NMR; -; A=70-162.
DR PDB; 6AKO; X-ray; 2.40 A; C=72-172.
DR PDB; 6AKP; X-ray; 2.32 A; C=72-172.
DR PDB; 6LBM; X-ray; 2.84 A; C=72-172.
DR PDB; 6O3T; X-ray; 3.06 A; A/B=70-164.
DR PDBsum; 1D5V; -.
DR PDBsum; 6AKO; -.
DR PDBsum; 6AKP; -.
DR PDBsum; 6LBM; -.
DR PDBsum; 6O3T; -.
DR AlphaFoldDB; Q99958; -.
DR SMR; Q99958; -.
DR BioGRID; 108592; 40.
DR IntAct; Q99958; 38.
DR MINT; Q99958; -.
DR STRING; 9606.ENSP00000326371; -.
DR iPTMnet; Q99958; -.
DR PhosphoSitePlus; Q99958; -.
DR BioMuta; FOXC2; -.
DR DMDM; 3024149; -.
DR EPD; Q99958; -.
DR jPOST; Q99958; -.
DR MassIVE; Q99958; -.
DR MaxQB; Q99958; -.
DR PaxDb; Q99958; -.
DR PeptideAtlas; Q99958; -.
DR PRIDE; Q99958; -.
DR ProteomicsDB; 78542; -.
DR Antibodypedia; 17195; 567 antibodies from 36 providers.
DR CPTC; Q99958; 1 antibody.
DR DNASU; 2303; -.
DR Ensembl; ENST00000649859.1; ENSP00000497759.1; ENSG00000176692.8.
DR GeneID; 2303; -.
DR KEGG; hsa:2303; -.
DR MANE-Select; ENST00000649859.1; ENSP00000497759.1; NM_005251.3; NP_005242.1.
DR UCSC; uc002fjq.4; human.
DR CTD; 2303; -.
DR DisGeNET; 2303; -.
DR GeneCards; FOXC2; -.
DR GeneReviews; FOXC2; -.
DR HGNC; HGNC:3801; FOXC2.
DR HPA; ENSG00000176692; Low tissue specificity.
DR MalaCards; FOXC2; -.
DR MIM; 153400; phenotype.
DR MIM; 602402; gene.
DR neXtProt; NX_Q99958; -.
DR OpenTargets; ENSG00000176692; -.
DR Orphanet; 33001; Lymphedema-distichiasis syndrome.
DR PharmGKB; PA28218; -.
DR VEuPathDB; HostDB:ENSG00000176692; -.
DR eggNOG; KOG2294; Eukaryota.
DR GeneTree; ENSGT00940000162619; -.
DR HOGENOM; CLU_035722_3_1_1; -.
DR InParanoid; Q99958; -.
DR OMA; REMFTSH; -.
DR OrthoDB; 1270467at2759; -.
DR PhylomeDB; Q99958; -.
DR TreeFam; TF316127; -.
DR PathwayCommons; Q99958; -.
DR SignaLink; Q99958; -.
DR SIGNOR; Q99958; -.
DR BioGRID-ORCS; 2303; 37 hits in 1096 CRISPR screens.
DR EvolutionaryTrace; Q99958; -.
DR GeneWiki; FOXC2; -.
DR GenomeRNAi; 2303; -.
DR Pharos; Q99958; Tbio.
DR PRO; PR:Q99958; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q99958; protein.
DR Bgee; ENSG00000176692; Expressed in vena cava and 135 other tissues.
DR Genevisible; Q99958; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0016604; C:nuclear body; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0031490; F:chromatin DNA binding; IDA:UniProtKB.
DR GO; GO:0001216; F:DNA-binding transcription activator activity; IDA:UniProtKB.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:BHF-UCL.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:1990841; F:promoter-specific chromatin binding; ISS:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:BHF-UCL.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:BHF-UCL.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISS:BHF-UCL.
DR GO; GO:0009653; P:anatomical structure morphogenesis; IBA:GO_Central.
DR GO; GO:0003275; P:apoptotic process involved in outflow tract morphogenesis; IEA:Ensembl.
DR GO; GO:0048844; P:artery morphogenesis; IEA:Ensembl.
DR GO; GO:0097746; P:blood vessel diameter maintenance; IEA:Ensembl.
DR GO; GO:0001974; P:blood vessel remodeling; IEA:Ensembl.
DR GO; GO:0001569; P:branching involved in blood vessel morphogenesis; IEA:Ensembl.
DR GO; GO:0043010; P:camera-type eye development; IEA:Ensembl.
DR GO; GO:0060038; P:cardiac muscle cell proliferation; IEA:Ensembl.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0030199; P:collagen fibril organization; IEA:Ensembl.
DR GO; GO:0035050; P:embryonic heart tube development; IEA:Ensembl.
DR GO; GO:0048703; P:embryonic viscerocranium morphogenesis; IEA:Ensembl.
DR GO; GO:0072011; P:glomerular endothelium development; IEA:Ensembl.
DR GO; GO:0072144; P:glomerular mesangial cell development; IEA:Ensembl.
DR GO; GO:0007507; P:heart development; IMP:DFLAT.
DR GO; GO:0008286; P:insulin receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0001946; P:lymphangiogenesis; IMP:UniProtKB.
DR GO; GO:0007498; P:mesoderm development; NAS:UniProtKB.
DR GO; GO:0001656; P:metanephros development; IEA:Ensembl.
DR GO; GO:1902257; P:negative regulation of apoptotic process involved in outflow tract morphogenesis; IEA:Ensembl.
DR GO; GO:0120163; P:negative regulation of cold-induced thermogenesis; IMP:YuBioLab.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:BHF-UCL.
DR GO; GO:0014032; P:neural crest cell development; IEA:Ensembl.
DR GO; GO:0007219; P:Notch signaling pathway; IEA:Ensembl.
DR GO; GO:0001503; P:ossification; IEA:Ensembl.
DR GO; GO:0048343; P:paraxial mesodermal cell fate commitment; IEA:Ensembl.
DR GO; GO:0072112; P:podocyte differentiation; IEA:Ensembl.
DR GO; GO:0033630; P:positive regulation of cell adhesion mediated by integrin; ISS:BHF-UCL.
DR GO; GO:0090050; P:positive regulation of cell migration involved in sprouting angiogenesis; ISS:BHF-UCL.
DR GO; GO:0010595; P:positive regulation of endothelial cell migration; ISS:BHF-UCL.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0035470; P:positive regulation of vascular wound healing; ISS:BHF-UCL.
DR GO; GO:0046620; P:regulation of organ growth; IEA:Ensembl.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0009725; P:response to hormone; IDA:UniProtKB.
DR GO; GO:0001756; P:somitogenesis; IEA:Ensembl.
DR GO; GO:0001657; P:ureteric bud development; IEA:Ensembl.
DR GO; GO:0048010; P:vascular endothelial growth factor receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0055010; P:ventricular cardiac muscle tissue morphogenesis; IEA:Ensembl.
DR CDD; cd00059; FH; 1.
DR DisProt; DP02231; -.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR001766; Fork_head_dom.
DR InterPro; IPR018122; TF_fork_head_CS_1.
DR InterPro; IPR030456; TF_fork_head_CS_2.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR Pfam; PF00250; Forkhead; 1.
DR PRINTS; PR00053; FORKHEAD.
DR SMART; SM00339; FH; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR PROSITE; PS00657; FORK_HEAD_1; 1.
DR PROSITE; PS00658; FORK_HEAD_2; 1.
DR PROSITE; PS50039; FORK_HEAD_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Developmental protein; Disease variant;
KW DNA-binding; Isopeptide bond; Methylation; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation;
KW Ubl conjugation.
FT CHAIN 1..501
FT /note="Forkhead box protein C2"
FT /id="PRO_0000091808"
FT DNA_BIND 71..162
FT /note="Fork-head"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00089"
FT REGION 167..208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 232..268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 383..420
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 172..186
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 232..250
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 397..413
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 215
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 219
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:23878394,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 232
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:23878394,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 235
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18220336"
FT MOD_RES 240
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:23878394,
FT ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18220336,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 247
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:23878394"
FT MOD_RES 251
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:23878394"
FT MOD_RES 279
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q61850"
FT MOD_RES 281
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:23878394"
FT MOD_RES 288
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:23878394,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163"
FT MOD_RES 293
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q61850"
FT MOD_RES 367
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:23878394"
FT MOD_RES 458
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q61850"
FT CROSSLNK 184
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 214
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:28112733"
FT VARIANT 125
FT /note="S -> L (in LPHDST; dbSNP:rs121909106)"
FT /evidence="ECO:0000269|PubMed:11499682"
FT /id="VAR_018418"
FT VARIANT 191
FT /note="S -> F (in dbSNP:rs78018668)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_060950"
FT HELIX 77..87
FT /evidence="ECO:0007829|PDB:6AKP"
FT STRAND 88..91
FT /evidence="ECO:0007829|PDB:6O3T"
FT HELIX 95..105
FT /evidence="ECO:0007829|PDB:6AKP"
FT HELIX 107..110
FT /evidence="ECO:0007829|PDB:6AKP"
FT HELIX 113..126
FT /evidence="ECO:0007829|PDB:6AKP"
FT STRAND 130..133
FT /evidence="ECO:0007829|PDB:6AKP"
FT STRAND 140..143
FT /evidence="ECO:0007829|PDB:6AKO"
FT STRAND 145..148
FT /evidence="ECO:0007829|PDB:6AKP"
FT HELIX 150..152
FT /evidence="ECO:0007829|PDB:6AKP"
FT STRAND 159..163
FT /evidence="ECO:0007829|PDB:6AKP"
SQ SEQUENCE 501 AA; 53719 MW; F66513878EDC3A87 CRC64;
MQARYSVSDP NALGVVPYLS EQNYYRAAGS YGGMASPMGV YSGHPEQYSA GMGRSYAPYH
HHQPAAPKDL VKPPYSYIAL ITMAIQNAPE KKITLNGIYQ FIMDRFPFYR ENKQGWQNSI
RHNLSLNECF VKVPRDDKKP GKGSYWTLDP DSYNMFENGS FLRRRRRFKK KDVSKEKEER
AHLKEPPPAA SKGAPATPHL ADAPKEAEKK VVIKSEAASP ALPVITKVET LSPESALQGS
PRSAASTPAG SPDGSLPEHH AAAPNGLPGF SVENIMTLRT SPPGGELSPG AGRAGLVVPP
LALPYAAAPP AAYGQPCAQG LEAGAAGGYQ CSMRAMSLYT GAERPAHMCV PPALDEALSD
HPSGPTSPLS ALNLAAGQEG ALAATGHHHQ HHGHHHPQAP PPPPAPQPQP TPQPGAAAAQ
AASWYLNHSG DLNHLPGHTF AAQQQTFPNV REMFNSHRLG IENSTLGESQ VSGNASCQLP
YRSTPPLYRH AAPYSYDCTK Y
